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Items: 1 to 20 of 43

1.

All-atom empirical potential for molecular modeling and dynamics studies of proteins.

MacKerell AD, Bashford D, Bellott M, Dunbrack RL, Evanseck JD, Field MJ, Fischer S, Gao J, Guo H, Ha S, Joseph-McCarthy D, Kuchnir L, Kuczera K, Lau FT, Mattos C, Michnick S, Ngo T, Nguyen DT, Prodhom B, Reiher WE, Roux B, Schlenkrich M, Smith JC, Stote R, Straub J, Watanabe M, Wiórkiewicz-Kuczera J, Yin D, Karplus M.

J Phys Chem B. 1998 Apr 30;102(18):3586-616. doi: 10.1021/jp973084f.

PMID:
24889800
2.

Structure of a nanobody-stabilized active state of the β(2) adrenoceptor.

Rasmussen SG, Choi HJ, Fung JJ, Pardon E, Casarosa P, Chae PS, Devree BT, Rosenbaum DM, Thian FS, Kobilka TS, Schnapp A, Konetzki I, Sunahara RK, Gellman SH, Pautsch A, Steyaert J, Weis WI, Kobilka BK.

Nature. 2011 Jan 13;469(7329):175-80. doi: 10.1038/nature09648.

3.

Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins.

Chae PS, Rasmussen SG, Rana RR, Gotfryd K, Chandra R, Goren MA, Kruse AC, Nurva S, Loland CJ, Pierre Y, Drew D, Popot JL, Picot D, Fox BG, Guan L, Gether U, Byrne B, Kobilka B, Gellman SH.

Nat Methods. 2010 Dec;7(12):1003-8. doi: 10.1038/nmeth.1526. Epub 2010 Oct 31.

4.

Energy landscapes as a tool to integrate GPCR structure, dynamics, and function.

Deupi X, Kobilka BK.

Physiology (Bethesda). 2010 Oct;25(5):293-303. doi: 10.1152/physiol.00002.2010. Review.

5.

Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types.

Klauda JB, Venable RM, Freites JA, O'Connor JW, Tobias DJ, Mondragon-Ramirez C, Vorobyov I, MacKerell AD Jr, Pastor RW.

J Phys Chem B. 2010 Jun 17;114(23):7830-43. doi: 10.1021/jp101759q.

6.

A conserved protonation-induced switch can trigger "ionic-lock" formation in adrenergic receptors.

Vanni S, Neri M, Tavernelli I, Rothlisberger U.

J Mol Biol. 2010 Apr 16;397(5):1339-49. doi: 10.1016/j.jmb.2010.01.060. Epub 2010 Feb 2.

PMID:
20132827
7.

Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor.

Bokoch MP, Zou Y, Rasmussen SG, Liu CW, Nygaard R, Rosenbaum DM, Fung JJ, Choi HJ, Thian FS, Kobilka TS, Puglisi JD, Weis WI, Pardo L, Prosser RS, Mueller L, Kobilka BK.

Nature. 2010 Jan 7;463(7277):108-12. doi: 10.1038/nature08650.

8.

CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields.

Vanommeslaeghe K, Hatcher E, Acharya C, Kundu S, Zhong S, Shim J, Darian E, Guvench O, Lopes P, Vorobyov I, Mackerell AD Jr.

J Comput Chem. 2010 Mar;31(4):671-90. doi: 10.1002/jcc.21367.

9.

Phaser crystallographic software.

McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ.

J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. Epub 2007 Jul 13.

10.

The structure and function of G-protein-coupled receptors.

Rosenbaum DM, Rasmussen SG, Kobilka BK.

Nature. 2009 May 21;459(7245):356-63. doi: 10.1038/nature08144. Review.

11.

Crystallizing membrane proteins using lipidic mesophases.

Caffrey M, Cherezov V.

Nat Protoc. 2009;4(5):706-31. doi: 10.1038/nprot.2009.31.

12.

Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations.

Dror RO, Arlow DH, Borhani DW, Jensen MØ, Piana S, Shaw DE.

Proc Natl Acad Sci U S A. 2009 Mar 24;106(12):4689-94. doi: 10.1073/pnas.0811065106. Epub 2009 Mar 3.

13.

Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation.

Ahuja S, Hornak V, Yan EC, Syrett N, Goncalves JA, Hirshfeld A, Ziliox M, Sakmar TP, Sheves M, Reeves PJ, Smith SO, Eilers M.

Nat Struct Mol Biol. 2009 Feb;16(2):168-75. doi: 10.1038/nsmb.1549. Epub 2009 Feb 1.

14.

Crystallizing membrane proteins for structure determination: use of lipidic mesophases.

Caffrey M.

Annu Rev Biophys. 2009;38:29-51. doi: 10.1146/annurev.biophys.050708.133655. Review.

PMID:
19086821
15.

Crystal structure of opsin in its G-protein-interacting conformation.

Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krauss N, Choe HW, Hofmann KP, Ernst OP.

Nature. 2008 Sep 25;455(7212):497-502. doi: 10.1038/nature07330.

PMID:
18818650
16.

Crystal structure of the ligand-free G-protein-coupled receptor opsin.

Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP.

Nature. 2008 Jul 10;454(7201):183-7. doi: 10.1038/nature07063. Epub 2008 Jun 18.

PMID:
18563085
17.

Functional role of the "ionic lock"--an interhelical hydrogen-bond network in family A heptahelical receptors.

Vogel R, Mahalingam M, Lüdeke S, Huber T, Siebert F, Sakmar TP.

J Mol Biol. 2008 Jul 18;380(4):648-55. doi: 10.1016/j.jmb.2008.05.022. Epub 2008 May 17.

PMID:
18554610
18.

GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function.

Rosenbaum DM, Cherezov V, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Yao XJ, Weis WI, Stevens RC, Kobilka BK.

Science. 2007 Nov 23;318(5854):1266-73. Epub 2007 Oct 25.

19.

A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein.

Whorton MR, Bokoch MP, Rasmussen SG, Huang B, Zare RN, Kobilka B, Sunahara RK.

Proc Natl Acad Sci U S A. 2007 May 1;104(18):7682-7. Epub 2007 Apr 23.

20.

Coupling ligand structure to specific conformational switches in the beta2-adrenoceptor.

Yao X, Parnot C, Deupi X, Ratnala VR, Swaminath G, Farrens D, Kobilka B.

Nat Chem Biol. 2006 Aug;2(8):417-22. Epub 2006 Jun 25.

PMID:
16799554

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