Sergey A Vishnivetskiy
Overview
Explore the profile of Sergey A Vishnivetskiy including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
64
Citations
2785
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Vishnivetskiy S, Paul T, Gurevich E, Gurevich V
Int J Mol Sci
. 2025 Jan;
26(2).
PMID: 39859432
Sequences and three-dimensional structures of the four vertebrate arrestins are very similar, yet in sharp contrast to other subtypes, arrestin-1 demonstrates exquisite selectivity for the active phosphorylated form of its...
2.
Zheng C, Nguyen K, Vishnivetskiy S, Gurevich V, Gurevich E
J Neurochem
. 2024 Jan;
169(1):e16043.
PMID: 38196269
Arrestins were discovered for their role in homologous desensitization of G-protein-coupled receptors (GPCRs). Later non-visual arrestins were shown to regulate several signaling pathways. Some of these pathways require arrestin binding...
3.
Vishnivetskiy S, Zhan X, Gurevich V
Curr Protoc
. 2023 Sep;
3(9):e832.
PMID: 37671938
Purified arrestin proteins are necessary for biochemical, biophysical, and structural studies of these versatile regulators of cell signaling. Described herein is a basic protocol for arrestin expression in Escherichia coli...
4.
Vishnivetskiy S, Weinstein L, Zheng C, Gurevich E, Gurevich V
Int J Mol Sci
. 2023 May;
24(10).
PMID: 37240250
Arrestin-1, or visual arrestin, exhibits an exquisite selectivity for light-activated phosphorylated rhodopsin (P-Rh*) over its other functional forms. That selectivity is believed to be mediated by two well-established structural elements...
5.
Vishnivetskiy S, Huh E, Karnam P, Oviedo S, Gurevich E, Gurevich V
Int J Mol Sci
. 2022 Nov;
23(22).
PMID: 36430370
Arrestins preferentially bind active phosphorylated G protein-coupled receptors (GPCRs). The middle loop, highly conserved in all arrestin subtypes, is localized in the central crest on the GPCR-binding side. Upon receptor...
6.
Perry-Hauser N, Hopkins J, Zhuo Y, Zheng C, Perez I, Schultz K, et al.
J Mol Biol
. 2022 Jan;
434(7):167465.
PMID: 35077767
Arrestin binding to active phosphorylated G protein-coupled receptors terminates G protein coupling and initiates another wave of signaling. Among the effectors that bind directly to receptor-associated arrestins are extracellular signal-regulated...
7.
Perez I, Berndt S, Agarwal R, Castro M, Vishnivetskiy S, Smith J, et al.
J Mol Biol
. 2021 Dec;
434(2):167400.
PMID: 34902430
Arrestins regulate a wide range of signaling events, most notably when bound to active G protein-coupled receptors (GPCRs). Among the known effectors recruited by GPCR-bound arrestins are Src family kinases,...
8.
Karnam P, Vishnivetskiy S, Gurevich V
Int J Mol Sci
. 2021 Nov;
22(22).
PMID: 34830362
Arrestins are a small family of proteins that bind G protein-coupled receptors (GPCRs). Arrestin binds to active phosphorylated GPCRs with higher affinity than to all other functional forms of the...
9.
Chen Q, Zhuo Y, Sharma P, Perez I, Francis D, Chakravarthy S, et al.
J Mol Biol
. 2021 Jan;
433(4):166790.
PMID: 33387531
G protein coupled receptors signal through G proteins or arrestins. A long-standing mystery in the field is why vertebrates have two non-visual arrestins, arrestin-2 and arrestin-3. These isoforms are ~75%...
10.
Vishnivetskiy S, Huh E, Gurevich E, Gurevich V
J Neurochem
. 2020 Nov;
157(4):1138-1152.
PMID: 33159335
The finger loop in the central crest of the receptor-binding site of arrestins engages the cavity between the transmembrane helices of activated G-protein-coupled receptors. Therefore, it was hypothesized to serve...