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Journal Abstract Search

224 related items for PubMed ID: 20660160

  • 1. The BNIP-2 and Cdc42GAP homology (BCH) domain of p50RhoGAP/Cdc42GAP sequesters RhoA from inactivation by the adjacent GTPase-activating protein domain.
    Zhou YT, Chew LL, Lin SC, Low BC.
    Mol Biol Cell; 2010 Sep 15; 21(18):3232-46. PubMed ID: 20660160
    [Abstract] [Full Text] [Related]

  • 2. Structural basis for p50RhoGAP BCH domain-mediated regulation of Rho inactivation.
    Chichili VPR, Chew TW, Shankar S, Er SY, Chin CF, Jobichen C, Qiurong Pan C, Zhou Y, Yeong FM, Low BC, Sivaraman J.
    Proc Natl Acad Sci U S A; 2021 May 25; 118(21):. PubMed ID: 34006635
    [Abstract] [Full Text] [Related]

  • 3. BNIP-Salpha induces cell rounding and apoptosis by displacing p50RhoGAP and facilitating RhoA activation via its unique motifs in the BNIP-2 and Cdc42GAP homology domain.
    Zhou YT, Guy GR, Low BC.
    Oncogene; 2006 Apr 13; 25(16):2393-408. PubMed ID: 16331259
    [Abstract] [Full Text] [Related]

  • 4. Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP.
    Shankar S, Chew TW, Chichili VPR, Low BC, Sivaraman J.
    Cell Mol Life Sci; 2024 May 13; 81(1):216. PubMed ID: 38740643
    [Abstract] [Full Text] [Related]

  • 5. BNIP-2 induces cell elongation and membrane protrusions by interacting with Cdc42 via a unique Cdc42-binding motif within its BNIP-2 and Cdc42GAP homology domain.
    Zhou YT, Guy GR, Low BC.
    Exp Cell Res; 2005 Feb 15; 303(2):263-74. PubMed ID: 15652341
    [Abstract] [Full Text] [Related]

  • 6. Concerted regulation of cell dynamics by BNIP-2 and Cdc42GAP homology/Sec14p-like, proline-rich, and GTPase-activating protein domains of a novel Rho GTPase-activating protein, BPGAP1.
    Shang X, Zhou YT, Low BC.
    J Biol Chem; 2003 Nov 14; 278(46):45903-14. PubMed ID: 12944407
    [Abstract] [Full Text] [Related]

  • 7. The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP.
    Low BC, Seow KT, Guy GR.
    J Biol Chem; 2000 Dec 01; 275(48):37742-51. PubMed ID: 10954711
    [Abstract] [Full Text] [Related]

  • 8. Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2.
    Low BC, Seow KT, Guy GR.
    J Biol Chem; 2000 May 12; 275(19):14415-22. PubMed ID: 10799524
    [Abstract] [Full Text] [Related]

  • 9. Regulation of RhoA GTP hydrolysis by the GTPase-activating proteins p190, p50RhoGAP, Bcr, and 3BP-1.
    Zhang B, Zheng Y.
    Biochemistry; 1998 Apr 14; 37(15):5249-57. PubMed ID: 9548756
    [Abstract] [Full Text] [Related]

  • 10. ARHGAP8 is a novel member of the RHOGAP family related to ARHGAP1/CDC42GAP/p50RHOGAP: mutation and expression analyses in colorectal and breast cancers.
    Johnstone CN, Castellví-Bel S, Chang LM, Bessa X, Nakagawa H, Harada H, Sung RK, Piqué JM, Castells A, Rustgi AK.
    Gene; 2004 Jul 07; 336(1):59-71. PubMed ID: 15225876
    [Abstract] [Full Text] [Related]

  • 11. Sec14 homology domain targets p50RhoGAP to endosomes and provides a link between Rab and Rho GTPases.
    Sirokmány G, Szidonya L, Káldi K, Gáborik Z, Ligeti E, Geiszt M.
    J Biol Chem; 2006 Mar 03; 281(9):6096-105. PubMed ID: 16380373
    [Abstract] [Full Text] [Related]

  • 12. Cross-species analyses identify the BNIP-2 and Cdc42GAP homology (BCH) domain as a distinct functional subclass of the CRAL_TRIO/Sec14 superfamily.
    Gupta AB, Wee LE, Zhou YT, Hortsch M, Low BC.
    PLoS One; 2012 Mar 03; 7(3):e33863. PubMed ID: 22479462
    [Abstract] [Full Text] [Related]

  • 13. Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA.
    Zhang B, Chernoff J, Zheng Y.
    J Biol Chem; 1998 Apr 10; 273(15):8776-82. PubMed ID: 9535855
    [Abstract] [Full Text] [Related]

  • 14. Understanding the catalytic mechanism of GTPase-activating proteins: demonstration of the importance of switch domain stabilization in the stimulation of GTP hydrolysis.
    Fidyk NJ, Cerione RA.
    Biochemistry; 2002 Dec 31; 41(52):15644-53. PubMed ID: 12501193
    [Abstract] [Full Text] [Related]

  • 15. The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a novel apoptosis-inducing sequence.
    Zhou YT, Soh UJ, Shang X, Guy GR, Low BC.
    J Biol Chem; 2002 Mar 01; 277(9):7483-92. PubMed ID: 11741952
    [Abstract] [Full Text] [Related]

  • 16. Dissecting the thermodynamics of GAP-RhoA interactions.
    Jelen F, Lachowicz P, Apostoluk W, Mateja A, Derewenda ZS, Otlewski J.
    J Struct Biol; 2009 Jan 01; 165(1):10-8. PubMed ID: 18929667
    [Abstract] [Full Text] [Related]

  • 17. BNIP2 extra long inhibits RhoA and cellular transformation by Lbc RhoGEF via its BCH domain.
    Soh UJ, Low BC.
    J Cell Sci; 2008 May 15; 121(Pt 10):1739-49. PubMed ID: 18445682
    [Abstract] [Full Text] [Related]

  • 18. GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2.
    Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS.
    J Biol Chem; 2003 Sep 05; 278(36):34641-53. PubMed ID: 12819203
    [Abstract] [Full Text] [Related]

  • 19. 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 08; 275(49):38605-10. PubMed ID: 10982819
    [Abstract] [Full Text] [Related]

  • 20. Drosophila RhoGAP68F is a putative GTPase activating protein for RhoA participating in gastrulation.
    Sanny J, Chui V, Langmann C, Pereira C, Zahedi B, Harden N.
    Dev Genes Evol; 2006 Sep 08; 216(9):543-50. PubMed ID: 16609869
    [Abstract] [Full Text] [Related]

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