V
Vadim Cherezov
Researcher at University of Southern California
Publications - 196
Citations - 32307
Vadim Cherezov is an academic researcher from University of Southern California. The author has contributed to research in topics: G protein-coupled receptor & Receptor. The author has an hindex of 72, co-authored 180 publications receiving 28950 citations. Previous affiliations of Vadim Cherezov include Indiana University – Purdue University Indianapolis & Moscow Institute of Physics and Technology.
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Journal ArticleDOI
Fusion partner toolchest for the stabilization and crystallization of G protein-coupled receptors
Eugene Chun,Aaron Thompson,Wei Liu,Christopher B. Roth,Mark T. Griffith,Vsevolod Katritch,Joshua Kunken,Fei Xu,Vadim Cherezov,Michael A. Hanson,Raymond C. Stevens +10 more
TL;DR: Use of the thermostabilized apocytochrome b(562)RIL as a fusion partner displays certain advantages over previously utilized fusion proteins, resulting in a significant improvement in stability and structure of GPCR-fusion constructs.
Journal ArticleDOI
Generic GPCR residue numbers – aligning topology maps while minding the gaps
Vignir Isberg,Chris de Graaf,Andrea Bortolato,Vadim Cherezov,Vsevolod Katritch,Fiona H. Marshall,Stefan Mordalski,Stefan Mordalski,Jean-Philippe Pin,Jean-Philippe Pin,Raymond C. Stevens,Gerrit Vriend,David E. Gloriam +12 more
TL;DR: This work reviews the generic residue numbering schemes for each GPCR class, as well as a complementary structure-based scheme, and provides illustrative examples and G PCR database (GPCRDB) web tools to number any receptor sequence or structure.
Journal ArticleDOI
Conserved Binding Mode of Human β2 Adrenergic Receptor Inverse Agonists and Antagonist Revealed by X-ray Crystallography
Daniel Wacker,Gustavo Fenalti,Monica A. Brown,Vsevolod Katritch,Ruben Abagyan,Vadim Cherezov,Raymond C. Stevens +6 more
TL;DR: Receptor ligand cross-docking experiments revealed that a single beta(2)AR complex can be suitable for docking of a range of antagonists and inverse agonists but also indicate that additional ligand-receptor structures may be useful to further improve performance for in-silico docking or lead-optimization in drug design.
Journal ArticleDOI
Structure of the human P2Y12 receptor in complex with an antithrombotic drug
Kaihua Zhang,Jin Zhang,Zhan-Guo Gao,Dandan Zhang,Lan Zhu,Gye Won Han,Steven M. Moss,Silvia Paoletta,Evgeny Kiselev,Weizhen Lu,Gustavo Fenalti,Wenru Zhang,Christa E. Müller,Huaiyu Yang,Hualiang Jiang,Vadim Cherezov,Vsevolod Katritch,Kenneth A. Jacobson,Raymond C. Stevens,Beili Wu,Qiang Zhao +20 more
TL;DR: The 2.6 Å resolution crystal structure of human P2Y12R in complex with a non-nucleotide reversible antagonist, AZD1283, reveals a distinct straight conformation of helix V, which sets P2y12R apart from all other known class A GPCR structures.
Journal ArticleDOI
Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors
X. Edward Zhou,X. Edward Zhou,Yuanzheng He,Parker W. de Waal,Xiang Gao,Yanyong Kang,Ned Van Eps,Yanting Yin,Yanting Yin,Kuntal Pal,Devrishi Goswami,Thomas A. White,Anton Barty,Naomi R. Latorraca,Henry N. Chapman,Wayne L. Hubbell,Ron O. Dror,Raymond C. Stevens,Raymond C. Stevens,Vadim Cherezov,Vsevolod V. Gurevich,Patrick R. Griffin,Oliver P. Ernst,Karsten Melcher,H. Eric Xu,H. Eric Xu +25 more
TL;DR: An X-ray free electron laser (XFEL) crystal structure of the rhodopsin-arrestin complex is reported, in which the phosphorylated C terminus of r Rhodopsin forms an extended intermolecular β sheet with the N-terminal β strands of arrestin.