GTPase-activating proteins: helping hands to complement an active site.

[1]  P. Novick,et al.  Identification of a Sec4p GTPase-activating Protein (GAP) as a Novel Member of a Rab GAP Family* , 1998, The Journal of Biological Chemistry.

[2]  J. Moss,et al.  Molecular Characterization of the GTPase-activating Domain of ADP-ribosylation Factor Domain Protein 1 (ARD1)* , 1998, The Journal of Biological Chemistry.

[3]  Yi Zheng,et al.  Structural Determinants Required for the Interaction between Rho GTPase and the GTPase-activating Domain of p190* , 1997, The Journal of Biological Chemistry.

[4]  I. Hariharan,et al.  Biological characterization of Drosophila Rapgap1, a GTPase activating protein for Rap1. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[5]  A. Wittinghofer.  Signaling mechanistics: Aluminum fluoride for molecule of the year , 1997, Current Biology.

[6]  Katrin Rittinger,et al.  Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue , 1997, Nature.

[7]  Mohammad Reza Ahmadian,et al.  Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras , 1997, Nature Structural Biology.

[8]  S. Smerdon,et al.  Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP , 1997, Nature.

[9]  W. Kabsch,et al.  The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. , 1997, Science.

[10]  A. Wittinghofer,et al.  The interaction of Ras with GTPase‐activating proteins , 1997, FEBS letters.

[11]  A. Wittinghofer,et al.  Aluminium fluoride associates with the small guanine nucleotide binding proteins , 1997, FEBS letters.

[12]  S. Sprang,et al.  Structure of RGS4 Bound to AlF4 −-Activated Giα1: Stabilization of the Transition State for GTP Hydrolysis , 1997, Cell.

[13]  J. Thorner,et al.  RGS Proteins and Signaling by Heterotrimeric G Proteins* , 1997, The Journal of Biological Chemistry.

[14]  M. Hirshberg,et al.  The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue , 1997, Nature Structural Biology.

[15]  S. Smerdon,et al.  The structure of the GTPase-activating domain from p50rhoGAP , 1997, Nature.

[16]  E A Merritt,et al.  Raster3D: photorealistic molecular graphics. , 1997, Methods in enzymology.

[17]  W. Kabsch,et al.  Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras , 1996, Nature.

[18]  S. Harrison,et al.  Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[19]  M Geyer,et al.  Linear free energy relationships in the intrinsic and GTPase activating protein-stimulated guanosine 5'-triphosphate hydrolysis of p21ras. , 1996, Biochemistry.

[20]  M Geyer,et al.  Conformational transitions in p21ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP. , 1996, Biochemistry.

[21]  D. Herschlag,et al.  Ras-catalyzed hydrolysis of GTP: a new perspective from model studies. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[22]  F. Bischoff,et al.  Structural Differences in the Minimal Catalytic Domains of the GTPase-activating Proteins p120GAP and Neurofibromin* , 1996, The Journal of Biological Chemistry.

[23]  R. Goody,et al.  Formation of a Transition-State Analog of the Ras GTPase Reaction by Ras·GDP, Tetrafluoroaluminate, and GTPase-Activating Proteins , 1996, Science.

[24]  C A Smith,et al.  X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. , 1996, Biochemistry.

[25]  E. Cukierman,et al.  The ARF1 GTPase-Activating Protein: Zinc Finger Motif and Golgi Complex Localization , 1995, Science.

[26]  M. Webb,et al.  Kinetics of inorganic phosphate release during the interaction of p21ras with the GTPase-activating proteins, p120-GAP and neurofibromin. , 1995, Biochemistry.

[27]  T. Powers,et al.  Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases , 1995, Science.

[28]  F. Bischoff,et al.  Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[29]  H. Kalbitzer,et al.  Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins , 1995, Nature Structural Biology.

[30]  A. Hall,et al.  GAPs for rho-related GTPases. , 1994, Trends in genetics : TIG.

[31]  H. Hamm,et al.  GTPase mechanism of Gproteins from the 1.7-Å crystal structure of transducin α - GDP AIF−4 , 1994, Nature.

[32]  S. Sprang,et al.  Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. , 1994, Science.

[33]  H. Bercovier,et al.  Identification and nucleotide sequence of Brucella melitensis L7/L12 ribosomal protein. , 1994, FEMS Microbiology Letters.

[34]  P. Kraulis,et al.  Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. , 1994, Biochemistry.

[35]  A. Hall,et al.  Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases. , 1994, The Journal of biological chemistry.

[36]  Mark S. Boguski,et al.  Proteins regulating Ras and its relatives , 1993, Nature.

[37]  T. Pawson,et al.  The N‐terminal region of GAP regulates cytoskeletal structure and cell adhesion. , 1993, The EMBO journal.

[38]  J. Eccleston,et al.  Mechanism of GTP hydrolysis by p21N-ras catalyzed by GAP: studies with a fluorescent GTP analogue. , 1993, Biochemistry.

[39]  F. McCormick,et al.  Structural requirements for the interaction of p21ras with GAP, exchange factors, and its biological effector target. , 1993, The Journal of biological chemistry.

[40]  F. Collins,et al.  The neurofibromatosis type 1 gene and its protein product, neurofibromin , 1993, Neuron.

[41]  D. Lowy,et al.  Function and regulation of ras. , 1993, Annual review of biochemistry.

[42]  A. Wittinghofer,et al.  Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity , 1992, Molecular and cellular biology.

[43]  G. Schulz,et al.  Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. , 1992, Journal of molecular biology.

[44]  R. Goody,et al.  Is there a rate-limiting step before GTP cleavage by H-ras p21? , 1991, Biochemistry.

[45]  P. Kraulis.  A program to produce both detailed and schematic plots of protein structures , 1991 .

[46]  R. Kahn.  Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins. , 1991, The Journal of biological chemistry.

[47]  Frank McCormick,et al.  The GTPase superfamily: conserved structure and molecular mechanism , 1991, Nature.

[48]  S H Kim,et al.  Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. , 1992, Science.

[49]  Frank McCormick,et al.  The GTPase superfamily: a conserved switch for diverse cell functions , 1990, Nature.

[50]  W. Kabsch,et al.  Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. , 1990, The EMBO journal.

[51]  J. Eccleston,et al.  Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[52]  M. Chabre,et al.  Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology. , 1990, Trends in biochemical sciences.

[53]  R. Goody,et al.  Biochemical properties of Ha-ras encoded p21 mutants and mechanism of the autophosphorylation reaction. , 1988, The Journal of biological chemistry.

[54]  F. McCormick,et al.  A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants. , 1987, Science.

[55]  C. Der,et al.  Biological and biochemical properties of human ras H genes mutated at codon 61 , 1986, Cell.

[56]  P. Seeburg,et al.  Biological properties of human c-Ha-ras1 genes mutated at codon 12 , 1984, Nature.