N‐linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H + ‐ATPase (V‐ATPase) biosynthesis
Author:
Affiliation:
1. Faculty of Dentistry, Dental Research InstituteUniversity of TorontoTorontoOntarioCanada
2. Department of BiochemistryUniversity of TorontoTorontoOntarioCanada
Funder
Canadian Institutes of Health Research
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/jcb.26250
Reference42 articles.
1. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
2. Rotational catalysis in proton pumping ATPases: From E. coli F-ATPase to mammalian V-ATPase
3. The Vacuolar Proton ATPase (V-ATPase): Regulation and Therapeutic Targeting
4. Vacuolar H+-ATPase—an enzyme for all seasons
5. Definition of Membrane Topology and Identification of Residues Important for Transport in Subunit a of the Vacuolar ATPase
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3. Advances in understanding N-glycosylation structure, function, and regulation in health and disease;European Journal of Cell Biology;2021-09
4. Purification of active human vacuolar H+-ATPase in native lipid-containing nanodiscs;Journal of Biological Chemistry;2021-08
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