Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase. - Wikidata - wikimedia - TriplyDB

Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

http://www.wikidata.org/entity/Q35921635

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Probing subunit-subunit interactions in the yeast vacuolar ATPase by peptide arrays Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy Organelle acidification negatively regulates vacuole membrane fusion in vivo.Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGChead Peripheral Stalk Complex Biochemical and biophysical properties of interactions between subunits of the peripheral stalk region of human V-ATPase 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.The V-ATPase membrane domain is a sensor of granular pH that controls the exocytotic machinery.Subunit positioning and stator filament stiffness in regulation and power transmission in the V1 motor of the Manduca sexta V-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.Glu-44 in the amino-terminal α-helix of yeast vacuolar ATPase E subunit (Vma4p) has a role for VoV1 assembly The RAVE complex is an isoform-specific V-ATPase assembly factor in yeast.The signaling lipid PI(3,5)P₂ stabilizes V₁-V(o) sector interactions and activates the V-ATPase Recent Insights into the Structure, Regulation, and Function of the V-ATPases Proton Transport and pH Control in Fungi.Regulation of V-ATPase assembly and function of V-ATPases in tumor cell invasiveness.Chemical screening identifies ATM as a target for alleviating senescence.Crystal structure of yeast V1-ATPase in the autoinhibited state.Direct interaction of the Golgi V-ATPase a-subunit isoform with PI(4)P drives localization of Golgi V-ATPases in yeast.Biolayer interferometry of lipid nanodisc-reconstituted yeast vacuolar H+ -ATPase.Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity.The Peripheral Stalk of Rotary ATPases Vacuolar H+-ATPase: An Essential Multitasking Enzyme in Physiology and Pathophysiology

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P2860

Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

http://www.wikidata.org/entity/Q35921635

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

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Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

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Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

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Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

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Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

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Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

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JBC.M112.343962

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Journal of Biological Chemistry

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Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.

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Rebecca A Oot

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Stephan Wilkens

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P2860

Regulation of the V-ATPase along the endocytic pathway occurs through reversible subunit association and membrane localization

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway

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

Structure of the yeast vacuolar ATPase

Crystal Structure of the Cytoplasmic N-Terminal Domain of Subunit I, a Homolog of Subunit a, of V-ATPase

Crystal structure of the central axis DF complex of the prokaryotic V-ATPase

Protein secondary structure prediction based on position-specific scoring matrices

UCSF Chimera--a visualization system for exploratory research and analysis

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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13396-13406

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scholarly article

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10.1074/JBC.M112.343962

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16

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287

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2012-02-24T00:00:00Z

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3339975

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