A Different Conformation for EGC Stator Subcomplex in Solution and in the Assembled Yeast V-ATPase: Possible Implications for Regulatory Disassembly-Reference-Cited by-同舟云学术

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A Different Conformation for EGC Stator Subcomplex in Solution and in the Assembled Yeast V-ATPase: Possible Implications for Regulatory Disassembly

Published:2008-12 Issue:12 Volume:16 Page:1789-1798
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Diepholz Meikel,Venzke David,Prinz Simone,Batisse Claire,Flörchinger Beate,Rössle Manfred,Svergun Dmitri I.,Böttcher Bettina,Féthière James

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference53 articles.

1. Cysteine-directed cross-linking to subunit B suggests that subunit E forms part of the peripheral stalk of the vacuolar H+-ATPase;Arata;J. Biol. Chem.,2002

2. Structural analysis of the stalk subunit Vma5p of the yeast V-ATPase in solution;Armbrüster;FEBS Lett.,2004

3. Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy;Bernal;Structure,2004

4. Biological motors: connecting stalks in V-type ATPase;Boekema;Nature,1999

5. Crystal structure of yeast V-ATPase subunit C reveals its stator function;Drory;EMBO Rep.,2004

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1. Eukaryotic yeast V1-ATPase rotary mechanism insights revealed by high-resolution single-molecule studies;Frontiers in Molecular Biosciences;2024-03-19

2. Tender love and disassembly: How a TLDc domain protein breaks the V‐ATPase;BioEssays;2023-05-15

3. Membrane Proteins | Structure and Mechanism of the Vacuolar H+-ATPase;Encyclopedia of Biological Chemistry III;2021

4. Structure and Roles of V-type ATPases;Trends in Biochemical Sciences;2020-04

5. The Peripheral Stalk of Rotary ATPases;Frontiers in Physiology;2018-09-04

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