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Igor E. Kasheverov
Researcher at Russian Academy of Sciences
Publications - 103
Citations - 1837
Igor E. Kasheverov is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Nicotinic agonist & Acetylcholine receptor. The author has an hindex of 21, co-authored 95 publications receiving 1595 citations. Previous affiliations of Igor E. Kasheverov include I.M. Sechenov First Moscow State Medical University & Russian Academy.
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Journal ArticleDOI
Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant.
Patrick H.N. Celie,Igor E. Kasheverov,Dmitry Y. Mordvintsev,Ron C. Hogg,Pim van Nierop,René van Elk,Sarah E. van Rossum-Fikkert,Maxim N. Zhmak,Daniel Bertrand,Victor I. Tsetlin,Titia K. Sixma,August B. Smit +11 more
TL;DR: The structure at a resolution of 2.4 Å of α-Ctx PnIA (A10L D14K), a potent blocker of the α7-nAChR, bound with high affinity to acetylcholine binding protein (AChBP), the prototype for the ligand-binding domains of the nA ChR superfamily is presented.
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NMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1
Ekaterina N. Lyukmanova,Zakhar O. Shenkarev,Mikhail A. Shulepko,Konstantin S. Mineev,Dieter D’hoedt,Igor E. Kasheverov,Sergey Yu. Filkin,Alexandra P. Krivolapova,Helena Janickova,Vladimir Dolezal,Dmitry A. Dolgikh,Dmitry A. Dolgikh,Alexander S. Arseniev,Daniel Bertrand,Victor I. Tsetlin,Mikhail P. Kirpichnikov,Mikhail P. Kirpichnikov +16 more
TL;DR: The NMR spatial structure for the water-soluble domain of human LYNX1 lacking a GPI anchor and its concentration-dependent activity on nicotinic acetylcholine receptors (nAChRs) is reported and computer modeling revealed a possible mode of ws-LYNX1 binding.
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Assembly of nicotinic and other Cys‐loop receptors
TL;DR: In this paper, the role of the extracellular ligand-binding, membrane and cytoplasmic domains in the assembly of Cys-loop receptors is discussed.
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Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1) Is a Selective Allosteric Antagonist of α7 Nicotinic Acetylcholine Receptor
Ekaterina N. Lyukmanova,Ekaterina N. Lyukmanova,Mikhail A. Shulepko,Mikhail A. Shulepko,Denis S. Kudryavtsev,M L Bychkov,M L Bychkov,D.S. Kulbatskii,D.S. Kulbatskii,Igor E. Kasheverov,M. V. Astapova,Alexey V. Feofanov,Alexey V. Feofanov,Morten S. Thomsen,Jens D. Mikkelsen,Zakhar O. Shenkarev,Zakhar O. Shenkarev,Zakhar O. Shenkarev,Victor I. Tsetlin,Dmitry A. Dolgikh,Dmitry A. Dolgikh,Mikhail P. Kirpichnikov,Mikhail P. Kirpichnikov +22 more
TL;DR: It was shown that rSLURP-1 binds to α7-nAChRs overexpressed in GH4Cl cells, but does not compete with 125I-α-bungarotoxin for binding to the receptor, implying an allosteric antagonist-like mode of SLURp-1 interaction with α 7-n AChRs outside the classical ligand-binding site.
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Naturally occurring disulfide-bound dimers of three-fingered toxins: a paradigm for biological activity diversification.
Alexey V. Osipov,Igor E. Kasheverov,Yana V. Makarova,Vladislav G. Starkov,Olga V. Vorontsova,Rustam Ziganshin,T. V. Andreeva,Marina V. Serebryakova,Audrey Benoit,Ron C Hogg,Daniel Bertrand,Victor I. Tsetlin,Yuri N. Utkin +12 more
TL;DR: Electrophysiological experiments on neuronal nAChRs expressed in Xenopus oocytes have shown that α-cobratoxin dimer not only interacts with α7 nA chR but, in contrast to α- cobrat toxin monomer, also blocks α3β2 nA ChR.