Functional model of metabolite gating by human voltage-dependent anion channel 2. - Wikidata - awgldk - TriplyDB

Functional model of metabolite gating by human voltage-dependent anion channel 2.

Functional model of metabolite gating by human voltage-dependent anion channel 2.

http://www.wikidata.org/entity/Q34866153

about

Mechanisms of ferroptosis Structure Determination of a Membrane Protein in Proteoliposomes High Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage-dependent Anion Channel 2 Reveal an Oligomeric Population Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial β-barrel anion channel hVDAC-2 Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2 Membrane protein structure determination in membrana.Ferroptosis: process and function.Sites and functional consequence of VDAC-alkylphenol anesthetic interactions.Mitochondria-associated endoplasmic reticulum membrane (MAM) regulates steroidogenic activity via steroidogenic acute regulatory protein (StAR)-voltage-dependent anion channel 2 (VDAC2) interaction NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs.Molecular Plasticity of the Human Voltage-Dependent Anion Channel Embedded Into a Membrane.N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry.Voltage-dependent anion channels modulate mitochondrial metabolism in cancer cells: regulation by free tubulin and erastin.Modulation of human mitochondrial voltage-dependent anion channel 2 (hVDAC-2) structural stability by cysteine-assisted barrel-lipid interactions.Voltage-dependant anion channels: novel insights into isoform function through genetic models.Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities.

P2860

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P2860

Functional model of metabolite gating by human voltage-dependent anion channel 2.

http://www.wikidata.org/entity/Q34866153

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@ast

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@en

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@nl

type

label

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@ast

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@en

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@nl

prefLabel

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@ast

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@en

Functional model of metabolite gating by human voltage-dependent anion channel 2.

@nl

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Functional model of metabolite gating by human voltage-dependent anion channel 2.

@en

P2093

Andras J Bauer

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

Brent R Stockwell

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

Kathryn M Lemberg

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

Simone Gieschler

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P2860

Probability-based protein secondary structure identification using combined NMR chemical-shift data

Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles

The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating

VDAC2 inhibits BAK activation and mitochondrial apoptosis

Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.

RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels.

On the role of VDAC in apoptosis: fact and fiction.

Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy.

The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins.

The published 3D structure of the VDAC channel: native or not?

P304

3408-3410

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scholarly article

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10.1021/BI2003247

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17

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50

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Ann E. McDermott

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2011-04-06T00:00:00Z

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50806954

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21425834

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3082971

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