Modifications to the C-terminus of Arf1 alter cell functions and protein interactions. - sprookjes - yvandenbroek - TriplyDB

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

http://www.wikidata.org/entity/Q30432201

about

Regulating the large Sec7 ARF guanine nucleotide exchange factors: the when, where and how of activation Dynamic structure of membrane-anchored Arf•GTP Arl13b regulates ciliogenesis and the dynamic localization of Shh signaling proteins Advantages and limitations of cell-based assays for GTPase activation and regulation.Phosphatidylinositol-4-phosphate 5-kinase and GEP100/Brag2 protein mediate antiangiogenic signaling by semaphorin 3E-plexin-D1 through Arf6 protein Arf6 regulation of Gyrating-clathrin Chlamydia Hijacks ARF GTPases To Coordinate Microtubule Posttranslational Modifications and Golgi Complex Positioning Arf3 is activated uniquely at the trans-Golgi network by brefeldin A-inhibited guanine nucleotide exchange factors Sar1 assembly regulates membrane constriction and ER export Quantitative Analysis of Guanine Nucleotide Exchange Factors (GEFs) as Enzymes.GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.Inhibition of Cytohesins Protects against Genetic Models of Motor Neuron Disease.GTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic activity.The pleckstrin homology (PH) domain of the Arf exchange factor Brag2 is an allosteric binding site.Nucleotide exchange factors: Kinetic analyses and the rationale for studying kinetics of GEFs.Rab7 mutants associated with Charcot-Marie-Tooth disease cause delayed growth factor receptor transport and altered endosomal and nuclear signaling.A role for cargo in Arf-dependent adaptor recruitment GTPase cross talk regulates TRAPPII activation of Rab11 homologues during vesicle biogenesis Approaches to studying Arf GAPs in cells: in vitro assay with isolated focal adhesions.ADP-ribosylation factor 1 (ARF1) takes part in cell proliferation and cell adhesion-mediated drug resistance (CAM-DR).Tool box: Plasmids for the expression or knockdown of human ARF Family GTPases (ARF/ARL/SAR) and their co-expression in bacteria with N-myristoyltransferases In vivo monitoring of the recruitment and activation of AP-1 by Arf1.The small GTPase ARL2 is required for cytokinesis in Trypanosoma brucei.A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi A role for the vesicle-associated tubulin binding protein ARL6 (BBS3) in flagellum extension in Trypanosoma brucei.G protein coupled receptor signaling complexes in live cells.Four GTPases differentially regulate the Sec7 Arf-GEF to direct traffic at the trans-golgi network.Multiple interactions between an Arf/GEF complex and charged lipids determine activation kinetics on the membrane.Nucleotide Binding to ARL2 in the TBCD∙ARL2∙β-Tubulin Complex Drives Conformational Changes in β-Tubulin.Pex35 is a regulator of peroxisome abundance.

P2860

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P2860

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

http://www.wikidata.org/entity/Q30432201

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

@ast

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

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type

label

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

@ast

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

@en

prefLabel

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

@ast

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

@en

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J.1600-0854.2010.01054.X

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P1476

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

@en

P2093

James M Gruschus

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

Margaret Cavenagh

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

Paul A Randazzo

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

Richard A Kahn

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

Xiaoying Jian

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

P2860

Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors

ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter

Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor

Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins

Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication.

ADP-ribosylation factor is functionally and physically associated with the Golgi complex

Phylogenetic analysis of Sec7-domain-containing Arf nucleotide exchangers

Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31

Bound structures of novel P3-P1' beta-strand mimetic inhibitors of thrombin

Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity

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732-742

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scholarly article

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10.1111/J.1600-0854.2010.01054.X

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6

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11

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20214751

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2874613

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