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Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.

Vishnivetskiy SA, Gimenez LE, Francis DJ, Hanson SM, Hubbell WL, Klug CS, Gurevich VV.

J Biol Chem. 2011 Jul 8;286(27):24288-99. doi: 10.1074/jbc.M110.213835. Epub 2011 Apr 6.


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

Vishnivetskiy SA, Hosey MM, Benovic JL, Gurevich VV.

J Biol Chem. 2004 Jan 9;279(2):1262-8. Epub 2003 Oct 6.


Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.

Gimenez LE, Kook S, Vishnivetskiy SA, Ahmed MR, Gurevich EV, Gurevich VV.

J Biol Chem. 2012 Mar 16;287(12):9028-40. doi: 10.1074/jbc.M111.311803. Epub 2012 Jan 24.


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

Hanson SM, Gurevich VV.

J Biol Chem. 2006 Feb 10;281(6):3458-62. Epub 2005 Dec 8.


Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors.

Gurevich VV, Dion SB, Onorato JJ, Ptasienski J, Kim CM, Sterne-Marr R, Hosey MM, Benovic JL.

J Biol Chem. 1995 Jan 13;270(2):720-31.


Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors.

Prokop S, Perry NA, Vishnivetskiy SA, Toth AD, Inoue A, Milligan G, Iverson TM, Hunyady L, Gurevich VV.

Cell Signal. 2017 Aug;36:98-107. doi: 10.1016/j.cellsig.2017.04.021. Epub 2017 Apr 28.


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

Vishnivetskiy SA, Hirsch JA, Velez MG, Gurevich YV, Gurevich VV.

J Biol Chem. 2002 Nov 15;277(46):43961-7. Epub 2002 Sep 4.


Binding of wild type and chimeric arrestins to the m2 muscarinic cholinergic receptor.

Gurevich VV, Richardson RM, Kim CM, Hosey MM, Benovic JL.

J Biol Chem. 1993 Aug 15;268(23):16879-82.


Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins.

Gimenez LE, Vishnivetskiy SA, Baameur F, Gurevich VV.

J Biol Chem. 2012 Aug 24;287(35):29495-505. doi: 10.1074/jbc.M112.366674. Epub 2012 Jul 11.


Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites.

Song X, Gurevich EV, Gurevich VV.

J Neurochem. 2007 Nov;103(3):1053-62. Epub 2007 Aug 6.


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.

J Mol Biol. 2005 Dec 16;354(5):1069-80. Epub 2005 Nov 2.


Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process.

Kirchberg K, Kim TY, Möller M, Skegro D, Dasara Raju G, Granzin J, Büldt G, Schlesinger R, Alexiev U.

Proc Natl Acad Sci U S A. 2011 Nov 15;108(46):18690-5. doi: 10.1073/pnas.1015461108. Epub 2011 Oct 28.


An intracellular loop 2 amino acid residue determines differential binding of arrestin to the dopamine D2 and D3 receptors.

Lan H, Teeter MM, Gurevich VV, Neve KA.

Mol Pharmacol. 2009 Jan;75(1):19-26. doi: 10.1124/mol.108.050542. Epub 2008 Sep 26.


Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.

Hanson SM, Francis DJ, Vishnivetskiy SA, Kolobova EA, Hubbell WL, Klug CS, Gurevich VV.

Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4900-5. Epub 2006 Mar 17.


Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes.

Zhan X, Gimenez LE, Gurevich VV, Spiller BW.

J Mol Biol. 2011 Feb 25;406(3):467-78. doi: 10.1016/j.jmb.2010.12.034. Epub 2011 Jan 6.


A beta-arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors.

Marion S, Oakley RH, Kim KM, Caron MG, Barak LS.

J Biol Chem. 2006 Feb 3;281(5):2932-8. Epub 2005 Nov 30.


Interaction of arrestins with intracellular domains of muscarinic and alpha2-adrenergic receptors.

Wu G, Krupnick JG, Benovic JL, Lanier SM.

J Biol Chem. 1997 Jul 11;272(28):17836-42.


Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus.

Potter RM, Key TA, Gurevich VV, Sklar LA, Prossnitz ER.

J Biol Chem. 2002 Mar 15;277(11):8970-8. Epub 2002 Jan 3.


Functional map of arrestin binding to phosphorylated opsin, with and without agonist.

Peterhans C, Lally CC, Ostermaier MK, Sommer ME, Standfuss J.

Sci Rep. 2016 Jun 28;6:28686. doi: 10.1038/srep28686. Erratum in: Sci Rep. 2016 Jul 22;6:30224.

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