TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. - Wikidata - awgldk - TriplyDB

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

http://www.wikidata.org/entity/Q34549396

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OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation TBC1D24, an ARF6-interacting protein, is mutated in familial infantile myoclonic epilepsy The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers RAB3GAP1 and RAB3GAP2 modulate basal and rapamycin-induced autophagy Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways RabGEFs are a major determinant for specific Rab membrane targeting RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues A Rab-GAP TBC domain protein binds hepatitis C virus NS5A and mediates viral replication Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5 Identification of Rab11 as a small GTPase binding protein for the Evi5 oncogene Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1 Regulation of small GTPases by GEFs, GAPs, and GDIs GTPase networks in membrane traffic TBC-8, a putative RAB-2 GAP, regulates dense core vesicle maturation in Caenorhabditis elegans Structure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinase Mechanism of ATP turnover inhibition in the EJC The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b Crystal Structures of Human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating Protein (RabGAP) Domains Reveal Critical Elements for GLUT4 Translocation Crystal structure of the intraflagellar transport complex 25/27 Protein LidA from Legionella is a Rab GTPase supereffector Catalytic mechanism of a mammalian Rab{middle dot}RabGAP complex in atomic detail Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP The Legionella pneumophila GTPase Activating Protein LepB Accelerates Rab1 Deactivation by a Non-canonical Hydrolytic Mechanism Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold Structures of PI4KIII complexes show simultaneous recruitment of Rab11 and its effectors Crystal structure of a Chlamydomonas reinhardtii flagellar RabGAP TBC-domain at 1.8 Å resolution Noncanonical Myo9b-RhoGAP Accelerates RhoA GTP Hydrolysis by a Dual-Arginine-Finger Mechanism Skywalker-TBC1D24 has a lipid-binding pocket mutated in epilepsy and required for synaptic function Asymmetry of the budding yeast Tem1 GTPase at spindle poles is required for spindle positioning but not for mitotic exit.The Msb3/Gyp3 GAP controls the activity of the Rab GTPases Vps21 and Ypt7 at endosomes and vacuoles Vps9 family protein Muk1 is the second Rab5 guanosine nucleotide exchange factor in budding yeast.Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase.Termination of isoform-selective Vps21/Rab5 signaling at endolysosomal organelles by Msb3/Gyp3.ACBD3 interaction with TBC1 domain 22 protein is differentially affected by enteroviral and kobuviral 3A protein binding TBCK influences cell proliferation, cell size and mTOR signaling pathway RUTBC1 Functions as a GTPase-activating Protein for Rab32/38 and Regulates Melanogenic Enzyme Trafficking in Melanocytes

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P2860

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

http://www.wikidata.org/entity/Q34549396

description

2006 nî lūn-bûn

@nan

2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@ast

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@en

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@nl

type

label

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@ast

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@en

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@nl

prefLabel

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@ast

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@en

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.

@nl

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TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism

@en

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David G Lambright

http://www.w3.org/2001/XMLSchema#string

Sudharshan Eathiraj

http://www.w3.org/2001/XMLSchema#string

Xiaojing Pan

http://www.w3.org/2001/XMLSchema#string

P2860

Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP

Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome

The GTPase-activating protein Rap1GAP uses a catalytic asparagine

Structural basis of family-wide Rab GTPase recognition by rabenosyn-5

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue

AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain

Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins

Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A

GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4

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303-306

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scholarly article

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10.1038/NATURE04847

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7100

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442

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2006-07-01T00:00:00Z

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1033640020

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16855591

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P921

RAB33B, member RAS oncogene family