Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 80


Structure and function of the visual arrestin oligomer.

Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, Klug CS, Hubbell WL, Gurevich VV.

EMBO J. 2007 Mar 21;26(6):1726-36. Epub 2007 Mar 1.


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.


Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant.

Song X, Seo J, Baameur F, Vishnivetskiy SA, Chen Q, Kook S, Kim M, Brooks EK, Altenbach C, Hong Y, Hanson SM, Palazzo MC, Chen J, Hubbell WL, Gurevich EV, Gurevich VV.

Cell Signal. 2013 Dec;25(12):2613-24. doi: 10.1016/j.cellsig.2013.08.022. Epub 2013 Sep 3.


Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin.

Zhuang T, Chen Q, Cho MK, Vishnivetskiy SA, Iverson TM, Gurevich VV, Sanders CR.

Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):942-7. doi: 10.1073/pnas.1215176110. Epub 2012 Dec 31.


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.

Structure. 2008 Jun;16(6):924-34. doi: 10.1016/j.str.2008.03.006.


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.

J Biol Chem. 2004 Sep 24;279(39):41240-8. Epub 2004 Jul 21.


N-terminal and C-terminal domains of arrestin both contribute in binding to rhodopsin.

Skegro D, Pulvermüller A, Krafft B, Granzin J, Hofmann KP, Büldt G, Schlesinger R.

Photochem Photobiol. 2007 Mar-Apr;83(2):385-92.


Crystal structure of p44, a constitutively active splice variant of visual arrestin.

Granzin J, Cousin A, Weirauch M, Schlesinger R, Büldt G, Batra-Safferling R.

J Mol Biol. 2012 Mar 9;416(5):611-8. doi: 10.1016/j.jmb.2012.01.028. Epub 2012 Jan 27.


Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors.

Sommer ME, Hofmann KP, Heck M.

J Biol Chem. 2011 Mar 4;286(9):7359-69. doi: 10.1074/jbc.M110.204941. Epub 2010 Dec 17.


Dynamics of arrestin-rhodopsin interactions: loop movement is involved in arrestin activation and receptor binding.

Sommer ME, Farrens DL, McDowell JH, Weber LA, Smith WC.

J Biol Chem. 2007 Aug 31;282(35):25560-8. Epub 2007 Jul 2.


Robust self-association is a common feature of mammalian visual arrestin-1.

Kim M, Hanson SM, Vishnivetskiy SA, Song X, Cleghorn WM, Hubbell WL, Gurevich VV.

Biochemistry. 2011 Mar 29;50(12):2235-42. doi: 10.1021/bi1018607. Epub 2011 Feb 18.


The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin.

Kisselev OG, McDowell JH, Hargrave PA.

FEBS Lett. 2004 Apr 30;564(3):307-11.


Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashion.

Gray-Keller MP, Detwiler PB, Benovic JL, Gurevich VV.

Biochemistry. 1997 Jun 10;36(23):7058-63.


How does arrestin respond to the phosphorylated state of rhodopsin?

Vishnivetskiy SA, Paz CL, Schubert C, Hirsch JA, Sigler PB, Gurevich VV.

J Biol Chem. 1999 Apr 23;274(17):11451-4.


Visual arrestin binding to microtubules involves a distinct conformational change.

Hanson SM, Francis DJ, Vishnivetskiy SA, Klug CS, Gurevich VV.

J Biol Chem. 2006 Apr 7;281(14):9765-72. Epub 2006 Feb 6.


Concentration-dependent tetramerization of bovine visual arrestin.

Imamoto Y, Tamura C, Kamikubo H, Kataoka M.

Biophys J. 2003 Aug;85(2):1186-95.


Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association.

Hanson SM, Vishnivetskiy SA, Hubbell WL, Gurevich VV.

Biochemistry. 2008 Jan 22;47(3):1070-5. Epub 2007 Dec 28.


Arrestin and its splice variant Arr1-370A (p44). Mechanism and biological role of their interaction with rhodopsin.

Schröder K, Pulvermüller A, Hofmann KP.

J Biol Chem. 2002 Nov 15;277(46):43987-96. Epub 2002 Aug 22.


Functional differences in the interaction of arrestin and its splice variant, p44, with rhodopsin.

Pulvermüller A, Maretzki D, Rudnicka-Nawrot M, Smith WC, Palczewski K, Hofmann KP.

Biochemistry. 1997 Jul 29;36(30):9253-60.


Supplemental Content

Support Center