Subunit interactions and requirements for inhibition of the yeast V1-ATPase. - Wikidata - awgldk - TriplyDB

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

http://www.wikidata.org/entity/Q43131524

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Probing subunit-subunit interactions in the yeast vacuolar ATPase by peptide arrays Rotating with the brakes on and other unresolved features of the vacuolar ATPase Structural Basis of Molecular Recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at Membrane Surfaces Crystal Structure of the Cytoplasmic N-Terminal Domain of Subunit I, a Homolog of Subunit a, of V-ATPase Regulation of Vacuolar H+-ATPase (V-ATPase) Reassembly by Glycolysis Flow in 6-Phosphofructo-1-kinase (PFK-1)-deficient Yeast Cells.Extracellular glucose increases the coupling capacity of the yeast V H+-ATPase and the resistance of its H+ transport activity to nitrate inhibition Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.Breaking up and making up: The secret life of the vacuolar H+ -ATPase.Subunit positioning and stator filament stiffness in regulation and power transmission in the V1 motor of the Manduca sexta V-ATPase.Regulation and isoform function of the V-ATPases.Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.Molecular Interactions and Cellular Itinerary of the Yeast RAVE (Regulator of the H+-ATPase of Vacuolar and Endosomal Membranes) Complex Structural analysis of the N-terminal domain of subunit a of the yeast vacuolar ATPase (V-ATPase) using accessibility of single cysteine substitutions to chemical modification.The RAVE complex is an isoform-specific V-ATPase assembly factor in yeast.Structural divergence of the rotary ATPases.Targeting reversible disassembly as a mechanism of controlling V-ATPase activity Saccharomyces cerevisiae vacuolar H+-ATPase regulation by disassembly and reassembly: one structure and multiple signals.Recent Insights into the Structure, Regulation, and Function of the V-ATPases Crystal structure of yeast V1-ATPase in the autoinhibited state.Elevated expression of the V-ATPase C subunit triggers JNK-dependent cell invasion and overgrowth in a Drosophila epithelium.Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution.Single-molecule analysis of inhibitory pausing states of V1-ATPase.Regulation of vacuolar H+-ATPase activity by the Cdc42 effector Ste20 in Saccharomyces cerevisiae Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity.

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P2860

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

http://www.wikidata.org/entity/Q43131524

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh-hant

name

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

@en

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

@nl

type

label

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

@en

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

@nl

prefLabel

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

@en

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

@nl

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P1433

Journal of Biological Chemistry

P1476

Subunit interactions and requirements for inhibition of the yeast V1-ATPase.

@en

P2093

Ester Cobb

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Heba Diab

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Mali Liu

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Masashi Ohira

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Patricia M Kane

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P2860

Crystal structure of yeast V-ATPase subunit C reveals its stator function

Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae

The structure of bovine F1-ATPase in complex with its regulatory protein IF1

How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria

Novel vacuolar H+-ATPase complexes resulting from overproduction of Vma5p and Vma13p.

Assembly and targeting of peripheral and integral membrane subunits of the yeast vacuolar H(+)-ATPase.

The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex.

Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast

Vacuolar and plasma membrane proton-adenosinetriphosphatases

The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes

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13316-13325

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scholarly article

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10.1074/JBC.M900475200

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20

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284

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2009-03-19T00:00:00Z

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19299516

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2679431

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