Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase. - Wikidata - awgldk - TriplyDB

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

http://www.wikidata.org/entity/Q27933274

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Rotating with the brakes on and other unresolved features of the vacuolar ATPase PKR1 encodes an assembly factor for the yeast V-type ATPase.Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.Disruption of iron homeostasis in Saccharomyces cerevisiae by high zinc levels: a genome-wide study.Organelle-specific isoenzymes of plant V-ATPase as revealed by in vivo-FRET analysis.Saccharomyces cerevisiae genome-wide mutant screen for sensitivity to 2,4-diacetylphloroglucinol, an antibiotic produced by Pseudomonas fluorescens.Arabidopsis has two functional orthologs of the yeast V-ATPase assembly factor Vma21p A genome-wide enhancer screen implicates sphingolipid composition in vacuolar ATPase function in Saccharomyces cerevisiae.Glu-44 in the amino-terminal α-helix of yeast vacuolar ATPase E subunit (Vma4p) has a role for VoV1 assembly Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution.The binding site of the V-ATPase inhibitor apicularen is in the vicinity of those for bafilomycin and archazolid.Atomic model for the membrane-embedded VO motor of a eukaryotic V-ATPase.

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Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

http://www.wikidata.org/entity/Q27933274

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2006年の論文

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2006年論文

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2006年論文

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2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@ast

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@en

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@nl

type

label

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@ast

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@en

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@nl

prefLabel

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@ast

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@en

Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.

@nl

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Journal of Biological Chemistry

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Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase

@en

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Laurie A Graham

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

Mark A Compton

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

P2860

Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness

Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules

Structure, function and regulation of the vacuolar (H+)-ATPase

Role of Vma21p in assembly and transport of the yeast vacuolar ATPase

Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex

Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex

Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase

Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis

VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H+-ATPase assembly

Topological characterization of the c, c', and c" subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae.

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15312-15319

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scholarly article

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1134122

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10.1074/JBC.M600890200

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22

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281

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2006-03-27T00:00:00Z

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16569636

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