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213 related items for PubMed ID: 15652341

  • 1. 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]

  • 2. 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]

  • 3. 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]

  • 4. 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]

  • 5. 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]

  • 6. 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
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  • 8. Functional plasticity of the BNIP-2 and Cdc42GAP Homology (BCH) domain in cell signaling and cell dynamics.
    Pan CQ, Low BC.
    FEBS Lett; 2012 Aug 14; 586(17):2674-91. PubMed ID: 22710163
    [Abstract] [Full Text] [Related]

  • 9. Activation of EGF receptor endocytosis and ERK1/2 signaling by BPGAP1 requires direct interaction with EEN/endophilin II and a functional RhoGAP domain.
    Lua BL, Low BC.
    J Cell Sci; 2005 Jun 15; 118(Pt 12):2707-21. PubMed ID: 15944398
    [Abstract] [Full Text] [Related]

  • 10. 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
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  • 13. Influencing cellular transformation by modulating the rates of GTP hydrolysis by Cdc42.
    Fidyk N, Wang JB, Cerione RA.
    Biochemistry; 2006 Jun 27; 45(25):7750-62. PubMed ID: 16784226
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  • 16. Selective activation by the guanine nucleotide exchange factor Don1 is a main determinant of Cdc42 signalling specificity in Ustilago maydis.
    Hlubek A, Schink KO, Mahlert M, Sandrock B, Bölker M.
    Mol Microbiol; 2008 May 27; 68(3):615-23. PubMed ID: 18394145
    [Abstract] [Full Text] [Related]

  • 17. The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading.
    Degani S, Balzac F, Brancaccio M, Guazzone S, Retta SF, Silengo L, Eva A, Tarone G.
    J Cell Biol; 2002 Jan 21; 156(2):377-87. PubMed ID: 11807099
    [Abstract] [Full Text] [Related]

  • 18. Biochemical characterization of distinct regions of SPEC molecules and their role in phagocytosis.
    Ching KH, Kisailus AE, Burbelo PD.
    Exp Cell Res; 2007 Jan 01; 313(1):10-21. PubMed ID: 17045588
    [Abstract] [Full Text] [Related]

  • 19. Tyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42.
    Low BC, Lim YP, Lim J, Wong ES, Guy GR.
    J Biol Chem; 1999 Nov 12; 274(46):33123-30. PubMed ID: 10551883
    [Abstract] [Full Text] [Related]

  • 20. A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases.
    Aresta S, de Tand-Heim MF, Béranger F, de Gunzburg J.
    Biochem J; 2002 Oct 01; 367(Pt 1):57-65. PubMed ID: 12093360
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