{"id":904,"date":"2021-03-23T16:59:14","date_gmt":"2021-03-23T15:59:14","guid":{"rendered":"http:\/\/www.afmb.univ-mrs.fr\/?post_type=member&#038;p=904"},"modified":"2026-03-30T12:52:44","modified_gmt":"2026-03-30T11:52:44","slug":"pascale-marchot","status":"publish","type":"member","link":"https:\/\/www.afmb.univ-mrs.fr\/en\/member\/pascale-marchot\/","title":{"rendered":"Pascale Marchot"},"content":{"rendered":"\n<p>PI of the <strong>Neurobiology<\/strong> theme of the team<\/p>\n\n\n\n<p>Ph.D. Univ Aix-Marseille-II (now Aix-Marseille Univ.)<\/p>\n\n\n\n<p>HDR Univ. de la M\u00e9diterran\u00e9e (now Aix-Marseille Univ.)<\/p>\n\n\n\n<p>DR1-CNRS<\/p>\n\n\n\n<p>Vice-president of the <a href=\"http:\/\/sfet.asso.fr\/international\/board-directors\/board-of-directors.html\">SFET<\/a><\/p>\n\n\n\n<div class=\"wp-block-group imageSlider\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\"><div class=\"wp-block-image is-resized\">\n<figure class=\"aligncenter size-large\"><img loading=\"lazy\" decoding=\"async\" width=\"600\" height=\"500\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-crystalline-du-complexe-dimerique.png\" alt=\"\" class=\"wp-image-241\" style=\"width:462px;height:auto\" srcset=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-crystalline-du-complexe-dimerique.png 600w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-crystalline-du-complexe-dimerique-300x250.png 300w\" sizes=\"auto, (max-width: 600px) 100vw, 600px\" \/><figcaption class=\"wp-element-caption\">Crystal structure of the pentameric complex formed between AChBP, a soluble surrogate of the extracellular ligand-binding domain of the nicotinic receptor to ACh (yellow), and alpha-conotoxin IM1, a cysteine-rich peptidic toxin from cone snail venom (magenta) (Hansen et al, EMBO J 2005; copyright Yves Bourne &amp; Pascale Marchot, AFMB).<\/figcaption><\/figure><\/div>\n\n<div class=\"wp-block-image is-resized\">\n<figure class=\"aligncenter size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"509\" height=\"321\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/structure-crystalline-du-complexe-dimerique-2.png\" alt=\"\" class=\"wp-image-2115\" style=\"width:449px;height:auto\" srcset=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/structure-crystalline-du-complexe-dimerique-2.png 509w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/structure-crystalline-du-complexe-dimerique-2-500x315.png 500w\" sizes=\"auto, (max-width: 509px) 100vw, 509px\" \/><figcaption class=\"wp-element-caption\">Crystal structure of the dimeric complex formed between acetylcholinesterase, a key enzyme for cholinergic synapse functioning (yellow), and fasciculin, a three-fingered toxin from mamba venom (purple) (Bourne et al, Cell 1995; copyright Yves Bourne &amp; Pascale Marchot, AFMB).<\/figcaption><\/figure><\/div>\n\n<div class=\"wp-block-image is-resized\">\n<figure class=\"aligncenter size-large\"><img loading=\"lazy\" decoding=\"async\" width=\"600\" height=\"500\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-cristalline-du-dimere-de-neuroligine.jpg\" alt=\"\" class=\"wp-image-244\" style=\"width:466px;height:auto\" srcset=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-cristalline-du-dimere-de-neuroligine.jpg 600w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-cristalline-du-dimere-de-neuroligine-300x250.jpg 300w\" sizes=\"auto, (max-width: 600px) 100vw, 600px\" \/><figcaption class=\"wp-element-caption\">Crystal structure of the neuroligin dimer (yellow subunits, purple dimerization domain) associated with two neurexin-beta molecules (green). The red spheres on the neuroligin denote the positions of mutations found in some autistic patients (Fabrichny et al, Neuron 2004; Leone et al, EMBO J 2010; design by Michael E. Pique, TSRI, La Jolla, CA; child outline provided by the Waisman Laboratory for Brain Imaging and Behavior, University of Wisconsin-Madison, WI, USA).<\/figcaption><\/figure><\/div>\n\n<div class=\"wp-block-image is-resized\">\n<figure class=\"aligncenter size-large\"><img loading=\"lazy\" decoding=\"async\" width=\"600\" height=\"500\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-cristalline-du-complexe-pentamerique.jpg\" alt=\"\" class=\"wp-image-245\" style=\"width:462px;height:auto\" srcset=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-cristalline-du-complexe-pentamerique.jpg 600w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/03\/structure-cristalline-du-complexe-pentamerique-300x250.jpg 300w\" sizes=\"auto, (max-width: 600px) 100vw, 600px\" \/><figcaption class=\"wp-element-caption\">Crystal structure of the pentameric complex formed between AChBP, a soluble surrogate of the extracellular ligand-binding domain of the nicotinic receptor to ACh (yellow), and alpha-cobratoxin, a three-fingered toxin from cobra venom (purple); the figure background displays the layout of the complexes in the crystal (Bourne et al, EMBO J 2005; copyright Yves Bourne &amp; Pascale Marchot, AFMB).<\/figcaption><\/figure><\/div>\n\n<div class=\"wp-block-image is-resized\">\n<figure class=\"aligncenter size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"320\" height=\"94\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/Logo-LIA-villes-tutelles-cropped.png\" alt=\"\" class=\"wp-image-2093\"\/><figcaption class=\"wp-element-caption\">International Associated Laboratory &#8216;Structure-Guided Investigations into Disease States and Therapeutic Strategies (SGIDSTS)&#8221; between the AFMB lab in Marseille, France, and the Palmer Taylor Laboratory, Skaggs School of Pharmacy and Pharmaceutical Sciences (SSPPS) in La Jolla (CA), signed by the CNRS, AMU, and UCSD for years 2013-2016.<\/figcaption><\/figure><\/div>\n\n<div class=\"wp-block-image is-resized\">\n<figure class=\"aligncenter size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"980\" height=\"289\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/Bandeau-1.png\" alt=\"\" class=\"wp-image-2924\" style=\"width:516px;height:auto\" srcset=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/Bandeau-1.png 980w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/Bandeau-1-500x147.png 500w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/Bandeau-1-768x226.png 768w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/01\/Bandeau-1-800x235.png 800w\" sizes=\"auto, (max-width: 980px) 100vw, 980px\" \/><figcaption class=\"wp-element-caption\">Banner of the XVth International Symposium on Cholinergic Mechanisms organized in Marseille in Oct-2016 by Pascale Marchot and Yves Bourne.<\/figcaption><\/figure><\/div>\n\n<div class=\"wp-block-image is-resized\">\n<figure class=\"aligncenter size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"556\" height=\"417\" src=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/12\/Molecule-of-the-Month-Click-Chemistry-2xCropped-3.png\" alt=\"\" class=\"wp-image-5309\" style=\"width:442px;height:auto\" srcset=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/12\/Molecule-of-the-Month-Click-Chemistry-2xCropped-3.png 556w, https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2022\/12\/Molecule-of-the-Month-Click-Chemistry-2xCropped-3-500x375.png 500w\" sizes=\"auto, (max-width: 556px) 100vw, 556px\" \/><figcaption class=\"wp-element-caption\"><br><a href=\"https:\/\/pdb101.rcsb.org\/motm\/276\">RCSB PDB-101, December 2022<\/a>: the \u201cMolecule of the month\u201d was about click-chemistry with, as an example, our works on acetylcholinesterase in collaboration with K. Barry Sharpless (Bourne et al, PNAS 2004, JACS 2016).<\/figcaption><\/figure><\/div><\/div><\/div>\n\n\n\n<div class=\"wp-block-group\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading\" id=\"interests\">Interests<\/h4>\n\n\n\n<div class=\"wp-block-group\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p>My research addresses the structure-function relationships of animal toxins, enzymes, receptors\/channels, and cell-adhesion molecules that are of a considerable neurobiological interest due to their involvement(s) in the genesis, physiology, pathology, or aging of central and peripheral synaptic structures. My objectives are to document (i) the molecular and structural bases of these enzymes, receptors and adhesion molecules and those of the reactivity and specificity of their peptidic or organic partners; (ii) the molecular mechanisms and dynamic events associated with the formation and stabilization of the complex and leading to a modification of the activity of these enzymes, receptors and adhesion molecules.<\/p>\n\n\n\n<p>Fields of investigation: Biochemistry &#8211; Molecular toxinology, pharmacology and enzymology &#8211; Reactivity and structure of biological molecules &#8211; Molecular neuroscience and neurobiology &#8211; Physiology, pathology, and aging of the synapse.<\/p>\n\n\n\n<p><a href=\"https:\/\/hal.science\/search\/index\/?q=pascale+marchot&amp;rows=30&amp;sort=producedDate_tdate+desc\">HAL<\/a>, <a href=\"https:\/\/orcid.org\/0000-0003-0630-0541\">ORCID<\/a><a href=\"https:\/\/scholar.google.com\/citations?hl=fr&amp;user=KvAFsUYAAAAJ&amp;view_op=list_works&amp;sortby=pubdate\">,<\/a> <a href=\"https:\/\/scholar.google.com\/citations?hl=fr&amp;user=KvAFsUYAAAAJ&amp;view_op=list_works&amp;sortby=pubdate\">Google Scholar<\/a>, <a href=\"https:\/\/www.scopus.com\/authid\/detail.uri?authorId=7005343936\">Scopus<\/a><\/p>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"career\">Career<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li>2014 &#8211; current: co-PI (with Yves Bourne) of team &#8220;Structural Neurobiology and Glycobiology&#8221;, AFMB lab, Marseille<\/li>\n\n\n\n<li>2013 &#8211; 2016: French coordinator of the International Associated Laboratory &#8220;SGIDSTS&#8221; (CNRS\/AMU\/UCSD) (US coordinator: Palmer Taylor)<\/li>\n\n\n\n<li>2012 &#8211; 2013: PI of theme &#8220;Structural Neurobiology&#8221;, team &#8220;Structural Neurobiology and Glycobiology&#8221;, lab &#8220;Architecture et Fonction des Macromol\u00e9cules Biologiques&#8221; (AFMB), Marseille<\/li>\n\n\n\n<li>2008 &#8211; 2011: PI of team &#8220;Toxines Animales et Cibles Macromoleculaires&#8221; (ToxCiM), lab CRN2M, Marseille<\/li>\n\n\n\n<li>2000 &#8211; 2007: PI of team &#8220;R\u00e9activit\u00e9 et Structure de Macromol\u00e9cules Biologiques&#8221;, lab &#8220;Ing\u00e9nierie des Prot\u00e9ines&#8221;\/&#8221;BIMC&#8221;, Marseille<\/li>\n<\/ul>\n\n\n\n<p><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>2012 &#8211; current: Permanent CNRS Researcher, lab &#8220;Architecture et Fonction des Macromol\u00e9cules Biologiques&#8221; (AFMB), Marseille<\/li>\n\n\n\n<li>1996 &#8211; 2011: Permanent CNRS Researcher, labs &#8220;Ing\u00e9nierie des Prot\u00e9ines&#8221;, then &#8220;Biologie des Interactions Mol\u00e9culaires et Cellulaires&#8221; (BIMC), then &#8220;Centre de Recherches en Neurobiologie et Neurophysiologie de Marseille&#8221; (CRN2M), Marseille (same lab, different names).<\/li>\n\n\n\n<li>1994 &#8211; 1995: Permanent CNRS Researcher, sabbatical 2 yrs at the Dept Pharmacology, UCSD, La Jolla CA (USA)<\/li>\n\n\n\n<li>1989 &#8211; 1993: Permanent CNRS Researcher, lab &#8220;Biochimie &#8211; Ing\u00e9nierie des Prot\u00e9ines&#8221;, Marseille<\/li>\n\n\n\n<li>1988, October 15: recruted by the CNRS<\/li>\n\n\n\n<li>1987 &#8211; 1988: Post-doc, lab &#8220;Biochimie &#8211; Ing\u00e9nierie des Prot\u00e9ines&#8221;, Marseille<\/li>\n\n\n\n<li>1983 &#8211; 1986: DEA + PhD thesis Sp. Neurosciences Mol\u00e9culaires, lab &#8220;Biochimie&#8221;, Marseille<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"univ-diploma\">Univ Diploma<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li>1999 &#8211; Habilitation \u00e0 Diriger les Recherches (HDR), sp. Neuroscience, Univ. M\u00e9diterran\u00e9e, Marseille &#8220;Fasciculines et ac\u00e9tylcholinest\u00e9rase, une histoire d\u2019atomes crochus&#8221;. Jury: Cassian Bon, Jacques Grassi, Andr\u00e9 Nieoullon, Herv\u00e9 Rochat, Herman van Tilbeurgh, Robert Verger.<\/li>\n\n\n\n<li>1986 &#8211; Th\u00e8se Univ. Aix-Marseille II, sp. Neurosciences, Marseille &#8220;Contribution \u00e0 l\u2019\u00e9tude de la purification et du mode d\u2019action des toxines des venins de serpents Elapidae&#8221;. Thesis director: Herv\u00e9 Rochat; supervisor: Pierre E. Bougis. Jury: Pierre Fromageot, Fran\u00e7ois Miranda, Herv\u00e9 Rochat, Rolland Rosset.<\/li>\n\n\n\n<li>1983 &#8211; Dipl\u00f4me d\u2019Etudes Approfondies (DEA, now Master-2), sp. Biologie Cellulaire et Mol\u00e9culaire, Univ. Aix-Marseille II &#8220;Chromatographie d\u2019immunoaffinit\u00e9 anti-phospholipase A2 et iodation d\u2019une cardiotoxine du venin de <em>Naja mossambica mossambica<\/em>&#8220;. Director: Herv\u00e9 Rochat; supervisor: Pierre E. Bougis.<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"awards\">Awards<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li>2017 : Nomination to the Club-M-Ambassadeurs de la Ville de Marseille<\/li>\n\n\n\n<li>2017: Trophy of Attractivness &#8211; Congress by the Ville de Marseille, for having organized the XVth International Symposium on Cholinergic Mechanisms (XVth ISCM) in 2016<\/li>\n\n\n\n<li>2016&nbsp;: B.P. Doctor Memorial Young Investigator Travel Award, <em>honoris causa<\/em><\/li>\n\n\n\n<li>2013-2016&nbsp;: Prime d\u2019Excellence Scientifique (PES) by the CNRS<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"councils-committees\">Councils &amp; Committees<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p><strong>Councils and committees<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li>Toxins (MDPI), Editorial Board Member, current.<\/li>\n\n\n\n<li>Integrative Structural Biology Meeting 2023 (<a href=\"https:\/\/bsi-2023.cnrs.fr\/\">BSI-2023<\/a>, Marseille, France), Organizing Committee.<\/li>\n\n\n\n<li>Supervisor <a href=\"https:\/\/marie-sklodowska-curie-actions.ec.europa.eu\/actions\/postdoctoral-fellowships\">MSCA Postdoctoral Fellowship<\/a> and advisor <a href=\"https:\/\/civis3i.univ-amu.fr\/en\/find-advisor\">CIVIS 3i<\/a> for the AFMB lab, since 2021.<\/li>\n\n\n\n<li>Participant\/member European Venom Network (<a href=\"https:\/\/euven-network.eu\/\">EUVEN<\/a>) Working Groups WG1 &#8220;Novel targets in venom research&#8221;, WG4 &#8220;Web ressources&#8221; and WG5 &#8220;Training&#8221;, since 2021.<\/li>\n\n\n\n<li>Volunteer for the National Research Infrastructure and epidemiological cohort <a href=\"https:\/\/www.constances.fr\/\">Constance<\/a>, since 2018.<\/li>\n\n\n\n<li>J. Biol. Chem., editorial board member, 2016-2021.<\/li>\n\n\n\n<li>GTBio 2014, scientific committee, solicited member.<\/li>\n\n\n\n<li>XIV-th ISCM (2013, China), <a href=\"http:\/\/tox.umh.es\/12thChE\/index.html\">12-th ChE<\/a> (2015, Spain), <a href=\"https:\/\/iscm.sciencesconf.org\/\">XV-th ISCM<\/a> (2016, France): Organizing Committees &amp; International Advisory Boards, elected member.<\/li>\n\n\n\n<li>Soci\u00e9t\u00e9 Fran\u00e7aise pour l\u2019Etude des Toxines (<a href=\"http:\/\/sfet.asso.fr\/\">SFET<\/a>), Scientific, Administrative, Meeting organization &amp; Edition Committees, elected member, 2007 \u2013 current, and vice-president 2025-current.<\/li>\n\n\n\n<li>Vaincre la Mucoviscidose (VLM, ex- AFLM), Scientific Committee, elected member, 2002-2008.<\/li>\n<\/ul>\n\n\n\n<p><strong>PhD theses and HDR committees<\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><em>St\u00e9phanie Simon<\/em>, Laboratoire de Neurobiologie Cellulaire et Mol\u00e9culaire, ENS, Paris, May 1999, &#8220;Structure fonctionnelle de l&#8217;ac\u00e9tylcholinest\u00e9rase: mise en \u00e9vidence d&#8217;un nouveau site r\u00e9gulateur &#8211; organisation des oligom\u00e8res&#8221;, Ph.D. Univ. Pierre et Marie Curie (Paris VI), sp. Siences de la vie &#8211; Pharmacologie mol\u00e9culaire et cellulaire. As an examiner, with Jean-Pierre Toutant and Richard Rotundo (rapporteurs), Jacques Grassi (examiner), Michel Morange (president), Jean Massouli\u00e9 (supervisor).<\/li>\n\n\n\n<li><em>St\u00e9phanie Antil-Delbeke<\/em>, DIEP, CEA Saclay, Gif-sur-Yvette, Oct 2000, &#8220;Quels sont les m\u00e9canismes mol\u00e9culaires impliqu\u00e9s dans la sp\u00e9cificit\u00e9 d&#8217;interaction de neurotoxines pour les r\u00e9cepteurs nicotiniques de type musculaire et neuronal alpha7?&#8221;, Ph.D. Univ. Ren\u00e9 Descartes (Paris V), Discipline: Sciences pharmaceutiques, sp. Pharmacologie mol\u00e9culaire, pharmacologie exp\u00e9rimentale, m\u00e9tabolisme. En tant que rapporteur, with Hugues Bedouelle (rapporteur), Daniel Bertrand, Pierre-Jean Corringer, Andr\u00e9 M\u00e9nez (examiners), Christiane Garbay (president), Denis Servent (supervisor).<\/li>\n\n\n\n<li><em>Carole Fruchart-Gaillard<\/em>, DIEP, CEA Saclay, Gif-sur-Yvette, June 2003, &#8220;Caract\u00e9risation pharmacologique et structurale de l\u2019interaction de neurotoxines sur des r\u00e9cepteurs cholinergiques&#8221;, Ph.D. Univ. Paris VI, sp. Biologie cellulaire et mol\u00e9culaire. As a rapporteur, with Jean-Louis Galzi (rapporteur), Pierre Nicolas and Andr\u00e9 M\u00e9nez (examiners), Denis Servent (supervisor).<\/li>\n\n\n\n<li><em>Ludovic Renault<\/em>, Laboratoire d\u2019Ing\u00e9nierie des Prot\u00e9ines, IFR Jean Roche, Marseille, Dec 2005, &#8220;Approche structurale de l\u2019inhibition de l\u2019ac\u00e9tylcholinest\u00e9rase par des anticorps monoclonaux&#8221;, Ph.D. Univ. de la M\u00e9diterran\u00e9e, sp. Neurosciences, As the thesis supervisor, with Jean Massouli\u00e9 and Herman van Tilbeurgh (rapporteurs), Jacques Grassi and Yves Bourne (examiners), Alain Enjalbert (president).<\/li>\n\n\n\n<li><em>No\u00ebl Perrier<\/em>, Laboratoire de Neurobiologie, ENS, Paris, Dec 2005, &#8220;Expression et accumulation fonctionnelle de l\u2019ac\u00e9tylcholinest\u00e9rase dans le syst\u00e8me nerveux central&#8221;, Ph.D. Univ. Ren\u00e9 Descartes (Paris V), Discipline Sciences de la Vie et de la Mati\u00e8re, sp. Biologie de la cellule normale et pathologique. As a rapporteur, with Nicolas Morel (rapporteur), Mich\u00e8le Garlatti and Jacques Mallet (examiners), Pierre-Olivier Couraud (president), Jean Massouli\u00e9 (supervisor).<\/li>\n\n\n\n<li><em>S\u00e9verine Marconi<\/em>, Neurobiologie des Canaux Ioniques, IFR Jean Roche, Marseille, Nov 2008, &#8220;Dosage de l\u2019activit\u00e9 endoprot\u00e9olytique de neurotoxines clostridiales&#8221;, Ph.D. Univ. de la M\u00e9diterran\u00e9e, sp. Neurosciences. As an examiner, with Marie-Bernadette Villiers and Michel R. Popoff (rapporteurs), Claire Dane and Christian L\u00e9v\u00eaque (examiners), Alain Enjalbert (president), Nicole Moutot (supervisor).<\/li>\n\n\n\n<li><em>Gr\u00e9goire Mondielli<\/em>, team ToxCiM, CRN2M, IFR Jean Roche, Marseille, Dec 2011, &#8220;\u00c9tude fonctionnelle de l\u2019AChE&nbsp;: r\u00e9gulation de la catalyse par la r\u00e9gion de la porte arri\u00e8re, et recherche d\u2019un partenaire non-catalytique endog\u00e8ne. Mise en \u00e9vidence et caract\u00e9risation d\u2019une nouvelle cible de la fasciculine&#8221;, Ph.D. Univ. de la M\u00e9diterran\u00e9e, sp. Neurosciences. As the thesis supervisor, with Eric Krejci and Denis Servent (rapporteurs), St\u00e9phanie Simon (examiner), Herv\u00e9 Darbon (examiner and president).<\/li>\n\n\n\n<li><em>Guillaume Blanchet<\/em>, team Toxines, R\u00e9cepteurs et Canaux, Service d&#8217;Ing\u00e9nierie Mol\u00e9culaire des Prot\u00e9ines (DSV\/iBiTEC-S\/SIMOPRO), CEA Saclay, Gif sur Yvette, Oct 2013, &#8220;Pharmacologie, phylog\u00e9nie et ing\u00e9nierie mol\u00e9culaire des toxines aminergiques du venin de mamba ciblant les RCPG amines biog\u00e8nes&#8221;, Ph.D. Univ. Paris VI, sp. Biologie cellulaire et mol\u00e9culaire. As a rapporteur, with Brigitte Ilien (rapporteur), Sylvie Diochot and Thierry Foulon (examiners), Manolo Gouy (president), Denis Servent (supervisor).<\/li>\n\n\n\n<li><em>Lamia Mebarki<\/em>, team Steructural Glycobiology and Neurobiology, AFMB lab and SARL BioXtal\/Theranyx, Marseille, Oct 2017, &#8220;Recherche ou d\u00e9veloppement, et caract\u00e9risation fonctionnelle et structurale d\u2019effecteurs peptidiques de deux r\u00e9cepteurs membranaires \u00e0 incidences physiopathologiques&#8221;, Ph.D. Univ. Aix-Marseille, discipline Biologie, sp. Biochimie structurale. As the thesis supervisor, with Gh\u00e9rici Hassaine (co-supervisor), Denis Servent and Jean-Louis Baneres (rapporteurs), Pierre Edouard Bougis (examiner), James Sturgis (examiner and president), Sylvie Diochot (guest).<\/li>\n\n\n\n<li><em>Rana El Masri<\/em>, team Structure et Activit\u00e9 des Glycosaminoglycanes, Institut de Biologie Structurale, Grenoble, Sept 2019, &#8220;Functional and structural characterization of human endosulfatase HSulf-2&#8221;, Ph.D. Communaut\u00e9 Univ. Grenoble Alpes, sp. Biologie structurale et nanobiologie. As a rapporteur, with Kenji Uchimura (rapporteur), R\u00e9gis Daniel (examiner), Nicole Thielens (examiner and president), Romain Viv\u00e8s (supervisor).<\/li>\n\n\n\n<li><em>Oph\u00e9lie Da Silva<\/em>, Institut de Recherche Biom\u00e9dicale des Arm\u00e9es (IRBA), D\u00e9pt. de Toxicologie et Risques Chimiques, Unit\u00e9 Neurotoxiques, Br\u00e9tigny-sur-Orge, Dec 2021, &#8220;Etudes enzymatiques et structurales de r\u00e9activateurs de l\u2019ac\u00e9tylcholinest\u00e9rase inhib\u00e9e par des neurotoxiques organophosphor\u00e9s&#8221;, Ph.D. Univ. Paris-Saclay, Doctoral school Innovation th\u00e9rapeutique : du fondamental \u00e0 l\u2019appliqu\u00e9 (ITFA), sp. Biochimie et biologie structurale. As a rapporteur, with Luc Belzunces (rapporteur), Julie Mennetrey and Jacques-Philippe Colletier (examiners), Herman Van Tilbeurgh (examiner and president), Florian Nachon and Jos\u00e9 Diaz (co-supervisors).<\/li>\n\n\n\n<li><em>Jonathan Elegheert<\/em>, team Structural Neurobiology, Interactions, and Protein Engineering of Receptors, Interdisciplinary Institute for NeuroScience (IINS), Univ. Bordeaux, Centre Broca Nouvelle Aquitaine, Bordeaux, May 2024, \u201cStructural biology and engineering of neuronal proteins\u201d, H.D.R. Univ. Bordeaux. As an examiner, with Laetitia Mony, Hugues Nury, Fekrije Selimi (rapporteurs), Pierre-Jean Corringer (examiner and president).<\/li>\n\n\n\n<li><em>Anushka Nair<\/em>, team Structural Neurobiology, Interactions, and Protein Engineering of Receptors, IINS, Univ. Bordeaux, Centre Broca Nouvelle Aquitaine, Bordeaux, Sept 2025, \u201cNanobody discovery and affinity engineering approaches for targeting ionotropic glutamate receptors\u201d, Ph.D. Univ. Bordeaux. As a rapporteur, with Miriam Stoeber and Rob Meijers (rapporteurs), Derrick Robinson (examiner), S\u00e9bastien Fribourg (examiner and president), Jonathan Elegheert (supervisor).<\/li>\n\n\n\n<li><em>Arnaud Billet<\/em>, BTSB lab, INU Jean-Fran\u00e7ois Champollion, Albi, Dec 2025, &#8220;Peptides issus de venins de fourmis : identification et caract\u00e9risation fonctionnelle des peptides et de leurs m\u00e9canismes d\u2019action&#8221;, HDR Univ. Paul Sabatier-Toulouse III. As an examiner, with Aur\u00e9lien Chatelier, Pierre Charnet and Christian Legros (rapporteurs) and Elsa Bonnaf\u00e9 (supervisor).<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"memberships\">Memberships<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li>American Society for Biochemistry and Molecular Biology (ASBMB)<em> <\/em>(Adhering Body of the International<em> <\/em>Union of Biochemistry and Molecular Biology (IUBMB)): 2012 &#8211; 2021<\/li>\n\n\n\n<li>International Society for Neurochemistry (ISN): 2015 &#8211; 2018<\/li>\n\n\n\n<li>International Society on Toxinology (IST): 2007 &#8211; 2020<\/li>\n\n\n\n<li>Society for Neuroscience (SfN): 2013 &#8211; 2018<\/li>\n\n\n\n<li>National Geographic Society USA: 1994 &#8211; 2008<\/li>\n\n\n\n<li>Association de Cristallographie d\u2019Aix-Marseille (ACAM): 2013 &#8211; 2023<\/li>\n\n\n\n<li>Association Fran\u00e7aise de Cristallographie (AFC): 2012 &#8211; 2023<\/li>\n\n\n\n<li>Association pour l\u2019Etude des Cholinest\u00e9rases: since 1996  (but no longer active)<\/li>\n\n\n\n<li>Association pour la Recherche sur la Scl\u00e9rose Lat\u00e9rale Amyotrophique &amp; autres maladies du motoneurone (ARSla): 2007 &#8211; 2018<\/li>\n\n\n\n<li>Association pour les Femmes en Science et en Ing\u00e9nierie (AFSI): since 2015 (but no longer active)<\/li>\n\n\n\n<li>Club -M- Ambassadeurs de la Ville de Marseille: 2017 &#8211; 2020<\/li>\n\n\n\n<li>Soci\u00e9t\u00e9 des Neurosciences (SN) (Adhering Body of the International Brain Research Organization (IBRO) and the Federation of European Neuroscience Societies (FENS)): 2011 &#8211; 2022<\/li>\n\n\n\n<li>Soci\u00e9t\u00e9 Fran\u00e7aise d\u2019Endocrinologie (SFE): 2018<\/li>\n\n\n\n<li>Soci\u00e9t\u00e9 Fran\u00e7aise de Biophysique (SFB): 2016, 2018<\/li>\n\n\n\n<li>Soci\u00e9t\u00e9 Fran\u00e7aise pour l\u2019Etude des Toxines (SFET): member since 1999, board member since 2007, vice-president since 2025<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"ongoing-collaborations\">Collaborations<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li>AgroM Diff\u00e9renciation Cellulaire et Croissance (INRA) et Unit\u00e9 Informatique de Centre INRA, Montpellier, France<\/li>\n\n\n\n<li>Laboratoire de&nbsp;Neurobiologie Cellulaire et Mol\u00e9culaire, CNRS, Institut F\u00e9d\u00e9ratif de Neurobiologie Alfred Fessard, Gif-sur-Yvette, France<\/li>\n\n\n\n<li>Laboratoire de Toxinologie Mol\u00e9culaire, Service d\u2019Ing\u00e9nierie Mol\u00e9culaire des Prot\u00e9ines, Institut de biologie &amp; de technologies de Saclay, CEA, Gif-sur-Yvette, France<\/li>\n\n\n\n<li>Institut Interdisciplinaire de Neuroscience (IIN), CNRS\/Univ Bordeaux2, Centre de G\u00e9nomique Fonctionnelle, Bordeaux, France<\/li>\n\n\n\n<li>Soci\u00e9t\u00e9 BioXtal, campus Luminy, Marseille, France<\/li>\n\n\n\n<li>Lab Synapse Biology, VIB Center for the Biology of Disease, KU Leuven, Center for Human Genetics, Leuven, Belgium<\/li>\n\n\n\n<li>Skaggs School of Pharmacy and Pharmaceutical Sciences (SSPPS), Dept of Pharmacology, University of California at San Diego (UCSD), La Jolla, CA, USA<\/li>\n\n\n\n<li>Dept of Neuroscience and Cell Biology, UMDNJ-Robert Wood Johnson Medical School, Child Health Institute of New Jersey, New Brunswick, NJ, USA<\/li>\n\n\n\n<li>Dept of Chemistry and Biochemistry, University of California at Santa Barbara (UCSB), Santa Barbara, CA, USA<\/li>\n\n\n\n<li>Institut NeuroMyoGene, Univ Claude Bernard Lyon 1\/CNRS\/INSERM, Villeurbanne<\/li>\n\n\n\n<li>Unit\u00e9 de Neurobiologie des canaux Ioniques et de la Synapse (UNIS), INSERM, Marseille<\/li>\n\n\n\n<li>Institut du D\u00e9veloppement de Marseille (IBDM), CNRS\/AMU, Marseille<\/li>\n\n\n\n<li>Institut de Pharmacologie Mol\u00e9culaire et Cellulaire (IPMC), CNRS\/Universit\u00e9 C\u00f4te d&#8217;Azur, Sophia-Antipolis<\/li>\n\n\n\n<li>Centre de Recherche en Canc\u00e9rologie de Marseille (CRCM), Inserm\/CNRS\/AMU\/IPC), Marseille<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"financements\">Study and research funding<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li>1982 (1 mth, Sept) : Temporary CNRS contract.<\/li>\n\n\n\n<li>1982-1983 (1 yr) : Study scholarship for a &#8220;Dipl\u00f4me d&#8217;Etudes Approfondies (DEA, now Master-2)&#8221;.<\/li>\n\n\n\n<li>1983-1986 (3 yrs) : Research scholarship from the &#8220;Minist\u00e8re de la Recherche et de la Technologie (MRT)&#8221; to develop a Ph.D. Thesis.<\/li>\n\n\n\n<li>1984 : &#8220;Information Scientifique et Technique&#8221; allowance (BIST) from the &#8220;Minist\u00e8re de la Recherche et de la Technologie (MRT) &#8211; Mission Interminist\u00e9rielle de l&#8217;Information Scientifique et Technologique (MIDIST)&#8221;.<\/li>\n\n\n\n<li>1987 (1 yr) : Bridging scholarship from the Fondation pour la Recherche M\u00e9dicale (FRM).<\/li>\n\n\n\n<li>1988 (5 mths) : Vacations on a contract with the &#8220;Direction des Recherches et Etudes Techniques (DRET) &#8211; D\u00e9l\u00e9gation G\u00e9n\u00e9rale pour l&#8217;Armement (DGA)&#8221;.<\/li>\n\n\n\n<li>1994 (9 mths): CNAM &#8211; NATO, Complementary grant for studying abroad.<\/li>\n\n\n\n<li>1995 (10 mths) : &#8220;Visiting Scholar&#8221; salary, Dept. Pharmacology, UCSD, la Jolla, CA.<\/li>\n\n\n\n<li>1997-1999 (3 yrs): ACI CNRS-NSF, P Marchot &amp; P Taylor (UCSD, La Jolla, CA) coordinators.<\/li>\n\n\n\n<li>1997-1999 (3 yrs): AFM, P Marchot &amp; PE Bougis (CNRS Marseille) coordinators.<\/li>\n\n\n\n<li>2000-2002 (3 yrs): PAI France-Germany PROCOPE, P Marchot &amp; O Pongs (ZMNH, Hambourg) coordinators.<\/li>\n\n\n\n<li>2001-2002 (2 yrs): AFM, P Marchot coordinator.<\/li>\n\n\n\n<li>2003-2004 (2 yrs): Programme Bioinformatique inter EPST, P Marchot &amp; A Chatonnet (INRA Montpellier) coordinators.<\/li>\n\n\n\n<li>2003-2004 (2 yrs): AFM, P Marchot coordinator.<\/li>\n\n\n\n<li>2005-2007 (3 yrs): Action CNRS\/USA, P Marchot &amp; P Taylor (UCSD, La Jolla, CA) coordinators.<\/li>\n\n\n\n<li>2005 (1 yr): AFM, P Marchot coordinator.<\/li>\n\n\n\n<li>2006-2008 (3 yrs): GIP-ANR Sant\u00e9-environnement &#8211; Sant\u00e9-travail, partner.<\/li>\n\n\n\n<li>2006-2009 (48 mths): Project Int\u00e9gr\u00e9 Structural Proteomics in Europe SPINE2-COMPLEXES &amp; TEACH-SG, Work Package WP1.3.1, partner 14; Y Bourne (CNRS Marseille) coordinator, P Marchot deputy.<\/li>\n\n\n\n<li>2009 (1 yr): PEPS INSB-CNRS, MF Martin-Eauclaire (CNRS Marseille) coordinator; P Marchot, PE Bougis, B C\u00e9ard participants.<\/li>\n\n\n\n<li>2010-2012 (3 yrs): PICS CNRS, P Marchot &amp; Y Bourne coordinators; P Taylor (UCSD, La Jolla, CA) partner.<\/li>\n\n\n\n<li>2011-2014 (45 mths): ANR-Blanc SVSE 2 &#8211; Progr Biologie cellulaire &amp; d\u00e9veloppement, coordinator.<\/li>\n\n\n\n<li>2013-2016 (4 yrs): CNRS INSB, LIA France-USA SGIDSTS, P Marchot &amp; P Taylor (UCSD, La Jolla, CA) coordinators.<\/li>\n\n\n\n<li>2014-2017 (3.5 yrs): ANR-Blanc SVSE 4 \u2013 Progr Neurosciences, partner.<\/li>\n\n\n\n<li>2015-2019 (4 yrs): ANR &#8211; Progr Exploration du syst\u00e8me nerveux dans son fonctionnement normal et pathologique (DS0407), partner.<\/li>\n\n\n\n<li>2017-2022 (5 yrs): ANR &#8211; Progr Vie, sant\u00e9 et bien-\u00eatre (DS04), partner.<\/li>\n\n\n\n<li>2024-2026 (3 yrs): ANR &#8211; Generic call, CE11, coordinator.<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"lia-sgidsts\">LIA SGIDSTS<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p>The agreement for the creation of an International Associated Laboratory (LIA \u2013 Laboratoire International Associ\u00e9) between the laboratory Architecture et Fonction des Macromol\u00e9cules Biologiques (AFMB) in Marseille, France, and the Palmer Taylor laboratory, Skaggs School of Pharmacy and Pharmaceutical Sciences (SSPPS) in La Jolla, California, was signed by the French institutions, Centre National de la Recherche Scientifique (CNRS) and Aix-Marseille Universit\u00e9 (AMU), and the American institution, University of California San Diego (UCSD), in February-April 2015. This LIA was named Structure-Guided Investigations into Disease States and Therapeutic Strategies (acronym SGIDSTS) and it effectively started January 1st, 2013, for 4 years. It was coordinated on the French side by Pascale Marchot, a CNRS researcher, and on the American side by Palmer Taylor, a UCSD researcher and professor. The activities of the LIA SGIDSTS covered fundamental research in molecular neuropharmacology and structural biochemistry. (See <a href=\"http:\/\/fr.calameo.com\/read\/0024881609caea48ef098\">http:\/\/fr.calameo.com\/read\/00248816&#8230;<\/a> page 7; <a href=\"https:\/\/www.nature.com\/nature-index\/institution-outputs\/france\/laboratoire-international-associe-structure-guided-investigations-into-disease-states-and-therapeutic-strategies-lia-sgidsts\/5971647f140ba0fb368b456b\">https:\/\/www.nature.com\/nature-index\/institution-outputs\/france\/laboratoire-international-associe-structure-guided-investigations-into-disease-states-and-therapeutic-strategies-lia-sgidsts\/5971647f140ba0fb368b456b<\/a> ; <a href=\"https:\/\/www.cnrs.fr\/CNRS-Hebdo\/provence-corse\/Lettre\/343\/Lettre.aspx\">https:\/\/www.cnrs.fr\/CNRS-Hebdo\/provence-corse\/Lettre\/343\/Lettre.aspx<\/a> ; <a href=\"https:\/\/www.univ-amu.fr\/system\/files\/2019-02\/DIRCOM-lettre_amu_n17_janv2014.pdf\">https:\/\/www.univ-amu.fr\/system\/files\/2019-02\/DIRCOM-lettre_amu_n17_janv2014.pdf<\/a> pages 17-18; <a href=\"https:\/\/www.france-science.com\/IMG\/pdf\/rapport_activite_mst_2013.compressed.pdf\">https:\/\/www.france-science.com\/IMG\/pdf\/rapport_activite_mst_2013.compressed.pdf<\/a> pages 80-81.)<\/p>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"staff-research-assoc\">Staff Research Associates<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li><em>Joan R. Kanter<\/em>, staff research associate UCSD, 1994-1995 (now a Faculty Admin Assistant in Roger Tsien Lab, UCSD)<\/li>\n\n\n\n<li><em>Marianick Juin<\/em>, technician CNRS (permanent position), 2000-2005 (now working at the Institut M\u00e9diterran\u00e9en de Biodiversit\u00e9 et d\u2019Ecologie Marine et Continentale &#8211; IMBE- campus Arbois, Aix-en-Provence)<\/li>\n\n\n\n<li><em>Sandrine Conrod<\/em>, technician CNRS (permanent position), 2005-2011 (afterward: technician at the Institut de Neurophysiopathologie de Marseille; now working at the Centre Europ\u00e9en de Recherche et d\u2019Enseignement en G\u00e9osciences de l\u2019Environnement &#8211; CEREGE &#8211; in Aix-en-Provence)<\/li>\n\n\n\n<li><em>Claire Debarnot<\/em>, study engineer AMU (permanent position), 2010-2011 (now a member of the AFMB lab and our team, since Jan 2017)<\/li>\n\n\n\n<li><em>Audrey Blanchard<\/em>, study engineer, 2011-2014 (now working at Innate Pharma, Marseille)<\/li>\n\n\n\n<li><em>Supanee (&#8220;Ann&#8221;) Potisopon<\/em>, research engineer\/postdoc, Oct-Dec 2014 (afterward: a postdoc at Harvard Medical School, Boston, MA; now working for BIOASTER, Lyon, FR)<\/li>\n\n\n\n<li><em>Aur\u00e9lien Assice-Vivoni<\/em>, study engineer, Sept 2015 (now an alternating project manager for quality\/hygiene\/security\/environment at EDF)<\/li>\n\n\n\n<li><em>Julie Baptiste<\/em>, study engineer, Nov 2015 &#8211; Sept 2016 (afterward: engineer at the Institute of Human Genetics, Montpellier; now engineer at Sys2Diag, Montpellier)<\/li>\n\n\n\n<li><em>Maria Mate<\/em>, research engineer CNRS (permanent position), Oct 2013 &#8211; May 2017 (now working with another team of the AFMB lab)<\/li>\n\n\n\n<li><em>Marie-Julie Dejardin<\/em>, study engineer, Oct 2016 &#8211; Jun 2017 (now working at the NeuroMyoGene Institute (INMG) Lyon)<\/li>\n\n\n\n<li><em>Jean-Baptiste Boitel<\/em>, study engineer, Feb 2018 &#8211; Nov 2019 (afterward: engineer at the Adhesion &amp; Inflammation Lab, Campus Luminy, Marseille, in collaboration with another team of the AFMB lab ; now Cadre de laboratoire Sanofi Montpellier)<\/li>\n\n\n\n<li><em>Marine Papin<\/em>, study engineer, Sept 2020 &#8211; Feb 2021 (now a PhD student in Dijon)<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"students-postdocs-visitors\">Students, postdocs, visitors<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p><strong><strong>Trainees<\/strong><\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><em>Rozenn Guegan<\/em>, Maitrise Biologie Cellulaire et Physiologie, Univ Rennes, Apr-Jun 1998, then DEA Neurosciences, Univ M\u00e9diterran\u00e9e, Sept-Nov 1998 (abandoned)<\/li>\n\n\n\n<li><em>C\u00e9line Hamel<\/em>, BTS Ecole Nationale de Chimie Physique et Biologie, Paris, May-Jul 1999 &amp; March 2000<\/li>\n\n\n\n<li><em>Romain Morichon<\/em>, Licence Biochimie, Univ Franche-Comt\u00e9, UFR Sciences et Techniques, Besan\u00e7on, Jun-Aug 2000<\/li>\n\n\n\n<li><em>Ludovic Renault<\/em>, Magist\u00e8re Univ Rouen (3rd yr) &amp; DEA Biochimie Biologie Structurale et G\u00e9nomique, Univ Aix-Marseille, Sept 2001- Jun 2002<\/li>\n\n\n\n<li><em>Raja Noufir (now Bonifay)<\/em>, BTS Lyc\u00e9e Pro Marie Curie, Marseille, May-June 2003 &amp; Nov-Dec 2003 (2 x 8 wks)<\/li>\n\n\n\n<li><em>Virginie Fabre<\/em>, 4th yr INSA Lyon, Dept Biosciences, Jun-Jul 2004 (8 wks)<\/li>\n\n\n\n<li><em>Audrey Luzergues<\/em>, 2nd yr ESIL, Dept G\u00e9nie Biologique et Microbiologie Appliqu\u00e9e, Marseille, Feb-Apr 2005 (8 wks)<\/li>\n\n\n\n<li><em>Marion Traverse<\/em>, 2nd yr ESIL, Dept G\u00e9nie Biologique et Microbiologie Appliqu\u00e9e, Marseille, Mar-Apr 2006 (8 wks)<\/li>\n\n\n\n<li><em>Carole Rosenberger<\/em>, Master-1 Nutrition &#8211; S\u00e9curit\u00e9 Alimentaire, option Biochimie, Univ M\u00e9diterran\u00e9e, Marseille, Apr-Jun 2006 (8 wks)<\/li>\n\n\n\n<li><em>Delphine Chaduli<\/em>, BTS Lyc\u00e9e Pro Marie Curie, Marseille, May-Jun 2006 &amp; Oct-Dec 2006 (2 x 8 wks)<\/li>\n\n\n\n<li><em>Gr\u00e9goire Mondielli<\/em>, Master-2 Neurosciences, Univ M\u00e9diterran\u00e9e, Jan-Jun 2007<\/li>\n\n\n\n<li><em>David Menahem<\/em>, 2nd yr ESIL, Dept Biotechnologie, Marseille, Feb-Apr 2010 (8 wks)<\/li>\n\n\n\n<li><em>Pauline Dressayre<\/em>, 2nd yr ESIL, Dept Biotechnologie, Marseille, Feb-Apr 2011 (8 wks) (co-mentor G Mondielli)<\/li>\n\n\n\n<li><em>Julie Prats<\/em>, 2nd yr ESIL, Dept Biotechnologie, Marseille, Feb-Apr 2012 (8 wks) (co-mentor A Blanchard)<\/li>\n\n\n\n<li><em>Camille Ribeyre<\/em>, Master-1 Biochimie Biologie Structurale et G\u00e9nomique (BBSG), Aix-Marseille Univ, Apr-May 2013 (8 wks) (co-mentor A Blanchard)<\/li>\n\n\n\n<li><em>Florian Mourey<\/em>, 2nd yr AgroParisTech, Institut des sciences et industries du vivant et de l\u2019environnement, Centre de Paris, Jun-Jul 2014 (8 wks) (co-mentor A Goulet)<\/li>\n\n\n\n<li><em>Farida Nezlioui<\/em>, Master-2 Biochimie Biologie Structurale et G\u00e9nomique (BBSG), Aix-Marseille Univ, Jan-Jun 2016 (co-mentor A Goulet)<\/li>\n\n\n\n<li><em>Yoann Cr\u00e9tinon<\/em>, Master-1 Biochimie Biologie Structurale et G\u00e9nomique (BBSG), Aix-Marseille Univ, Mar-Apr 2017 (7 wks) (co-mentors A Goulet, S Platsaki)<\/li>\n\n\n\n<li><em>Melvin Boumedour<\/em>, BTS Lyc\u00e9e La Forbine, Marseille, May-Jul (6 wks) &amp; Nov-Dec 2017 (8 wks) (main mentor S Platsaki)<\/li>\n\n\n\n<li><em>Sarah Coulibaly Martineau<\/em>, Master-2 Biologie Structurale, G\u00e9nomique (BSG), Aix-Marseille Univ, Jan-Jun 2019 (6 mths) (co-mentor C Debarnot)<\/li>\n\n\n\n<li><em>Djouhaina Benmehidi<\/em>, 2nd yr Sup\u2019Biotech Paris, June-July 2019 (8 wks) (main mentor S Platsaki)<\/li>\n\n\n\n<li><em>Nafisatou Drame<\/em>, Master-2 Biologie Structurale, G\u00e9nomique (BSG), Aix-Marseille Univ, Jan-Jun 2021 (6 mths) (co-mentor C Debarnot)<\/li>\n\n\n\n<li><em>Cynthia Lohberger<\/em>, Master-1 Biologie Structurale, G\u00e9nomique (BSG), Aix-Marseille Univ, Apr-May 2021 (7 wks) (co-mentor C Debarnot)<\/li>\n\n\n\n<li><em>Cynthia Lohberger<\/em>, Master-2 Biologie Structurale, G\u00e9nomique (BSG), Aix-Marseille Univ, Jan-Jun 2022 (6 mths) (co-mentor C Debarnot)<\/li>\n\n\n\n<li><em>Malorie Spies<\/em>, Master-1 Biologie Structurale, G\u00e9nomique (BSG), Aix-Marseille Univ, Apr-May 2025 (7 wks) (co-mentor I. Prabudiansyah)<\/li>\n<\/ul>\n\n\n\n<p><strong><strong>PhD students<\/strong><\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><em>Fatima Laraba-Djebari<\/em>, Thesis Univ Aix-Marseille II, sp. Cell biology and microbiology, 1993-1995, co-mentoring (thesis mentor: Marie-France Martin-Eauclaire).\n<ul class=\"wp-block-list\">\n<li>Now: Dean of the Faculty of Biological Sciences, University of Sciences and Technology Houari Boum\u00e9di\u00e8ne (FSB-USTHB), Algiers, Algeria.<\/li>\n<\/ul>\n<\/li>\n\n\n\n<li><em>Ludovic Renault<\/em>, Thesis Univ M\u00e9diterran\u00e9e, sp Neurosciences, Sept 2002 &#8211; Dec 2005.\n<ul class=\"wp-block-list\">\n<li>Funding: Association France Alzheimer&nbsp;; Association Fran\u00e7aise contre les Myopathies&nbsp;; Programme Bioinformatique inter-EPST.<\/li>\n\n\n\n<li>Then: Postdoc Stahlberg Lab, Molecular &amp; Cellular Biology, College of Biological Sciences, Univ California, Davis, CA, USA, 2006-2009 \/ Research associate, Howard Young Lab, Dept Biochemistry, Univ Alberta, Edmonton, Canada, 2009-2012 \/ Senior scientific officer, Cancer Research UK, London Research Inst, UK, 2013 &#8211; 2015.<\/li>\n\n\n\n<li>Then: Research Scientist &amp; Facility Manager, NeCEN, Leiden University, NL, 2016.<\/li>\n\n\n\n<li>Now: Research Scientist &amp; Head of NeCEN Facility, Leiden University, NL, since 2018.<\/li>\n<\/ul>\n<\/li>\n\n\n\n<li><em>Gr\u00e9goire Mondielli<\/em>, Thesis Univ M\u00e9diterran\u00e9e, sp. Neurosciences, Sept 2007 \u2013 Dec 2011.\n<ul class=\"wp-block-list\">\n<li>Funding: Association Fran\u00e7aise contre les Myopathies&nbsp;; CNRS ; Fondation pour la Recherche M\u00e9dicale.<\/li>\n\n\n\n<li>Then: Research engineer, CRN2M Marseille, team Gliotransmission &amp; synaptopathies, 2013 &#8211; 2016 \/ team SIGnalling in NeuroEndocrine Tumors (SIG-NET), 2016 &#8211; 2018.<\/li>\n\n\n\n<li>Now: Research engineer, Institute of NeuroPhysiopathology, Marseille Medical Genetics, team DIP-NET, since 2018 (see <a href=\"https:\/\/fr.linkedin.com\/in\/gregoire-mondielli-96453420\">https:\/\/fr.linkedin.com\/in\/gregoire&#8230;<\/a>)<\/li>\n<\/ul>\n<\/li>\n\n\n\n<li><em>Lamia Mebarki<\/em>, Thesis Aix-Marseille Univ, sp Structural Biology &amp; Biochemistry, Nov 2013 &#8211; Oct 2017.\n<ul class=\"wp-block-list\">\n<li>Funding: BioXtal Nov 2013 &#8211; Mar 2014; CIFRE-ANRT BioXtal-AFMB Apr 2014 &#8211; Mar 2017; Theranyx Apr &#8211; June 2017; AFMB Jul &#8211; Dec 2017.<\/li>\n\n\n\n<li>Then: R&amp;D engineer, Promise Advanced Proteomics, Grenoble, Jan-May 2019.<\/li>\n\n\n\n<li>Now: Project Manager, Covalab, Lyon, May 2019 &#8211; ongoing<\/li>\n<\/ul>\n<\/li>\n<\/ul>\n\n\n\n<p><strong><strong>Postdocs<\/strong><\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><em>Igor Fabrichny<\/em>, after a PhD Univ Lomonosov Moscow RU (1995-1999) then a 1rst postdoc at the Institute of Biotechnology, Univ Helsinki FI (2000-2005).\n<ul class=\"wp-block-list\">\n<li>Funding: CNRS \u00ab&nbsp;Proposition d\u2019accueil pour un post-doctorant au CNRS&nbsp;\u00bb (Oct 2005 &#8211; Sept 2006); Fondation pour la Recherche M\u00e9dicale \u00ab&nbsp;Accueil de post-doctorant \u00e9tranger&nbsp;\u00bb (Oct 2006 &#8211; Sept 2008).<\/li>\n\n\n\n<li>Now: Product Manager, International Biotechnology Center GENERIUM, Volginskiy, RU (2011-ongoing).<\/li>\n<\/ul>\n<\/li>\n\n\n\n<li><em>Adeline Goulet<\/em>, after (i) a PhD Univ Aix-Marseille (AFMB lab, 2006-2009), (ii) a 1rst postdoc at the CBS Montpellier (2009-2010), &amp; (iii) a 2nd postdoc at Birkbeck College, London, UK (2010-2013).\n<ul class=\"wp-block-list\">\n<li>3rd postdoc in our team, funding: Fondation pour la Recherche M\u00e9dicale (Sept 2013 &#8211; Sept 2015).<\/li>\n\n\n\n<li>Then: CNRS Researcher (CR2) in our team (Oct 2015 &#8211; Sept 2017).<\/li>\n\n\n\n<li>Then: CNRS Researcher (CR2) in AFMB team Host-pathogen interactions (Sept 2017 &#8211; Dec 2021).<\/li>\n\n\n\n<li>Now: CNRS Researcher (CR2) in LISM team Host-pathogen interactions (Jan 2022 &#8211; ).<\/li>\n<\/ul>\n<\/li>\n\n\n\n<li><em>Semeli Platsaki<\/em>, after (i) a PhD in Protein Biochemistry at the Institute for Cell and Molecular Biosciences, Newcastle Univ (UK) 2010-2015, (ii) a 1rst postdoc at the Northern Institute for Cancer Research, Newcastle Univ (UK) 2015-2016.\n<ul class=\"wp-block-list\">\n<li>2nd postdoc in our team, funding ANR June 2016 &#8211; Sept 2019 along with PRESTIGE (Marie Sk\u0142odowska-Curie actions, Campus France) Sept 2017 &#8211; Sept 2018.<\/li>\n\n\n\n<li>3rd postdoc in team Genetics and Neurobiology of C. elegans, INMG, Lyon, with assignement to work in our team, funding ANR Nov 2019 &#8211; Jan 2020.<\/li>\n\n\n\n<li>Then: 4th postdoc in team Viral replicases: structure, function and drug-design of the AFMB lab, Marseille, funding Janssen Apr &#8211; Nov 2020.<\/li>\n\n\n\n<li>Now: employed by the European Virus Archive &#8211; GLOBAL (EVAg), Marseille<\/li>\n<\/ul>\n<\/li>\n<\/ul>\n\n\n\n<p><strong><strong>Long-term visitors<\/strong><\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><em>Sventja von Daake<\/em>, visitor Dept of Pharmacology, UCSD (Nov 2003 &#8211; Oct 2004) &#8211; Funding: Pharmacology Education Research Foundation.\n<ul class=\"wp-block-list\">\n<li>Then: Research associate, Susan Taylor Lab, UCSD, La Jolla, CA, USA.<\/li>\n\n\n\n<li>Then: Lab manager, Comoletti Lab, Dept Neuroscience &amp; Cell Biology, UMDNJ-RWMS, Child Health Institute of New Jersey, New Brunswick, NJ, USA.<\/li>\n\n\n\n<li>Now: Staff Scientist Cytomics Specialist, Malaghan Institute of Medical Research, Wellington, New Zealand<\/li>\n<\/ul>\n<\/li>\n\n\n\n<li><em>Nicolas Lenfant<\/em>, visitor postdoc from lab Dynamique Musculaire et M\u00e9tabolisme, INRA, Montpellier (Jun 2011 &#8211; Dec 2013) &#8211; Funding: ANR.\n<ul class=\"wp-block-list\">\n<li>Then: postdoc in AFMB team Glycogenomics (Jan 2014 &#8211; Dec 2016).<\/li>\n\n\n\n<li>Now: engineer Marseille Medical Genetics, Facult\u00e9 de M\u00e9decine Timone, Marseille (March 2018 &#8211; ongoing)<\/li>\n<\/ul>\n<\/li>\n\n\n\n<li><em>Nafisatou Drame<\/em>, engineer &#8220;CDD&#8221; Tafalgie Therapeutics SAS, hosted at the AFMB lab within the frame of an official agreement, Oct 2021 &#8211; Apr 2024\n<ul class=\"wp-block-list\">\n<li>Now: engineer &#8220;CDI&#8221; Tafalgie Therapeutics SAS, Marseille (April 2024 &#8211; ongoing)<\/li>\n<\/ul>\n<\/li>\n<\/ul>\n\n\n\n<p><strong><strong>Other trainees &amp; visitors<\/strong><\/strong><\/p>\n\n\n\n<ul class=\"wp-block-list\">\n<li><em>Kael Duprey<\/em>, trainee UCSD, Jun-Oct 1994 &amp; Jun-Oct 1995 (in the US)<\/li>\n\n\n\n<li><em>Claudine N. Prowse<\/em>, trainee UCSD, Jan 1994 &#8211; Dec 1995 (in the US)<\/li>\n\n\n\n<li><em>Verena Pollmann<\/em>, visitor PhD Univ Hambourg (PhD mentor: O. Pongs), Mar 2000 &amp; Jun 2000 (2 &amp; 1 wks)<\/li>\n\n\n\n<li><em>Jens Dannenberg<\/em>, visitor Postdoc Institut fuer Neurale Signalverarbeitung, ZMNH, Hamburg, Oct 2001 (2 wks)<\/li>\n\n\n\n<li><em>Scott B. Hansen<\/em>, visitor PhD UCSD (PhD mentor, Palmer Taylor), Apr-Jun 2004 &amp; Nov-Dec 2004 (7 &amp; 8 wks)<\/li>\n\n\n\n<li><em>Ryan Hibbs<\/em>, visitor Postdoc UCSD, Nov-Dec 2006<\/li>\n\n\n\n<li><em>C\u00e9cile Tardif &amp; Marion Leblanc<\/em>, &#8220;1\u00e8re S&#8221;, Lyc\u00e9e des Pierres Vives, Carri\u00e8res-sur-Seine, Dec2013 &#8211; Mar2014, by email only!<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"original-publications-and-reviews\">Original publications and reviews<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p><strong>1986<\/strong><\/p>\n\n\n\n<p>Bougis PE, Marchot P, Rochat H (1986) Characterization of <em>Elapidae<\/em> snake venom components using optimized reverse-phase high performance liquid chromatographic conditions and screening assays for \u03b1-neurotoxin and phospholipase A2 activities. <em>Biochemistry<\/em> <strong>25<\/strong>, 7235-7243.<\/p>\n\n\n\n<p><strong>1987<\/strong><\/p>\n\n\n\n<p>Bougis PE, Marchot P, Rochat H (1987) <em>In vivo<\/em> synergy of cardiotoxin and phospholipase A2 from the Elapid snake <em>Naja mossambica mossambica<\/em>. <em>Toxicon<\/em> <strong>25<\/strong>, 427-431.<\/p>\n\n\n\n<p>Martin MF, Rochat H, Marchot P, Bougis PE (1987) Use of high performance liquid chromatography to demonstrate quantitative variation in components of venom from the scorpion <em>Androctonus australis Hector<\/em>. <em>Toxicon<\/em> <strong>25<\/strong>, 569-573.<\/p>\n\n\n\n<p>Otting G, Marchot P, Bougis PE, Rochat H, W\u00fcthrich K (1987) Monitoring the purification by high performance liquid chromatography of cardiotoxins from <em>Naja mossambica mossambica<\/em> using phase-sensitive two dimensional nuclear magnetic resonance. <em>Eur J Biochem<\/em> <strong>168<\/strong>, 603-607.<\/p>\n\n\n\n<p><strong>1988<\/strong><\/p>\n\n\n\n<p>Marchot P, Bougis PE, C\u00e9ard B, Van Rietschoten J, Rochat H (1988) Localization of the toxic site of <em>Naja mossambica mossambica<\/em> cardiotoxins&nbsp;: small synthetic peptides express an <em>in vivo<\/em> lethality. <em>Biochem Biophys Res Comm<\/em> <strong>153<\/strong>, 642-647.<\/p>\n\n\n\n<p>Marchot P, Frachon P, Bougis PE (1988) Selective distinction at equilibrium between the two \u03b1-neurotoxin binding sites of <em>Torpedo<\/em> acetylcholine receptor by microtitration. <em>Eur J Biochem<\/em> <strong>174<\/strong>, 537-542.<\/p>\n\n\n\n<p>Zeghloul S, Marchot P, Bougis PE, Ronin C (1988) Selective loss of binding sites for the iodinated \u03b1-neurotoxin I from <em>Naja mossambica mossambica<\/em> upon enzymatic deglycosylation of <em>Torpedo<\/em> electric organ membranes. <em>Eur J Biochem<\/em> <strong>174<\/strong>, 543-550.<\/p>\n\n\n\n<p><strong>1989<\/strong><\/p>\n\n\n\n<p>Le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC (1989) Crystals of fasciculin 2 from green mamba snake venom&nbsp;: preparation and preliminary X-ray analysis. <em>J Biol Chem<\/em> <strong>264<\/strong>, 21401-21402.<\/p>\n\n\n\n<p><strong>1990<\/strong><\/p>\n\n\n\n<p>Muniz ZM, Tibbs GR, Marchot P, Bougis PE, Nicholls DG, Dolly JO (1990) Homologues of a K+ channel blocker \u03b1-dendrotoxin&nbsp;: characterization of synaptosomal binding sites and their coupling to elevation of cytosolic free calcium concentration. <em>Neurochem Int<\/em> <strong>16<\/strong>, 105-112.<\/p>\n\n\n\n<p>Gourdou I, Mabrouk K, Harkiss G, Marchot P, Watt N, Hery F, Vigne R (1990) Neurotoxicit\u00e9 chez la souris de portions riches en cyst\u00e9ines des prot\u00e9ines Tat du virus visna et de VIH-1 [en fran\u00e7ais&nbsp;; r\u00e9sum\u00e9 en anglais]. <em>C R Acad Sci (Paris)<\/em> <strong>311<\/strong>, S\u00e9rie III, pp. 149-155.<\/p>\n\n\n\n<p><strong>1992<\/strong><\/p>\n\n\n\n<p>Le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC (1992) 1.9 \u00c5 resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom. <em>J Biol Chem<\/em> <strong>267<\/strong>, 22122-22130.<\/p>\n\n\n\n<p>Laraba-Djebari F, Martin-Eauclaire MF, Marchot P (1992) A fibrinogen-clotting serine proteinase from <em>Cerastes cerastes<\/em> (horned viper) venom with arginine-esterase and amidase activities&nbsp;: purification, characterization and kinetic parameter determination. <em>Toxicon<\/em> <strong>30<\/strong>, 1399-1410.<\/p>\n\n\n\n<p><strong>1993<\/strong><\/p>\n\n\n\n<p>Marchot P, Kh\u00e9lif A, Ji YH, Mansuelle P, Bougis PE (1993) Binding of 125I-fasciculin to rat brain acetylcholinesterase&nbsp;: the complex still binds diisopropyl fluorophosphate. <em>J Biol Chem<\/em> <strong>268<\/strong>, 12458-12467.<\/p>\n\n\n\n<p><strong>1995<\/strong><\/p>\n\n\n\n<p>van den Born HKL, Radi\u0107 Z, Marchot P, Taylor P, Tsigelny I (1995) Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase. <em>Protein Sci<\/em> <strong>4<\/strong>, 703-715.<\/p>\n\n\n\n<p>Laraba-Djebari F, Martin-Eauclaire MF, Mauco G, Marchot P (1995) Afa\u00e2cytin, an \u03b1\u03b2-fibrinogenase from <em>Cerastes cerastes<\/em> (Horned Viper) venom, activates purified factor X and induces serotonin release from human blood platelets. <em>Eur J Biochem<\/em> <strong>233<\/strong>, 756-765.<\/p>\n\n\n\n<p>Bourne Y, Taylor P, Marchot P (1995) Acetylcholinesterase inhibition by fasciculin&nbsp;: crystal structure of the complex. <em>Cell<\/em> <strong>83<\/strong>, 503-512.<\/p>\n\n\n\n<p>Taylor P, Radi\u0107 Z, Hosea NA, Camp S, Marchot P, Berman HA (1995) Structural bases for the specificity of cholinesterase catalysis and inhibition. <em>Toxicol Lett<\/em> <strong>82-83<\/strong>, 453-458.<\/p>\n\n\n\n<p><strong>1996<\/strong><\/p>\n\n\n\n<p>Le Du MH, Housset D, Marchot P, Bougis PE, Navaza J, Fontecilla-Camps JC (1996) Crystal structure of fasciculin 2 from green mamba snake venom&nbsp;: evidence for unusual loop flexibility. <em>Acta Cryst<\/em> <strong>D52<\/strong>, 87-92.<\/p>\n\n\n\n<p>Marchot P, Ravelli RBG, Raves ML, Bourne Y, Vellom DC, Kanter J, Camp S, Sussman JL, Taylor P (1996) Soluble monomeric acetylcholinesterase from mouse&nbsp;: expression, purification, and crystallization in complex with fasciculin. <em>Protein Sci<\/em> <strong>5<\/strong>, 672-679.<\/p>\n\n\n\n<p><strong>1997<\/strong><\/p>\n\n\n\n<p>Marchot P, Prowse CN, Kanter J, Camp S, Ackermann EJ, Radi\u0107 Z, Bougis PE, Taylor P (1997) Expression and inhibitory activity of mutants of fasciculin, a peptidic acetylcholinesterase inhibitor from mamba venom. <em>J Biol Chem<\/em> <strong>272<\/strong>, 3502-3510.<\/p>\n\n\n\n<p><strong>1998<\/strong><\/p>\n\n\n\n<p>Sugiyama N, Marchot P, Kawanishi C, Osaka H, Molles B, Sine S, Taylor P (1998) Residues at the subunit interfaces of the nicotinic acetylcholine receptor that contribute to \u03b1-conotoxin M1 binding. <em>Molec Pharmacol<\/em> <strong>53<\/strong>, 787-794.<\/p>\n\n\n\n<p>Marchot P, Bourne Y, Prowse CN, Bougis PE, Taylor P (1998) Highlights in toxin research &#8211; Inhibition of mouse acetylcholinesterase by fasciculin&nbsp;: crystal structure of the complex and mutagenesis of fasciculin. <em>Toxicon<\/em> <strong>36<\/strong>, 1613-1622.<\/p>\n\n\n\n<p>Taylor P, Osaka H, Molles BE, Sugiyama N, Marchot P, Malany S, McArdle JJ, Sine SM, Tsigelny I (1998) Toxins selective for subunit interfaces as probes of nicotinic acetylcholine receptor structure. <em>J Physiol (Paris)<\/em> <strong>92<\/strong>, 79-83.<\/p>\n\n\n\n<p><strong>1999<\/strong><\/p>\n\n\n\n<p>Bourne Y, Taylor P, Bougis PE, Marchot P (1999) Crystal structure of mouse acetylcholinesterase&nbsp;: a peripheral site-occluding loop in a tetrameric assembly. <em>J Biol Chem<\/em> <strong>274<\/strong>, 2963-2970.<\/p>\n\n\n\n<p>Sentjurc M, Pecar S, Stojan J, Marchot P, Radi\u0107 Z, Grubi\u010d Z (1999) Electron paramagnetic resonance reveals altered topography of the active site gorge of acetylcholinesterase after binding of fasciculin to the peripheral site. <em>Biochem Biophys Acta<\/em> <strong>1430<\/strong>, 349-358.<\/p>\n\n\n\n<p>Bourne Y, Grassi J, Bougis PE, Marchot P (1999) Conformational flexibility of the acetylcholinesterase tetramer revealed by X-ray crystallography. <em>J Biol Chem<\/em> <strong>274<\/strong>, 30370-30376.<\/p>\n\n\n\n<p>Marchot P (1999) L\u2019interaction fasciculine-ac\u00e9tylcholinest\u00e9rase [Monographie en fran\u00e7ais&nbsp;; r\u00e9sum\u00e9 en anglais]. <em>J Soc Biol<\/em> <strong>193<\/strong>, 505-508.<\/p>\n\n\n\n<p><strong>2000<\/strong><\/p>\n\n\n\n<p>Tricaud N, Marchot P, Martin-Eauclaire MF (2000) On the kaliotoxin and dendrotoxin binding sites on rat brain synaptosomes. <em>Toxicon<\/em> <strong>38<\/strong>, 1749-1758.<\/p>\n\n\n\n<p><strong>2001<\/strong><\/p>\n\n\n\n<p>Bourne Y, Dannenberg J, Pollmann V, Marchot P, Pongs O (2001) Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1). <em>J Biol Chem<\/em> <strong>276<\/strong>, 11949-11955.<\/p>\n\n\n\n<p><strong>2002<\/strong><\/p>\n\n\n\n<p>Tai K, Shen T, Henchman RH, Bourne Y, Marchot P, McCammon JA (2002) Mechanism of acetylcholinesterase inhibition by fasciculin&nbsp;: a 5 ns molecular dynamics simulation. <em>J Am Chem Soc<\/em> <strong>124<\/strong>, 6153-6161.<\/p>\n\n\n\n<p>Geib S, Sandoz G, Mabrouk K, Matavel A, Marchot P, Hoshi T, Villaz M, Ronjat M, Miquelis R, L\u00e9v\u00eaque C, De Waard M (2002) Use of a purified and functional recombinant Ca2+ channel \u03b24 subunit in surface plasmon resonance studies. <em>Biochem J<\/em> <strong>364<\/strong>, 285-292.<\/p>\n\n\n\n<p><strong>2003<\/strong><\/p>\n\n\n\n<p>Bourne Y, Taylor P, Radi\u0107 Z, Marchot P (2003) Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. <em>EMBO J<\/em> <strong>22<\/strong>, 1-12.<\/p>\n\n\n\n<p><strong>2004<\/strong><\/p>\n\n\n\n<p>Hotelier T, Renault L, Cousin X, N\u00e8gre V, Marchot P, Chatonnet A (2004) ESTHER, the database of the \u03b1\/\u03b2-hydrolase fold superfamily of proteins. <em>Nucleic Acids Res<\/em> <strong>32<\/strong>, D145-147.<\/p>\n\n\n\n<p>Bourne Y, Kolb HC, Radi\u0107 Z, Sharpless KB, Taylor P, Marchot P (2004) Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation. <em>Proc Natl Acad Sci USA<\/em> <strong>101<\/strong>, 1449-1454.<\/p>\n\n\n\n<p>Bourne Y, Hasper AA, Chahinian H, Juin M, de Graaff LH, Marchot P (2004) <em>Aspergillus niger<\/em> protein EstA defines a new class of fungal esterases within the \u03b1\/\u03b2-hydrolase fold family of proteins. <em>Structure (Camb) <\/em><strong>12<\/strong>, 677-687 [Erratum in <em>Structure (Camb)<\/em> <strong>12<\/strong>, 1545]. (See also Preview \u201cDefining substrate characteristics from 3D structure&nbsp;: perspective on EstA structure\u201d by Schrag JD &amp; Cygler M, <em>Structure (Camb)<\/em> <strong>12<\/strong>, 521-522.)<\/p>\n\n\n\n<p><strong>2005<\/strong><\/p>\n\n\n\n<p>Legros C, C\u00e9ard B, Vacher H, Marchot P, Bougis PE, Martin-Eauclaire MF (2005) Expression of the scorpion \u03b1-toxin of reference AaH-II and mutants for identification of some key bioactive elements. <em>Biochem Biophys Acta<\/em> <strong>1723<\/strong>, 91-99.<\/p>\n\n\n\n<p>Bourne Y, Talley TT, Hansen SB, Taylor P, Marchot P (2005) Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake \u03b1-neurotoxins and nicotinic receptors. <em>EMBO J<\/em> <strong>24<\/strong>, 1512\u20131522 [Corrigendum in <em>EMBO J.<\/em> <strong>25<\/strong>, 266 (2006)].<\/p>\n\n\n\n<p>Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y (2005) Structures of <em>Aplysia<\/em> AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. <em>EMBO J<\/em> <strong>24<\/strong>, 3635\u20133646.<\/p>\n\n\n\n<p>Bourne Y, Radi\u0107 Z, Kolb HC, Sharpless KB, Taylor P, Marchot P (2005) Structural insights into conformational flexibility at the AChE peripheral site and active site gorge [Revue]. <em>Chem Biol Interact<\/em> <strong>157-158<\/strong>, 159-165.<\/p>\n\n\n\n<p>Renault L, N\u00e8gre V, Hotelier T, Cousin X, Marchot P, Chatonnet A (2005) New friendly tools for users of ESTHER, the database of the \u03b1\/\u03b2-hydrolase fold superfamily of proteins. <em>Chem Biol Interact<\/em> <strong>157-158<\/strong>, 339-343.<\/p>\n\n\n\n<p>Bourne Y, Hasper AA, Chahinian H, Renault L, Juin MA, de Graaff LH, Marchot P (2005) <em>A. niger<\/em> protein &#8220;EstA&#8221;, perhaps a new electrotactin, defines a new class of fungal esterases within the \u03b1\/\u03b2-hydrolase fold superfamily. <em>Chem Biol Interact<\/em> <strong>157-158<\/strong>, 395-396.<\/p>\n\n\n\n<p>Renault L, Essono S, Boquet D, Juin M, Grassi J, Bourne Y, Marchot P (2005) Structural insights into AChE inhibition by monoclonal antibodies. <em>Chem Biol Interact<\/em> <strong>157-158<\/strong>, 397-400.<\/p>\n\n\n\n<p><strong>2006<\/strong><\/p>\n\n\n\n<p>Bourne Y, Radi\u0107 Z, Sulzenbacher G, Kim E, Taylor P, Marchot P (2006) Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding. <em>J Biol Chem<\/em> <strong>281<\/strong>, 29256-29267.<\/p>\n\n\n\n<p>Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Bourne Y, Taylor P (2006) Structural characterization of agonist and antagonist-bound acetylcholine-binding protein from <em>Aplysia californica<\/em>. <em>J Mol Neurosci<\/em> <strong>30<\/strong> (1-2), 101-102.<\/p>\n\n\n\n<p>Bourne Y, Hansen SB, Sulzenbacher G, Talley TT, Huxford T, Taylor P, Marchot P (2006) Structural comparison of three crystalline complexes of a peptidic toxin with a synaptic acetylcholine recognition protein. <em>J Mol Neurosci<\/em> <strong>30<\/strong> (1-2), 103-104.<\/p>\n\n\n\n<p>Hansen S, Sulzenbacher G, Huxford T, Marchot P, Bourne Y, Taylor P (2006) Conformational states of AChBP revealed by X-ray crystal structures of bound nAChR agonists, antagonists and non-competitive ligands. <em>Acta Pharmacol Sin<\/em> <strong>27<\/strong>, 390-390.<\/p>\n\n\n\n<p><strong>2007<\/strong><\/p>\n\n\n\n<p>Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P (2007) Structural analysis of the synaptic protein neuroligin and its \u03b2-neurexin complex&nbsp;: determinants for folding and cell adhesion. <em>Neuron<\/em> <strong>56<\/strong>, 979-991. (See also Preview \u201cA Crystal-Clear Interaction&nbsp;: Relating Neuroligin\/Neurexin Complex Structure to Function at the Synapse\u201d by Levinson J.N. &amp; El-Husseini A. <em>Neuron<\/em> <strong>56<\/strong>, 937-939.)<\/p>\n\n\n\n<p><strong>2009<\/strong><\/p>\n\n\n\n<p>Hibbs RE*, Sulzenbacher G*, Shi J, Talley TT, Conrod S, Kem WR, Taylor P, Marchot P, Bourne Y (2009) Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal \u03b17 nicotinic acetylcholine receptor. <em>EMBO J<\/em> <strong>28<\/strong>, 3040-3051.<\/p>\n\n\n\n<p><strong>2010<\/strong><\/p>\n\n\n\n<p>Bourne Y, Radi\u0107 Z, Ar\u00e1oz R, Talley TT, Benoit E, Servent D, Taylor P, Molg\u00f3 J, Marchot P (2010) Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism. <em>Proc Natl Acad Sci USA<\/em> <strong>107<\/strong>, 6076-6081.<\/p>\n\n\n\n<p>Leone P, Comoletti D, Ferracci G, Conrod S, Garcia SU, Taylor P, Bourne Y, Marchot P (2010) Structural insights into the exquisite selectivity of neurexin\/neuroligin synaptic interactions. <em>EMBO J<\/em> <strong>29<\/strong>, 2461-2471.<\/p>\n\n\n\n<p>Leone P, Comoletti D, Taylor P, Bourne Y, Marchot P (2010) Structure-function relationship of the \u03b1\/\u03b2-hydrolase fold domain of neuroligin&nbsp;: a comparison with acetylcholinesterase [Revue]. <em>Chem Biol Interact<\/em> <strong>187<\/strong>, 49\u201355.<\/p>\n\n\n\n<p>Hotelier T, N\u00e8gre V, Marchot P, Chatonnet A (2010) Insecticide resistance through mutations in cholinesterases or carboxylesterases&nbsp;: data mining in ESTHER database. <em>J Pestic Sci<\/em> <strong>35<\/strong>, 315-320.<\/p>\n\n\n\n<p>Bourne Y, Radi\u0107 Z, Taylor P, Marchot P (2010) Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state. <em>J Am Chem Soc<\/em> <strong>132<\/strong>, 18292-18300.<\/p>\n\n\n\n<p><strong>2012<\/strong><\/p>\n\n\n\n<p>Marchot P, Chatonnet A (2012) <em>Editorial to<\/em> the Special Issue on \u201cHydrolase versus other functions of members of the \u03b1\/\u03b2-hydrolase fold superfamily of proteins\u201d. <em>Protein Peptide Lett<\/em> <strong>19<\/strong>, 130-131.<\/p>\n\n\n\n<p>Marchot P, Chatonnet A (2012) Enzymatic activity and protein interactions in \u03b1\/\u03b2-hydrolase fold proteins&nbsp;: moonlighting <em>versus<\/em> promiscuity. <em>In&nbsp;:<\/em> Special Issue on \u201cHydrolase versus other functions of members of the \u03b1\/\u03b2-hydrolase fold superfamily of proteins\u201d. <em>Protein Peptide Lett<\/em> <strong>19<\/strong>, 132-143.<\/p>\n\n\n\n<p>Fabrichny IP, Mondielli G, Conrod S, Martin-Eauclaire MF, Bourne Y, Marchot P (2012) Structural insights into antibody sequestering and neutralizing of Na+-channel \u03b1-type modulator from Old World scorpion venom. <em>J Biol Chem<\/em> <strong>287<\/strong>, 14136-14148.<\/p>\n\n\n\n<p><strong>2013<\/strong><\/p>\n\n\n\n<p>Lenfant N, Hotelier T, Velluet E, Bourne Y, Marchot P, Chatonnet A (2013) ESTHER, the database of the \u03b1\/\u03b2-hydrolase fold superfamily of proteins&nbsp;: tools to explore diversity of functions. <em>Nucleic Acids Res (Database Issue)<\/em> <strong>41<\/strong>, D423-D429.<\/p>\n\n\n\n<p>Lenfant N, Hotelier T, Bourne Y, Marchot P, Chatonnet A (2013) Proteins with an \u03b1\/\u03b2-hydrolase fold&nbsp;: relationships between subfamilies in an ever-growing superfamily. <em>Chem Biol Interact<\/em> <strong>203<\/strong>, 266-268.<\/p>\n\n\n\n<p>Martin-Eauclaire MF, Benoit E, Marchot P, Barbier J, Molg\u00f3 J, Servent D (2013) <em>Editorial to<\/em> the Special Issue on \u201cToxins&nbsp;: From Threats to Benefits\u201d (Molg\u00f3 J, Benoit E, Barbier J, Marchot P, Servent D, Guest Eds), <em>Toxicon<\/em> <strong>75<\/strong>, 1-2.<\/p>\n\n\n\n<p>Bourne Y*, Renault L*, Essono S, Mondielli G, Lamourette P, Boquet D, Grassi J, Marchot P (2013) Molecular characterization of monoclonal antibodies that inhibit acetylcholinesterase by targeting the peripheral site and backdoor region. <em>PLOS One<\/em> <strong>8<\/strong>, e77226.<\/p>\n\n\n\n<p><strong>2014<\/strong><\/p>\n\n\n\n<p>Lenfant N, Hotelier T, Bourne Y, Marchot P, Chatonnet A (2014) Tracking the origin and divergence of cholinesterases and neuroligins&nbsp;: the evolution of synaptic proteins. <em>J Mol Neurosci<\/em> <strong>53<\/strong>, 362-369.<\/p>\n\n\n\n<p>Bourne Y, Marchot P (2014) The neuroligins and their ligands&nbsp;: from structure to function at the synapse. <em>J Mol Neurosci<\/em> <strong>53<\/strong>, 387-396.<\/p>\n\n\n\n<p>Benoit E, Mattei C, Barbier J, Marchot P, Molg\u00f3 J, Servent D (2014) <em>Editorial to<\/em> the Special Issue on \u201cFreshwater and Marine Toxins\u201d (Molg\u00f3 J, Benoit E, Barbier J, Marchot P, Servent D, Guest Eds), <em>Toxicon<\/em> <strong>91<\/strong>, 1-4.<\/p>\n\n\n\n<p><strong>2015<\/strong><\/p>\n\n\n\n<p>Bourne Y*, Renault L*, Marchot P (2015) Crystal structure of snake venom acetylcholinesterase in complex with inhibitory antibody fragment Fab410 bound at the peripheral site&nbsp;: evidence for open and closed states of a back door channel. <em>J Biol Chem<\/em> <strong>290<\/strong>, 1522\u20131535.<\/p>\n\n\n\n<p>Bourne Y, Sulzenbacher G, Radi\u0107 Z, Ar\u00e1oz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molg\u00f3 J, Taylor P, Marchot P (2015) Marine macrocyclic imines, pinnatoxins A and G&nbsp;: structural determinants and functional properties to distinguish neuronal \u03b17 from muscle (\u03b11)2\u03b2\u03b3\u03b4 nAChRs. <em>Structure<\/em> <strong>23<\/strong>, 1106-1115. (See also Preview &#8220;From Shellfish Poisoning to Neuroscience&#8221; by Shahsavar A and Balle T, <em>Structure<\/em> <strong>23<\/strong>, 979-980.)<\/p>\n\n\n\n<p><strong>2016<\/strong><\/p>\n\n\n\n<p>Bourne Y, Sharpless KB, Taylor P, Marchot P (2016) Steric and dynamic parameters influencing in situ cycloadditions to form triazole inhibitors with crystalline acetylcholinesterase. <em>J Am Chem Soc<\/em> <strong>138<\/strong>, 1611\u22121621.<\/p>\n\n\n\n<p>Lenfant N, Bourne Y, Marchot P, Chatonnet A (2016) Relationships of human \u03b1\/\u03b2 hydrolase fold proteins and other organophosphate-interacting proteins. <em>Chem Biol Interact<\/em> <strong>259<\/strong>, 343-351.<\/p>\n\n\n\n<p><strong>2017<\/strong><\/p>\n\n\n\n<p>Prado MAM, Marchot P, Silman I (2017) <em>Preface to the<\/em> Special Issue &#8220;Cholinergic Mechanisms&#8221;. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 3-6.<\/p>\n\n\n\n<p>Kessler P, Marchot P, Silva M, Servent D (2017) The three-finger toxin fold&nbsp;: a multifunctional structural scaffold able to modulate the cholinergic functions. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 7-18.<\/p>\n\n\n\n<p>Molg\u00f3 J, Marchot P, Ar\u00e1oz R, Benoit E, Iorga BI, Zakarian A, Taylor P, Bourne Y, Servent D (2017) Cyclic imine toxins from dinoflagellates&nbsp;: a growing family of potent antagonists of the nicotinic acetylcholine receptors. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 41-51.<\/p>\n\n\n\n<p>Chatonnet A, Lenfant N, Marchot P, Selkirk ME (2017) Natural genomic amplification of cholinesterase genes in animals. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 73-81.<\/p>\n\n\n\n<p>Thoumine O, Marchot P (2017) A triad of crystals sheds light on MDGA interference with neuroligation. <em>Neuron<\/em> <strong>95<\/strong>, 729-731.<\/p>\n\n\n\n<p><strong>2018<\/strong><\/p>\n\n\n\n<p>Bourne Y, Marchot P (2018) Hot spots for protein partnership at the surface of cholinesterases and related alpha\/beta hydrolase fold proteins or domains &#8211; a structural perspective. <em>Molecules<\/em> <strong>23<\/strong>, 35.<\/p>\n\n\n\n<p><strong>2019<\/strong><\/p>\n\n\n\n<p>Chatonnet A, Brazzolotto X, Hotelier T, Lenfant N, Marchot P, Bourne Y (2019) An evolutionary perspective on the first disulfide bond in members of the cholinesterase-carboxylesterase (COesterase) family&nbsp;: Possible outcomes for cholinesterase expression in prokaryotes. <em>Chem Biol Interact<\/em> <strong>308<\/strong>, 179-184.<\/p>\n\n\n\n<p><strong>2020<\/strong><\/p>\n\n\n\n<p>Trobiani L, Meringolo M, Diamanti T, Bourne Y, Marchot P, Martella G, Dini L, Pisani A, De Jaco A, Bonsi P (2020) The neuroligins and the synaptic pathway in Autism Spectrum Disorder (Review). <em>Neurosci Biobehav Rev<\/em> <strong>119<\/strong>, 37-51.<\/p>\n\n\n\n<p>Platsaki S, Zhou X, Pinan-Lucarr\u00e9 B, Delauzun V, Tu H, Mansuelle P, Fourquet P, Bourne Y, Bessereau J-L, Marchot P (2020) The Ig-like domain of Punctin\/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1. <em>J Biol Chem<\/em> <strong>295<\/strong>, 16267-16279.<\/p>\n\n\n\n<p><strong>2021<\/strong><\/p>\n\n\n\n<p>Comoletti D, Trobiani L, Chatonnet A, Bourne Y, Marchot P (2021) Comparative mapping of selected structural determinants on the extracellular domains of cholinesterase-like cell-adhesion molecules (Review). Special Issue on \u2018Acetylcholinesterase Inhibitors\u2019 (Guest Editor, Maria Braga). <em>Neuropharmacology<\/em> <strong>184<\/strong>, 108381.<\/p>\n\n\n\n<p><strong>2022<\/strong><\/p>\n\n\n\n<p>Ramirez-Franco J, Debreux K, Extremet J, Maulet Y, Belghazi M, Villard C, Sangiardi M, Youssouf F, El Far L, L\u00e9v\u00eaque C, Debarnot C, Marchot P, Paneva S, Debanne D, Russier M, Seagar M, Irani SR, El Far O. Patient-derived antibodies reveal the subcellular distribution and heterogeneous interactome of LGI1. <em><em>Brain<\/em> <\/em><strong>145<\/strong>, 3843-3858.<\/p>\n\n\n\n<p><strong>2023<\/strong><\/p>\n\n\n\n<p>Chatonnet A, Perochon M, Velluet E, Marchot P (2023) The ESTHER database on alpha\/beta hydrolase fold proteins &#8211; An overview of recent developments. <em>Chem Biol Interact<\/em> <strong>383<\/strong>, 110671.<\/p>\n\n\n\n<p>Martin-Eauclaire MF, Marchot P (2023) Obituary &#8211; Herv\u00e9 Paul Marie Antoine ROCHAT 1937\u20132023. <em>Toxicon<\/em> <strong>233<\/strong>, 107249.<\/p>\n\n\n\n<p><strong>2024<\/strong><\/p>\n\n\n\n<p>Bourne Y, Sulzenbacher G, Chabaud L, Ar\u00e1oz R, Radi\u0107 Z, Conrod S, Taylor P, Guillou C, Molg\u00f3 J, Marchot P (2024) The cyclic imine core common to the marine macrocyclic toxins is sufficient to dictate nicotinic acetylcholine receptor antagonism. <em>Mar. Drugs<\/em> <strong>22<\/strong>, 149. [This article belongs to the Special Issue &#8216;Marine Biotoxins 2.0&#8217; of <em>Marine Drugs<\/em> (Molgo J., Guest ed).]<\/p>\n\n\n\n<p>Zancolli G*, von Reumont BM*, Anderluh G, Caliskan F, Chiusano ML, Fr\u00f6hlich J, Hapeshi E, Hempel BF, Ikonomopoulou MP, Jungo F, Marchot P, Mendes de Farias T, Modica MV, Moran Y, Nalbantsoy A, Proch\u00e1zka Y, Tarallo A, Tonello F, Vitorino R, Zammit ML, Antunes A (2024) Web of venom: exploration of big data resources in animal toxin research. GigaScience <strong>13<\/strong>, giae054.<\/p>\n\n\n\n<p><strong>2025<\/strong><\/p>\n\n\n\n<p>Jenner R*, Anderluh G, Antunes A, Caliskan F, Damm M, Gruber CW, Hempel BF, Holford M, Ikonomopoulou M, Keke\u00e7o\u011flu M, Kirchhoff K, Kool J, Laku\u0161i\u0107 M, Ben Mansour R, Marchot P, Modica MV, Nalbantsoy A, Oukkache N, Po\u017eek K, von Reumont BM, Sarigiannis Y, Tarallo A, Tonello F, Vitorino R, Vrenozi B, Zammit ML (2025) Syllabus for a Master\u2019s-level course on animal venomics. Zenodo DOI <a href=\"https:\/\/doi.org\/10.5281\/zenodo.15304515\">10.5281\/zenodo.15304515<\/a>.<\/p>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"editorial-production\">Editorial production<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p>Book <em>Toxines &amp; cancer<\/em> (Goudey-Perri\u00e8re F, Benoit E, Goyffon M, Marchot P, eds) Coll. <em>Rencontres en Toxinologie<\/em>, Editions Lavoisier, Cachan, 2006 (326 pages) (ISBN&nbsp;: 2-7430-0958-6).<\/p>\n\n\n\n<p>Book <em>Toxines \u00e9mergentes&nbsp;: nouveaux risques<\/em> (Goudey-Perri\u00e8re F, Benoit E, Marchot P, Popoff M, eds) Coll <em>Rencontres en Toxinologie<\/em>, Editions Lavoisier, Cachan, 2007 (208 pages) (ISBN&nbsp;: 978-2-7430-1037-9).<\/p>\n\n\n\n<p>E-book <em>Toxines &amp; fonctions cholinergiques neuronales &amp; non neuronales<\/em> (Benoit E, Goudey-Perri\u00e8re F, Marchot P, Servent D, eds) Coll <em>Rencontres en Toxinologie<\/em>, Publications de la SFET, Ch\u00e2tenay-Malabry, 2008 (160 pages) (ISSN&nbsp;: 1760-6004).<\/p>\n\n\n\n<p>E-book <em>Toxines &amp; signalisation<\/em> (Benoit E, Goudey-Perri\u00e8re F, Marchot P, Servent D, eds) Coll <em>Rencontres en Toxinologie<\/em>, Publications de la SFET, Ch\u00e2tenay-Malabry, 2009 (206 pages) (ISSN&nbsp;: 1760-6004).<\/p>\n\n\n\n<p>E-book <em>Advances and new technologies in toxinology<\/em> (Barbier J, Benoit E, Marchot P, Mattei C, Servent D, eds) Coll <em>Rencontres en Toxinologie<\/em>, Publications de la SFET, Ch\u00e2tenay-Malabry, 2010 (184 pages) (ISSN&nbsp;: 1760-6004).<\/p>\n\n\n\n<p>Special Issue <em>Hydrolase versus other functions of members of the \u03b1\/\u03b2-hydrolase fold superfamily of proteins<\/em> (Chatonnet A, Marchot P, Guest eds). <em>Protein &amp; Peptide Letters<\/em>, Bentham Science Publishers Ltd., 2012, vol 19(2), pp 130-197 (ISSN&nbsp;: 0929-8665).<\/p>\n\n\n\n<p>Special Issue <em>Toxins&nbsp;: From Threats to Benefits, 20th Meeting of the French Society of Toxinology (SFET)<\/em> (Molg\u00f3 J, Benoit E, Barbier J, Marchot P, Servent D, Guest eds), <em>Toxicon<\/em> (ISSN&nbsp;: 0041-0101), Elsevier, 2013, vol 75, pp 1-224.<\/p>\n\n\n\n<p>Special Issue <em>Freshwater and Marine Toxins, 21th Meeting of the French Society of Toxinology (SFET)<\/em> (Molg\u00f3 J, Benoit E, Barbier J, Marchot P, Servent D, Guest eds), <em>Toxicon<\/em> (ISSN&nbsp;: 0041-0101), Elsevier, 2014, vol 91, pp 1-184.<\/p>\n\n\n\n<p>Special Issue <em>Cholinergic Mechanisms<\/em> (Silman I, Guest ed&nbsp;; Marchot P, Prado MAM, Assoc Guest eds), <em>J Neurochem<\/em> (ISSN&nbsp;: 1471-4159), Wiley, 2017, vol 142 &#8211; Suppl 2, pp 1-226.<\/p>\n\n\n\n<p>Special Issue <em>Toxins&nbsp;: From the Wild to the Lab, 29th Meeting of t<em>he French Society of Toxinology (SFET)<\/em> <\/em>(Marchot P, Benoit E, Diochot S, Guest eds). <em>Toxins<\/em> (ISSN: 2072-6651), MDPI, 2024.<\/p>\n\n\n\n<p>Special Issue <em>Unlocking the Deep Secrets of Toxins, 30th Meeting of t<em>he French Society of Toxinology (SFET)<\/em> <\/em>(Marchot P, Diochot S, Comte K, Popoff MR, Guest eds). <em>Toxins<\/em> (ISSN: 2072-6651), MDPI, 2025.<\/p>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"book-chapters-and-proceedings\">Book chapters and proceedings<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p>Marchot P, Bougis PE, C\u00e9ard B, Van Rietschoten J, Rochat H (1989) Lethal synthetic peptides as models of the toxic site of <em>Naja mossambica mossambica<\/em> cardiotoxins. In <em>Second Forum on Peptides<\/em> (Aubry A, Marraud M, Vitoux B, eds) Colloque INSERM \/ John Libbey Eurotext Ltd <strong>174<\/strong>, 461-464.<\/p>\n\n\n\n<p>Le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC (1993) Fasciculin 1 (Green mamba). In <em>Macromolecular Structures <\/em>(Hendrickson WA, W\u00fcthrich K, eds) pp. 152-153, Current Biology Ltd, Philadelphia.<\/p>\n\n\n\n<p>Marchot P, Camp S, Radi\u0107 Z, Bougis PE, Taylor P (1995) Structural determinants of fasciculin specificity for acetylcholinesterase. In <em>Enzymes of the Cholinesterase Family<\/em> (Quinn DM, Balasubramanian AS, Doctor BP, Taylor P, eds) pp. 197-202, Plenum Publishing Corp, NY.<\/p>\n\n\n\n<p>Bourne Y, Taylor P, Marchot P (1996) Acetylcholinesterase, recombinant monomeric form (mouse) \/ fasciculin 2 (mamba) complex. In <em>Macromolecular Structures <\/em>(Hendrickson WA, W\u00fcthrich K, eds) pp. 8-9, Current Biology Ltd, London, UK.<\/p>\n\n\n\n<p>Bourne Y, Taylor P, Kanter JR, Bougis PE, Marchot P (1998) Crystal structure of mouse acetylcholinesterase. In <em>Structure and Function of Cholinesterases and Related Proteins<\/em> (Doctor BP, Taylor P, Quinn DM, Rotundo RL, Gentry MK, eds) pp. 315-322, Plenum Publishing Corp, NY.<\/p>\n\n\n\n<p>Marchot P, Bourne Y, Prowse CN, Kanter JR, Eads J, Bougis PE, Taylor P (1998) Fasciculin inhibition of mouse acetylcholinesterase&nbsp;: crystal structure of the complex and mutagenesis of fasciculin. In <em>Structure and Function of Cholinesterases and Related Proteins<\/em> (Doctor BP, Taylor P, Quinn DM, Rotundo RL, Gentry MK, eds) pp. 331-338, Plenum Publishing Corp., NY.<\/p>\n\n\n\n<p>Kanter JR, Eads J, Camp S, Marchot P, Taylor P (1998) Expression and purification of recombinant mutants of fasciculin from mammalian cells. In <em>Structure and Function of Cholinesterases and Related Proteins<\/em> (Doctor BP, Taylor P, Quinn DM, Rotundo RL, Gentry MK, eds) pp. 240-241, Plenum Publishing Corp, NY.<\/p>\n\n\n\n<p>Marchot P, Bougis PE (2000) The fasciculins, and their interaction with acetylcholinesterase. In&nbsp;: <em>Animal Toxins. Facts and Protocols<\/em> (Rochat H, Martin-Eauclaire MF, eds) pp. 246-275, Birkh\u00e4user Verlag, Basel.<\/p>\n\n\n\n<p>Bourne Y, Marchot P (2002) Fasciculines et autres ligands de l\u2019AChE&nbsp;: d\u00e9veloppements structuraux r\u00e9cents [Revue en fran\u00e7ais&nbsp;; r\u00e9sum\u00e9 en anglais]. In&nbsp;: <em>Toxines et Recherches Biom\u00e9dicales<\/em> (Goudey-Perri\u00e8re F, Bon C, Puiseux-Dao S, Sauviat MP, eds) pp. 287-296, Coll. <em>Rencontres en Toxinologie<\/em>, Editions Scientifiques et M\u00e9dicales Elsevier, Paris.<\/p>\n\n\n\n<p>Comoletti D, Flynn R, Jennings L, Hoffman R, Marchot P, Bourne Y, S\u00fcdhof T, Taylor P (2004) Interaction of recombinant soluble neuroligin-1 with neurexin-1-\u03b2. In <em>Cholinergic Mechanisms &#8211; function and dysfunction<\/em> <em>Symposium Proceedings<\/em> (Silman I, Michaelson DM, Anglister L, Fisher A, Soreq H, eds) pp. 523-525, Taylor &amp; Francis group, UK.<\/p>\n\n\n\n<p>Tai K, Shen T, Henchman RH, Bourne Y, Marchot P, McCammon JA (2004) Mechanism of acetylcholinesterase inhibition by fasciculin&nbsp;: A 5ns molecular dynamics simulation. In <em>Cholinergic Mechanisms &#8211; function and dysfunction<\/em> <em>Symposium Proceedings<\/em> (Silman I, Michaelson DM, Anglister I, Fisher A, Soreq H, eds) pp. 727-728, Taylor &amp; Francis group, UK.<\/p>\n\n\n\n<p>Bourne Y, Hansen SB, Sulzenbacher G, Talley TT, Huxford T, Taylor P, Marchot P (2005) Comparaison structurale de trois complexes entre une toxine peptidique et une prot\u00e9ine synaptique liant l\u2019ac\u00e9tylcholine. [Revue en fran\u00e7ais&nbsp;; r\u00e9sum\u00e9 en anglais]. In <em>Toxines et Douleur<\/em> (Bon C, Goudey-Perri\u00e8re F, Goyffon M, Sauviat MP, eds), pp. 213-216, Coll <em>Rencontres en Toxinologie<\/em>, Editions Lavoisier, Cachan, France.<\/p>\n\n\n\n<p>Fabrichny I, Conrod S, Martin-Eauclaire MF, Devaux C, Bourne Y, Marchot P (2007) Immunoth\u00e9rapie antiscorpionique&nbsp;: approche structurale. [En fran\u00e7ais&nbsp;; r\u00e9sum\u00e9 &amp; l\u00e9gendes en anglais]. In <em>Toxines \u00e9mergentes&nbsp;: nouveaux risques<\/em> (Goudey-Perri\u00e8re F, Benoit E, Marchot P, Popoff M, eds), pp. 197-202, Coll <em>Rencontres en Toxinologie<\/em>, Editions Lavoisier, Cachan, France.<\/p>\n\n\n\n<p>Bourne Y, Radi\u0107 Z, Talley TT, Conrod S, Taylor P, Molg\u00f3 J, Marchot P (2008) Utilisation des \u00ab&nbsp;prot\u00e9ines liant l\u2019ACh&nbsp;\u00bb (AChBP) en toxinologie structurale&nbsp;: nouveaux exemples. [En fran\u00e7ais&nbsp;; r\u00e9sum\u00e9 &amp; l\u00e9gendes en anglais]. In <em>Toxines et fonctions cholinergiques neuronales et non neuronales<\/em> (Benoit E, Goudey-Perri\u00e8re F, Marchot P, Servent D, eds), pp. 27-28, Coll <em>Rencontres en Toxinologie<\/em>, Publications de la SFET, Ch\u00e2tenay-Malabry, France.<\/p>\n\n\n\n<p>Taylor P, Radi\u0107 Z, Talley TT, Nemecz A, De Jaco A, Comoletti D, Fabrichny IP. Leone P, Miller MT, Dubi N, Fokin VV, Sharpless KB, Bourne Y, Marchot P (2008) Retrogenomics &#8211; Proceeding from gene product back to the gene&nbsp;: applications in drug discovery and uncovering linkages in congenital disorders. [Revue en anglais&nbsp;; r\u00e9sum\u00e9 &amp; l\u00e9gendes en fran\u00e7ais]. In <em>Toxines et fonctions cholinergiques neuronales et non neuronales<\/em> (Benoit E, Goudey-Perri\u00e8re F, Marchot P, Servent D, eds), pp. 29-32, Coll <em>Rencontres en Toxinologie<\/em>, Publications de la SFET, Ch\u00e2tenay-Malabry, France.<\/p>\n\n\n\n<p>Douzi B, Geerlof A, Gilles N, Darbon H, Marchot P, Vincentelli R (2010) A new system for expressing recombinant animal toxins in <em>E. coli<\/em>&nbsp;? In <em>Advances and new technologies in toxinology<\/em> (Barbier J, Benoit E, Marchot P, Mattei C, Servent D, eds), pp. 149-152, Coll <em>Rencontres en Toxinologie<\/em>, Publications de la SFET, Ch\u00e2tenay-Malabry, France.<\/p>\n\n\n\n<p>Marchot P, Diochot S, Popoff MR, Benoit E (2020) Report from the 26th Meeting on Toxinology, \u201cBioengineering of Toxins\u201d, Organized by the French Society of Toxinology (SFET) and Held in Paris, France, 4\u20135 December 2019. In <em>Special Issue &#8220;Selected Papers from the 26th Meeting of the French Society for Toxinology- Bioengineering of Toxins&#8221;<\/em> (Popoff MR, Benoit E, Guest eds). <em>Toxins<\/em> <strong>12<\/strong>, 31\/pp. 1-29. (doi:10.3390\/toxins12010031)<\/p>\n\n\n\n<p>Ladant D, Marchot P, Diochot S, Pr\u00e9vost G, Popoff MR, Benoit E (2022) Report from the 27th (Virtual) Meeting on Toxinology, \u201cToxins&nbsp;: Mr&nbsp;Hyde or Dr Jekyll&nbsp;?\u201d, Organized by the French Society of Toxinology, 9-10 December 2021. In <em>Special Issue &#8220;Toxins&nbsp;: Mr&nbsp;Hyde or Dr Jekyll&nbsp;?&#8221;<\/em> (Ladant D, Pr\u00e9vost G, Popoff MR, Benoit E, Guest eds). <em><em>Toxins<\/em> <\/em><strong>14<\/strong>(2), 110\/pp. 1-32. (doi: 10.3390\/toxins14020110)<\/p>\n\n\n\n<p>Marchot P, Benoit E, Fajloun Z, Diochot S (2023) Report from the 28th Meeting on Toxinology, \u201cToxins: What\u2019s up, Doc?\u201d, Organized by the French Society of Toxinology on November 28-29, 2022. <em>Toxins <\/em><strong>15<\/strong>(2), 126\/pp. 1-25. (doi: 10.3390\/toxins15020126)<\/p>\n\n\n\n<p>Marchot P, Fajloun Z, Legros C, Benoit E, Diochot S (2024) Report from the 29th Meeting on Toxinology, \u201cToxins: From the wild to the lab\u201d, Organized by the French Society of Toxinology on November 30-December 01, 2023. In <em>Special Issue &#8220;Toxins&nbsp;: From the wild to the lab&#8221;<\/em> (Marchot P, Benoit E, Diochot S, Guest eds). <em>Toxins<\/em> <strong>16<\/strong>, 147\/pp. 1-34. (doi: 10.3390\/toxins16030147)<\/p>\n\n\n\n<p>Marchot P, Fajloun Z, Benoit E, Diochot S (2025) Report from the 30th Meeting on Toxinology, \u201cUnlocking the Deep Secrets of Toxins\u201d, Organized by the French Society of Toxinology on 2\u20133 December 2024. In <em>Special Issue &#8220;Unlocking the Deep Secrets of Toxins&#8221;<\/em> (Marchot P, Diochot S, Comte K, Popoff MR, Guest eds). Toxins <strong>17<\/strong>, 94\/pp. 1-31. (doi: 10.3390\/toxins17020094)<\/p>\n\n\n\n<p>Diochot S, Le Garrec R, Dugon MM, Marchot P (2026) Report from the 31st Meeting on Toxinology, \u201cToxins: Playing with and fighting them!\u201d, Organized by the French Society for Toxinology on December 1-2, 2025. <em>Toxins <\/em><strong>18<\/strong>, 138\/pp. 1-32. (doi: 10.3390\/toxins18030138)<\/p>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"published-abstracts\">Published abstracts<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p>Bougis PE, Marchot P, Rochat H (1985) Reverse-phase high performance liquid chromatography of <em>Elapidae<\/em> snake venoms. <em>Toxicon<\/em> <strong>23<\/strong>, p. 554<\/p>\n\n\n\n<p>Marchot P, Kh\u00e9lif A, Bougis PE (1985) Brain acetylcholinesterase inhibitor from mamba snake venom&nbsp;: reverse-phase HPLC isolation and characterisation. <em>Toxicon<\/em> <strong>23<\/strong>, p. 592<\/p>\n\n\n\n<p>Marchot P, Bougis PE, Rochat H (1987) High performance liquid chromatography of <em>Elapidae<\/em> snake venoms. <em>Toxicon<\/em> <strong>25<\/strong>, p. 372<\/p>\n\n\n\n<p>Laraba-Djebari F, Martin-Eauclaire MF, Marchot P (1993) Two thrombin-like proteinases from <em>Cerastes cerastes<\/em> (Horn viper) venom&nbsp;: purification, characterization and kinetic parameter determination. <em>Toxicon<\/em> <strong>31<\/strong>, p. 528<\/p>\n\n\n\n<p>Laraba-Djebari F, Martin-Eauclaire MF, Marchot P (1994) Afa\u00e2cytin, a thrombin-like enzyme from the venom of <em>Cerastes cerastes<\/em>&nbsp;: structural and functional properties. <em>Toxicon<\/em> <strong>32<\/strong>, p. 400<\/p>\n\n\n\n<p>Marchot P, Kh\u00e9lif A, Ji YH, Mansuelle P, Bougis PE (1994) Binding of 125I-fasciculin to rat brain acetylcholinesterase. <em>Toxicon<\/em> <strong>32<\/strong>, p. 401<\/p>\n\n\n\n<p>Kanter J, Marchot P, Prowse C, Camp S, Taylor P (1997) Contributions of individual amino acid residues to the stability of the fasciculin-acetylcholinesterase interaction. <em>Pharmacologist<\/em> <strong>39<\/strong>, p. 104<\/p>\n\n\n\n<p>Marchot P, Taylor P, Kanter JR, Bougis PE, Bourne Y (1998) Tetrameric assembly and peripheral site-occluding loop of mouse acetylcholinesterase. <em>J Physiol (Paris)<\/em> <strong>92<\/strong>, p. 465<\/p>\n\n\n\n<p>Bougis PE, Taylor P, Marchot P (1998) Biotinylation of the tyrosine residues of fasciculin. <em>J Physiol (Paris)<\/em> <strong>92<\/strong>, p. 416<\/p>\n\n\n\n<p>Marchot P (1999) Acetylcholinesterase inhibition by fasciculin. <em>Toxicon<\/em> <strong>37<\/strong>, 1209-1210<\/p>\n\n\n\n<p>Bougis PE, Taylor P, Marchot P (2000) Biotinylated fasciculins&nbsp;: potential tools for histochemical studies of acetylcholinesterase. <em>Toxicon<\/em> <strong>38<\/strong>, 1637-1638<\/p>\n\n\n\n<p>Flynn R, Comoletti D, Marchot P, Bourne Y, S\u00fcdhof T, &amp; Taylor P (2003) Interaction of recombinant soluble neuroligins-1 with neurexin-\u00df. <em>FASEB J.<\/em> <strong>17 (4)<\/strong>, A640<\/p>\n\n\n\n<p>Bourne Y, Sulzenbacher G, Radi\u0107 Z, Ar\u00e1oz R, Reynaud M, Benoit E, Talley TT, Zakarian A, Taylor P, Servent D, Molg\u00f3 J, Marchot P (2014) Diversity in the binding interactions of marine toxins to AChBP, the soluble nAChR surrogate. <em>Toxicon<\/em> <strong>91<\/strong>, 171-172.<\/p>\n\n\n\n<p>Marchot P, Sharpless KB, Taylor P, Bourne Y (2016) Structural and functional analysis of acetylcholinesterase complexes with \u201cin situ click-chemistry\u201d inhibitors. <em>FASEB J<\/em> <strong>30 Suppl 1<\/strong>, 833.10.<\/p>\n\n\n\n<p>Bourne Y, Radi\u0107 Z, Sharpless KB, Taylor P, Marchot P (2017) Structural and functional analysis of acetylcholinesterase complexes with in situ click-chemistry inhibitors. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 189.<\/p>\n\n\n\n<p>Marchot P, Sulzenbacher G, Radi\u0107 Z, Ar\u00e1oz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molg\u00f3 J, Taylor P, Bourne Y (2017) Diversity in the binding interactions of marine phycotoxins to AChBP, the soluble nAChR surrogate. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 196.<\/p>\n\n\n\n<p>Chatonnet A, Marchot P, Bourne Y, Lenfant N, Hotelier T (2017) ESTHER database&nbsp;: update on the alpha\/beta hydrolase fold superfamily of proteins. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 209.<\/p>\n\n\n\n<p>Lenfant N, Selkirk ME, Hotelier T, Bourne Y, Marchot P, Chatonnet A (2017) Evolution of animal cholinesterases. <em>J Neurochem<\/em> <strong>142 Suppl 2<\/strong>, 214.<\/p>\n\n\n\n<p>Chatonnet A, Brazzolotto X, Hotelier T, Lenfant N, Marchot P (2018) Evolution of the first disulfide bond in the cholinesterase-carboxylesterase (coesterase) family: possible consequences for cholinesterase expression in prokaryotes. <em>Mil Med Sci Lett (Voj Zdrav Listy)<\/em> <strong>87 Suppl 1<\/strong>, 55.<\/p>\n\n\n\n<p>Bourne Y, Sulzenbacher G, Radi\u0107 Z, Chabaud L, Ar\u00e1oz R, Benoit E, Zakarian A, Servent D, Guillou C, Taylor P, Molg\u00f3 J, Marchot P (2020) Diversity in the binding interactions of nicotinic ligands and toxins to the nAChRs and associated conformational fluctuations-Insights into the core motif dictating antagonism. In &#8220;Marchot P, Diochot S, Popoff MR, Benoit E. Report from the 26th Meeting on Toxinology, &#8220;Bioengineering of Toxins&#8221;, Organized by the French Society of Toxinology (SFET) and Held in Paris, France, 4-5 December 2019. <em>Toxins <\/em><strong>12:31<\/strong>, pp. 9-10.<\/p>\n\n\n\n<p>Bourne Y, Sulzenbacher G, Chabaud L, Ar\u00e1oz R, Radi\u0107 Z, Conrod S, Taylor P, Guillou C, Molg\u00f3 J, Marchot P (2024) Is the cyclic imine core common to the marine macrocyclic toxins sufficient to dictate nicotinic acetylcholine receptor antagonism? In Marchot P, Fajloun Z, Legros C, Benoit E, Diochot S. Report from the 29th Meeting on Toxinology, \u201cToxins: From the Wild to the Lab\u201d, Organized by the French Society of Toxinology on 30 November\u20131 December 2023. <em>Toxins<\/em> <strong>16:147<\/strong>, pp. 16-17.<\/p>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"crystal-structures\">Crystal structures<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li><strong>1FAS<\/strong> Fasciculin 1 (LeDu, Marchot, Bougis, Fontecilla-Camps, 1993)<\/li>\n\n\n\n<li><strong>1FSC<\/strong> Fasciculin 2 (LeDu, Housset, Marchot, Bougis, Navaza, Fontecilla-Camps, 1995)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1MAH<\/strong> Mouse AChE, fasciculin 2 complex (Bourne, Taylor, Marchot, 1995)<\/li>\n\n\n\n<li><strong>1KU6<\/strong> Mouse AChE, revisited fasciculin 2 complex (Bourne, Burmeister, Taylor, Marchot, 2002)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1C2B<\/strong> Eel AChE, natural tetramer, structure A (Bourne, Marchot, 1999)<\/li>\n\n\n\n<li><strong>1C2O<\/strong> Eel AChE, natural tetramer, structure B (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1MAA<\/strong> Mouse AChE, crystalline tetramer (Bourne, Taylor, Bougis, Marchot, 1998)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1J06<\/strong> Mouse AChE, first apo form (Bourne, Taylor, Radi\u0107, Marchot, 2002)<\/li>\n\n\n\n<li><strong>1J07<\/strong> Mouse AChE, decidium complex (id.)<\/li>\n\n\n\n<li><strong>1N5R<\/strong> Mouse AChE, propidium complex (id.)<\/li>\n\n\n\n<li><strong>1N5M<\/strong> Mouse AChE, gallamine complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2H9Y<\/strong> Mouse AChE, complex with TMTFA (Bourne, Radi\u0107, Sulzenbacher, Kim, Taylor, Marchot, 2006)<\/li>\n\n\n\n<li><strong>2HA0<\/strong> Mouse AChE, complex with 4K-TMA (id.)<\/li>\n\n\n\n<li><strong>2HA2<\/strong> Mouse AChE, complex with succinyldicholine (id.)<\/li>\n\n\n\n<li><strong>2HA3<\/strong> Mouse AChE, complex with choline (id.)<\/li>\n\n\n\n<li><strong>2HA4<\/strong> Mouse AChE S203A mutant, complex with acetylcholine (id.)<\/li>\n\n\n\n<li><strong>2HA5<\/strong> Mouse AChE S203A mutant, complex with acetylthiocholine (id.)<\/li>\n\n\n\n<li><strong>2HA6<\/strong> Mouse AChE S203A mutant, complex with succinyldicholine (id.)<\/li>\n\n\n\n<li><strong>2HA7<\/strong> Mouse AChE S203A mutant, complex with butyrylthiocholine (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1Q83<\/strong> Mouse AChE, TZ2PA6 <em>syn1<\/em> complex (Bourne, Kolb, Radi\u0107, Sharpless, Taylor, Marchot, 2003)<\/li>\n\n\n\n<li><strong>1Q84<\/strong> Mouse AChE, TZ2PA6 <em>anti1<\/em> complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>5EHN<\/strong> mouse AChE, <em>syn<\/em>-TZ2PA5 complex (Bourne, Sharpless, Taylor, Marchot, 2016)<\/li>\n\n\n\n<li><strong>5EHQ<\/strong> mouse AChE, <em>anti<\/em>-TZ2PA5 complex (id.)<\/li>\n\n\n\n<li><strong>5EHZ<\/strong> mouse AChE, <em>syn<\/em>-TZ2PA5 complex from a 1:1 <em>syn<\/em>\/<em>anti<\/em> mixture (id.)<\/li>\n\n\n\n<li><strong>5EIA<\/strong> mouse AChE, <em>anti<\/em>-TZ2PA5 complex from a 1:6 <em>syn<\/em>\/<em>anti<\/em> mixture (id.)<\/li>\n\n\n\n<li><strong>5EIE<\/strong> mouse AChE, TZ2 complex (id.)<\/li>\n\n\n\n<li><strong>5EIH<\/strong> mouse AChE, TZ2+PA5 complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2XUD<\/strong> Mouse AChE Tyr337Ala mutant (Bourne, Radi\u0107, Taylor, Marchot, 2010)<\/li>\n\n\n\n<li><strong>2XUG<\/strong> Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 <em>anti1<\/em> (1-wk) (id.)<\/li>\n\n\n\n<li><strong>2XUF<\/strong> Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 <em>anti1<\/em> (1-mth) (id.)<\/li>\n\n\n\n<li><strong>2XUH<\/strong> Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 <em>anti1<\/em> (10-mths) (id)<\/li>\n\n\n\n<li><strong>2XUI<\/strong> Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 <em>syn1<\/em> (1-wk) (id)<\/li>\n\n\n\n<li><strong>2XUJ<\/strong> Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 <em>syn1<\/em> (1-mth) (id)<\/li>\n\n\n\n<li><strong>2XUK<\/strong> Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 <em>syn1<\/em> (10-mths) (id)<\/li>\n\n\n\n<li><strong>2XUO<\/strong> Mouse AChE, Tyr337Ala mutant, soaking complex with TZ2PA6 <em>anti1<\/em> (id)<\/li>\n\n\n\n<li><strong>2XUP<\/strong> Mouse AChE, Tyr337Ala mutant, soaking complex with TZ2PA6 <em>syn1<\/em> (id.)<\/li>\n\n\n\n<li><strong>2XUQ<\/strong> Mouse AChE, Tyr337Ala mutant, soaking complex with mixed TZ2PA6 <em>anti1<\/em>\/<em>syn1<\/em> (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2YMX<\/strong> Inhibitory anti-AChE Fab408 (Bourne, Renault, Essono, Mondielli, Lamourette, Bocquet, Grassi, Marchot, 2013)<\/li>\n\n\n\n<li><strong>4QWW<\/strong> Fab410-BfAChE complex (Bourne, Renault, Marchot, 2015)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1YI5<\/strong> Lymnaea AChBP, \u03b1-cobratoxin complex (Bourne, Talley, Hansen, Taylor, Marchot, 2005)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2BYN<\/strong> Aplysia AChBP, apo (Hansen, Sulzenbacher, Huxford, Marchot, Taylor, Bourne, 2005)<\/li>\n\n\n\n<li><strong>2BYP<\/strong> Aplysia AChBP, \u03b1-conotoxin Im1 complex (id.)<\/li>\n\n\n\n<li><strong>2BYQ<\/strong> Aplysia AChBP, epibatidine complex (id.)<\/li>\n\n\n\n<li><strong>2BYR<\/strong> Aplysia AChBP, methyllycaconitine complex (id.)<\/li>\n\n\n\n<li><strong>2BYS<\/strong> Aplysia AChBP, lobeline complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2WNL<\/strong> Aplysia AChBP, anabaseine complex (Hibbs, Sulzenbacher, Shi, Talley, Conrod, Kem, Taylor, Marchot, Bourne, 2009)<\/li>\n\n\n\n<li><strong>2WNJ<\/strong> Aplysia AChBP, DMXBA complex (id.)<\/li>\n\n\n\n<li><strong>2WN9<\/strong> Aplysia AChBP, 4-OH-DMXBA complex (id.)<\/li>\n\n\n\n<li><strong>2WNC<\/strong> Aplysia AChBP, tropisetron complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2WZY<\/strong> Aplysia AChBP, SPX complex (Bourne, Radic, Ar\u00e1oz, Talley, Benoit, Servent, Taylor, Molgo, Marchot, 2010)<\/li>\n\n\n\n<li><strong>2X00<\/strong> Aplysia AChBP, GYM complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>4XHE<\/strong> Aplysia AChBP, PnTx-A complex (Bourne, Sulzenbacher, Marchot, 2015)<\/li>\n\n\n\n<li><strong>4XK9<\/strong> Aplysia AChBP, PnTx-G complex (id)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>8Q1M<\/strong> Aplysia AChBP, spiroimine (+)-4 R complex (Sulzenbacher, Bourne, Marchot, 2024)<\/li>\n\n\n\n<li><strong>8QTL<\/strong> Aplysia AChBP, spiroimine (\u2013)-4 S complex (id.)<\/li>\n\n\n\n<li><strong>8QX2<\/strong> Aplysia AChBP, spiroimine (\u00b1)-4 complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>3BE8<\/strong> NL4 (Fabrichny, Leone, Sulzenbacher, Comoletti, Miller, Taylor, Bourne, Marchot, 2007)<\/li>\n\n\n\n<li><strong>2VH8<\/strong> Nrx\u03b21-NL4 complex (id.)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2WQZ<\/strong> Nrx\u03b21-NL4 complex, aternative refinement (replaces 2VH8) 2009<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>2XB6<\/strong> Revisited Nrx\u03b21-NL4 complex (Leone, Comoletti, Ferracci, Conrod, Taylor, Bourne, Marchot, 2010)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>4AEI<\/strong> Fab4C1 bound with scorpion toxin AahII (Fabrichny, Mondielli, Conrod, Martin-Eauclaire, Bourne, Marchot, 2011)<\/li>\n\n\n\n<li><strong>4AEH<\/strong> Fab9C2 in the absence of a bound scorpion toxin AahI (id)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1G8I<\/strong> Human frequenin (NCS-1) (Bourne, Dannenberg, Pollmann, Marchot, Pongs, 2000)<\/li>\n<\/ul>\n\n\n\n<ul class=\"wp-block-list\">\n<li><strong>1UKC<\/strong> Aspergillus niger EstA (Bourne, Hasper, Chahinian, Juin, de Graff, Marchot, 2003)<\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"press-alerts\">Press alerts<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p><strong>For \u201cBourne et al., Structure (Camb) 2004\u201d&nbsp;:<\/strong><\/p>\n\n\n\n<p>\u201cDefining substrate characteristics from 3D structure&nbsp;: perspective on EstA structure\u201d by Schrag JD &amp; Cygler M, Structure (Camb) 12, 521-522.<\/p>\n\n\n\n<p><strong>For \u00ab&nbsp;Bourne et al., PNAS 2004\u201d&nbsp;:<\/strong><\/p>\n\n\n\n<p>\u201cEnzyme manufactures its own inhibitor\u201d PNAS News Archive [Feb 2004]<\/p>\n\n\n\n<p>\u201cSharpless clicks at Informex 2004\u201d Chem. Eng. News 82, 63-65 [Feb 2004] <a href=\"https:\/\/cen.acs.org\/articles\/82\/i7\/SHARPLESS-CLICKS-INFORMEX-2004.html\">https:\/\/cen.acs.org\/articles\/82\/i7\/SHARPLESS-CLICKS-INFORMEX-2004.html<\/a><\/p>\n\n\n\n<p>\u201cClicking on to the chemistry of Alzheimer\u2019s\u201d Chem. World 3 [Mar 2004]<\/p>\n\n\n\n<p>\u201cNew approach to drug design\u201d UCSD News \/ Health Sciences [Mar 2004] <a href=\"http:\/\/ucsdnews.ucsd.edu\/archive\/newsrel\/health\/03_22_Taylor.asp\">http:\/\/ucsdnews.ucsd.edu\/archive\/ne&#8230;<\/a><\/p>\n\n\n\n<p>\u201cEnzyme acetylcholinesterase, new approach to drug design\u201d News-Medical.Net&#8230; Medical News [Mar 2004] <a href=\"http:\/\/www.news-medical.net\/?id=87\">http:\/\/www.news-medical.net\/?id=87<\/a><\/p>\n\n\n\n<p>\u201cPharmacologists collaborate on new approach to drug design\u201d MediLexicon\/Medical News Headlines [Mar 2004] <a href=\"http:\/\/www.pharma-lexicon.com\/medicalnews.php?language=spanish&amp;newsid=6735&amp;token=phuvNdB2EE1iU\">http:\/\/www.pharma-lexicon.com\/medic&#8230;<\/a><\/p>\n\n\n\n<p>&#8220;Alzheimer&#8217;s enzyme creates its own inhibitor&#8221; Chemistry World News \/ Royal Society of Chemistry [Mar 2004] <a href=\"https:\/\/www.chemistryworld.com\/news\/alzheimers-enzyme-creates-its-own-inhibitor\/3000321.article\">https:\/\/www.chemistryworld.com\/news\/alzheimers-enzyme-creates-its-own-inhibitor\/3000321.article<\/a><\/p>\n\n\n\n<p>\u201cEnzymes are doing it for themselves\u201d Biotechniques Euro-edition [Apr 2004]<\/p>\n\n\n\n<p><strong>For \u201cFabrichny et al., Neuron 2007\u201d&nbsp;:<\/strong><\/p>\n\n\n\n<p>Preview \u201cA Crystal-Clear Interaction&nbsp;: Relating Neuroligin\/Neurexin Complex Structure to Function at the Synapse\u201d by Levinson J.N. &amp; El-Husseini A., Neuron 56 (2007) 937-939<\/p>\n\n\n\n<p>\u201cSnapshot of proteins linked to autism\u201d, Royal Society of Chemistry, UK [Dec 2007] <a href=\"http:\/\/www.rsc.org\/chemistryworld\/News\/2007\/December\/19120702.asp\">http:\/\/www.rsc.org\/chemistryworld\/N&#8230;<\/a><\/p>\n\n\n\n<p>\u201cAtomic Structure of Proteins Altered in Autism\u201d Newswise [Dec 2007] <a href=\"http:\/\/www.newswise.com\/articles\/view\/536233\/\">http:\/\/www.newswise.com\/articles\/vi&#8230;<\/a><\/p>\n\n\n\n<p>\u201cStudy Details Atomic Structure of Proteins Altered in Autism\u201d, UCSD Medical Center [Dec 2007] <a href=\"http:\/\/ucsdnews.ucsd.edu\/archive\/newsrel\/health\/12-07ProteinsAutism.html\">http:\/\/ucsdnews.ucsd.edu\/archive\/ne&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;L\u2019autisme&nbsp;: un syndrome complexe approch\u00e9 de tr\u00e8s pr\u00e8s par les chercheurs de l\u2019Universit\u00e9 de la M\u00e9diterran\u00e9e et du CNRS&nbsp;: Des prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme vues en 3D&nbsp;\u00bb, Communiqu\u00e9 de Presse de l\u2019Universit\u00e9 de la M\u00e9diterrann\u00e9e [Dec 2007] <a href=\"http:\/\/www.univmed.fr\/communication\/default.aspx?id=92228\">http:\/\/www.univmed.fr\/communication&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Observation en 3D de prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme&nbsp;\u00bb, Communiqu\u00e9 de presse du CNRS [Dec 2007] <a href=\"http:\/\/www2.cnrs.fr\/presse\/communique\/1253.htm\">http:\/\/www2.cnrs.fr\/presse\/communiq&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Observation en 3D de prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme&nbsp;\u00bb, TV5.org &#8211; Infos &#8211; Les communiqu\u00e9s de presse [Dec 2007] <a href=\"http:\/\/www.tv5.org\/TV5Site\/info\/communiques-de-presse-article.php?NPID=FR196695\">http:\/\/www.tv5.org\/TV5Site\/info\/com&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Observation en 3D de prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme&nbsp;\u00bb, News Press Le Monde [Dec 2007] <a href=\"http:\/\/www.newsfrance.org\/communique_196695_641.aspx\">http:\/\/www.newsfrance.org\/communiqu&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;En direct des labos &#8211; Autisme&nbsp;: des prot\u00e9ines neuronales incrimin\u00e9es observ\u00e9es en 3D&nbsp;\u00bb, BE France 203 &#8211; Veille technologique internationale, ADIT &#8211; Minist\u00e8re des Affaires Etrang\u00e8res et Europ\u00e9ennes [Jan 2008] <a href=\"http:\/\/www.bulletins-electroniques.com\/actualites\/52477.htm\">http:\/\/www.bulletins-electroniques&#8230;.<\/a><\/p>\n\n\n\n<p>\u201cLive from the Labs &#8211; 3D Observation of Neuroligins Involved in Autism\u201d, BE France 203 &#8211; Veille technologique internationale, ADIT &#8211; Minist\u00e8re des Affaires Etrang\u00e8res et Europ\u00e9ennes [Jan 2008] <a href=\"http:\/\/www.bulletins-electroniques.com\/actualites\/52585.htm\">http:\/\/www.bulletins-electroniques&#8230;.<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Des prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme observ\u00e9es en trois dimensions&nbsp;\u00bb, Centre de Ressources Autisme Rh\u00f4ne-Alpes, Revue de presse n\u00b022&nbsp;: 16\/12\/07 &#8211; 31\/12\/07 [Jan 2008] <a href=\"http:\/\/www.cra-rhone-alpes.org\/spip.php?article237\">http:\/\/www.cra-rhone-alpes.org\/spip&#8230;<\/a><\/p>\n\n\n\n<p>F1000Prime &#8211; Article Recommendations [Feb 2008] [<a href=\"http:\/\/f1000.com\/prime\/1100169\">http:\/\/f1000.com\/prime\/1100169<\/a>]<\/p>\n\n\n\n<p>\u00ab&nbsp;Analyse en 3D de prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme&nbsp;\u00bb, La Lettre de l\u2019Universit\u00e9 de la M\u00e9diterran\u00e9e, n\u00b0125 F\u00e9vrier 2008 p.25 <a href=\"http:\/\/www.univmed.fr\/communication\/default.aspx?id=7814\">http:\/\/www.univmed.fr\/communication&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Observation en 3D de prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme&nbsp;\u00bb, Paris Presse Actualit\u00e9 [Feb 2008] <a href=\"http:\/\/www.parispresse.eu\/__n87678__actualite-observation_en_3d_de_proteines_neuronales_incriminees_dans_lautisme.html?PHPSESSID=797011e0cced52e05b2287785b29cffa\">http:\/\/www.parispresse.eu\/__n87678_&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Observation en 3D de prot\u00e9ines neuronales incrimin\u00e9es dans l\u2019autisme&nbsp;\u00bb, Journal du CNRS, n\u00b0218 Mars 2008<\/p>\n\n\n\n<p>\u00ab&nbsp;Des prot\u00e9ines incrimin\u00e9es dans l\u2019autisme vues en 3D&nbsp;\u00bb, Neurosciences &#8211; D\u00e9couvertes en rafale sur le cerveau [Mar 2008] <a href=\"http:\/\/www2.cnrs.fr\/presse\/journal\/3787.htm\">http:\/\/www2.cnrs.fr\/presse\/journal\/&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Pierres fondamentales&nbsp;\u00bb, Revue de l\u2019UNAPEI, Septembre 2008<\/p>\n\n\n\n<p><strong>For \u201cBourne et al., PNAS 2010\u201d&nbsp;:<\/strong><\/p>\n\n\n\n<p>\u00ab&nbsp;Comment agissent certaines toxines accumul\u00e9es dans les fruits de mer&nbsp;\u00bb [Mar 2010] Communiqu\u00e9 de presse du CNRS <a href=\"http:\/\/www2.cnrs.fr\/presse\/communique\/1823.htm\">http:\/\/www2.cnrs.fr\/presse\/communiq&#8230;<\/a><\/p>\n\n\n\n<p>\u00ab&nbsp;Comment agissent certaines toxines accumul\u00e9es dans les fruits de mer&nbsp;\u00bb [Mar 2010] Communiqu\u00e9 de presse du CEA \u2013 Sciences du vivant <a href=\"http:\/\/www-dsv.cea.fr\/la-dsv\/toute-l-actualite\/en-direct-des-labos\/comment-agissent-certaines-toxines-accumulees-dans-les-fruits-de-mer\">http:\/\/www-dsv.cea.fr\/la-dsv\/toute-&#8230;<\/a>]<\/p>\n\n\n\n<p>\u201dThe mode of action of certain toxins that accumulate in seafood\u201d [Mar 2010] Communiqu\u00e9 de presse du CNRS page internationale <a href=\"http:\/\/www2.cnrs.fr\/en\/1709.htm\">http:\/\/www2.cnrs.fr\/en\/1709.htm<\/a><\/p>\n\n\n\n<p>&#8220;Comment des coquillages deviennent toxiques&#8221; [Mar 2010] Ma Plan\u00e8te [<a href=\"http:\/\/ma-planete.com\/blog\/view\/id_6422\/title_Comment-des-coquillages-deviennent-toxiques\/\">http:\/\/ma-planete.com\/blog\/view\/id_&#8230;<\/a>]<\/p>\n\n\n\n<p>\u00ab&nbsp;Deux toxines des poissons et fruits de mer perc\u00e9es \u00e0 jour&nbsp;\u00bb [Mar 2010] RTL Info [ <a href=\"https:\/\/www.rtl.be\/art\/info\/magazine\/science-nature\/deux-toxines-des-poissons-et-fruits-de-mer-percees-a-jour-156483.aspx\">https:\/\/www.rtl.be\/art\/info\/magazine\/science-nature\/deux-toxines-des-poissons-et-fruits-de-mer-percees-a-jour-156483.aspx<\/a> ]<\/p>\n\n\n\n<p>\u00ab&nbsp;Certains fruits de mer contiennent des toxines provoquant des dysfonctionnements c\u00e9r\u00e9braux&nbsp;\u00bb [Mar 2010] Communiqu\u00e9 de presse dans La D\u00e9p\u00eache, relay\u00e9 par Le Quotidien du M\u00e9decin [ <a href=\"https:\/\/www.ladepeche.fr\/article\/2010\/03\/10\/793935-certains-fruits-mer-contiennent-toxines-provoquant-dysfonctionnements-cerebraux.html\">https:\/\/www.ladepeche.fr\/article\/2010\/03\/10\/793935-certains-fruits-mer-contiennent-toxines-provoquant-dysfonctionnements-cerebraux.html<\/a> ]<\/p>\n\n\n\n<p><strong>For &#8220;Bourne et al., Structure 2015\u201d&nbsp;:<\/strong><\/p>\n\n\n\n<p>Preview &#8220;From Shellfish Poisoning to Neuroscience&#8221; by Shahsavar A and Balle T, Structure 23, 979-980 [<a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0969212615001860\">https:\/\/www.sciencedirect.com\/scien&#8230;<\/a>].<\/p>\n\n\n\n<p>La lettre IBITECS &#8211; June 2015: Synth\u00e8se et caract\u00e9risation fonctionnelle de phycotoxines marines \u00e9mergentes [<a href=\"https:\/\/joliot.cea.fr\/drf\/joliot\/Pages\/ARCHIVES\/IBITECS\/Actualites\/La%20lettre\/lettre.aspx?Type=Chapitre&amp;numero=8\">https:\/\/joliot.cea.fr\/drf\/joliot\/Pages\/ARCHIVES\/IBITECS\/Actualites\/La%20lettre\/lettre.aspx?Type=Chapitre&amp;numero=8<\/a>]<\/p>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"popular-scientific-information\">Popular scientific information<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<p>Eurom\u00e9decine 1987, Montpellier: animation of a booth, and design and distribution of flyer &#8220;L\u2019information et la vie &#8211; Identification et purification d\u2019une toxine de venin animal&#8221;<em>.<\/em><\/p>\n\n\n\n<figure class=\"wp-block-image size-full is-resized\"><img loading=\"lazy\" decoding=\"async\" width=\"500\" height=\"354\" src=\"https:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2023\/05\/EuroMedecine-1987-500x354-1.jpg\" alt=\"\" class=\"wp-image-7723\" style=\"width:552px;height:auto\"\/><\/figure>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"links-of-interest\">Links of interest<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<ul class=\"wp-block-list\">\n<li>ESTHER database: <a href=\"https:\/\/bioweb.supagro.inrae.fr\/ESTHER\/\">https:\/\/bioweb.supagro.inrae.fr\/ESTHER\/<\/a><\/li>\n\n\n\n<li>French Society on Toxinology: <a href=\"http:\/\/sfet.asso.fr\/international\/\">http:\/\/sfet.asso.fr\/international\/<\/a><\/li>\n\n\n\n<li>International Society on Toxinology&nbsp;: <a href=\"http:\/\/www.toxinology.org\/\">http:\/\/www.toxinology.org\/<\/a><\/li>\n\n\n\n<li>Society for Neurosciences&nbsp;: <a href=\"http:\/\/www.sfn.org\/\">http:\/\/www.sfn.org\/<\/a><\/li>\n\n\n\n<li>Soci\u00e9t\u00e9 des Neurosciences: <a href=\"https:\/\/www.neurosciences.asso.fr\/en\/\">https:\/\/www.neurosciences.asso.fr\/en\/<\/a><\/li>\n\n\n\n<li>International Society for Neurochemistry: <a href=\"https:\/\/www.neurochemistry.org\/\">https:\/\/www.neurochemistry.org\/<\/a><\/li>\n\n\n\n<li>XVth ISCM, Marseille, oct 2016: <a href=\"http:\/\/iscm.sciencesconf.org\/?lang=en\">http:\/\/iscm.sciencesconf.org\/?lang=en<\/a><\/li>\n\n\n\n<li>COST Action CA19144 European Venom Network (EUVEN): <a href=\"https:\/\/www.cost.eu\/actions\/CA19144\/\">https:\/\/www.cost.eu\/actions\/CA19144\/<\/a> and <a href=\"https:\/\/euven-network.eu\/\">https:\/\/euven-network.eu\/<\/a><\/li>\n\n\n\n<li>RCSB PDB-101 Molecule of the Month: Acetylcholinesterase: <a href=\"https:\/\/pdb101.rcsb.org\/motm\/54\">https:\/\/pdb101.rcsb.org\/motm\/54<\/a><\/li>\n\n\n\n<li>RCSB PDB-101 Molecule of the Month: Acetylcholine Receptor: <a href=\"https:\/\/pdb101.rcsb.org\/motm\/71\">https:\/\/pdb101.rcsb.org\/motm\/71<\/a><\/li>\n\n\n\n<li>RCSB PDB-101 Molecule of the Month: Click Chemistry: <a href=\"https:\/\/pdb101.rcsb.org\/motm\/276\">https:\/\/pdb101.rcsb.org\/motm\/276<\/a><\/li>\n\n\n\n<li>RCSB PDB-101 Molecular Landscapes: Excitatory and Inhibitory Synapses: <a href=\"https:\/\/pdb101.rcsb.org\/sci-art\/goodsell-gallery\/excitatory-and-inhibitory-synapses\">https:\/\/pdb101.rcsb.org\/sci-art\/goodsell-gallery\/excitatory-and-inhibitory-synapses<\/a><\/li>\n\n\n\n<li>Acetylcholinesterase inhibition by fasciculin: <a href=\"https:\/\/www.youtube.com\/watch?v=zLuObW3huks\">https:\/\/www.youtube.com\/watch?v=zLuObW3huks<\/a><\/li>\n\n\n\n<li>Stucture of acetylcholinesterases, by Zoran Radic:<a href=\"https:\/\/www.youtube.com\/watch?v=sKCDx_2s66w&amp;t=467s\"> https:\/\/www.youtube.com\/watch?v=sKCDx_2s66w<\/a><\/li>\n\n\n\n<li>Acetylcholinesterase: A gorge-ous enzyme: <a href=\"https:\/\/www.youtube.com\/watch?v=ZrJVVP8Nxtk\">https:\/\/www.youtube.com\/watch?v=ZrJVVP8Nxtk<\/a><\/li>\n\n\n\n<li>Electric Eel, by Irwin Moon: <a href=\"https:\/\/archive.org\/details\/electric_eel\/electric_eel.mpeg\">https:\/\/archive.org\/details\/electric_eel\/electric_eel.mpeg<\/a><\/li>\n\n\n\n<li>Les substances actives sur le r\u00e9cepteur nicotinique \u00e0 l&#8217;ac\u00e9tylcholine &#8211; Un exemple d&#8217;enjeu de pr\u00e9servation de la biodiversit\u00e9: <a href=\"https:\/\/www.pedagogie.ac-nice.fr\/svt\/productions\/html\/recepteur-nicotinique-biodiversite\/recepteur_nicotinique_biodiversite\/index.html\">https:\/\/www.pedagogie.ac-nice.fr\/svt\/productions\/html\/recepteur-nicotinique-biodiversite\/recepteur_nicotinique_biodiversite\/index.html<\/a><\/li>\n\n\n\n<li>Naturally Obsessed: The Making of a Scientist: <a href=\"https:\/\/web.archive.org\/web\/20180304013635\/http:\/\/www.thirteen.org:80\/naturally-obsessed\/wp-content\/blogs.dir\/30\/files\/2013\/01\/Naturally_Obsessed_The_Making_of_a_Scientist.mp4\">https:\/\/drive.google.com\/file\/d\/1uOO9gClGwPYY206N7Y-MCBfYWyP0L3x1\/view?usp=sharing<\/a><\/li>\n\n\n\n<li>On Being a Scientist: <a href=\"https:\/\/www.youtube.com\/watch?v=tCgZSjoxF7c\">https:\/\/www.youtube.com\/watch?v=tCgZSjoxF7<\/a><\/li>\n\n\n\n<li>Nobel Prize lecture: Barry Sharpless, Chemistry 2022: <a href=\"https:\/\/youtu.be\/55trnYorBhQ\">https:\/\/youtu.be\/55trnYorBhQ<\/a><\/li>\n\n\n\n<li>Palmer Taylor Research Symposiums at SSPPS, 2016 and 2025: <a href=\"https:\/\/pharmacy.ucsd.edu\/researchsymposiumhome\">https:\/\/pharmacy.ucsd.edu\/researchsymposiumhome<\/a><\/li>\n\n\n\n<li>Videos of the 2025 Symposium presentations: <a href=\"https:\/\/pharmacy.ucsd.edu\/researchsymposium\/symposium-lecture-videos\">https:\/\/pharmacy.ucsd.edu\/researchsymposium\/symposium-lecture-videos<\/a><\/li>\n\n\n\n<li>Top of the Prots: <a href=\"https:\/\/topoftheprots.com\/\">https:\/\/topoftheprots.com\/<\/a><\/li>\n<\/ul>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-group accordeon\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<h4 class=\"wp-block-heading accordeonTitle\" id=\"cover-pictures\">Cover pictures<\/h4>\n\n\n\n<div class=\"wp-block-group accordeonContent\"><div class=\"wp-block-group__inner-container is-layout-flow wp-block-group-is-layout-flow\">\n<div class=\"wp-block-media-text alignwide is-stacked-on-mobile\" style=\"grid-template-columns:28% auto\"><figure class=\"wp-block-media-text__media\"><img loading=\"lazy\" decoding=\"async\" width=\"164\" height=\"245\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/10\/Structure-and-Function-of-Cholinesterases-and-Related-Proteins.jpg\" alt=\"\" class=\"wp-image-1614 size-full\"\/><\/figure><div class=\"wp-block-media-text__content\">\n<p>Book <em>Structure and Function of Cholinesterases and Related Proteins <\/em>(Doctor BP, Taylor P, Quinn DM, Rotundo RL, &amp; Gentry MK, eds) Plenum Publishing Corp, NY, <strong>1998<\/strong> (630 pages) (ISBN&nbsp;: 0-306-46050-5).<\/p>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-media-text alignwide is-stacked-on-mobile\" style=\"grid-template-columns:28% auto\"><figure class=\"wp-block-media-text__media\"><img loading=\"lazy\" decoding=\"async\" width=\"181\" height=\"257\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/10\/Toxines-et-fonctions-cholinergiques-neuronales-et-non-neuronales.png\" alt=\"\" class=\"wp-image-1618 size-full\"\/><\/figure><div class=\"wp-block-media-text__content\">\n<p>E-book <em><em><em>Toxines et fonctions cholinergiques neuronales et non neuronales<\/em> (Benoit E, Goudey-Perri\u00e8re F, Marchot P, Servent D, eds) Coll. <em>Rencontres en Toxinologie<\/em>, Publications de la SFET, Ch\u00e2tenay-Malabry, <strong>2008<\/strong> (160 pages) (ISSN&nbsp;: 1760-6004).<\/em><\/em><\/p>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-media-text alignwide is-stacked-on-mobile\" style=\"grid-template-columns:28% auto\"><figure class=\"wp-block-media-text__media\"><img loading=\"lazy\" decoding=\"async\" width=\"184\" height=\"245\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/10\/jacs-8ba1b.jpg\" alt=\"\" class=\"wp-image-1620 size-full\"\/><\/figure><div class=\"wp-block-media-text__content\">\n<p><em><em><em>Journal <em>J. Am. Chem. Soc.<\/em> Vol. 132, Iss. 51, December 29, <strong>2010<\/strong><\/em><\/em><\/em><\/p>\n<\/div><\/div>\n\n\n\n<div class=\"wp-block-media-text alignwide is-stacked-on-mobile\" style=\"grid-template-columns:28% auto\"><figure class=\"wp-block-media-text__media\"><img loading=\"lazy\" decoding=\"async\" width=\"181\" height=\"240\" src=\"http:\/\/www.afmb.univ-mrs.fr\/wp-content\/uploads\/2021\/10\/Cholinergic-Mechanisms.png\" alt=\"\" class=\"wp-image-1622 size-full\"\/><\/figure><div class=\"wp-block-media-text__content\">\n<p><em><em><em><em>Special Issue on <em>Cholinergic Mechanisms<\/em> (Silman I, Guest Ed&nbsp;; Marchot P, Prado MAM, Assoc Guest Eds), <em>J. Neurochem.<\/em> Wiley <strong>2017<\/strong> vol 142 &#8211; Suppl 2, pp 1-226 (ISSN&nbsp;: 1471-4159).<\/em><\/em><\/em><\/em><\/p>\n<\/div><\/div>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n","protected":false},"excerpt":{"rendered":"<p>Senior researcher<\/p>\n","protected":false},"author":1,"featured_media":10514,"template":"","class_list":["post-904","member","type-member","status-publish","has-post-thumbnail","hentry","entry"],"_links":{"self":[{"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/member\/904","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/member"}],"about":[{"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/types\/member"}],"author":[{"embeddable":true,"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/users\/1"}],"version-history":[{"count":263,"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/member\/904\/revisions"}],"predecessor-version":[{"id":12034,"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/member\/904\/revisions\/12034"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/media\/10514"}],"wp:attachment":[{"href":"https:\/\/www.afmb.univ-mrs.fr\/en\/wp-json\/wp\/v2\/media?parent=904"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}