a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
about
V1 and V0 domains of the human H+-ATPase are linked by an interaction between the G and a subunitsV-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathwayHuman H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1Optic nerve compression and retinal degeneration in Tcirg1 mutant mice lacking the vacuolar-type H-ATPase a3 subunitAldolase directly interacts with ARNO and modulates cell morphology and acidic vesicle distribution.Differential localization of the vacuolar H+ pump with G subunit isoforms (G1 and G2) in mouse neuronsRelocalization of the V-ATPase B2 subunit to the apical membrane of epididymal clear cells of mice deficient in the B1 subunitDistinct expression patterns of different subunit isoforms of the V-ATPase in the rat epididymisAlternative splicing controls neuronal expression of v-ATPase subunit a1 and sorting to nerve terminalsA proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidificationAn isoform of the vacuolar (H(+))-ATPase accessory subunit Ac45.Seventeen a-subunit isoforms of paramecium V-ATPase provide high specialization in localization and function.Renal vacuolar H+-ATPase.Activity of plasma membrane V-ATPases is critical for the invasion of MDA-MB231 breast cancer cells.The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae.Vacuolar ATPase 'a2' isoform exhibits distinct cell surface accumulation and modulates matrix metalloproteinase activity in ovarian cancerSorting of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase): identification of a necessary and sufficient Golgi/endosomal retention signal in Stv1pExtra-renal locations of the a4 subunit of H(+)ATPase.Rational identification of enoxacin as a novel V-ATPase-directed osteoclast inhibitor.Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity.Towards a better understanding and new therapeutics of osteopetrosis.The Function of V-ATPases in CancerThe yeast lysosome-like vacuole: endpoint and crossroadsFunction of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells.The function of vacuolar ATPase (V-ATPase) a subunit isoforms in invasiveness of MCF10a and MCF10CA1a human breast cancer cells.The a3 isoform of subunit a of the vacuolar ATPase localizes to the plasma membrane of invasive breast tumor cells and is overexpressed in human breast cancer.Uriniferous tubule: structural and functional organization.Our research on proton pumping ATPases over three decades: their biochemistry, molecular biology and cell biology.Vacuolar H(+)-ATPase subunits Voa1 and Voa2 cooperatively regulate secretory vesicle acidification, transmitter uptake, and storage.Vacuolar H+-ATPase in the nuclear membranes regulates nucleo-cytosolic proton gradients.Extracellular and Luminal pH Regulation by Vacuolar H+-ATPase Isoform Expression and Targeting to the Plasma Membrane and Endosomes.Acidification of uterine epithelium during embryo implantation in mice.Binding interactions of the peripheral stalk subunit isoforms from human V-ATPase.Osteopetrosis mutation R444L causes endoplasmic reticulum retention and misprocessing of vacuolar H+-ATPase a3 subunit.Cytoplasmic terminus of vacuolar type proton pump accessory subunit Ac45 is required for proper interaction with V(0) domain subunits and efficient osteoclastic bone resorption.Regulation of vacuolar H(+)-ATPase in microglia by RANKL.The a3 isoform of the 100-kDa V-ATPase subunit is highly but differentially expressed in large (>or=10 nuclei) and small (<or= nuclei) osteoclasts.From lysosomes to the plasma membrane: localization of vacuolar-type H+ -ATPase with the a3 isoform during osteoclast differentiation.Loss of G2 subunit of vacuolar-type proton transporting ATPase leads to G1 subunit upregulation in the brain.Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and C subunits.
P2860
Q24300220-89ED1B3E-C79C-498F-99E9-5F9D9345D38EQ24301314-5AD87E1C-F614-4A4F-AF9C-FC599915C023Q24314455-56745C99-61DC-4A73-9865-B6FA5B40E522Q27321701-4576C5BE-1D97-4EF7-874D-AD758684E3BCQ28305063-DCB19E07-A4BC-4769-B210-2A4EB6111E56Q28511629-B3E4F468-7073-4327-92DE-BF0255B8F11FQ28512781-0A022F73-1165-4230-A32B-B8BF90959206Q28566043-1EE4B0F7-553C-4A6B-9B56-5F6708B03C6AQ28574990-F9148C7B-CE40-4ADD-9EF3-97D1352704D6Q28595083-02370A56-7F24-415A-949E-5E639C5E10FAQ33614728-C2771FBF-FEE0-465D-991C-77B279B11DB6Q34325793-1CF2EB1B-B059-48AE-8AAA-1D7F4D5610FEQ34350645-85709D64-89D8-4EC7-9AAB-ADA37C9E67A4Q35055604-02A66013-936E-4D30-9A21-D1CA05FB4D1DQ35188597-EA3D974B-15F3-4214-976E-8D02F3CFC103Q35551874-B9B28162-DC29-4CF0-B6BD-1E6214FCA7DFQ36003848-6B70DE2D-0995-4067-B274-652410C06E2AQ36066201-2ED071F9-967C-4BDF-9B8A-00DC0B4EF673Q36131284-86AC57C6-6394-4F14-90E3-00B1CC3771A9Q36672123-2A5BECFE-9816-404F-BB6D-F5A0C7D1EA02Q37074250-1C41053B-873B-4DA1-B4C2-A7C1B00763F0Q37169505-26AC9AC8-E4E6-4A20-9DF6-5DCC83C7686FQ37266848-CE607D03-0661-44B6-B524-A1F2D65ED568Q37269119-3E1BFF65-914B-4EF2-806F-5AA2A31B19BAQ37289316-A34D3AFF-9D64-4F9E-810D-20F54CA890ADQ37564675-57A835EB-1008-4F8D-B0BF-1B4081B0E23EQ38130285-7C498493-4F56-40CB-BFA6-5312AD18D9C4Q38384916-4700D161-8521-47EB-A46C-A138CB653E67Q38394728-700D6AA9-5314-49F4-93B6-6348E4DF07D3Q38752612-043FEEFD-6C36-4D7F-B551-B56630E6DA11Q38791228-B3B8E393-CE6B-4BB6-BD70-547246E8410FQ38844059-654F3959-F852-4CEB-AE4D-2C16AF30D7C3Q38909718-264D9B6C-1B52-422B-88AA-E996F8FF3752Q39333661-CD4A3732-55EB-4743-9978-68D6385A81FFQ39647984-AA8F3105-F876-45F2-9C0F-B6B11B89E199Q39806751-A1736F93-180E-46BB-B4A8-938FCC9694E0Q40632473-67D25899-8104-47AB-A37F-3639E02369E1Q40658848-8F2B9CA2-633E-48C7-8BAC-3CF15887A4B3Q42582674-EBBCAC22-DFA7-4D00-BEE7-6DB1B847BB32Q44387465-D58CD92B-EEF5-4081-BAB2-18F3CB6054F3
P2860
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
description
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2001
@ast
im Oktober 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/10/26)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/10/26)
@nl
наукова стаття, опублікована в жовтні 2001
@uk
name
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@ast
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@en
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@nl
type
label
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@ast
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@en
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@nl
prefLabel
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@ast
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@en
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@nl
P2093
P2860
P3181
P356
P1476
a4, a unique kidney-specific isoform of mouse vacuolar H+-ATPase subunit a
@en
P2093
Hamasaki N
Sun-Wada GH
Toyomura T
Yamamoto A
P2860
P304
40050-40054
P3181
P356
10.1074/JBC.M106488200
P407
P577
2001-08-09T00:00:00Z