The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis.
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Regulation of the V-ATPase along the endocytic pathway occurs through reversible subunit association and membrane localizationV1 and V0 domains of the human H+-ATPase are linked by an interaction between the G and a subunitsHuman H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complexLysosomal membrane proteins and their central role in physiologyCharacterization of an M28 metalloprotease family member residing in the yeast vacuole.Organelle acidification is important for localisation of vacuolar proteins in Saccharomyces cerevisiae.Regulation of Vacuolar H+-ATPase (V-ATPase) Reassembly by Glycolysis Flow in 6-Phosphofructo-1-kinase (PFK-1)-deficient Yeast Cells.Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase.PKR1 encodes an assembly factor for the yeast V-type ATPase.Topological characterization of the c, c', and c" subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae.Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulumThe yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to control vesicle traffickingProton translocation driven by ATP hydrolysis in V-ATPasescDNA cloning and characterization of a novel gene encoding the MLF1-interacting protein MLF1IPAlternative splicing controls neuronal expression of v-ATPase subunit a1 and sorting to nerve terminalsA mouse model for distal renal tubular acidosis reveals a previously unrecognized role of the V-ATPase a4 subunit in the proximal tubule.V-ATPase V1 sector is required for corpse clearance and neurotransmission in Caenorhabditis elegansThe vacuolar ATPase from Entamoeba histolytica: molecular cloning of the gene encoding for the B subunit and subcellular localization of the protein.Inhibition of osteoclast bone resorption by disrupting vacuolar H+-ATPase a3-B2 subunit interaction.Glucose starvation inhibits autophagy via vacuolar hydrolysis and induces plasma membrane internalization by down-regulating recycling.Regulation and isoform function of the V-ATPases.Quantitative proteomic analysis reveals posttranslational responses to aneuploidy in yeast.Seventeen a-subunit isoforms of paramecium V-ATPase provide high specialization in localization and function.Luteolin inhibition of V-ATPase a3-d2 interaction decreases osteoclast resorptive activity.Atp6v0d2 is an essential component of the osteoclast-specific proton pump that mediates extracellular acidification in bone resorption.Conserved Arabidopsis ECHIDNA protein mediates trans-Golgi-network trafficking and cell elongationActivity of plasma membrane V-ATPases is critical for the invasion of MDA-MB231 breast cancer cells.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.Lansoprazole as a rescue agent in chemoresistant tumors: a phase I/II study in companion animals with spontaneously occurring tumors.Sorting of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase): identification of a necessary and sufficient Golgi/endosomal retention signal in Stv1pThe where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase.Role of transmembrane segment M8 in the biogenesis and function of yeast plasma-membrane H(+)-ATPaseTissue specific expression of the splice variants of the mouse vacuolar proton-translocating ATPase a4 subunitDeletion of vacuolar proton-translocating ATPase V(o)a isoforms clarifies the role of vacuolar pH as a determinant of virulence-associated traits in Candida albicansCellular environment is important in controlling V-ATPase dissociation and its dependence on activity.Function 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.
P2860
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P2860
The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@ast
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@en
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@nl
type
label
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@ast
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@en
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@nl
prefLabel
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@ast
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@en
The amino-terminal domain of t ...... transport and ATP hydrolysis.
@nl
P2093
P2860
P3181
P356
P1476
The amino-terminal domain of t ...... n transport and ATP hydrolysis
@en
P2093
S Kawasaki-Nishi
P2860
P304
47411-47420
P3181
P356
10.1074/JBC.M108310200
P407
P577
2001-10-09T00:00:00Z