GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential. - sprookjes - yvandenbroek - TriplyDB

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

http://www.wikidata.org/entity/Q34395820

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Mitochondria, calcium, and tumor suppressor Fus1: At the crossroad of cancer, inflammation, and autoimmunity Transcriptome profile of the early stages of breast cancer tumoral spheroids Higher order signaling: ARL2 as regulator of both mitochondrial fusion and microtubule dynamics allows integration of 2 essential cell functions.The ARL2 GTPase regulates mitochondrial fusion from the intermembrane space.ADP-ribosylation factor-like 4C binding to filamin-A modulates filopodium formation and cell migration.

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P2860

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

http://www.wikidata.org/entity/Q34395820

description

2012 nî lūn-bûn

@nan

2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@ast

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@en

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@nl

type

label

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@ast

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@en

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@nl

prefLabel

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@ast

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@en

GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.

@nl

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JOURNAL.PONE.0043552

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GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential

@en

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Chun-Chun Li

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Chun-Fang Huang

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Li-Ting Jang

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Shu-Ting You

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

Tsung-Sheng Wu

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

Yu-Tsan Liu

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P2860

ADP-ribosylation factor (ARF)-like 4, 6, and 7 represent a subgroup of the ARF family characterization by rapid nucleotide exchange and a nuclear localization signal

Structures and Proton-Pumping Strategies of Mitochondrial Respiratory Enzymes

ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli

ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter

The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane

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

Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins.

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Structure and Membrane Interaction of Myristoylated ARF1

Mutations in a member of the Ras superfamily of small GTP-binding proteins causes Bardet-Biedl syndrome.

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e43552

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8

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Gunn-Guang Liou

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2012-08-21T00:00:00Z

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230749430

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