Structural and mechanistic insights into the interaction between Rho and mammalian Dia
暂无分享,去创建一个
M. Weyand | A. Wittinghofer | M. Ahmadian | M. Weyand | T. Ishizaki | R. Rose | M. Lammers | T. Ishizaki | M. R. Ahmadian | A. Wittinghofer | M. Lammers | R. Rose | Alfred Wittinghofer | Rolf Rose | Michael Weyand | Michael Lammers | Toshimasa Ishizaki
[1] A. Krebs,et al. Characterization of functional domains of mDia1, a link between the small GTPase Rho and the actin cytoskeleton. , 2001, Journal of cell science.
[2] Takayuki Kato,et al. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization , 1999, Nature Cell Biology.
[3] William I. Weis,et al. Three-Dimensional Structure of the Armadillo Repeat Region of β-Catenin , 1997, Cell.
[4] Jun Peng,et al. Disruption of the Diaphanous-Related Formin Drf1 Gene Encoding mDia1 Reveals a Role for Drf3 as an Effector for Cdc42 , 2003, Current Biology.
[5] I. Vetter,et al. The Guanine Nucleotide-Binding Switch in Three Dimensions , 2001, Science.
[6] H. Higgs,et al. Dissecting Requirements for Auto-inhibition of Actin Nucleation by the Formin, mDia1* , 2005, Journal of Biological Chemistry.
[7] Charles Boone,et al. Role of Formins in Actin Assembly: Nucleation and Barbed-End Association , 2002, Science.
[8] A. Alberts,et al. The formins: active scaffolds that remodel the cytoskeleton. , 2003, Trends in cell biology.
[9] I. Vetter,et al. Structural Insights into the Interaction of ROCKI with the Switch Regions of RhoA* , 2004, Journal of Biological Chemistry.
[10] A. Hall,et al. Rho GTPases in cell biology , 2002, Nature.
[11] K. Nakao,et al. p140mDia, a mammalian homolog of Drosophila diaphanous,is a target protein for Rho small GTPase and is a ligand for profilin , 1997, The EMBO journal.
[12] S. Narumiya,et al. Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells. , 2001, Journal of cell science.
[13] S. Smerdon,et al. Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP , 1997, Nature.
[14] James Moseley,et al. An actin nucleation mechanism mediated by Bni1 and Profilin , 2002, Nature Cell Biology.
[15] Arthur S. Alberts,et al. Identification of a Carboxyl-terminal Diaphanous-related Formin Homology Protein Autoregulatory Domain* , 2001, The Journal of Biological Chemistry.
[16] R. Treisman,et al. RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation , 1998, The EMBO journal.
[17] B. Ehresmann,et al. Spectrophotometric determination of protein concentration in cell extracts containing tRNA's and rRNA's. , 1973, Analytical biochemistry.
[18] S. Zigmond. Formin-induced nucleation of actin filaments. , 2004, Current opinion in cell biology.
[19] M. Ahmadian,et al. Models of the Cooperative Mechanism for Rho Effector Recognition , 2004, Journal of Biological Chemistry.
[20] Michael J. Eck,et al. Crystal Structures of a Formin Homology-2 Domain Reveal a Tethered Dimer Architecture , 2004, Cell.
[21] Charles Boone,et al. Formin Leaky Cap Allows Elongation in the Presence of Tight Capping Proteins , 2003, Current Biology.
[22] M. Peter,et al. Formins Set the Record Straight , 2002, Science.
[23] Gudrun Horn,et al. Differential Interaction of the Ras Family GTP-binding Proteins H-Ras, Rap1A, and R-Ras with the Putative Effector Molecules Raf Kinase and Ral-Guanine Nucleotide Exchange Factor , 1996, The Journal of Biological Chemistry.
[24] T. Pollard,et al. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin , 2003, The Journal of cell biology.
[25] W J Nelson,et al. Three-dimensional structure of the armadillo repeat region of beta-catenin. , 1997, Cell.
[26] I. Vetter,et al. The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization. , 2004, Molecular cell.
[27] H. Higgs,et al. The Mouse Formin mDia1 Is a Potent Actin Nucleation Factor Regulated by Autoinhibition , 2003, Current Biology.
[28] S. Kuroda,et al. The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. , 1999, Molecular cell.
[29] S. Kuroda,et al. An Open Conformation of Switch I Revealed by the Crystal Structure of a Mg2+-free Form of RHOA Complexed with GDP , 2000, The Journal of Biological Chemistry.
[30] Y. Kalaidzidis,et al. RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase , 2003, Nature Cell Biology.