Tissue-specific variations in the expression and regulation of the small GTP-binding protein Rho.

[1]  P. Chavrier,et al.  Characterization of a monoclonal antibody specific for the Ras-related GTP-binding protein Rho A. , 1993, Biochemical and biophysical research communications.

[2]  S. Y. Cajal,et al.  Tumorigenic activity of rho genes from Aplysia californica. , 1993, Oncogene.

[3]  J. Garin,et al.  Copurification of rho protein and the rho-GDP dissociation inhibitor from bovine neutrophil cytosol. Effect of phosphoinositides on rho ADP-ribosylation by the C3 exoenzyme of Clostridium botulinum. , 1992, Biochemistry.

[4]  P. Adamson,et al.  Intracellular localization of the P21rho proteins , 1992, The Journal of cell biology.

[5]  R. Weinberg,et al.  Association between GTPase activators for Rho and Ras families , 1992, Nature.

[6]  C. Wollheim,et al.  The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins. , 1992, The Journal of biological chemistry.

[7]  C. Hall,et al.  Diversity and versatility of GTPase activating proteins for the p21rho subfamily of ras G proteins detected by a novel overlay assay. , 1992, Journal of Biological Chemistry.

[8]  Anne J. Ridley,et al.  The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors , 1992, Cell.

[9]  T. Sasaki,et al.  Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein. , 1992, The Journal of biological chemistry.

[10]  R. Stancou,et al.  ADP-ribosylation of the ras-related, GTP-binding protein RhoA inhibits lymphocyte-mediated cytotoxicity. , 1992, The Journal of biological chemistry.

[11]  P. Casey,et al.  Rac1, a low-molecular-mass GTP-binding-protein with high intrinsic GTPase activity and distinct biochemical properties. , 1992, European journal of biochemistry.

[12]  K. Aktories,et al.  ADP-ribosylation of small GTP-binding proteins by Bacillus cereus. , 1992, Biochemical and biophysical research communications.

[13]  K. Aktories,et al.  Clostridium botulinum C3 ADP-ribosyltransferase. , 1992, Current topics in microbiology and immunology.

[14]  P. Boquet,et al.  ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility. , 1991, Biochemical and biophysical research communications.

[15]  T. Hunter,et al.  The ras-related gene rhoB is an immediate-early gene inducible by v-Fps, epidermal growth factor, and platelet-derived growth factor in rat fibroblasts , 1991, Molecular and cellular biology.

[16]  M. Garrett,et al.  Purification and N-terminal sequence of the p21rho GTPase-activating protein, rho GAP. , 1991, The Biochemical journal.

[17]  S. Narumiya,et al.  Purification of GTPase-activating protein specific for the rho gene products. , 1991, The Journal of biological chemistry.

[18]  P. Traub,et al.  Alteration of the cytoskeleton of mammalian cells cultured in vitro by Clostridium botulinum C2 toxin and C3 ADP-ribosyltransferase. , 1991, European journal of cell biology.

[19]  Y. Takai,et al.  Regulation of binding of rhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor. , 1991, Oncogene.

[20]  G M Bokoch,et al.  rac, a novel ras-related family of proteins that are botulinum toxin substrates. , 1989, The Journal of biological chemistry.

[21]  T. Katada,et al.  Activator protein supporting the botulinum ADP-ribosyltransferase reaction. , 1989, The Journal of biological chemistry.

[22]  R. Weinberg,et al.  Characterization and expression of the human rhoH12 gene product , 1989, Molecular and cellular biology.

[23]  P. Boquet,et al.  The mammalian G protein rhoC is ADP‐ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. , 1989, The EMBO journal.

[24]  A. Hall,et al.  The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3. , 1989, Biochemical and biophysical research communications.

[25]  A. Hall,et al.  Identification of distinct cytoplasmic targets for ras/R-ras and rho regulatory proteins. , 1989, The Journal of biological chemistry.

[26]  E. L. Harris,et al.  Protein purification methods : a practical approach , 1989 .

[27]  S. Narumiya,et al.  Substrate for botulinum ADP-ribosyltransferase, Gb, has an amino acid sequence homologous to a putative rho gene product. , 1988, The Journal of biological chemistry.

[28]  Y. Takai,et al.  ADP-ribosylation of the bovine brain rho protein by botulinum toxin type C1. , 1988, The Journal of biological chemistry.

[29]  H. Bourne Do GTPases direct membrane traffic in secretion? , 1988, Cell.

[30]  P. Chardin,et al.  Coding sequence of human rho cDNAs clone 6 and clone 9. , 1988, Nucleic acids research.

[31]  K. Aktories,et al.  Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes. , 1988, European journal of biochemistry.

[32]  E. Rubin,et al.  Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. , 1988, Molecular and cellular biology.

[33]  P. Chardin,et al.  Nucleotide sequence of human rho cDNA clone 12. , 1987, Nucleic acids research.

[34]  K. Aktories,et al.  Clostridium botulinum type C produces a novel ADP‐ribosyltransferase distinct from botulinum C2 toxin , 1987, FEBS letters.

[35]  F. Schachat,et al.  The presence of two skeletal muscle alpha-actinins correlates with troponin-tropomyosin expression and Z-line width , 1985, The Journal of cell biology.

[36]  R. Axel,et al.  A novel ras-related gene family , 1985, Cell.

[37]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[38]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.