Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases-Reference-Cited by-同舟云学术

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Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases

Published:2016-07 Issue:7 Volume:2 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Mazhab-Jafari Mohammad T.¹,Rubinstein John L.¹²³^ORCID

Affiliation:

1. Molecular Structure and Function Program, The Hospital for Sick Children Research Institute, 686 Bay Street, Toronto, Ontario M5G 0A4, Canada.

2. Department of Biochemistry, The University of Toronto, 1 King’s College Circle, Toronto, Ontario M5S 1A8, Canada.

3. Department of Medical Biophysics, The University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.

Abstract

V-ATPases are fascinating molecular machines; cryo-EM is providing unprecedented insight into their structure and dynamics.

Funder

Canadian Institutes of Health Research

Canada Research Chairs

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference127 articles.

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5. Present status and future prospects of spherical aberration corrected TEM/STEM for study of nanomaterials;Tanaka N.;Sci. Technol. Adv. Mater.,2008

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1. CRISPR/Cas9-mediated gene editing of vacuolar ATPase subunit d mediates phytohormone biosynthesis and virus resistance in rice;Frontiers in Plant Science;2023-02-01

2. Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding;Journal of Biological Chemistry;2023-02

3. ATP Proton Pumps. Function and Regulation;Encyclopedia of Cell Biology;2023

4. Structural transition of the ground-state structure to steady-state structures by sequential binding of ATP to V/A-ATPase;2022-10-05

5. Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis;Nature Communications;2022-05-24

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