The structure of the GTPase-activating domain from p50rhoGAP
about
Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2Physical and functional interaction of Fyn tyrosine kinase with a brain-enriched Rho GTPase-activating protein TCGAPStructure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogueCrystal structure of a small G protein in complex with the GTPase-activating protein rhoGAPARHGAP18, a GTPase-activating protein for RhoA, controls cell shape, spreading, and motilityExportin 7 defines a novel general nuclear export pathwayA vascular cell-restricted RhoGAP, p73RhoGAP, is a key regulator of angiogenesisCrystal structure of the GTPase-activating protein-related domain from IQGAP1p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signalingStructure of the BH domain from graf and its implications for Rho GTPase recognitionStructure of the ExoS GTPase activating domainThe Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the MembraneThe BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAPCharacterization of the interactions between the small GTPase Cdc42 and its GTPase-activating proteins and putative effectors. Comparison of kinetic properties of Cdc42 binding to the Cdc42-interactive domainsStructural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoAThe rat myosin myr 5 is a GTPase-activating protein for Rho in vivo: essential role of arginine 1695The function of the p190 Rho GTPase-activating protein is controlled by its N-terminal GTP binding domainRegulation of CDC42 GTPase by proline-rich tyrosine kinase 2 interacting with PSGAP, a novel pleckstrin homology and Src homology 3 domain containing rhoGAP protein.Sec14 homology domain targets p50RhoGAP to endosomes and provides a link between Rab and Rho GTPasesCloning and characterization of a rhoGAP homolog from Dictyostelium discoideum.Deciphering the Molecular and Functional Basis of RHOGAP Family Proteins: A SYSTEMATIC APPROACH TOWARD SELECTIVE INACTIVATION OF RHO FAMILY PROTEINS.Overview of protein structural and functional folds.Loss of the RhoGAP SRGP-1 promotes the clearance of dead and injured cells in Caenorhabditis elegansSRGP-1 regulation, targets, and contribution to cell killing in C. elegansDissecting the thermodynamics of GAP-RhoA interactions.Sequence analysis of a human RhoGAP domain-containing gene and characterization of its expression in human multiple tissues.The BNIP-2 and Cdc42GAP homology (BCH) domain of p50RhoGAP/Cdc42GAP sequesters RhoA from inactivation by the adjacent GTPase-activating protein domain.RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is involved in the beta-catenin-N-cadherin and N-methyl-D-aspartate receptor signaling.Characterization of a novel GTPase-activating protein associated with focal adhesions and the actin cytoskeleton.Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1).Differential proteomic profiling unveils new molecular mechanisms associated with mitochondrial complex III deficiency.Purification, crystallization and initial X-ray crystallographic analysis of the putative GTPase PH0525 from Pyrococcus horikoshii OT3.Functional plasticity of the BNIP-2 and Cdc42GAP Homology (BCH) domain in cell signaling and cell dynamics.In Silico Approach for SAR Analysis of the Predicted Model of DEPDC1B: A Novel Target for Oral CancerThe Rho-GAP Bem2p plays a GAP-independent role in the morphogenesis checkpointA new nucleocytoplasmic RhoGAP protein contributes to control the pathogenicity of Entamoeba histolytica by regulating EhRacC and EhRacD activity.ExoS Rho GTPase-activating protein activity stimulates reorganization of the actin cytoskeleton through Rho GTPase guanine nucleotide disassociation inhibitor.Morphological changes and detachment of adherent cells induced by p122, a GTPase-activating protein for Rho.The interaction of Ras with GTPase-activating proteins.
P2860
Q22254035-5C4BE502-D5C6-43D4-8AF2-F45EBD4F0680Q24293647-1D0C1130-BE72-45C1-8CED-07187F1056B2Q24319143-1AFE5622-67C9-4205-9654-CA83931BFE85Q24324015-F29E83DC-D1AB-4D6A-8025-E19079CFCBA4Q24329072-00A414D4-148B-41D0-A790-1F414056199EQ24563375-A5AE9B66-84BB-4BE3-9AE8-EFDA62332605Q24563457-DF21C1E3-6AAE-4763-A7D4-6318908D5F4EQ24657246-0F90FAE7-A6D4-4E69-9F19-B0614D85D6C4Q24681364-8D25F979-68ED-4149-98D0-9AF096EB7A95Q27626985-F0379A14-93E3-465F-B42A-E4CF2530D9CDQ27630200-769B03F6-FD5A-4724-A7BE-E3E05300A71CQ27680559-2FE1D275-EC9A-4262-B611-D8559767829BQ28144356-4D8393EB-A3F2-494D-ACB1-E70F9E75A056Q28246965-B8EE5F29-0301-43DC-8A10-1C5296244F04Q28257299-04B1EC89-AC38-4049-91C0-0C54BE9123D8Q28267082-052CCDB1-F67C-44D3-8BC6-3BE0C720BDC5Q28578515-7399BF4F-719F-4F3B-AF7B-C657E9534CEFQ28584342-D36AFE3C-A4E1-412B-9F47-AE2498530E21Q28592539-99C0B582-E5D7-4385-98CD-935C8CAC06E9Q28910420-998326C7-6B9F-415F-A93F-66BEE9EEBCA3Q30176506-02AF3DBA-34FF-453C-AC6A-3125545974ECQ30276221-3A95C4DA-26A2-4FF2-AD6D-01681DBEDDDAQ30368988-8A497099-0DA2-4407-8CF4-BCF1AC4B3614Q30416737-B3D6F4D6-AC19-4FC2-8A7A-22747DCFA098Q30431363-B602287E-E642-4404-A2E5-3EA2069A75FAQ30437529-650D1AC3-BAE9-4537-8621-E7B24CF393D9Q33282566-022699BE-F103-45D8-8015-CB76439884DEQ34123413-EE75BC73-517F-49D4-AFC8-E2E58233D8B4Q34171099-EE08584D-E7F1-497F-AA96-8AC484FAA086Q34378405-DF3BF9DE-EB91-4FDE-8153-95D362BEF34BQ34454079-0C2A0CAC-F538-4FF7-8769-794D2E03ABE3Q34657128-91EB0869-99F4-407C-8A4E-7ACEDCAAA8A9Q36010073-DB49F417-5188-443D-8CD9-B96E13128455Q38019705-302EA70C-1A46-4CC4-9382-1E9840CB807CQ38961231-CDD2FB9B-A30D-4159-8649-611BEF409823Q39647851-A32DF12B-062B-4D21-9733-3ACD271988B4Q40488638-48C04C90-E1C2-4D5F-B5D1-D75F548DA06BQ40528901-24BF1BF2-B233-4BDD-8423-8975FCC7290DQ40949147-043BE0AC-0451-497C-B5E5-FCF1BB57E19EQ41554070-C348C8BB-00EF-4F44-8435-7DFC7771636C
P2860
The structure of the GTPase-activating domain from p50rhoGAP
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The structure of the GTPase-activating domain from p50rhoGAP
@ast
The structure of the GTPase-activating domain from p50rhoGAP
@en
The structure of the GTPase-activating domain from p50rhoGAP
@nl
type
label
The structure of the GTPase-activating domain from p50rhoGAP
@ast
The structure of the GTPase-activating domain from p50rhoGAP
@en
The structure of the GTPase-activating domain from p50rhoGAP
@nl
prefLabel
The structure of the GTPase-activating domain from p50rhoGAP
@ast
The structure of the GTPase-activating domain from p50rhoGAP
@en
The structure of the GTPase-activating domain from p50rhoGAP
@nl
P2093
P356
P1433
P1476
The structure of the GTPase-activating domain from p50rhoGAP
@en
P2093
E J Dodson
J F Eccleston
K Nurmahomed
S B Ludbrook
S J Gamblin
S J Smerdon
P2888
P304
P356
10.1038/385458A0
P407
P577
1997-01-30T00:00:00Z
P6179
1024724313