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Items: 1 to 20 of 37

1.

Current knowledge of the large RhoGAP family of proteins.

Tcherkezian J, Lamarche-Vane N.

Biol Cell. 2007 Feb;99(2):67-86. Review.

PMID:
17222083
2.

Rho GTPases and the control of cell behaviour.

Hall A.

Biochem Soc Trans. 2005 Nov;33(Pt 5):891-5. Review.

PMID:
16246005
3.

Rho GTPases: biochemistry and biology.

Jaffe AB, Hall A.

Annu Rev Cell Dev Biol. 2005;21:247-69. Review.

PMID:
16212495
4.

ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures.

Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, Pupko T, Ben-Tal N.

Nucleic Acids Res. 2005 Jul 1;33(Web Server issue):W299-302.

5.

GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors.

Rossman KL, Der CJ, Sondek J.

Nat Rev Mol Cell Biol. 2005 Feb;6(2):167-80. Review.

PMID:
15688002
6.

The crystal structure of RhoA in complex with the DH/PH fragment of PDZRhoGEF, an activator of the Ca(2+) sensitization pathway in smooth muscle.

Derewenda U, Oleksy A, Stevenson AS, Korczynska J, Dauter Z, Somlyo AP, Otlewski J, Somlyo AV, Derewenda ZS.

Structure. 2004 Nov;12(11):1955-65.

7.

Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor.

Kristelly R, Gao G, Tesmer JJ.

J Biol Chem. 2004 Nov 5;279(45):47352-62. Epub 2004 Aug 25.

8.

UCSF Chimera--a visualization system for exploratory research and analysis.

Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE.

J Comput Chem. 2004 Oct;25(13):1605-12.

PMID:
15264254
9.

Cell migration: Rho GTPases lead the way.

Raftopoulou M, Hall A.

Dev Biol. 2004 Jan 1;265(1):23-32. Review.

10.

Rho GTPase-activating proteins in cell regulation.

Moon SY, Zheng Y.

Trends Cell Biol. 2003 Jan;13(1):13-22. Review.

PMID:
12480336
11.

Rho GTPases in cell biology.

Etienne-Manneville S, Hall A.

Nature. 2002 Dec 12;420(6916):629-35. Review.

PMID:
12478284
12.

Thermodynamic consequences of burial of polar and non-polar amino acid residues in the protein interior.

Loladze VV, Ermolenko DN, Makhatadze GI.

J Mol Biol. 2002 Jul 5;320(2):343-57.

PMID:
12079391
13.

Structural basis for the selective activation of Rho GTPases by Dbl exchange factors.

Snyder JT, Worthylake DK, Rossman KL, Betts L, Pruitt WM, Siderovski DP, Der CJ, Sondek J.

Nat Struct Biol. 2002 Jun;9(6):468-75.

PMID:
12006984
14.

Thermodynamics of Ras/effector and Cdc42/effector interactions probed by isothermal titration calorimetry.

Rudolph MG, Linnemann T, Grunewald P, Wittinghofer A, Vetter IR, Herrmann C.

J Biol Chem. 2001 Jun 29;276(26):23914-21. Epub 2001 Apr 5.

15.

Structure of the BH domain from graf and its implications for Rho GTPase recognition.

Longenecker KL, Zhang B, Derewenda U, Sheffield PJ, Dauter Z, Parsons JT, Zheng Y, Derewenda ZS.

J Biol Chem. 2000 Dec 8;275(49):38605-10.

16.
17.

ESPript: analysis of multiple sequence alignments in PostScript.

Gouet P, Courcelle E, Stuart DI, M├ętoz F.

Bioinformatics. 1999 Apr;15(4):305-8.

PMID:
10320398
18.

Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors.

Sheffield P, Garrard S, Derewenda Z.

Protein Expr Purif. 1999 Feb;15(1):34-9.

PMID:
10024467
20.

Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP.

Nassar N, Hoffman GR, Manor D, Clardy JC, Cerione RA.

Nat Struct Biol. 1998 Dec;5(12):1047-52.

PMID:
9846874

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