Vishnivetskiy SA - Search Results

1

G Protein-Coupled Receptor Kinase 2 (GRK2) and 5 (GRK5) Exhibit Selective Phosphorylation of the Neurotensin Receptor in Vitro.

Inagaki S, Ghirlando R, Vishnivetskiy SA, Homan KT, White JF, Tesmer JJ, Gurevich VV, Grisshammer R. Inagaki S, et al. Among authors: vishnivetskiy sa. Biochemistry. 2015 Jul 21;54(28):4320-9. doi: 10.1021/acs.biochem.5b00285. Epub 2015 Jul 8. Biochemistry. 2015. PMID: 26120872 Free PMC article.

2

How does arrestin respond to the phosphorylated state of rhodopsin?

Vishnivetskiy SA, Paz CL, Schubert C, Hirsch JA, Sigler PB, Gurevich VV. Vishnivetskiy SA, et al. J Biol Chem. 1999 Apr 23;274(17):11451-4. doi: 10.1074/jbc.274.17.11451. J Biol Chem. 1999. PMID: 10206946 Free article.

3

Conserved phosphoprotein interaction motif is functionally interchangeable between ataxin-7 and arrestins.

Mushegian AR, Vishnivetskiy SA, Gurevich VV. Mushegian AR, et al. Among authors: vishnivetskiy sa. Biochemistry. 2000 Jun 13;39(23):6809-13. doi: 10.1021/bi992694y. Biochemistry. 2000. PMID: 10841760

4

An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation.

Vishnivetskiy SA, Schubert C, Climaco GC, Gurevich YV, Velez MG, Gurevich VV. Vishnivetskiy SA, et al. J Biol Chem. 2000 Dec 29;275(52):41049-57. doi: 10.1074/jbc.M007159200. J Biol Chem. 2000. PMID: 11024026 Free article.

5

Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation.

Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. Han M, et al. Among authors: vishnivetskiy sa. Structure. 2001 Sep;9(9):869-80. doi: 10.1016/s0969-2126(01)00644-x. Structure. 2001. PMID: 11566136 Free article.

6

Conservation of the phosphate-sensitive elements in the arrestin family of proteins.

Celver J, Vishnivetskiy SA, Chavkin C, Gurevich VV. Celver J, et al. Among authors: vishnivetskiy sa. J Biol Chem. 2002 Mar 15;277(11):9043-8. doi: 10.1074/jbc.M107400200. Epub 2002 Jan 8. J Biol Chem. 2002. PMID: 11782458 Free article.

7

Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge.

Vishnivetskiy SA, Hirsch JA, Velez MG, Gurevich YV, Gurevich VV. Vishnivetskiy SA, et al. J Biol Chem. 2002 Nov 15;277(46):43961-7. doi: 10.1074/jbc.M206951200. Epub 2002 Sep 4. J Biol Chem. 2002. PMID: 12215448 Free article.

8

Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins.

Vishnivetskiy SA, Hosey MM, Benovic JL, Gurevich VV. Vishnivetskiy SA, et al. J Biol Chem. 2004 Jan 9;279(2):1262-8. doi: 10.1074/jbc.M308834200. Epub 2003 Oct 6. J Biol Chem. 2004. PMID: 14530255 Free article.

9

Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.

Nair KS, Hanson SM, Mendez A, Gurevich EV, Kennedy MJ, Shestopalov VI, Vishnivetskiy SA, Chen J, Hurley JB, Gurevich VV, Slepak VZ. Nair KS, et al. Among authors: vishnivetskiy sa. Neuron. 2005 May 19;46(4):555-67. doi: 10.1016/j.neuron.2005.03.023. Neuron. 2005. PMID: 15944125 Free PMC article.

10

Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity.

Sutton RB, Vishnivetskiy SA, Robert J, Hanson SM, Raman D, Knox BE, Kono M, Navarro J, Gurevich VV. Sutton RB, et al. Among authors: vishnivetskiy sa. J Mol Biol. 2005 Dec 16;354(5):1069-80. doi: 10.1016/j.jmb.2005.10.023. Epub 2005 Nov 2. J Mol Biol. 2005. PMID: 16289201

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