17109408 17606620 26510463 29944985 24449856 29170031 17132044 19835414 24724832 21777183 33690974 22871814 16943619 15591052 17167410 22306737 21051714 23091036 21766795 26872787 23466875 24183695 - Search Results

Year	Number of Results
2004	1
2005	1
2006	2
2007	3
2009	1
2011	2
2012	4
2013	2
2014	3
2015	1
2016	1
2017	1
2018	2
2021	1
2023	0

1

How a small change in retinal leads to G-protein activation: initial events suggested by molecular dynamics calculations.

Crozier PS, Stevens MJ, Woolf TB. Crozier PS, et al. Proteins. 2007 Feb 15;66(3):559-74. doi: 10.1002/prot.21175. Proteins. 2007. PMID: 17109408 Free PMC article.

2

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. Sommer ME, et al. J Biol Chem. 2007 Aug 31;282(35):25560-8. doi: 10.1074/jbc.M702155200. Epub 2007 Jul 2. J Biol Chem. 2007. PMID: 17606620 Free article.

3

Structural evidence for the role of polar core residue Arg175 in arrestin activation.

Granzin J, Stadler A, Cousin A, Schlesinger R, Batra-Safferling R. Granzin J, et al. Sci Rep. 2015 Oct 29;5:15808. doi: 10.1038/srep15808. Sci Rep. 2015. PMID: 26510463 Free PMC article.

4

Different mode of arrestin-3 binding at the human Y₁ and Y₂ receptor.

Wanka L, Babilon S, Kaiser A, Mörl K, Beck-Sickinger AG. Wanka L, et al. Cell Signal. 2018 Oct;50:58-71. doi: 10.1016/j.cellsig.2018.06.010. Epub 2018 Jun 23. Cell Signal. 2018. PMID: 29944985

5

Functional map of arrestin-1 at single amino acid resolution.

Ostermaier MK, Peterhans C, Jaussi R, Deupi X, Standfuss J. Ostermaier MK, et al. Proc Natl Acad Sci U S A. 2014 Feb 4;111(5):1825-30. doi: 10.1073/pnas.1319402111. Epub 2014 Jan 21. Proc Natl Acad Sci U S A. 2014. PMID: 24449856 Free PMC article.

6

Development of a new protein labeling system to map subunits and domains of macromolecular complexes for electron microscopy.

Brown ZP, Arimori T, Iwasaki K, Takagi J. Brown ZP, et al. J Struct Biol. 2018 Mar;201(3):247-251. doi: 10.1016/j.jsb.2017.11.006. Epub 2017 Nov 21. J Struct Biol. 2018. PMID: 29170031

7

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. Skegro D, et al. Photochem Photobiol. 2007 Mar-Apr;83(2):385-92. doi: 10.1562/2006-08-25-RA-1014. Photochem Photobiol. 2007. PMID: 17132044

8

Helix formation in arrestin accompanies recognition of photoactivated rhodopsin.

Feuerstein SE, Pulvermüller A, Hartmann R, Granzin J, Stoldt M, Henklein P, Ernst OP, Heck M, Willbold D, Koenig BW. Feuerstein SE, et al. Biochemistry. 2009 Nov 17;48(45):10733-42. doi: 10.1021/bi900544p. Biochemistry. 2009. PMID: 19835414

9

Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding.

Sinha A, Jones Brunette AM, Fay JF, Schafer CT, Farrens DL. Sinha A, et al. Biochemistry. 2014 May 27;53(20):3294-307. doi: 10.1021/bi401534y. Epub 2014 May 13. Biochemistry. 2014. PMID: 24724832 Free PMC article.

10

The cytoplasmic rhodopsin-protein interface: potential for drug discovery.

Yanamala N, Gardner E, Riciutti A, Klein-Seetharaman J. Yanamala N, et al. Curr Drug Targets. 2012 Jan;13(1):3-14. doi: 10.2174/138945012798868461. Curr Drug Targets. 2012. PMID: 21777183 Free PMC article. Review.

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