The vacuolar (H+)-ATPases — nature's most versatile proton pumps

By T. Nishi, M. Forgac. Nature reviews. Molecular cell biology, 2002

1,233 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/d73a61a656fac6d8e6301d8433f567a10da2aa7f

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Citations in the corpus

Lipid-Based Drug Delivery Systems in Cancer Therapy: What Is Available and What Is Yet to Come (2016, background): “As the early endosome matures, vacuolar ATPase pumps are recruited to the endosome for the purpose of transporting H+ ions into the endosome decreasing the endosomal pH to as low as ;5.0 (Clague et al., 1994; Lee et al., 1996; Nishi and Forgac, 2002).”
Vacuolar H+-ATPase Activity Is Required for Endocytic and Secretory Trafficking in Arabidopsis[W] (2006, background): “…been found throughout the endomembrane system, including the endoplasmic reticulum, Golgi, and provacuoles (Chanson and Taiz, 1985; Ali and Akazawa, 1986; Herman et al., 1994; Oberbeck et al., 1994), the functions of the plant V-ATPase in secretory and endocytic trafficking are not well defined.”
Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology (2007, background): “This review focuses first on the structure and mechanism of V-ATPases, then on the regulation of V-ATPase activity and concludes with recent insights into the role that V-ATPases have in normal physiology (for recent reviews, see Ref”
The V-type H+ ATPase: molecular structure and function, physiological roles and regulation (2006, background): “Molecular architecture and mechanistic interpretations V-type H+ ATPases and F-ATPases share structural and functional similarities (Nishi and Forgac, 2002).”
Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo. (2008, neutral): “…step in the digestion process as the activity of digestive enzymes increases in a low-pH environment (Mellman et al., 1986). v-ATPases, the major cellular proton pumps, are multisubunit protein complexes consisting of the V0 and V1 sectors (Kawasaki-Nishi et al., 2003; Nishi and Forgac, 2002).”
Lysosomal Proteolysis and Autophagy Require Presenilin 1 and Are Disrupted by Alzheimer-Related PS1 Mutations (2010, neutral): “Its physical interaction with PS1 enables the N-glycosylation required for this subunit to be efficiently delivered to lysosomes (Gillespie et al., 1991; Nishi and Forgac, 2002).”