Pascale Marchot

• 2014 – current: co-PI (with Yves Bourne) of team “Structural Neurobiology and Glycobiology”, AFMB lab, Marseille
• 2013 – 2016: French coordinator of the International Associated Laboratory “SGIDSTS” (CNRS/AMU/UCSD) (US coordinator: Palmer Taylor)
• 2012 – 2013: PI of theme “Structural Neurobiology”, team “Structural Neurobiology and Glycobiology”, lab “Architecture et Fonction des Macromolécules Biologiques” (AFMB), Marseille
• 2008 – 2011: PI of team “Toxines Animales et Cibles Macromoleculaires” (ToxCiM), lab CRN2M, Marseille
• 2000 – 2007: PI of team “Réactivité et Structure de Macromolécules Biologiques”, lab “Ingénierie des Protéines”/”BIMC”, Marseille

• 2012 – current: Permanent CNRS Researcher, lab “Architecture et Fonction des Macromolécules Biologiques” (AFMB), Marseille
• 1996 – 2011: Permanent CNRS Researcher, labs “Ingénierie des Protéines”, then “Biologie des Interactions Moléculaires et Cellulaires” (BIMC), then “Centre de Recherches en Neurobiologie et Neurophysiologie de Marseille” (CRN2M), Marseille (same lab, different names).
• 1994 – 1995: Permanent CNRS Researcher, sabbatical 2 yrs at the Dept Pharmacology, UCSD, La Jolla CA (USA)
• 1989 – 1993: Permanent CNRS Researcher, lab “Biochimie – Ingénierie des Protéines”, Marseille
• 1988, October 15: recruted by the CNRS
• 1987 – 1988: Post-doc, lab “Biochimie – Ingénierie des Protéines”, Marseille
• 1983 – 1986: DEA + PhD thesis Sp. Neurosciences Moléculaires, lab “Biochimie”, Marseille

• 1999 – Habilitation à Diriger les Recherches (HDR), sp. Neuroscience, Univ. Méditerranée, Marseille “Fasciculines et acétylcholinestérase, une histoire d’atomes crochus”. Jury: Cassian Bon, Jacques Grassi, André Nieoullon, Hervé Rochat, Herman van Tilbeurgh, Robert Verger.
• 1986 – Thèse Univ. Aix-Marseille II, sp. Neurosciences, Marseille “Contribution à l’étude de la purification et du mode d’action des toxines des venins de serpents Elapidae”. Thesis director: Hervé Rochat; supervisor: Pierre E. Bougis. Jury: Pierre Fromageot, François Miranda, Hervé Rochat, Rolland Rosset.
• 1983 – Diplôme d’Etudes Approfondies (DEA, now Master-2), sp. Biologie Cellulaire et Moléculaire, Univ. Aix-Marseille II “Chromatographie d’immunoaffinité anti-phospholipase A2 et iodation d’une cardiotoxine du venin de Naja mossambica mossambica“. Director: Hervé Rochat; supervisor: Pierre E. Bougis.

• 2017 : Nomination to the Club-M-Ambassadeurs de la Ville de Marseille
• 2017: Trophy of Attractivness – Congress by the Ville de Marseille, for having organized the XVth International Symposium on Cholinergic Mechanisms (XVth ISCM) in 2016
• 2016 : B.P. Doctor Memorial Young Investigator Travel Award, honoris causa
• 2013-2016 : Prime d’Excellence Scientifique (PES) by the CNRS

• BSI-2023 (2023, Marseille, France), Organizing Committee
• Supervisor MSCA Postdoctoral Fellowship and advisor CIVIS 3i for the AFMB lab, since 2021
• Participant to the European Venom Network (EUVEN) Working Groups WG1 “Novel targets in venom research” and WG4 “Web ressources”, since 2021
• J. Biol. Chem., editorial board member, 2016-2021
• GTBio 2014, scientific committee, solicited member
• XIV-th ISCM (2013, China), 12-th ChE (2015, Spain), XV-th ISCM (2016, France): Organizing Committees & International Advisory Boards, elected member
• Société Française pour l’Etude des Toxines (SFET), Scientific, Administrative, Meeting organization & Edition Committees, elected member, 2007 – current
• Vaincre la Mucoviscidose (VLM, ex- AFLM), Scientific Committee, elected member, 2002 – 2008

• American Society for Biochemistry and Molecular Biology (ASBMB) (Adhering Body of the International Union of Biochemistry and Molecular Biology (IUBMB)): 2012 – 2021
• International Society for Neurochemistry (ISN): 2015 – 2018
• International Society on Toxinology (IST): 2007 – 2020
• Society for Neuroscience (SfN): 2013 – 2018
• National Geographic Society USA: 1994 – 2008
• Association de Cristallographie d’Aix-Marseille (ACAM): 2013 – 2023
• Association Française de Cristallographie (AFC): 2012 – 2023
• Association pour l’Etude des Cholinestérases: since 1996 (but no longer active)
• Association pour la Recherche sur la Sclérose Latérale Amyotrophique & autres maladies du motoneurone (ARSla): 2007 – 2018
• Association pour les Femmes en Science et en Ingénierie (AFSI): since 2015 (but no longer active)
• Club -M- Ambassadeurs de la Ville de Marseille: 2017 – 2020
• Société des Neurosciences (SN) (Adhering Body of the International Brain Research Organization (IBRO) and the Federation of European Neuroscience Societies (FENS)): 2011 – 2022
• Société Française d’Endocrinologie (SFE): 2018
• Société Française de Biophysique (SFB): 2016, 2018
• Société Française pour l’Etude des Toxines (SFET): 1999 – today

• AgroM Différenciation Cellulaire et Croissance (INRA) et Unité Informatique de Centre INRA, Montpellier, France
• Laboratoire de Neurobiologie Cellulaire et Moléculaire, CNRS, Institut Fédératif de Neurobiologie Alfred Fessard, Gif-sur-Yvette, France
• Laboratoire de Toxinologie Moléculaire, Service d’Ingénierie Moléculaire des Protéines, Institut de biologie & de technologies de Saclay, CEA, Gif-sur-Yvette, France
• Institut Interdisciplinaire de Neuroscience (IIN), CNRS/Univ Bordeaux2, Centre de Génomique Fonctionnelle, Bordeaux, France
• Société BioXtal, campus Luminy, Marseille, France
• Lab Synapse Biology, VIB Center for the Biology of Disease, KU Leuven, Center for Human Genetics, Leuven, Belgium
• Skaggs School of Pharmacy and Pharmaceutical Sciences (SSPPS), Dept of Pharmacology, University of California at San Diego (UCSD), La Jolla, CA, USA
• Dept of Neuroscience and Cell Biology, UMDNJ-Robert Wood Johnson Medical School, Child Health Institute of New Jersey, New Brunswick, NJ, USA
• Dept of Chemistry and Biochemistry, University of California at Santa Barbara (UCSB), Santa Barbara, CA, USA
• Institut NeuroMyoGene, Univ Claude Bernard Lyon 1/CNRS/INSERM, Villeurbanne
• Unité de Neurobiologie des canaux Ioniques et de la Synapse (UNIS), INSERM, Marseille
• Institut du Dévelopement de Marseille (IBDM), CNRS/AMU, Marseille
• Institut de Pharmacologie Moléculaire et Cellulaire (IPMC), CNRS/Université Côte d’Azur, Sophia-Antipolis

• 1982 (1 mth, Sept) : Temporary CNRS contract.
• 1982-1983 (1 yr) : Study scholarship for a “Diplôme d’Etudes Approfondies (DEA, now Master-2)”.
• 1983-1986 (3 yrs) : Research scholarship from the “Ministère de la Recherche et de la Technologie (MRT)” to develop a Ph.D. Thesis.
• 1984 : “Information Scientifique et Technique” allowance (BIST) from the “Ministère de la Recherche et de la Technologie (MRT) – Mission Interministérielle de l’Information Scientifique et Technologique (MIDIST)”.
• 1987 (1 yr) : Bridging scholarship from the Fondation pour la Recherche Médicale (FRM).
• 1988 (5 mths) : Vacations on a contract with the “Direction des Recherches et Etudes Techniques (DRET) – Délégation Générale pour l’Armement (DGA)”.
• 1994 (9 mths): CNAM – NATO, Complementary grant for studying abroad.
• 1995 (10 mths) : “Visiting Scholar” salary, Dept. Pharmacology, UCSD, la Jolla, CA.
• 1997-1999 (3 yrs): ACI CNRS-NSF, P Marchot & P Taylor (UCSD, La Jolla, CA) coordinators.
• 1997-1999 (3 yrs): AFM, P Marchot & PE Bougis (CNRS Marseille) coordinators.
• 2000-2002 (3 yrs): PAI France-Germany PROCOPE, P Marchot & O Pongs (ZMNH, Hambourg) coordinators.
• 2001-2002 (2 yrs): AFM, P Marchot coordinator.
• 2003-2004 (2 yrs): Programme Bioinformatique inter EPST, P Marchot & A Chatonnet (INRA Montpellier) coordinators.
• 2003-2004 (2 yrs): AFM, P Marchot coordinator.
• 2005-2007 (3 yrs): Action CNRS/USA, P Marchot & P Taylor (UCSD, La Jolla, CA) coordinators.
• 2005 (1 yr): AFM, P Marchot coordinator.
• 2006-2008 (3 yrs): GIP-ANR Santé-environnement – Santé-travail, partner.
• 2006-2009 (48 mths): Project Intégré Structural Proteomics in Europe SPINE2-COMPLEXES & TEACH-SG, Work Package WP1.3.1, partner 14; Y Bourne (CNRS Marseille) coordinator, P Marchot deputy.
• 2009 (1 yr): PEPS INSB-CNRS, MF Martin-Eauclaire (CNRS Marseille) coordinator; P Marchot, PE Bougis, B Céard participants.
• 2010-2012 (3 yrs): PICS CNRS, P Marchot & Y Bourne coordinators; P Taylor (UCSD, La Jolla, CA) partner.
• 2011-2014 (45 mths): ANR-Blanc SVSE 2 – Progr Biologie cellulaire & développement, coordinator.
• 2013-2016 (4 yrs): CNRS INSB, LIA France-USA SGIDSTS, P Marchot & P Taylor (UCSD, La Jolla, CA) coordinators.
• 2014-2017 (3.5 yrs): ANR-Blanc SVSE 4 – Progr Neurosciences, partner.
• 2015-2019 (4 yrs): ANR – Progr Exploration du système nerveux dans son fonctionnement normal et pathologique (DS0407), partner.
• 2017-2022 (5 yrs): ANR – Progr Vie, santé et bien-être (DS04), partner.
• 2024-2026 (3 yrs): ANR – Generic call, CE11, coordinator.

The agreement for the creation of an International Associated Laboratory (LIA – Laboratoire International Associé) between the laboratory Architecture et Fonction des Macromolécules 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 Université (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 http://fr.calameo.com/read/00248816… page 7; 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.cnrs.fr/CNRS-Hebdo/provence-corse/Lettre/343/Lettre.aspx ; https://www.univ-amu.fr/system/files/2019-02/DIRCOM-lettre_amu_n17_janv2014.pdf pages 17-18; https://www.france-science.com/IMG/pdf/rapport_activite_mst_2013.compressed.pdf pages 80-81.)

• Joan R. Kanter, staff research associate UCSD, 1994-1995 (now a Faculty Admin Assistant in Roger Tsien Lab, UCSD)
• Marianick Juin, technician CNRS (permanent position), 2000-2005 (now working at the Institut Méditerranéen de Biodiversité et d’Ecologie Marine et Continentale – IMBE- campus Arbois, Aix-en-Provence)
• Sandrine Conrod, technician CNRS (permanent position), 2005-2011 (afterward: technician at the Institut de Neurophysiopathologie de Marseille; now working at the Centre Européen de Recherche et d’Enseignement en Géosciences de l’Environnement – CEREGE – in Aix-en-Provence)
• Claire Debarnot, study engineer AMU (permanent position), 2010-2011 (now a member of the AFMB lab and our team, since Jan 2017)
• Audrey Blanchard, study engineer, 2011-2014 (now working at Innate Pharma, Marseille)
• Supanee (“Ann”) Potisopon, research engineer/postdoc, Oct-Dec 2014 (afterward: a postdoc at Harvard Medical School, Boston, MA; now working for BIOASTER, Lyon, FR)
• Aurélien Assice-Vivoni, study engineer, Sept 2015 (now an alternating project manager for quality/hygiene/security/environment at EDF)
• Julie Baptiste, study engineer, Nov 2015 – Sept 2016 (afterward: engineer at the Institute of Human Genetics, Montpellier; now engineer at Sys2Diag, Montpellier)
• Maria Mate, research engineer CNRS (permanent position), Oct 2013 – May 2017 (now working with another team of the AFMB lab)
• Marie-Julie Dejardin, study engineer, Oct 2016 – Jun 2017 (now working at the NeuroMyoGene Institute (INMG) Lyon)
• Jean-Baptiste Boitel, study engineer, Feb 2018 – Nov 2019 (afterward: engineer at the Adhesion & Inflammation Lab, Campus Luminy, Marseille, in collaboration with another team of the AFMB lab ; now Cadre de laboratoire Sanofi Montpellier)
• Marine Papin, study engineer, Sept 2020 – Feb 2021 (now a PhD student in Dijon)

Trainees

• Rozenn Guegan, Maitrise Biologie Cellulaire et Physiologie, Univ Rennes, Apr-Jun 1998, then DEA Neurosciences, Univ Méditerranée, Sept-Nov 1998 (abandoned)
• Céline Hamel, BTS Ecole Nationale de Chimie Physique et Biologie, Paris, May-Jul 1999 & March 2000
• Romain Morichon, Licence Biochimie, Univ Franche-Comté, UFR Sciences et Techniques, Besançon, Jun-Aug 2000
• Ludovic Renault, Magistère Univ Rouen (3rd yr) & DEA Biochimie Biologie Structurale et Génomique, Univ Aix-Marseille, Sept 2001- Jun 2002
• Raja Noufir (now Bonifay), BTS Lycée Pro Marie Curie, Marseille, May-June 2003 & Nov-Dec 2003 (2 x 8 wks)
• Virginie Fabre, 4th yr INSA Lyon, Dept Biosciences, Jun-Jul 2004 (8 wks)
• Audrey Luzergues, 2nd yr ESIL, Dept Génie Biologique et Microbiologie Appliquée, Marseille, Feb-Apr 2005 (8 wks)
• Marion Traverse, 2nd yr ESIL, Dept Génie Biologique et Microbiologie Appliquée, Marseille, Mar-Apr 2006 (8 wks)
• Carole Rosenberger, Master-1 Nutrition – Sécurité Alimentaire, option Biochimie, Univ Méditerranée, Marseille, Apr-Jun 2006 (8 wks)
• Delphine Chaduli, BTS Lycée Pro Marie Curie, Marseille, May-Jun 2006 & Oct-Dec 2006 (2 x 8 wks)
• Grégoire Mondielli, Master-2 Neurosciences, Univ Méditerranée, Jan-Jun 2007
• David Menahem, 2nd yr ESIL, Dept Biotechnologie, Marseille, Feb-Apr 2010 (8 wks)
• Pauline Dressayre, 2nd yr ESIL, Dept Biotechnologie, Marseille, Feb-Apr 2011 (8 wks) (co-mentor G Mondielli)
• Julie Prats, 2nd yr ESIL, Dept Biotechnologie, Marseille, Feb-Apr 2012 (8 wks) (co-mentor A Blanchard)
• Camille Ribeyre, Master-1 Biochimie Biologie Structurale et Génomique (BBSG), Aix-Marseille Univ, Apr-May 2013 (8 wks) (co-mentor A Blanchard)
• Florian Mourey, 2nd yr AgroParisTech, Institut des sciences et industries du vivant et de l’environnement, Centre de Paris, Jun-Jul 2014 (8 wks) (co-mentor A Goulet)
• Farida Nezlioui, Master-2 Biochimie Biologie Structurale et Génomique (BBSG), Aix-Marseille Univ, Jan-Jun 2016 (co-mentor A Goulet)
• Yoann Crétinon, Master-1 Biochimie Biologie Structurale et Génomique (BBSG), Aix-Marseille Univ, Mar-Apr 2017 (7 wks) (co-mentors A Goulet, S Platsaki)
• Melvin Boumedour, BTS Lycée La Forbine, Marseille, May-Jul (6 wks) & Nov-Dec 2017 (8 wks) (main mentor S Platsaki)
• Sarah Coulibaly Martineau, Master-2 Biologie Structurale, Génomique (BSG), Aix-Marseille Univ, Jan-Jun 2019 (6 mths) (co-mentor C Debarnot)
• Djouhaina Benmehidi, 2nd yr Sup’Biotech Paris, June-July 2019 (8 wks) (main mentor S Platsaki)
• Nafisatou Drame, Master-2 Biologie Structurale, Génomique (BSG), Aix-Marseille Univ, Jan-Jun 2021 (6 mths) (co-mentor C Debarnot)
• Cynthia Lohberger, Master-1 Biologie Structurale, Génomique (BSG), Aix-Marseille Univ, Apr-May 2021 (7 wks) (co-mentor C Debarnot)
• Cynthia Lohberger, Master-2 Biologie Structurale, Génomique (BSG), Aix-Marseille Univ, Jan-Jun 2022 (6 mths) (co-mentor C Debarnot)

PhD students

• Fatima Laraba-Djebari, Thesis Univ Aix-Marseille II, sp. Cell biology and microbiology, 1993-1995, co-mentoring (thesis mentor: Marie-France Martin-Eauclaire).
  • Now: Dean of the Faculty of Biological Sciences, University of Sciences and Technology Houari Boumédiène (FSB-USTHB), Algiers, Algeria.
• Ludovic Renault, Thesis Univ Méditerranée, sp Neurosciences, Sept 2002 – Dec 2005.
  • Funding: Association France Alzheimer ; Association Française contre les Myopathies ; Programme Bioinformatique inter-EPST.
  • Then: Postdoc Stahlberg Lab, Molecular & 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 – 2015.
  • Then: Research Scientist & Facility Manager, NeCEN, Leiden University, NL, 2016.
  • Now: Research Scientist & Head of NeCEN Facility, Leiden University, NL, since 2018.
• Grégoire Mondielli, Thesis Univ Méditerranée, sp. Neurosciences, Sept 2007 – Dec 2011.
  • Funding: Association Française contre les Myopathies ; CNRS ; Fondation pour la Recherche Médicale.
  • Then: Research engineer, CRN2M Marseille, team Gliotransmission & synaptopathies, 2013 – 2016 / team SIGnalling in NeuroEndocrine Tumors (SIG-NET), 2016 – 2018.
  • Now: Research engineer, Institute of NeuroPhysiopathology, Marseille Medical Genetics, team DIP-NET, since 2018 (see https://fr.linkedin.com/in/gregoire…)
• Lamia Mebarki, Thesis Aix-Marseille Univ, sp Structural Biology & Biochemistry, Nov 2013 – Oct 2017.
  • Funding: BioXtal Nov 2013 – Mar 2014; CIFRE-ANRT BioXtal-AFMB Apr 2014 – Mar 2017; Theranyx Apr – June 2017; AFMB Jul – Dec 2017.
  • Then: R&D engineer, Promise Advanced Proteomics, Grenoble, Jan-May 2019.
  • Now: Project Manager, Covalab, Lyon, May 2019 – ongoing

Postdocs

• Igor Fabrichny, after a PhD Univ Lomonosov Moscow RU (1995-1999) then a 1rst postdoc at the Institute of Biotechnology, Univ Helsinki FI (2000-2005).
  • Funding: CNRS « Proposition d’accueil pour un post-doctorant au CNRS » (Oct 2005 – Sept 2006); Fondation pour la Recherche Médicale « Accueil de post-doctorant étranger » (Oct 2006 – Sept 2008).
  • Now: Product Manager, International Biotechnology Center GENERIUM, Volginskiy, RU (2011-ongoing).
• Adeline Goulet, after (i) a PhD Univ Aix-Marseille (AFMB lab, 2006-2009), (ii) a 1rst postdoc at the CBS Montpellier (2009-2010), & (iii) a 2nd postdoc at Birkbeck College, London, UK (2010-2013).
  • 3rd postdoc in our team, funding: Fondation pour la Recherche Médicale (Sept 2013 – Sept 2015).
  • Then: CNRS Researcher (CR2) in our team (Oct 2015 – Sept 2017).
  • Then: CNRS Researcher (CR2) in AFMB team Host-pathogen interactions (Sept 2017 – Dec 2021).
  • Now: CNRS Researcher (CR2) in LISM team Host-pathogen interactions (Jan 2022 – ).
• Semeli Platsaki, 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.
  • 2nd postdoc in our team, funding ANR June 2016 – Sept 2019 along with PRESTIGE (Marie Skłodowska-Curie actions, Campus France) Sept 2017 – Sept 2018.
  • 3rd postdoc in team Genetics and Neurobiology of C. elegans, INMG, Lyon, with assignement to work in our team, funding ANR Nov 2019 – Jan 2020.
  • Then: 4th postdoc in team Viral replicases: structure, function and drug-design of the AFMB lab, Marseille, funding Janssen Apr – Nov 2020.
  • Now: employed by the European Virus Archive – GLOBAL (EVAg), Marseille

Long-term visitors

• Sventja von Daake, visitor Dept of Pharmacology, UCSD (Nov 2003 – Oct 2004) – Funding: Pharmacology Education Research Foundation.
  • Then: Research associate, Susan Taylor Lab, UCSD, La Jolla, CA, USA.
  • Then: Lab manager, Comoletti Lab, Dept Neuroscience & Cell Biology, UMDNJ-RWMS, Child Health Institute of New Jersey, New Brunswick, NJ, USA.
  • Now: Staff Scientist Cytomics Specialist, Malaghan Institute of Medical Research, Wellington, New Zealand
• Nicolas Lenfant, visitor postdoc from lab Dynamique Musculaire et Métabolisme, INRA, Montpellier (Jun 2011 – Dec 2013) – Funding: ANR.
  • Then: postdoc in AFMB team Glycogenomics (Jan 2014 – Dec 2016).
  • Now: engineer Marseille Medical Genetics, Faculté de Médecine Timone, Marseille (March 2018 – ongoing)
• Nafisatou Drame, engineer “CDD” Tafalgie Therapeutics SAS, hosted at the AFMB lab within the frame of an official agreement, Oct 2021 – Apr 2024
  • Now: engineer “CDI” Tafalgie Therapeutics SAS, Marseille (April 2024 – ongoing)

Other trainees & visitors

• Kael Duprey, trainee UCSD, Jun-Oct 1994 & Jun-Oct 1995 (in the US)
• Claudine N. Prowse, trainee UCSD, Jan 1994 – Dec 1995 (in the US)
• Verena Pollmann, visitor PhD Univ Hambourg (PhD mentor: O. Pongs), Mar 2000 & Jun 2000 (2 & 1 wks)
• Jens Dannenberg, visitor Postdoc Institut fuer Neurale Signalverarbeitung, ZMNH, Hamburg, Oct 2001 (2 wks)
• Scott B. Hansen, visitor PhD UCSD (PhD mentor, Palmer Taylor), Apr-Jun 2004 & Nov-Dec 2004 (7 & 8 wks)
• Ryan Hibbs, visitor Postdoc UCSD, Nov-Dec 2006
• Cécile Tardif & Marion Leblanc, “1ère S”, Lycée des Pierres Vives, Carrières-sur-Seine, Dec2013 – Mar2014, by email only!

1986

Bougis PE, Marchot P, Rochat H (1986) Characterization of Elapidae snake venom components using optimized reverse-phase high performance liquid chromatographic conditions and screening assays for α-neurotoxin and phospholipase A2 activities. Biochemistry 25, 7235-7243.

1987

Bougis PE, Marchot P, Rochat H (1987) In vivo synergy of cardiotoxin and phospholipase A2 from the Elapid snake Naja mossambica mossambica. Toxicon 25, 427-431.

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 Androctonus australis Hector. Toxicon 25, 569-573.

Otting G, Marchot P, Bougis PE, Rochat H, Wüthrich K (1987) Monitoring the purification by high performance liquid chromatography of cardiotoxins from Naja mossambica mossambica using phase-sensitive two dimensional nuclear magnetic resonance. Eur J Biochem 168, 603-607.

1988

Marchot P, Bougis PE, Céard B, Van Rietschoten J, Rochat H (1988) Localization of the toxic site of Naja mossambica mossambica cardiotoxins : small synthetic peptides express an in vivo lethality. Biochem Biophys Res Comm 153, 642-647.

Marchot P, Frachon P, Bougis PE (1988) Selective distinction at equilibrium between the two α-neurotoxin binding sites of Torpedo acetylcholine receptor by microtitration. Eur J Biochem 174, 537-542.

Zeghloul S, Marchot P, Bougis PE, Ronin C (1988) Selective loss of binding sites for the iodinated α-neurotoxin I from Naja mossambica mossambica upon enzymatic deglycosylation of Torpedo electric organ membranes. Eur J Biochem 174, 543-550.

1989

Le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC (1989) Crystals of fasciculin 2 from green mamba snake venom : preparation and preliminary X-ray analysis. J Biol Chem 264, 21401-21402.

1990

Muniz ZM, Tibbs GR, Marchot P, Bougis PE, Nicholls DG, Dolly JO (1990) Homologues of a K+ channel blocker α-dendrotoxin : characterization of synaptosomal binding sites and their coupling to elevation of cytosolic free calcium concentration. Neurochem Int 16, 105-112.

Gourdou I, Mabrouk K, Harkiss G, Marchot P, Watt N, Hery F, Vigne R (1990) Neurotoxicité chez la souris de portions riches en cystéines des protéines Tat du virus visna et de VIH-1 [en français ; résumé en anglais]. C R Acad Sci (Paris) 311, Série III, pp. 149-155.

1992

Le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC (1992) 1.9 Å resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom. J Biol Chem 267, 22122-22130.

Laraba-Djebari F, Martin-Eauclaire MF, Marchot P (1992) A fibrinogen-clotting serine proteinase from Cerastes cerastes (horned viper) venom with arginine-esterase and amidase activities : purification, characterization and kinetic parameter determination. Toxicon 30, 1399-1410.

1993

Marchot P, Khélif A, Ji YH, Mansuelle P, Bougis PE (1993) Binding of 125I-fasciculin to rat brain acetylcholinesterase : the complex still binds diisopropyl fluorophosphate. J Biol Chem 268, 12458-12467.

1995

van den Born HKL, Radić Z, Marchot P, Taylor P, Tsigelny I (1995) Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase. Protein Sci 4, 703-715.

Laraba-Djebari F, Martin-Eauclaire MF, Mauco G, Marchot P (1995) Afaâcytin, an αβ-fibrinogenase from Cerastes cerastes (Horned Viper) venom, activates purified factor X and induces serotonin release from human blood platelets. Eur J Biochem 233, 756-765.

Bourne Y, Taylor P, Marchot P (1995) Acetylcholinesterase inhibition by fasciculin : crystal structure of the complex. Cell 83, 503-512.

Taylor P, Radić Z, Hosea NA, Camp S, Marchot P, Berman HA (1995) Structural bases for the specificity of cholinesterase catalysis and inhibition. Toxicol Lett 82-83, 453-458.

1996

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 : evidence for unusual loop flexibility. Acta Cryst D52, 87-92.

Marchot P, Ravelli RBG, Raves ML, Bourne Y, Vellom DC, Kanter J, Camp S, Sussman JL, Taylor P (1996) Soluble monomeric acetylcholinesterase from mouse : expression, purification, and crystallization in complex with fasciculin. Protein Sci 5, 672-679.

1997

Marchot P, Prowse CN, Kanter J, Camp S, Ackermann EJ, Radić Z, Bougis PE, Taylor P (1997) Expression and inhibitory activity of mutants of fasciculin, a peptidic acetylcholinesterase inhibitor from mamba venom. J Biol Chem 272, 3502-3510.

1998

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 α-conotoxin M1 binding. Molec Pharmacol 53, 787-794.

Marchot P, Bourne Y, Prowse CN, Bougis PE, Taylor P (1998) Highlights in toxin research – Inhibition of mouse acetylcholinesterase by fasciculin : crystal structure of the complex and mutagenesis of fasciculin. Toxicon 36, 1613-1622.

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. J Physiol (Paris) 92, 79-83.

1999

Bourne Y, Taylor P, Bougis PE, Marchot P (1999) Crystal structure of mouse acetylcholinesterase : a peripheral site-occluding loop in a tetrameric assembly. J Biol Chem 274, 2963-2970.

Sentjurc M, Pecar S, Stojan J, Marchot P, Radić Z, Grubič Z (1999) Electron paramagnetic resonance reveals altered topography of the active site gorge of acetylcholinesterase after binding of fasciculin to the peripheral site. Biochem Biophys Acta 1430, 349-358.

Bourne Y, Grassi J, Bougis PE, Marchot P (1999) Conformational flexibility of the acetylcholinesterase tetramer revealed by X-ray crystallography. J Biol Chem 274, 30370-30376.

Marchot P (1999) L’interaction fasciculine-acétylcholinestérase [Monographie en français ; résumé en anglais]. J Soc Biol 193, 505-508.

2000

Tricaud N, Marchot P, Martin-Eauclaire MF (2000) On the kaliotoxin and dendrotoxin binding sites on rat brain synaptosomes. Toxicon 38, 1749-1758.

2001

Bourne Y, Dannenberg J, Pollmann V, Marchot P, Pongs O (2001) Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1). J Biol Chem 276, 11949-11955.

2002

Tai K, Shen T, Henchman RH, Bourne Y, Marchot P, McCammon JA (2002) Mechanism of acetylcholinesterase inhibition by fasciculin : a 5 ns molecular dynamics simulation. J Am Chem Soc 124, 6153-6161.

Geib S, Sandoz G, Mabrouk K, Matavel A, Marchot P, Hoshi T, Villaz M, Ronjat M, Miquelis R, Lévêque C, De Waard M (2002) Use of a purified and functional recombinant Ca2+ channel β4 subunit in surface plasmon resonance studies. Biochem J 364, 285-292.

2003

Bourne Y, Taylor P, Radić Z, Marchot P (2003) Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 22, 1-12.

2004

Hotelier T, Renault L, Cousin X, Nègre V, Marchot P, Chatonnet A (2004) ESTHER, the database of the α/β-hydrolase fold superfamily of proteins. Nucleic Acids Res 32, D145-147.

Bourne Y, Kolb HC, Radić Z, Sharpless KB, Taylor P, Marchot P (2004) Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation. Proc Natl Acad Sci USA 101, 1449-1454.

Bourne Y, Hasper AA, Chahinian H, Juin M, de Graaff LH, Marchot P (2004) Aspergillus niger protein EstA defines a new class of fungal esterases within the α/β-hydrolase fold family of proteins. Structure (Camb) 12, 677-687 [Erratum in Structure (Camb) 12, 1545]. (See also Preview “Defining substrate characteristics from 3D structure : perspective on EstA structure” by Schrag JD & Cygler M, Structure (Camb) 12, 521-522.)

2005

Legros C, Céard B, Vacher H, Marchot P, Bougis PE, Martin-Eauclaire MF (2005) Expression of the scorpion α-toxin of reference AaH-II and mutants for identification of some key bioactive elements. Biochem Biophys Acta 1723, 91-99.

Bourne Y, Talley TT, Hansen SB, Taylor P, Marchot P (2005) Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake α-neurotoxins and nicotinic receptors. EMBO J 24, 1512–1522 [Corrigendum in EMBO J. 25, 266 (2006)].

Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y (2005) Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J 24, 3635–3646.

Bourne Y, Radić 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]. Chem Biol Interact 157-158, 159-165.

Renault L, Nègre V, Hotelier T, Cousin X, Marchot P, Chatonnet A (2005) New friendly tools for users of ESTHER, the database of the α/β-hydrolase fold superfamily of proteins. Chem Biol Interact 157-158, 339-343.

Bourne Y, Hasper AA, Chahinian H, Renault L, Juin MA, de Graaff LH, Marchot P (2005) A. niger protein “EstA”, perhaps a new electrotactin, defines a new class of fungal esterases within the α/β-hydrolase fold superfamily. Chem Biol Interact 157-158, 395-396.

Renault L, Essono S, Boquet D, Juin M, Grassi J, Bourne Y, Marchot P (2005) Structural insights into AChE inhibition by monoclonal antibodies. Chem Biol Interact 157-158, 397-400.

2006

Bourne Y, Radić 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. J Biol Chem 281, 29256-29267.

Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Bourne Y, Taylor P (2006) Structural characterization of agonist and antagonist-bound acetylcholine-binding protein from Aplysia californica. J Mol Neurosci 30 (1-2), 101-102.

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. J Mol Neurosci 30 (1-2), 103-104.

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. Acta Pharmacol Sin 27, 390-390.

2007

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 β-neurexin complex : determinants for folding and cell adhesion. Neuron 56, 979-991. (See also Preview “A Crystal-Clear Interaction : Relating Neuroligin/Neurexin Complex Structure to Function at the Synapse” by Levinson J.N. & El-Husseini A. Neuron 56, 937-939.)

2009

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 α7 nicotinic acetylcholine receptor. EMBO J 28, 3040-3051.

2010

Bourne Y, Radić Z, Aráoz R, Talley TT, Benoit E, Servent D, Taylor P, Molgó J, Marchot P (2010) Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism. Proc Natl Acad Sci USA 107, 6076-6081.

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. EMBO J 29, 2461-2471.

Leone P, Comoletti D, Taylor P, Bourne Y, Marchot P (2010) Structure-function relationship of the α/β-hydrolase fold domain of neuroligin : a comparison with acetylcholinesterase [Revue]. Chem Biol Interact 187, 49–55.

Hotelier T, Nègre V, Marchot P, Chatonnet A (2010) Insecticide resistance through mutations in cholinesterases or carboxylesterases : data mining in ESTHER database. J Pestic Sci 35, 315-320.

Bourne Y, Radić Z, Taylor P, Marchot P (2010) Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state. J Am Chem Soc 132, 18292-18300.

2012

Marchot P, Chatonnet A (2012) Editorial to the Special Issue on “Hydrolase versus other functions of members of the α/β-hydrolase fold superfamily of proteins”. Protein Peptide Lett 19, 130-131.

Marchot P, Chatonnet A (2012) Enzymatic activity and protein interactions in α/β-hydrolase fold proteins : moonlighting versus promiscuity. In : Special Issue on “Hydrolase versus other functions of members of the α/β-hydrolase fold superfamily of proteins”. Protein Peptide Lett 19, 132-143.

Fabrichny IP, Mondielli G, Conrod S, Martin-Eauclaire MF, Bourne Y, Marchot P (2012) Structural insights into antibody sequestering and neutralizing of Na+-channel α-type modulator from Old World scorpion venom. J Biol Chem 287, 14136-14148.

2013

Lenfant N, Hotelier T, Velluet E, Bourne Y, Marchot P, Chatonnet A (2013) ESTHER, the database of the α/β-hydrolase fold superfamily of proteins : tools to explore diversity of functions. Nucleic Acids Res (Database Issue) 41, D423-D429.

Lenfant N, Hotelier T, Bourne Y, Marchot P, Chatonnet A (2013) Proteins with an α/β-hydrolase fold : relationships between subfamilies in an ever-growing superfamily. Chem Biol Interact 203, 266-268.

Martin-Eauclaire MF, Benoit E, Marchot P, Barbier J, Molgó J, Servent D (2013) Editorial to the Special Issue on “Toxins : From Threats to Benefits” (Molgó J, Benoit E, Barbier J, Marchot P, Servent D, Guest Eds), Toxicon 75, 1-2.

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. PLOS One 8, e77226.

2014

Lenfant N, Hotelier T, Bourne Y, Marchot P, Chatonnet A (2014) Tracking the origin and divergence of cholinesterases and neuroligins : the evolution of synaptic proteins. J Mol Neurosci 53, 362-369.

Bourne Y, Marchot P (2014) The neuroligins and their ligands : from structure to function at the synapse. J Mol Neurosci 53, 387-396.

Benoit E, Mattei C, Barbier J, Marchot P, Molgó J, Servent D (2014) Editorial to the Special Issue on “Freshwater and Marine Toxins” (Molgó J, Benoit E, Barbier J, Marchot P, Servent D, Guest Eds), Toxicon 91, 1-4.

2015

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 : evidence for open and closed states of a back door channel. J Biol Chem 290, 1522–1535.

Bourne Y, Sulzenbacher G, Radić Z, Aráoz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molgó J, Taylor P, Marchot P (2015) Marine macrocyclic imines, pinnatoxins A and G : structural determinants and functional properties to distinguish neuronal α7 from muscle (α1)2βγδ nAChRs. Structure 23, 1106-1115. (See also Preview “From Shellfish Poisoning to Neuroscience” by Shahsavar A and Balle T, Structure 23, 979-980.)

2016

Bourne Y, Sharpless KB, Taylor P, Marchot P (2016) Steric and dynamic parameters influencing in situ cycloadditions to form triazole inhibitors with crystalline acetylcholinesterase. J Am Chem Soc 138, 1611−1621.

Lenfant N, Bourne Y, Marchot P, Chatonnet A (2016) Relationships of human α/β hydrolase fold proteins and other organophosphate-interacting proteins. Chem Biol Interact 259, 343-351.

2017

Prado MAM, Marchot P, Silman I (2017) Preface to the Special Issue “Cholinergic Mechanisms”. J Neurochem 142 Suppl 2, 3-6.

Kessler P, Marchot P, Silva M, Servent D (2017) The three-finger toxin fold : a multifunctional structural scaffold able to modulate the cholinergic functions. J Neurochem 142 Suppl 2, 7-18.

Molgó J, Marchot P, Aráoz R, Benoit E, Iorga BI, Zakarian A, Taylor P, Bourne Y, Servent D (2017) Cyclic imine toxins from dinoflagellates : a growing family of potent antagonists of the nicotinic acetylcholine receptors. J Neurochem 142 Suppl 2, 41-51.

Chatonnet A, Lenfant N, Marchot P, Selkirk ME (2017) Natural genomic amplification of cholinesterase genes in animals. J Neurochem 142 Suppl 2, 73-81.

Thoumine O, Marchot P (2017) A triad of crystals sheds light on MDGA interference with neuroligation. Neuron 95, 729-731.

2018

Bourne Y, Marchot P (2018) Hot spots for protein partnership at the surface of cholinesterases and related alpha/beta hydrolase fold proteins or domains – a structural perspective. Molecules 23, 35.

2019

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 : Possible outcomes for cholinesterase expression in prokaryotes. Chem Biol Interact 308, 179-184.

2020

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). Neurosci Biobehav Rev 119, 37-51.

Platsaki S, Zhou X, Pinan-Lucarré 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. J Biol Chem 295, 16267-16279.

2021

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 ‘Acetylcholinesterase Inhibitors’ (Guest Editor, Maria Braga). Neuropharmacology 184, 108381.

2022

Ramirez-Franco J, Debreux K, Extremet J, Maulet Y, Belghazi M, Villard C, Sangiardi M, Youssouf F, El Far L, Lévêque 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. Brain 145, 3843-3858.

2023

Chatonnet A, Perochon M, Velluet E, Marchot P (2023) The ESTHER database on alpha/beta hydrolase fold proteins – An overview of recent developments. Chem Biol Interact 383, 110671.

Martin-Eauclaire MF, Marchot P (2023) Obituary – Hervé Paul Marie Antoine ROCHAT 1937–2023. Toxicon 233, 107249.

2024

Bourne Y, Sulzenbacher G, Chabaud L, Aráoz R, Radić Z, Conrod S, Taylor P, Guillou C, Molgó J, Marchot P (2024) The cyclic imine core common to the marine macrocyclic toxins is sufficient to dictate nicotinic acetylcholine receptor antagonism. Mar. Drugs 22, 149. [This article belongs to the Special Issue ‘Marine Biotoxins 2.0’ of Marine Drugs (Molgo J., Guest ed).]

Zancolli G*, von Reumont BM*, Anderluh G, Caliskan F, Chiusano ML, Fröhlich J, Hapeshi E, Hempel BF, Ikonomopoulou MP, Jungo F, Marchot P, Mendes de Farias T, Modica MV, Moran Y, Nalbantsoy A, Procházka 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 13, giae054.

Book Toxines & cancer (Goudey-Perrière F, Benoit E, Goyffon M, Marchot P, eds) Coll. Rencontres en Toxinologie, Editions Lavoisier, Cachan, 2006 (326 pages) (ISBN : 2-7430-0958-6).

Book Toxines émergentes : nouveaux risques (Goudey-Perrière F, Benoit E, Marchot P, Popoff M, eds) Coll Rencontres en Toxinologie, Editions Lavoisier, Cachan, 2007 (208 pages) (ISBN : 978-2-7430-1037-9).

E-book Toxines & fonctions cholinergiques neuronales & non neuronales (Benoit E, Goudey-Perrière F, Marchot P, Servent D, eds) Coll Rencontres en Toxinologie, Publications de la SFET, Châtenay-Malabry, 2008 (160 pages) (ISSN : 1760-6004).

E-book Toxines & signalisation (Benoit E, Goudey-Perrière F, Marchot P, Servent D, eds) Coll Rencontres en Toxinologie, Publications de la SFET, Châtenay-Malabry, 2009 (206 pages) (ISSN : 1760-6004).

E-book Advances and new technologies in toxinology (Barbier J, Benoit E, Marchot P, Mattei C, Servent D, eds) Coll Rencontres en Toxinologie, Publications de la SFET, Châtenay-Malabry, 2010 (184 pages) (ISSN : 1760-6004).

Special Issue Hydrolase versus other functions of members of the α/β-hydrolase fold superfamily of proteins (Chatonnet A, Marchot P, Guest eds). Protein & Peptide Letters, Bentham Science Publishers Ltd., 2012, vol 19(2), pp 130-197 (ISSN : 0929-8665).

Special Issue Toxins : From Threats to Benefits, 20th Meeting of the French Society of Toxinology (SFET) (Molgó J, Benoit E, Barbier J, Marchot P, Servent D, Guest eds), Toxicon (ISSN : 0041-0101), Elsevier, 2013, vol 75, pp 1-224.

Special Issue Freshwater and Marine Toxins, 21th Meeting of the French Society of Toxinology (SFET) (Molgó J, Benoit E, Barbier J, Marchot P, Servent D, Guest eds), Toxicon (ISSN : 0041-0101), Elsevier, 2014, vol 91, pp 1-184.

Special Issue Cholinergic Mechanisms (Silman I, Guest ed ; Marchot P, Prado MAM, Assoc Guest eds), J Neurochem (ISSN : 1471-4159), Wiley, 2017, vol 142 – Suppl 2, pp 1-226.

Special Issue Toxins : From the wild to the lab, 29th Meeting of the French Society of Toxinology (SFET) (Marchot P, Benoit E, Diochot S, Guest eds). Toxins (ISSN: 2072-6651), MDPI, 2024, open for submission.

Marchot P, Bougis PE, Céard B, Van Rietschoten J, Rochat H (1989) Lethal synthetic peptides as models of the toxic site of Naja mossambica mossambica cardiotoxins. In Second Forum on Peptides (Aubry A, Marraud M, Vitoux B, eds) Colloque INSERM / John Libbey Eurotext Ltd 174, 461-464.

Le Du MH, Marchot P, Bougis PE, Fontecilla-Camps JC (1993) Fasciculin 1 (Green mamba). In Macromolecular Structures (Hendrickson WA, Wüthrich K, eds) pp. 152-153, Current Biology Ltd, Philadelphia.

Marchot P, Camp S, Radić Z, Bougis PE, Taylor P (1995) Structural determinants of fasciculin specificity for acetylcholinesterase. In Enzymes of the Cholinesterase Family (Quinn DM, Balasubramanian AS, Doctor BP, Taylor P, eds) pp. 197-202, Plenum Publishing Corp, NY.

Bourne Y, Taylor P, Marchot P (1996) Acetylcholinesterase, recombinant monomeric form (mouse) / fasciculin 2 (mamba) complex. In Macromolecular Structures (Hendrickson WA, Wüthrich K, eds) pp. 8-9, Current Biology Ltd, London, UK.

Bourne Y, Taylor P, Kanter JR, Bougis PE, Marchot P (1998) Crystal structure of mouse acetylcholinesterase. In Structure and Function of Cholinesterases and Related Proteins (Doctor BP, Taylor P, Quinn DM, Rotundo RL, Gentry MK, eds) pp. 315-322, Plenum Publishing Corp, NY.

Marchot P, Bourne Y, Prowse CN, Kanter JR, Eads J, Bougis PE, Taylor P (1998) Fasciculin inhibition of mouse acetylcholinesterase : crystal structure of the complex and mutagenesis of fasciculin. In Structure and Function of Cholinesterases and Related Proteins (Doctor BP, Taylor P, Quinn DM, Rotundo RL, Gentry MK, eds) pp. 331-338, Plenum Publishing Corp., NY.

Kanter JR, Eads J, Camp S, Marchot P, Taylor P (1998) Expression and purification of recombinant mutants of fasciculin from mammalian cells. In Structure and Function of Cholinesterases and Related Proteins (Doctor BP, Taylor P, Quinn DM, Rotundo RL, Gentry MK, eds) pp. 240-241, Plenum Publishing Corp, NY.

Marchot P, Bougis PE (2000) The fasciculins, and their interaction with acetylcholinesterase. In : Animal Toxins. Facts and Protocols (Rochat H, Martin-Eauclaire MF, eds) pp. 246-275, Birkhäuser Verlag, Basel.

Bourne Y, Marchot P (2002) Fasciculines et autres ligands de l’AChE : développements structuraux récents [Revue en français ; résumé en anglais]. In : Toxines et Recherches Biomédicales (Goudey-Perrière F, Bon C, Puiseux-Dao S, Sauviat MP, eds) pp. 287-296, Coll. Rencontres en Toxinologie, Editions Scientifiques et Médicales Elsevier, Paris.

Comoletti D, Flynn R, Jennings L, Hoffman R, Marchot P, Bourne Y, Südhof T, Taylor P (2004) Interaction of recombinant soluble neuroligin-1 with neurexin-1-β. In Cholinergic Mechanisms – function and dysfunction Symposium Proceedings (Silman I, Michaelson DM, Anglister L, Fisher A, Soreq H, eds) pp. 523-525, Taylor & Francis group, UK.

Tai K, Shen T, Henchman RH, Bourne Y, Marchot P, McCammon JA (2004) Mechanism of acetylcholinesterase inhibition by fasciculin : A 5ns molecular dynamics simulation. In Cholinergic Mechanisms – function and dysfunction Symposium Proceedings (Silman I, Michaelson DM, Anglister I, Fisher A, Soreq H, eds) pp. 727-728, Taylor & Francis group, UK.

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 protéine synaptique liant l’acétylcholine. [Revue en français ; résumé en anglais]. In Toxines et Douleur (Bon C, Goudey-Perrière F, Goyffon M, Sauviat MP, eds), pp. 213-216, Coll Rencontres en Toxinologie, Editions Lavoisier, Cachan, France.

Fabrichny I, Conrod S, Martin-Eauclaire MF, Devaux C, Bourne Y, Marchot P (2007) Immunothérapie antiscorpionique : approche structurale. [En français ; résumé & légendes en anglais]. In Toxines émergentes : nouveaux risques (Goudey-Perrière F, Benoit E, Marchot P, Popoff M, eds), pp. 197-202, Coll Rencontres en Toxinologie, Editions Lavoisier, Cachan, France.

Bourne Y, Radić Z, Talley TT, Conrod S, Taylor P, Molgó J, Marchot P (2008) Utilisation des « protéines liant l’ACh » (AChBP) en toxinologie structurale : nouveaux exemples. [En français ; résumé & légendes en anglais]. In Toxines et fonctions cholinergiques neuronales et non neuronales (Benoit E, Goudey-Perrière F, Marchot P, Servent D, eds), pp. 27-28, Coll Rencontres en Toxinologie, Publications de la SFET, Châtenay-Malabry, France.

Taylor P, Radić 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 – Proceeding from gene product back to the gene : applications in drug discovery and uncovering linkages in congenital disorders. [Revue en anglais ; résumé & légendes en français]. In Toxines et fonctions cholinergiques neuronales et non neuronales (Benoit E, Goudey-Perrière F, Marchot P, Servent D, eds), pp. 29-32, Coll Rencontres en Toxinologie, Publications de la SFET, Châtenay-Malabry, France.

Douzi B, Geerlof A, Gilles N, Darbon H, Marchot P, Vincentelli R (2010) A new system for expressing recombinant animal toxins in E. coli ? In Advances and new technologies in toxinology (Barbier J, Benoit E, Marchot P, Mattei C, Servent D, eds), pp. 149-152, Coll Rencontres en Toxinologie, Publications de la SFET, Châtenay-Malabry, France.

Marchot P, Diochot S, Popoff MR, Benoit E (2020) Report from the 26th Meeting on Toxinology, “Bioengineering of Toxins”, Organized by the French Society of Toxinology (SFET) and Held in Paris, France, 4–5 December 2019. In Special Issue “Selected Papers from the 26th Meeting of the French Society for Toxinology- Bioengineering of Toxins” (Popoff MR, Benoit E, eds). Toxins 12, 31/pp. 1-29. (doi:10.3390/toxins12010031)

Ladant D, Marchot P, Diochot S, Prévost G, Popoff MR, Benoit E (2022) Report from the 27th (Virtual) Meeting on Toxinology, “Toxins : Mr Hyde or Dr Jekyll ?”, Organized by the French Society of Toxinology, 9-10 December 2021. In Special Issue “Toxins : Mr Hyde or Dr Jekyll ?” (Ladant D, Prévost G, Popoff MR, Benoit E, eds). Toxins 14(2), 110/pp. 1-32. (doi: 10.3390/toxins14020110)

Marchot P, Benoit E, Fajloun Z, Diochot S (2023) Report from the 28th Meeting on Toxinology, “Toxins: What’s up, Doc?”, Organized by the French Society of Toxinology on November 28-29, 2022. Toxins 15(2), 126/pp. 1-25. (doi: 10.3390/toxins15020126)

Marchot P, Fajloun Z, Legros C, Benoit E, Diochot S (2024) Report from the 29th Meeting on Toxinology, “Toxins: From the wild to the lab”, Organized by the French Society of Toxinology on November 30-December 01, 2023. In Special Issue “Toxins : From the wild to the lab” (Marchot P, Benoit E, Diochot S, eds). Toxins 16, 147/pp.1-34. (doi: 10.3390/toxins16030147)

Bougis PE, Marchot P, Rochat H (1985) Reverse-phase high performance liquid chromatography of Elapidae snake venoms. Toxicon 23, p. 554

Marchot P, Khélif A, Bougis PE (1985) Brain acetylcholinesterase inhibitor from mamba snake venom : reverse-phase HPLC isolation and characterisation. Toxicon 23, p. 592

Marchot P, Bougis PE, Rochat H (1987) High performance liquid chromatography of Elapidae snake venoms. Toxicon 25, p. 372

Laraba-Djebari F, Martin-Eauclaire MF, Marchot P (1993) Two thrombin-like proteinases from Cerastes cerastes (Horn viper) venom : purification, characterization and kinetic parameter determination. Toxicon 31, p. 528

Laraba-Djebari F, Martin-Eauclaire MF, Marchot P (1994) Afaâcytin, a thrombin-like enzyme from the venom of Cerastes cerastes : structural and functional properties. Toxicon 32, p. 400

Marchot P, Khélif A, Ji YH, Mansuelle P, Bougis PE (1994) Binding of 125I-fasciculin to rat brain acetylcholinesterase. Toxicon 32, p. 401

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. Pharmacologist 39, p. 104

Marchot P, Taylor P, Kanter JR, Bougis PE, Bourne Y (1998) Tetrameric assembly and peripheral site-occluding loop of mouse acetylcholinesterase. J Physiol (Paris) 92, p. 465

Bougis PE, Taylor P, Marchot P (1998) Biotinylation of the tyrosine residues of fasciculin. J Physiol (Paris) 92, p. 416

Marchot P (1999) Acetylcholinesterase inhibition by fasciculin. Toxicon 37, 1209-1210

Bougis PE, Taylor P, Marchot P (2000) Biotinylated fasciculins : potential tools for histochemical studies of acetylcholinesterase. Toxicon 38, 1637-1638

Flynn R, Comoletti D, Marchot P, Bourne Y, Südhof T, & Taylor P (2003) Interaction of recombinant soluble neuroligins-1 with neurexin-ß. FASEB J. 17 (4), A640

Bourne Y, Sulzenbacher G, Radić Z, Aráoz R, Reynaud M, Benoit E, Talley TT, Zakarian A, Taylor P, Servent D, Molgó J, Marchot P (2014) Diversity in the binding interactions of marine toxins to AChBP, the soluble nAChR surrogate. Toxicon 91, 171-172.

Marchot P, Sharpless KB, Taylor P, Bourne Y (2016) Structural and functional analysis of acetylcholinesterase complexes with “in situ click-chemistry” inhibitors. FASEB J 30 Suppl 1, 833.10.

Bourne Y, Radić Z, Sharpless KB, Taylor P, Marchot P (2017) Structural and functional analysis of acetylcholinesterase complexes with in situ click-chemistry inhibitors. J Neurochem 142 Suppl 2, 189.

Marchot P, Sulzenbacher G, Radić Z, Aráoz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molgó J, Taylor P, Bourne Y (2017) Diversity in the binding interactions of marine phycotoxins to AChBP, the soluble nAChR surrogate. J Neurochem 142 Suppl 2, 196.

Chatonnet A, Marchot P, Bourne Y, Lenfant N, Hotelier T (2017) ESTHER database : update on the alpha/beta hydrolase fold superfamily of proteins. J Neurochem 142 Suppl 2, 209.

Lenfant N, Selkirk ME, Hotelier T, Bourne Y, Marchot P, Chatonnet A (2017) Evolution of animal cholinesterases. J Neurochem 142 Suppl 2, 214.

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. Mil Med Sci Lett (Voj Zdrav Listy) 87 Suppl 1, 55.

Bourne Y, Sulzenbacher G, Radić Z, Chabaud L, Aráoz R, Benoit E, Zakarian A, Servent D, Guillou C, Taylor P, Molgó 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 “Marchot P, Diochot S, Popoff MR, Benoit E. Report from the 26th Meeting on Toxinology, “Bioengineering of Toxins”, Organized by the French Society of Toxinology (SFET) and Held in Paris, France, 4-5 December 2019. Toxins 12:31, pp. 9-10.

Bourne Y, Sulzenbacher G, Chabaud L, Aráoz R, Radić Z, Conrod S, Taylor P, Guillou C, Molgó 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, “Toxins: From the Wild to the Lab”, Organized by the French Society of Toxinology on 30 November–1 December 2023. Toxins 16:147, pp. 16-17.

• 1FAS Fasciculin 1 (LeDu, Marchot, Bougis, Fontecilla-Camps, 1993)
• 1FSC Fasciculin 2 (LeDu, Housset, Marchot, Bougis, Navaza, Fontecilla-Camps, 1995)

• 1MAH Mouse AChE, fasciculin 2 complex (Bourne, Taylor, Marchot, 1995)
• 1KU6 Mouse AChE, revisited fasciculin 2 complex (Bourne, Burmeister, Taylor, Marchot, 2002)

• 1C2B Eel AChE, natural tetramer, structure A (Bourne, Marchot, 1999)
• 1C2O Eel AChE, natural tetramer, structure B (id.)

• 1MAA Mouse AChE, crystalline tetramer (Bourne, Taylor, Bougis, Marchot, 1998)

• 1J06 Mouse AChE, first apo form (Bourne, Taylor, Radić, Marchot, 2002)
• 1J07 Mouse AChE, decidium complex (id.)
• 1N5R Mouse AChE, propidium complex (id.)
• 1N5M Mouse AChE, gallamine complex (id.)

• 2H9Y Mouse AChE, complex with TMTFA (Bourne, Radić, Sulzenbacher, Kim, Taylor, Marchot, 2006)
• 2HA0 Mouse AChE, complex with 4K-TMA (id.)
• 2HA2 Mouse AChE, complex with succinyldicholine (id.)
• 2HA3 Mouse AChE, complex with choline (id.)
• 2HA4 Mouse AChE S203A mutant, complex with acetylcholine (id.)
• 2HA5 Mouse AChE S203A mutant, complex with acetylthiocholine (id.)
• 2HA6 Mouse AChE S203A mutant, complex with succinyldicholine (id.)
• 2HA7 Mouse AChE S203A mutant, complex with butyrylthiocholine (id.)

• 1Q83 Mouse AChE, TZ2PA6 syn1 complex (Bourne, Kolb, Radić, Sharpless, Taylor, Marchot, 2003)
• 1Q84 Mouse AChE, TZ2PA6 anti1 complex (id.)

• 5EHN mouse AChE, syn-TZ2PA5 complex (Bourne, Sharpless, Taylor, Marchot, 2016)
• 5EHQ mouse AChE, anti-TZ2PA5 complex (id.)
• 5EHZ mouse AChE, syn-TZ2PA5 complex from a 1:1 syn/anti mixture (id.)
• 5EIA mouse AChE, anti-TZ2PA5 complex from a 1:6 syn/anti mixture (id.)
• 5EIE mouse AChE, TZ2 complex (id.)
• 5EIH mouse AChE, TZ2+PA5 complex (id.)

• 2XUD Mouse AChE Tyr337Ala mutant (Bourne, Radić, Taylor, Marchot, 2010)
• 2XUG Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 anti1 (1-wk) (id.)
• 2XUF Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 anti1 (1-mth) (id.)
• 2XUH Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 anti1 (10-mths) (id)
• 2XUI Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 syn1 (1-wk) (id)
• 2XUJ Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 syn1 (1-mth) (id)
• 2XUK Mouse AChE Tyr337Ala mutant, cocrystallized complex with TZ2PA6 syn1 (10-mths) (id)
• 2XUO Mouse AChE, Tyr337Ala mutant, soaking complex with TZ2PA6 anti1 (id)
• 2XUP Mouse AChE, Tyr337Ala mutant, soaking complex with TZ2PA6 syn1 (id.)
• 2XUQ Mouse AChE, Tyr337Ala mutant, soaking complex with mixed TZ2PA6 anti1/syn1 (id.)

• 2YMX Inhibitory anti-AChE Fab408 (Bourne, Renault, Essono, Mondielli, Lamourette, Bocquet, Grassi, Marchot, 2013)
• 4QWW Fab410-BfAChE complex (Bourne, Renault, Marchot, 2015)

• 1YI5 Lymnaea AChBP, α-cobratoxin complex (Bourne, Talley, Hansen, Taylor, Marchot, 2005)

• 2BYN Aplysia AChBP, apo (Hansen, Sulzenbacher, Huxford, Marchot, Taylor, Bourne, 2005)
• 2BYP Aplysia AChBP, α-conotoxin Im1 complex (id.)
• 2BYQ Aplysia AChBP, epibatidine complex (id.)
• 2BYR Aplysia AChBP, methyllycaconitine complex (id.)
• 2BYS Aplysia AChBP, lobeline complex (id.)

• 2WNL Aplysia AChBP, anabaseine complex (Hibbs, Sulzenbacher, Shi, Talley, Conrod, Kem, Taylor, Marchot, Bourne, 2009)
• 2WNJ Aplysia AChBP, DMXBA complex (id.)
• 2WN9 Aplysia AChBP, 4-OH-DMXBA complex (id.)
• 2WNC Aplysia AChBP, tropisetron complex (id.)

• 2WZY Aplysia AChBP, SPX complex (Bourne, Radic, Aráoz, Talley, Benoit, Servent, Taylor, Molgo, Marchot, 2010)
• 2X00 Aplysia AChBP, GYM complex (id.)

• 4XHE Aplysia AChBP, PnTx-A complex (Bourne, Sulzenbacher, Marchot, 2015)
• 4XK9 Aplysia AChBP, PnTx-G complex (id)

• 8Q1M Aplysia AChBP, spiroimine (+)-4 R complex (Sulzenbacher, Bourne, Marchot, 2024)
• 8QTL Aplysia AChBP, spiroimine (–)-4 S complex (id.)
• 8QX2 Aplysia AChBP, spiroimine (±)-4 complex (id.)

• 3BE8 NL4 (Fabrichny, Leone, Sulzenbacher, Comoletti, Miller, Taylor, Bourne, Marchot, 2007)
• 2VH8 Nrxβ1-NL4 complex (id.)

• 2WQZ Nrxβ1-NL4 complex, aternative refinement (replaces 2VH8) 2009

• 2XB6 Revisited Nrxβ1-NL4 complex (Leone, Comoletti, Ferracci, Conrod, Taylor, Bourne, Marchot, 2010)

• 4AEI Fab4C1 bound with scorpion toxin AahII (Fabrichny, Mondielli, Conrod, Martin-Eauclaire, Bourne, Marchot, 2011)
• 4AEH Fab9C2 in the absence of a bound scorpion toxin AahI (id)

• 1G8I Human frequenin (NCS-1) (Bourne, Dannenberg, Pollmann, Marchot, Pongs, 2000)

• 1UKC Aspergillus niger EstA (Bourne, Hasper, Chahinian, Juin, de Graff, Marchot, 2003)

For “Bourne et al., Structure (Camb) 2004” :

“Defining substrate characteristics from 3D structure : perspective on EstA structure” by Schrag JD & Cygler M, Structure (Camb) 12, 521-522.

For « Bourne et al., PNAS 2004” :

“Enzyme manufactures its own inhibitor” PNAS News Archive [Feb 2004]

“Sharpless clicks at Informex 2004” Chem. Eng. News 82, 63-65 [Feb 2004] https://cen.acs.org/articles/82/i7/SHARPLESS-CLICKS-INFORMEX-2004.html

“Clicking on to the chemistry of Alzheimer’s” Chem. World 3 [Mar 2004]

“New approach to drug design” UCSD News / Health Sciences [Mar 2004] http://ucsdnews.ucsd.edu/archive/ne…

“Enzyme acetylcholinesterase, new approach to drug design” News-Medical.Net… Medical News [Mar 2004] http://www.news-medical.net/?id=87

“Pharmacologists collaborate on new approach to drug design” MediLexicon/Medical News Headlines [Mar 2004] http://www.pharma-lexicon.com/medic…

“Enzymes are doing it for themselves” Biotechniques Euro-edition [Apr 2004]

For “Fabrichny et al., Neuron 2007” :

Preview “A Crystal-Clear Interaction : Relating Neuroligin/Neurexin Complex Structure to Function at the Synapse” by Levinson J.N. & El-Husseini A., Neuron 56 (2007) 937-939

“Snapshot of proteins linked to autism”, Royal Society of Chemistry, UK [Dec 2007] http://www.rsc.org/chemistryworld/N…

“Atomic Structure of Proteins Altered in Autism” Newswise [Dec 2007] http://www.newswise.com/articles/vi…

“Study Details Atomic Structure of Proteins Altered in Autism”, UCSD Medical Center [Dec 2007] http://ucsdnews.ucsd.edu/archive/ne…

« L’autisme : un syndrome complexe approché de très près par les chercheurs de l’Université de la Méditerranée et du CNRS : Des protéines neuronales incriminées dans l’autisme vues en 3D », Communiqué de Presse de l’Université de la Méditerrannée [Dec 2007] http://www.univmed.fr/communication…

« Observation en 3D de protéines neuronales incriminées dans l’autisme », Communiqué de presse du CNRS [Dec 2007] http://www2.cnrs.fr/presse/communiq…

« Observation en 3D de protéines neuronales incriminées dans l’autisme », TV5.org – Infos – Les communiqués de presse [Dec 2007] http://www.tv5.org/TV5Site/info/com…

« Observation en 3D de protéines neuronales incriminées dans l’autisme », News Press Le Monde [Dec 2007] http://www.newsfrance.org/communiqu…

« En direct des labos – Autisme : des protéines neuronales incriminées observées en 3D », BE France 203 – Veille technologique internationale, ADIT – Ministère des Affaires Etrangères et Européennes [Jan 2008] http://www.bulletins-electroniques….

“Live from the Labs – 3D Observation of Neuroligins Involved in Autism”, BE France 203 – Veille technologique internationale, ADIT – Ministère des Affaires Etrangères et Européennes [Jan 2008] http://www.bulletins-electroniques….

« Des protéines neuronales incriminées dans l’autisme observées en trois dimensions », Centre de Ressources Autisme Rhône-Alpes, Revue de presse n°22 : 16/12/07 – 31/12/07 [Jan 2008] http://www.cra-rhone-alpes.org/spip…

F1000Prime – Article Recommendations [Feb 2008] [http://f1000.com/prime/1100169]

« Analyse en 3D de protéines neuronales incriminées dans l’autisme », La Lettre de l’Université de la Méditerranée, n°125 Février 2008 p.25 http://www.univmed.fr/communication…

« Observation en 3D de protéines neuronales incriminées dans l’autisme », Paris Presse Actualité [Feb 2008] http://www.parispresse.eu/__n87678_…

« Observation en 3D de protéines neuronales incriminées dans l’autisme », Journal du CNRS, n°218 Mars 2008

« Des protéines incriminées dans l’autisme vues en 3D », Neurosciences – Découvertes en rafale sur le cerveau [Mar 2008] http://www2.cnrs.fr/presse/journal/…

« Pierres fondamentales », Revue de l’UNAPEI, Septembre 2008

For “Bourne et al., PNAS 2010” :

« Comment agissent certaines toxines accumulées dans les fruits de mer » [Mar 2010] Communiqué de presse du CNRS http://www2.cnrs.fr/presse/communiq…

« Comment agissent certaines toxines accumulées dans les fruits de mer » [Mar 2010] Communiqué de presse du CEA – Sciences du vivant http://www-dsv.cea.fr/la-dsv/toute-…]

”The mode of action of certain toxins that accumulate in seafood” [Mar 2010] Communiqué de presse du CNRS page internationale http://www2.cnrs.fr/en/1709.htm

“Comment des coquillages deviennent toxiques” [Mar 2010] Ma Planète [http://ma-planete.com/blog/view/id_…]

« Deux toxines des poissons et fruits de mer percées à jour » [Mar 2010] RTL Info [ https://www.rtl.be/art/info/magazine/science-nature/deux-toxines-des-poissons-et-fruits-de-mer-percees-a-jour-156483.aspx ]

« Certains fruits de mer contiennent des toxines provoquant des dysfonctionnements cérébraux » [Mar 2010] Communiqué de presse dans La Dépêche, relayé par Le Quotidien du Médecin [ https://www.ladepeche.fr/article/2010/03/10/793935-certains-fruits-mer-contiennent-toxines-provoquant-dysfonctionnements-cerebraux.html ]

For “Bourne et al., Structure 2015” :

Preview “From Shellfish Poisoning to Neuroscience” by Shahsavar A and Balle T, Structure 23, 979-980 [https://www.sciencedirect.com/scien…].

Euromédecine 1987, Montpellier: animation of a booth, and design and distribution of flyer “L’information et la vie – Identification et purification d’une toxine de venin animal”.

• ESTHER database : https://bioweb.supagro.inrae.fr/ESTHER/
• French Society on Toxinology: http://sfet.asso.fr/international/
• International Society on Toxinology : http://www.toxinology.org/
• Society for Neurosciences : http://www.sfn.org/
• Société des Neurosciences: https://www.neurosciences.asso.fr/en/
• International Society for Neurochemistry: https://www.neurochemistry.org/
• XVth ISCM, Marseille, oct 2016: http://iscm.sciencesconf.org/?lang=en
• European Venom Network (EUVEN): https://euven-network.eu/
• RCSB PDB-101 Molecule of the Month: Acetylcholinesterase: https://pdb101.rcsb.org/motm/54
• RCSB PDB-101 Molecule of the Month: Acetylcholine Receptor: https://pdb101.rcsb.org/motm/71
• RCSB PDB-101 Molecule of the Month: Click Chemistry: https://pdb101.rcsb.org/motm/276
• RCSB PDB-101 Molecular Landscapes: Excitatory and Inhibitory Synapses: https://pdb101.rcsb.org/sci-art/goodsell-gallery/excitatory-and-inhibitory-synapses
• Acetylcholinesterase inhibition by fasciculin: https://www.youtube.com/watch?v=zLuObW3huks
• Stucture of acetylcholinesterases, by Zoran Radic: https://www.youtube.com/watch?v=sKCDx_2s66w
• Acetylcholinesterase: A gorge-ous enzyme: https://www.youtube.com/watch?v=ZrJVVP8Nxtk
• Electric Eel, by Irwin Moon: https://archive.org/details/electric_eel/electric_eel.mpeg
• Les substances actives sur le récepteur nicotinique à l’acétylcholine – Un exemple d’enjeu de préservation de la biodiversité: https://www.pedagogie.ac-nice.fr/svt/productions/html/recepteur-nicotinique-biodiversite/recepteur_nicotinique_biodiversite/index.html