About: Vsevolod V. Gurevich

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

pharmacologist

Attributes	Values
rdf:type	Item
description	pharmacologist (en) фармаколог (ru) ikertzailea (eu) 연구원 (ko) ricercatore (it) 研究者 (ja) wetenschapper (nl) дослідник (uk) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtues (sq)
rdfs:label	Vsevolod V. Gurevich (en) Vsevolod V. Gurevich (es) Vsevolod V. Gurevich (nl) Vsevolod V. Gurevich (sl) Vsevolod V. Gurevich (ast) Всеволод В. Гуревич (ru)
skos:prefLabel	Vsevolod V. Gurevich (en) Vsevolod V. Gurevich (es) Vsevolod V. Gurevich (nl) Vsevolod V. Gurevich (sl) Vsevolod V. Gurevich (ast) Всеволод В. Гуревич (ru)
name	Vsevolod V. Gurevich (en) Vsevolod V. Gurevich (es) Vsevolod V. Gurevich (nl) Vsevolod V. Gurevich (sl) Vsevolod V. Gurevich (ast) Всеволод В. Гуревич (ru)
affiliation	wds:Q42173663-990A1726-CBD4-40EA-B14A-F9DBC9B9CBCB
affiliation	Vanderbilt Department of Pharmacology
Scopus author ID	wds:Q42173663-8D02034D-BD54-4BC2-A0EB-D8579A4768CE
Scopus author ID	24294144900
given name	wds:Q42173663-b64b5577-49ea-90b1-28c5-e32d35d153f6
given name	Vsevolod
instance of	wds:Q42173663-F459B365-0AC6-4199-A2FC-272D9C7697A7
instance of	Homo sapiens
skos:altLabel	Seva Gurevich (en) Vsevolod Gurevich (en) Wsewolod Gurewitsch (de) Всеволод Гуревич (ru) Гуревич, Всеволод В. (ru)
occupation	wds:Q42173663-F3C0477E-1BEE-4DAC-A608-5AB258F860F3 wds:Q42173663-dea0bb00-4625-de90-4841-3790e0ab2821
employer	wds:Q42173663-261293BC-7B60-4F27-BB25-2923C853AFA9
sex or gender	wds:Q42173663-5C462382-64D5-4A58-8196-BD1245BFE0B1
VIAF ID	wds:Q42173663-1ADE5093-A454-42E9-8EB2-D68B87382D33
Library of Congress authority ID	wds:Q42173663-04F40928-2DD7-41A3-A1C9-25570D1EC51F
IdRef ID	wds:Q42173663-F1F86FED-E120-4C27-BFE4-7BB1C3F4853D
educated at	wds:Q42173663-65714c7d-4248-360c-f512-aa2d981ed441
family name	wds:Q42173663-eb0c84bd-4439-86da-8153-8fed93899be4
WorldCat Identities ID (superseded)	wds:Q42173663-A773E9BC-8298-4116-976A-85232846528B
National Library of Israel J9U ID	wds:Q42173663-BFA763A6-F1DD-4BB0-9481-C218C51E564D
VIAF ID	http://viaf.org/viaf/306384070
Library of Congress authority ID	http://id.loc.gov/authorities/names/nb2014003571
IdRef ID	http://www.idref.fr/177320818/id
occupation	pharmacologist researcher
employer	Vanderbilt University
sex or gender	male
VIAF ID	306384070
Library of Congress authority ID	nb2014003571
IdRef ID	177320818
educated at	Moscow State University
family name	Gurevich
WorldCat Identities ID (superseded)	lccn-nb2014003571
National Library of Israel J9U ID	987007335853405171
ORCID iD	wds:Q42173663-89769C47-56CF-4E11-8974-A9AD794D9B45
ORCID iD	https://orcid.org/0000-0002-3950-5351
ORCID iD	0000-0002-3950-5351
ResearcherID	wds:Q42173663-20A5AD31-DCDE-42F9-8026-D25ED4DF28AF
Publons author ID	wds:Q42173663-250111e8-b310-4e88-99ef-a6b3db0eaa26
ResearcherID	A-3236-2008
Publons author ID	1378406
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42173663
is author of	Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation Arrestins: ubiquitous regulators of cellular signaling pathways The structural basis of arrestin-mediated regulation of G-protein-coupled receptors The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation The molecular acrobatics of arrestin activation Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin ARF6: a newly appreciated player in G protein-coupled receptor desensitization The new face of active receptor bound arrestin attracts new partners Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm Visual arrestin binding to microtubules involves a distinct conformational change The differential engagement of arrestin surface charges by the various functional forms of the receptor Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin. Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms. Conserved Phosphoprotein Interaction Motif Is Functionally Interchangeable between Ataxin-7 and Arrestins† Arrestin2 expression selectively increases during neural differentiation Lentiviral overexpression of GRK6 alleviates L-dopa-induced dyskinesia in experimental Parkinson's disease Altered expression and subcellular distribution of GRK subtypes in the dopamine-depleted rat basal ganglia is not normalized by l-DOPA treatment

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