Gurevich VV - Search Results

1

A model for the solution structure of the rod arrestin tetramer.

Hanson SM, Dawson ES, Francis DJ, Van Eps N, Klug CS, Hubbell WL, Meiler J, Gurevich VV. Hanson SM, et al. Among authors: gurevich vv. Structure. 2008 Jun;16(6):924-34. doi: 10.1016/j.str.2008.03.006. Structure. 2008. PMID: 18547524 Free PMC article.

2

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: gurevich vv. 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.

3

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. Among authors: gurevich vv, gurevich yv. 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.

4

The new face of active receptor bound arrestin attracts new partners.

Gurevich VV, Gurevich EV. Gurevich VV, et al. Among authors: gurevich ev. Structure. 2003 Sep;11(9):1037-42. doi: 10.1016/s0969-2126(03)00184-9. Structure. 2003. PMID: 12962621 Free article. Review.

5

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. Among authors: gurevich vv. 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.

6

Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors.

Nair KS, Hanson SM, Kennedy MJ, Hurley JB, Gurevich VV, Slepak VZ. Nair KS, et al. Among authors: gurevich vv. J Biol Chem. 2004 Sep 24;279(39):41240-8. doi: 10.1074/jbc.M406768200. Epub 2004 Jul 21. J Biol Chem. 2004. PMID: 15272005 Free article.

7

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: gurevich vv, gurevich ev. Neuron. 2005 May 19;46(4):555-67. doi: 10.1016/j.neuron.2005.03.023. Neuron. 2005. PMID: 15944125 Free PMC article.

8

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: gurevich vv. 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

9

The differential engagement of arrestin surface charges by the various functional forms of the receptor.

Hanson SM, Gurevich VV. Hanson SM, et al. Among authors: gurevich vv. J Biol Chem. 2006 Feb 10;281(6):3458-62. doi: 10.1074/jbc.M512148200. Epub 2005 Dec 8. J Biol Chem. 2006. PMID: 16339758 Free PMC article.

10

The structural basis of arrestin-mediated regulation of G-protein-coupled receptors.

Gurevich VV, Gurevich EV. Gurevich VV, et al. Among authors: gurevich ev. Pharmacol Ther. 2006 Jun;110(3):465-502. doi: 10.1016/j.pharmthera.2005.09.008. Epub 2006 Feb 3. Pharmacol Ther. 2006. PMID: 16460808 Free PMC article. Review.

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