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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

High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor

TL;DR: Although the location of carazolol in the β2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family.
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The 2.6 Angstrom Crystal Structure of a Human A2A Adenosine Receptor Bound to an Antagonist.

TL;DR: The crystal structure of the human A2A adenosine receptor is determined, in complex with a high-affinity subtype-selective antagonist, ZM241385, to 2.6 angstrom resolution and suggests a role for ZM 241385 in restricting the movement of a tryptophan residue important in the activation mechanism of the class A receptors.
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Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists.

TL;DR: Five independent crystal structures of CXCR4 bound to an antagonist small molecule IT1t and a cyclic peptide CVX15 at 2.5 to 3.2 angstrom resolution reveal a consistent homodimer with an interface including helices V and VI that may be involved in regulating signaling.
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GPCR Engineering Yields High-Resolution Structural Insights into β2-Adrenergic Receptor Function

TL;DR: Analysis of adrenergic receptor ligand-binding mutants within the context of the reported high-resolution structure of β2AR-T4L provides insights into inverse-agonist binding and the structural changes required to accommodate catecholamine agonists.
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Structure of the human dopamine d3 receptor in complex with a d2/d3 selective antagonist.

TL;DR: The crystal structure of the human dopamine D3 receptor in complex with the small molecule D2R/D3R-specific antagonist eticlopride reveals important features of the ligand binding pocket and extracellular loops.