Crossref
journal-article
Elsevier BV
Journal of Molecular Biology (78)
References
68
Referenced
374
10.1038/20726
/ Nature / Structure of Cdc42 in complex with the GTPase-binding domain of the “Wiskott-Aldrich syndrome” protein by Abdul-Manan (1999)10.1093/nar/25.17.3389
/ Nucl. Acids Res. / Gapped BLAST and PSI-BLAST by Altschul (1997)10.1006/jmbi.1999.2820
/ J. Mol. Biol. / Model of the Ran-RCC1 interaction using biochemical and docking experiments by Azuma (1999)10.1074/jbc.273.19.11596
/ J. Biol. Chem. / Determination of interaction sites on the small G protein RhoA for phospholipase D by Bae (1998)10.1146/annurev.bi.56.070187.004023
/ Annu. Rev. Biochem. / Ras genes by Barbacid (1987)10.1002/j.1460-2075.1991.tb08010.x
/ EMBO J. / Mutational analysis of the putative effector domain of the GTP-binding Ypt1 protein in yeast suggests specific regulation by a novel GAP activity by Becker (1991)10.1016/S0021-9258(17)36877-1
/ J. Biol. Chem. / Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase by Beranger (1994)10.1093/emboj/17.13.3651
/ EMBO J. / A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the β-phosphate to destabilize GDP on ARF1 by Béraud-Dufour (1998)10.1038/28548
/ Nature / The structural basis of the activation of Ras by Sos by Boriack-Sjodin (1998)10.1038/348125a0
/ Nature / The GTPase superfamily by Bourne (1990)10.1038/349117a0
/ Nature / The GTPase superfamily by Bourne (1991)10.1083/jcb.149.1.1-a
/ J. Cell Biol. / Reversal of fortune by Brennwald (2000)10.1038/362560a0
/ Nature / Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4 by Brennwald (1993)10.1016/S0021-9258(18)98366-3
/ J. Biol. Chem. / Mutants of Rab3A analogous to oncogenic Ras mutants. Sensitivity to Rab3A-GTPase activating protein and Rab3A-guanine nucleotide releasing factor by Brondyk (1993)10.1016/S0021-9258(18)50006-5
/ J. Biol. Chem. / Amino acid residues in the Ras-like GTPase Rab3A that specify sensitivity to factors that regulate the GTP/GDP cycling of Rab3A by Burstein (1992)10.1074/jbc.271.10.5289
/ J. Biol. Chem. / Protein prenyltransferases by Casey (1996)10.1016/S0955-0674(99)80067-2
/ Curr. Opin. Cell Biol. / The role of Arf and Rab GTPases in membrane transport by Chavrier (1999)10.1038/353769a0
/ Nature / Hypervariable C-terminal domain of rab proteins acts as a targeting signal by Chavrier (1991)10.1093/nar/16.22.10881
/ Nucl. Acids Res. / Multiple sequence alignment with hierarchical clustering by Corpet (1988)10.1128/MCB.18.12.7444
/ Mol. Cell Biol. / Distinct subclasses of small GTPases interact with guanine nucleotide exchange factors in a similar manner by Day (1998)10.1016/S0969-2126(99)80054-9
/ Structure / Structural basis of activation and GTP hydrolysis in Rab proteins by Dumas (1999)10.1038/362563a0
/ Nature / Specificity domains distinguish the Ras-related GTPases Ypt1 and Sec 4 by Dunn (1993)10.1016/S0959-440X(96)80056-X
/ Curr. Opin. Struct. Biol. / Hidden Markov models by Eddy (1996)10.1074/jbc.275.6.3848
/ J. Biol. Chem. / Rab24 is an atypical member of the Rab GTPase family by Erdman (2000)10.1111/j.1558-5646.1985.tb00420.x
/ Evolution / Confidence limits on phylogenies by Felsenstein (1985)10.1074/jbc.271.33.19794
/ J. Biol. Chem. / Rac “insert region” is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65 by Freeman (1996)10.1016/S0014-5793(98)00967-3
/ FEBS Letters / Distribution and functional diversification of the ras superfamily in Saccharomyces cerevisiae by Garcia-Ranea (1998)10.1016/S0092-8674(00)81754-7
/ Cell / Structural basis for activation of ARF GTPase by Goldberg (1998)10.1016/S0092-8674(00)80598-X
/ Cell / Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis by Goldberg (1999)10.1002/elps.1150181505
/ Electrophoresis / SWISS-MODEL and the Swiss-PdbViewer by Guex (1996)10.1096/fasebj.6.8.1592203
/ FASEB J. / The Ras superfamily of GTP-binding proteins by Kahn (1992)10.1016/S0968-0004(97)01150-X
/ Trends Biochem. Sci. / Vesicular transport by Lazar (1997)10.1074/jbc.272.8.4671
/ J. Biol. Chem. / Residues of the Rho family GTPases Rho and Cdc42 that specify sensitivity to Dbl-like guanine nucleotide exchange factors by Li (1997)10.1016/S1097-2765(00)80389-5
/ Mol. Cell / The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1 by Maesaki (1999)10.1016/S0021-9258(20)80546-8
/ J. Biol. Chem. / The Rab3A GTPase interacts with multiple factors through the same effector domain by McKiernan (1993)10.1016/S0968-0004(00)88939-2
/ Trends Biochem. Sci. / Subclass-specific sequence motifs identified in Rab GTPases by Moore (1995)10.1006/bbrc.1998.9968
/ Biochem. Biophys. Res. Commun. / Cloning and characterization of a novel Rab-family gene, Rab36, within the region at 22q11. 2 that is homozygously deleted in malignant rhabdoid tumors by Mori (1999)10.1016/S0092-8674(00)80933-2
/ Cell / Structure of the guanine nucleotide exchange factor Sec7 domain of human Arno and analysis of the interaction with ARF GTPase by Mossessova (1998)10.1038/20732
/ Nature / Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK by Mott (1999)10.1038/375554a0
/ Nature / The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue by Nassar (1995)10.1038/4156
/ Nature Struct. Biol. / Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP by Nassar (1998)10.1016/S0955-0674(97)80025-7
/ Curr. Opin. Cell Biol. / The diversity of Rab proteins in vesicle transport by Novick (1997)10.1016/S0074-7696(08)61608-3
/ Int. Rev. Cytol. / Role of Rab GTPases in membrane traffic by Olkkonen (1997)10.1016/S0092-8674(00)80549-8
/ Cell / Structural basis of Rab effector specificity by Ostermeier (1999)10.1091/mbc.9.1.223
/ Mol. Biol. Cell / The putative “switch 2“ domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein by Overmeyer (1998)10.1038/341209a0
/ Nature / Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation by Pai (1989)10.1016/0300-9084(96)84768-7
/ Biochimie / WWW-query by Perriere (1996)10.1242/jcs.113.2.183
/ J. Cell Sci. / RabGTPases coordinate endocytosis by Rodman (2000)10.1091/mbc.6.1.71
/ Mol. Biol. Cell / Properties of Rab5 N-terminal domain dictate prenylation of C-terminal cysteines by Sanford (1995)10.1126/science.277.5324.333
/ Science / The Ras-RasGAP complex by Scheffzek (1997)10.1074/jbc.273.35.22161
/ J. Biol. Chem. / Rab GTPases, directors of vesicle docking by Schimmoller (1998)10.1016/S0021-9258(19)49740-8
/ J. Biol. Chem. / Rab geranylgeranyl transferase by Seabra (1992)10.1159/000134591
/ Cytogenet. Cell Genet. / Cloning and chromosome assignment to 1q32 of a human cDNA (RAB7L1) encoding a small GTP-binding protein, a member of the RAS superfamily by Shimizu (1997)10.1006/geno.1996.4595
/ Genomics / Construction of a transcription map around the gene for ataxia telangiectasia by Stankovic (1997)10.1002/j.1460-2075.1994.tb06295.x
/ EMBO J. / Distinct structural elements of rab5 define its functional specificity by Stenmark (1994)10.1006/jmbi.1997.1602
/ J. Mol. Biol. / Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran by Stewart (1998)10.1093/nar/22.22.4673
/ Nucl. Acids Res. / CLUSTAL W by Thompson (1994)10.1093/nar/25.24.4876
/ Nucl. Acids Res. / The CLUSTAL_X windows interface by Thompson (1997)10.1016/0022-2836(91)90753-S
/ J. Mol. Biol. / Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP by Tong (1991)10.1021/bi00233a001
/ Biochemistry / The ras protein family by Valencia (1991)10.1016/S0092-8674(00)80774-6
/ Cell / Structural view of the Ran-Importin beta interaction at 2.3 Å resolution by Vetter (1999)10.1038/17969
/ Nature / Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue by Vetter (1999)10.1016/S0014-5793(99)00555-4
/ FEBS Letters / Structural and biochemical analysis of Ras-effector signaling via RalGDS by Vetter (1999)10.1016/0092-8674(95)90507-3
/ Cell / Multiple ras functions can contribute to mammalian cell transformation by White (1995)10.1016/S0021-9258(18)82364-X
/ J. Biol. Chem. / Isoprenylation of Rab1B is impaired by mutations in its effector domain by Wilson (1993)10.1074/jbc.271.18.10932
/ J. Biol. Chem. / Association of Rab1B with GDP-dissociation inhibitor (GDI) is required for recycling but not initial membrane targeting of the Rab protein by Wilson (1996)10.1006/geno.1999.5889
/ Genomics / Two novel human RAB genes with near identical sequence each map to a telomere-associated region by Wong (1999)10.1074/jbc.274.8.4551
/ J. Biol. Chem. / Loop 6 of RhoA confers specificity for effector binding, stress fiber formation, and cellular transformation by Zhong (1999)
Dates
Type | When |
---|---|
Created | 22 years, 11 months ago (Sept. 18, 2002, 3:24 p.m.) |
Deposited | 4 years, 3 months ago (May 2, 2021, 9:37 p.m.) |
Indexed | 3 days, 3 hours ago (Aug. 26, 2025, 2:33 a.m.) |
Issued | 25 years ago (Aug. 1, 2000) |
Published | 25 years ago (Aug. 1, 2000) |
Published Print | 25 years ago (Aug. 1, 2000) |
@article{Pereira_Leal_2000, title={The mammalian Rab family of small GTPases: definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily 1 1Edited by M. Yaniv}, volume={301}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.2000.4010}, DOI={10.1006/jmbi.2000.4010}, number={4}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Pereira-Leal, José B and Seabra, Miguel C}, year={2000}, month=aug, pages={1077–1087} }