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Volumn 435, Issue 3, 2013, Pages 367-372

Crystal structure of GTPase-activating domain from human MgcRacGAP

Author keywords

Cytokinesis; GTPase activating protein; MgcRacGAP; Rac1

Indexed keywords

GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; MONOMER; RAC1 PROTEIN;

EID: 84878992346     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.04.094     Document Type: Article
Times cited : (6)

References (27)
  • 1
    • 15244356577 scopus 로고    scopus 로고
    • The molecular requirements for cytokinesis
    • Glotzer M. The molecular requirements for cytokinesis. Science 2005, 307:1735-1739.
    • (2005) Science , vol.307 , pp. 1735-1739
    • Glotzer, M.1
  • 3
    • 33750011475 scopus 로고    scopus 로고
    • Rho GTPase activity zones and transient contractile arrays
    • Bement W.M., Miller A.L., von Dassow G. Rho GTPase activity zones and transient contractile arrays. BioEssays 2006, 28:983-993.
    • (2006) BioEssays , vol.28 , pp. 983-993
    • Bement, W.M.1    Miller, A.L.2    von Dassow, G.3
  • 4
    • 84869475587 scopus 로고    scopus 로고
    • Centralspindlin: at the heart of cytokinesis
    • White E.A., Glotzer M. Centralspindlin: at the heart of cytokinesis. Cytoskeleton 2012, 69:882-892.
    • (2012) Cytoskeleton , vol.69 , pp. 882-892
    • White, E.A.1    Glotzer, M.2
  • 5
    • 0035937180 scopus 로고    scopus 로고
    • MgcRacGAP is involved in cytokinesis through associating with mitotic Spindle and midbody
    • Hirose K., Kawashima T., Iwamoto I., Nosaka T., Kitamura T. MgcRacGAP is involved in cytokinesis through associating with mitotic Spindle and midbody. J. Biol. Chem. 2001, 276:5821-5828.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5821-5828
    • Hirose, K.1    Kawashima, T.2    Iwamoto, I.3    Nosaka, T.4    Kitamura, T.5
  • 6
    • 37049038634 scopus 로고    scopus 로고
    • Cooperative assembly of CYK-4/MgcRacGAP and ZEN-4/MKLP1 to form the centralspindlin complex
    • Pavicic-Kaltenbrunner V., Mishima M., Glotzer M. Cooperative assembly of CYK-4/MgcRacGAP and ZEN-4/MKLP1 to form the centralspindlin complex. Mol. Biol. Cell 2007, 18:4992-5003.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4992-5003
    • Pavicic-Kaltenbrunner, V.1    Mishima, M.2    Glotzer, M.3
  • 7
    • 24944480674 scopus 로고    scopus 로고
    • MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis
    • Zhao W.M., Fang G. MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis. Proc. Natl. Acad. Sci. USA 2005, 102:13158-13163.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13158-13163
    • Zhao, W.M.1    Fang, G.2
  • 8
    • 0032513234 scopus 로고    scopus 로고
    • MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 Similar to drosophila rotundRacGAP gene product, is expressed in male germ cells
    • Touré A., Dorseuil O., Morin L., Timmons P., Jégou B., Reibel L., Gacon G. MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 Similar to drosophila rotundRacGAP gene product, is expressed in male germ cells. J. Biol. Chem. 1998, 273:6019-6023.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6019-6023
    • Touré, A.1    Dorseuil, O.2    Morin, L.3    Timmons, P.4    Jégou, B.5    Reibel, L.6    Gacon, G.7
  • 10
    • 1942469374 scopus 로고    scopus 로고
    • Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase
    • Ban R., Irino Y., Fukami K., Tanaka H. Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase. J. Biol. Chem. 2004, 279:16394-16402.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16394-16402
    • Ban, R.1    Irino, Y.2    Fukami, K.3    Tanaka, H.4
  • 12
  • 15
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • Rittinger L., Walker P.A., Eccleston J.F., Smerdon S.J., Gamblin S.J. Structure at 1.65Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 1997, 389:758-762.
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, L.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 16
    • 0031762533 scopus 로고    scopus 로고
    • Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP
    • Nassar N., Hoffman G.R., Manor D., Clardy J.C., Cerione R.A. Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nat. Struct. Biol. 1998, 5:1047-1052.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1047-1052
    • Nassar, N.1    Hoffman, G.R.2    Manor, D.3    Clardy, J.C.4    Cerione, R.A.5
  • 19
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • Sheffield P., Garrard S., Derewenda Z. Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expr. Purif. 1999, 15:34-39.
    • (1999) Protein Expr. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Cryst. D 2004, 60:2126-2132.
    • (2004) Acta Cryst. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 23
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D 1997, 53:240-255.
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 24
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García de la Torre J., Huertas M.L., Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 2000, 78:719-730.
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • García de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 26
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L., Rosenström P. Dali server: conservation mapping in 3D. Nucleic Acid Res. 2010, 38:W545-549.
    • (2010) Nucleic Acid Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 27


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.