Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity.
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Organelle acidification negatively regulates vacuole membrane fusion in vivo.Aldolase directly interacts with ARNO and modulates cell morphology and acidic vesicle distribution.Organelle-specific isoenzymes of plant V-ATPase as revealed by in vivo-FRET analysis.The vacuolar ATPase from Entamoeba histolytica: molecular cloning of the gene encoding for the B subunit and subcellular localization of the protein.Regulation and isoform function of the V-ATPases.Consequences of loss of Vph1 protein-containing vacuolar ATPases (V-ATPases) for overall cellular pH homeostasisThe reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae.Sorting of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase): identification of a necessary and sufficient Golgi/endosomal retention signal in Stv1pFunction and subunit interactions of the N-terminal domain of subunit a (Vph1p) of the yeast V-ATPaseStructure and regulation of the vacuolar ATPases.Function, structure and regulation of the vacuolar (H+)-ATPases.The yeast lysosome-like vacuole: endpoint and crossroadsThe RAVE complex is an isoform-specific V-ATPase assembly factor in yeast.Targeting reversible disassembly as a mechanism of controlling V-ATPase activityThe membrane domain of vacuolar H(+)ATPase: a crucial player in neurotransmitter exocytotic release.Proton Transport and pH Control in Fungi.Disorders of lysosomal acidification-The emerging role of v-ATPase in aging and neurodegenerative disease.pH-dependent localization of Btn1p in the yeast model for Batten diseaseThe Ras/cAMP/protein kinase A pathway regulates glucose-dependent assembly of the vacuolar (H+)-ATPase in yeast.Direct interaction of the Golgi V-ATPase a-subunit isoform with PI(4)P drives localization of Golgi V-ATPases in yeast.H+ and Pi Byproducts of Glycosylation Affect Ca2+ Homeostasis and Are Retrieved from the Golgi Complex by Homologs of TMEM165 and XPR1.
P2860
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P2860
Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Cellular environment is import ...... nd its dependence on activity.
@ast
Cellular environment is import ...... nd its dependence on activity.
@en
type
label
Cellular environment is import ...... nd its dependence on activity.
@ast
Cellular environment is import ...... nd its dependence on activity.
@en
prefLabel
Cellular environment is import ...... nd its dependence on activity.
@ast
Cellular environment is import ...... nd its dependence on activity.
@en
P2860
P356
P1476
Cellular environment is import ...... nd its dependence on activity.
@en
P2093
Michael Forgac
P2860
P304
24743-24751
P356
10.1074/JBC.M700663200
P407
P577
2007-06-12T00:00:00Z