WorldCat Identities

Gurevich, Vsevolod V.

Works: 12 works in 51 publications in 2 languages and 774 library holdings
Genres: Laboratory manuals 
Roles: Editor, Author, htt, Contributor, Other, Publishing director
Classifications: QP905, 571.6
Publication Timeline
Most widely held works by Vsevolod V Gurevich
Arrestins--pharmacology and therapeutic potential by Vsevolod V Gurevich( )

20 editions published between 2014 and 2016 in English and held by 374 WorldCat member libraries worldwide

"This volume describes our current understanding of the biological role of visual and non-visual arrestins in different cells and tissues, focusing on the mechanisms of arrestin-mediated regulation of GPCRs and non-receptor signaling proteins in health and disease. The book covers wide range of arrestin functions, emphasizing therapeutic potential of targeting arrestin interactions with individual partners"--Publisher's description
The structural basis of arrestin functions( )

11 editions published between 2017 and 2018 in English and German and held by 247 WorldCat member libraries worldwide

This volume summarizes our current understanding of the structural basis of the functions of arrestin family of proteins. Arrestins were first discovered as key players in the desensitization of G protein-coupled receptors (GPCRs). Recent studies showed that arrestins are important signal transducers in their own right, organizing multi-protein complexes and scaffolding numerous signaling cascades that regulate cell proliferation, differentiation, and apoptotic death. Here arrestin functions are described primarily from the structural prospective. The book covers basal structure of arrestin proteins, receptor binding-induced conformational changes in arrestins, as well as the structure of "pre-activated" mutants. Particular focus is on the arrestin elements interacting with numerous binding partners, GPCRs and cytoplasmic signaling proteins. We expect that this information and insights will help to understand and exploit the phenomenon of signaling bias, which is a new promising direction in drug discovery. The chapters are written by the world-class specialists in the field, mostly the people who actually contributed the data discussed. The book gives coherent historical prospective and describes the most recent findings. The book would be particularly useful for scientists in academia and industry working in the fields of pharmacology, cell biology, structural biology, and drug discovery. We expect that the focus on the molecular basis of protein-protein interactions would help to develop novel tools for engaging this important type of targets for research and therapeutic purposes
G protein-coupled receptor kinases by Vsevolod V Gurevich( )

11 editions published in 2016 in English and held by 138 WorldCat member libraries worldwide

This collection explores up-to-date descriptions of known G protein-coupled receptor kinase (GRK)-dependent mechanisms, both associated with G protein-coupled receptor (GPCR) functions and the receptor-independent. The chapters cover a wide range of studies from invertebrates to humans, with sections of the volume covering GRK structure, mechanisms of activation, and interaction with GPCRs, GRKs in cell signaling, as well as physiological and pathophysiological mechanisms regulated by GRKs. Written for the Methods in Pharmacology and Toxicology series, this book features the kind of practical detail necessary for success in the laboratory. Authoritative and timely, G Protein-Coupled Receptor Kinases features the kind of comprehensive mechanistic elucidation of GRK functions and their regulation in cells necessary for a better understanding of cell biology as well as for devising novel research approaches and therapeutic strategies
Arrestins: ubiquitous regulators of cellular signaling pathways by Eugenia V Gurevich( )

1 edition published in 2006 in English and held by 2 WorldCat member libraries worldwide

Plethora of functions packed into 45 kDa arrestins: biological implications and possible therapeutic strategies by Vsevolod V Gurevich( )

1 edition published in 2019 in English and held by 2 WorldCat member libraries worldwide

Arrestins: structural disorder creates rich functionality by Vsevolod V Gurevich( )

1 edition published in 2018 in English and held by 2 WorldCat member libraries worldwide

Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes by Henrike Indrischek( )

1 edition published in 2017 in English and held by 2 WorldCat member libraries worldwide

Protein multi-functionality: introduction by Vsevolod V Gurevich( )

1 edition published in 2019 in English and held by 2 WorldCat member libraries worldwide

GPCR structure, function, drug discovery and crystallography: report from Academia-Industry International Conference (UK Royal Society) Chicheley Hall, 1-2 September 2014 by Alexander Heifetz( )

1 edition published in 2015 in English and held by 2 WorldCat member libraries worldwide

Arrestin-2 and arrestin-3 differentially modulate locomotor responses and sensitization to amphetamine( )

1 edition published in 2017 in English and held by 1 WorldCat member library worldwide

Abstract: Arrestins play a prominent role in shutting down signaling via G protein-coupled receptors. In recent years, a signaling role for arrestins independent of their function in receptor desensitization has been discovered. Two ubiquitously expressed arrestin isoforms, arrestin-2 and arrestin-3, perform similarly in the desensitization process and share many signaling functions, enabling them to substitute for one another. However, signaling roles specific to each isoform have also been described. Mice lacking arrestin-3 (ARR3KO) were reported to show blunted acute responsiveness to the locomotor stimulatory effect of amphetamine (AMPH). It has been suggested that mice with deletion of arrestin-2 display a similar phenotype. Here we demonstrate that the AMPH-induced locomotion of male ARR3KO mice is reduced over the 7-day treatment period and during AMPH challenge after a 7-day withdrawal. The data are consistent with impaired locomotor sensitization to AMPH and suggest a role for arrestin-3-mediated signaling in the sensitization process. In contrast, male ARR2KO mice showed enhanced early responsiveness to AMPH and the lack of further sensitization, suggesting a role for impaired receptor desensitization. The comparison of mice possessing one allele of arrestin-3 and no arrestin-2 with ARR2KO littermates revealed reduced activity of the former line, consistent with a contribution of arrestin-3-mediated signaling to AMPH responses. Surprisingly, ARR3KO mice with one arrestin-2 allele showed significantly reduced locomotor responses to AMPH combined with lower novelty-induced locomotion, as compared to the ARR3KO line. These data suggest that one allele of arrestin-2 is unable to support normal locomotor behavior due to signaling and/or developmental defects. Graphical abstract: Highlights: Mice lacking arrestin-2 show initially enhanced locomotor response to amphetamine. Mice lacking arrestin-3 are hyposensitive to amphetamine with poor sensitization. Single allele mice with only one arrestin-2 allele are grossly hyposensitive to amphetamine. Single allele mice with only one arrestin-2 allele show reduced basal locomotion
Structural Basis of Arrestin-Dependent Signal Transduction( )

1 edition published in 2018 in English and held by 1 WorldCat member library worldwide

Abstract : Arrestins are a small family of proteins with four isoforms in humans. Remarkably, two arrestins regulate signaling from>800 G protein-coupled receptors (GPCRs) or nonreceptor activators by simultaneously binding an activator and one out of hundreds of other signaling proteins. When arrestins are bound to GPCRs or other activators, the affinity for these signaling partners changes. Thus, it is proposed that an activator alters arrestin's ability to transduce a signal. The comparison of all available arrestin structures identifies several common conformational rearrangements associated with activation. In particular, it identifies elements that are directly involved in binding to GPCRs or other activators, elements that likely engage distinct downstream effectors, and elements that likely link the activator-binding sites with the effector-binding sites. Highlights: Free arrestins have very similar conformations in crystal structures, with the relative orientation of the two domains held by several intramolecular interactions. These interactions are destabilized by activators: active phosphorylated GPCRs and inositol hexakisphosphate (IP6), an inositol metabolite abundant in the cytoplasm. The latest high-resolution structure of the nonvisual arrestin-3 with IP6 suggests molecular mechanisms of arrestin activation that induce characteristic rearrangements in the arrestin molecule. Arrestin-1, -2, and -3, activated by different means, demonstrate a global conformational rearrangement. In particular, several elements of activated arrestins dramatically change their conformation from basal to active, which is very similar in all arrestin subtypes. These elements (that we propose to call 'arrestin switches', by analogy with G protein switch regions) are likely docking sites for the signaling and trafficking proteins that preferentially bind active arrestins. As arrestins bind numerous protein partners, narrowing the search of their docking sites to arrestin switch regions will greatly facilitate the identification of the elements and individual residues specific for each interaction. Identification of the binding sites of nonreceptor signaling proteins paves the way for the design of signaling-biased arrestins, where particular capabilities are specifically disabled or enhanced. This would be a novel, potent tool for targeted manipulation of cell signaling for research and therapy
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1 edition published in 2012 in English and held by 1 WorldCat member library worldwide

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  Kids General Special  
Audience level: 0.54 (from 0.49 for Arrestins- ... to 0.97 for G protein- ...)

G protein-coupled receptor kinases
G protein-coupled receptor kinases
Alternative Names
Gourevitch, Vsevolod

Gurevič, Vsevolod Veniaminovič

Gurevich, Seva

Gurevich, Vsevolod Veniaminovich

Vsevolod V. Gurevich pharmacologist

Vsevolod V. Gurevich wetenschapper

Гуревич, В. В.

Гуревич, Всеволод Вениаминович

English (50)

German (1)