Výsledky vyhledávání

Analysis of 51 cyclodipeptide synthases reveals the basis for substrate specificity

Autor: Jerzy Witwinowski, Emmanuelle Darbon, Steven Dubois, Isabelle Jacques, Jérôme Seguin, Robert Thai, Mireille Moutiez, Cécile Martel, Emmanuel Favry, Jean-Luc Pernodet, Alain Lecoq, Muriel Gondry, Pascal Belin

Publikováno v: Nature Chemical Biology
Nature Chemical Biology, Nature Publishing Group, 2015, 11 (9), pp.721-7. ⟨10.1038/nchembio.1868⟩
Nature Chemical Biology, Nature Publishing Group, 2015, 11 (9), pp.721-7. 〈10.1038/nchembio.1868〉
Nature Chemical Biology, 2015, 11 (9), pp.721-7. ⟨10.1038/nchembio.1868⟩

International audience; Cyclodipeptide synthases (CDPSs) constitute a family of peptide bond-forming enzymes that use aminoacyl-tRNAs for the synthesis of cyclodipeptides. Here, we describe the activity of 41 new CDPSs. We also show that CDPSs can be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50d26fe9b28ed1969a4990f0b81631d5
https://hal.archives-ouvertes.fr/hal-01430815

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Structure of the BgK-Kv1.1 Complex Based on Distance Restraints Identified by Double Mutant Cycles

Autor: Anja Wrisch, Bernard Gilquin, Judith Racapé, André Ménez, Stephan Grissmer, Sylvaine Gasparini, Alain Lecoq, Violeta Visan

Publikováno v: Journal of Biological Chemistry. 277:37406-37413

A structural model of BgK, a sea anemone toxin, complexed with the S5-S6 region of Kv1.1, a voltage-gated potassium channel, was determined by flexible docking under distance restraints identified by a double mutant cycles approach. This structure pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::63b08277bb6a3dc242c3098f32beccd2
https://doi.org/10.1074/jbc.m206205200

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Characterization of a Novel Radiolabeled Peptide Selective for a Subpopulation of Voltage-gated Potassium Channels in Mammalian Brain

Autor: Régine Romi-Lebrun, Alain Lecoq, Martin Köhler, Sylvaine Gasparini, André Ménez, Jessica Liu, Maria L. Garcia, Judith Racapé

Publikováno v: Journal of Biological Chemistry. 277:3886-3893

BgK, a 37-amino acid voltage-gated potassium (Kv) 1 channel blocker isolated from the sea anemone Bunodosoma granulifera, can be modified at certain positions to alter its pharmacological profile (Alessandri-Haber, N., Lecoq, A., Gasparini, S., Grang

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f30891e7aa094d6cef63fbe8e1910ad3
https://doi.org/10.1074/jbc.m109886200

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Delineation of the Functional Site of α-Dendrotoxin

Autor: Edward G. Rowan, Cleane C.L. de Medeiros, Alan L. Harvey, Suzanne Pinkasfeld, Alain Lecoq, Sylvaine Gasparini, Louise C. Young, André Ménez, Jean-Marc Danse, Sophie Zinn-Justin

Publikováno v: Journal of Biological Chemistry. 273:25393-25403

We identified the residues that are important for the binding of α-dendrotoxin (αDTX) to Kv1 potassium channels on rat brain synaptosomal membranes, using a mutational approach based on site-directed mutagenesis and chemical synthesis. Twenty-six o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::749562b3583f840f310ef47580d8c38a
https://doi.org/10.1074/jbc.273.39.25393

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On the Convergent Evolution of Animal Toxins

Autor: Marc Dauplais, Alain Lecoq, Jianxing Song, Joël Cotton, Nadège Jamin, Bernard Gilquin, Christian Roumestand, Claudio Vita, CleaneL.C. de Medeiros, Edward G. Rowan, Alan L. Harvey, André Ménez

Publikováno v: Journal of Biological Chemistry. 272:4302-4309

BgK is a K+ channel-blocking toxin from the sea anemone Bunodosoma granulifera It is a 37-residue protein that adopts a novel fold, as determined by NMR and modeling. An alanine-scanning-based analysis revealed the functional importance of five resid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b03afff710525b5cf190a8203023fd8a
https://doi.org/10.1074/jbc.272.7.4302

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Identification and functional characterization of a novel α-conotoxin (EIIA) from Conus ermineus

Autor: Nicolas Gilles, Emmanuelle Girard, El Ali Haidar, Jean-Pierre Le Caer, Denis Servent, Julia Chamot-Rooke, Jordi Molgó, Christian Malosse, Alain Lecoq, Loïc Quinton

Publikováno v: Analytical and Bioanalytical Chemistry
Analytical and Bioanalytical Chemistry, Springer Verlag, 2013, 405 (15), pp.5341-51. ⟨10.1007/s00216-013-6926-x⟩
Analytical and Bioanalytical Chemistry, 2013, 405 (15), pp.5341-51. ⟨10.1007/s00216-013-6926-x⟩

International audience; Nicotinic acetylcholine receptors (nAChRs) are one of the most important families in the ligand-gated ion channel superfamily due to their involvement in primordial brain functions and in several neurodegenerative pathologies.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d352681065f96d4d6c7b361d545300f
https://hal.archives-ouvertes.fr/hal-00850305

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Development of Highly Potent and Selective Phosphinic Peptide Inhibitors of Zinc Endopeptidase 24-15 Using Combinatorial Chemistry

Autor: Bruno Vincent, Vincent Dive, Alain Lecoq, Frédéric Checler, Athanasios Yiotakis, Anna Nicolaou, Jiri Jiracek

Publikováno v: Scopus-Elsevier
University of Manchester-PURE
ResearcherID

Several hundred phosphinic peptides having the general formula Z-(L,D)Phe psi (PO2CH2)(L,D)Xaa'-Yaa'-Zaa', where Xaa' = Gly or Ala and Yaa' and Zaa' represent 20 different amino acids, have been synthesized by the combinatorial chemistry approach. Pe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abff0967e5bab29de0379841765c5b38
https://doi.org/10.1074/jbc.270.37.21701

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Synthesis of 1-(N-Benzyloxycarbonylamino)-5-(N-terbutyloxycarbonylamino)pentylphosphinic Acid

Autor: Vincent Dive, Athanasis Yiotakis, Alain Lecoq

Publikováno v: Synthetic Communications. 24:2877-2882

A procedure for the preparation of the suitable protected phosphinic analogue of lysine is described, starting from the commercially available 3-4 dihydro-2H pyran.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::202531df0cd2680d0adbdaee88d30f5d
https://doi.org/10.1080/00397919408010608

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Cyclic Peptides with a Phosphinic Bond as Potent Inhibitors of a Zinc Bacterial Collagenase

Autor: Stamatia Vassiliou, Philippe Cuniasse, Alain Lecoq, Vincent Dive, Athanasios Yiotakis, Isabelle Raynal

Publikováno v: Journal of Medicinal Chemistry. 37:2713-2720

A series of cyclic peptides containing a phosphinic bond were synthesized and evaluated as inhibitors of a zinc bacterial collagenase from Corynebacterium rathaii. Among this series of pseudopeptides of different sizes of cycles, only two molecules I

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff754b42825e8813f122c03da76afbcd
https://doi.org/10.1021/jm00043a011

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