Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Differential localization of vacuolar H+-ATPases containing a1, a2, a3, or a4 (ATP6V0A1-4) subunit isoforms along the nephron.

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology - 1 Jan 2007

Schulz Nicole, Dave Mital H, Stehberger Paul A, Chau Tien, Wagner Carsten A

Abstract excerpt

Vacuolar H(+)-ATPase are multi-subunit containing pumps important for several processes along the nephron such as receptor mediated endocytosis, acidification of intracellular organelles, bicarbonate reabsorption and secretion, and H(+)- extrusion. Mutations in the human a4 (ATP6V0A4) subunit cause distal renal tubular acidosis (dRTA). There are 4 known isoforms of the 'a' subunit (a1-a4). Here we investigated...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acidosis, Renal Tubular
Share to DNA Primers

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Immunohistochemistry

Share to Isoenzymes

Share to Mice, Inbred C57BL

Share to Nephrons

Share to Protein Subunits

Share to Vacuolar Proton-Translocating ATPases

Source

Identifiers

PMID: 17595521
DOI: 10.1159/000104159

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Differential localization of vacuolar H+-ATPases containing a1, a2, a3, or a4 (ATP6V0A1-4) subunit isoforms along the nephron.PMID 17595521Read ↗

Atp6v0a4 knockout mouse is a model of distal renal tubular acidosis with hearing loss, with additional extrarenal phenotype.Semantic proximity Read ↗

Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis.Semantic proximity Read ↗

Proteomic analysis of V-ATPase-rich cells harvested from the kidney and epididymis by fluorescence-activated cell sorting.Semantic proximity Read ↗

Kidney-specific <i>Wdr72</i> deletion leads to incomplete distal renal tubular acidosis through impaired V-ATPase B1 subunit localizationSemantic proximity Read ↗

Mice deficient in H+-ATPase a4 subunit have severe hearing impairment associated with enlarged endolymphatic compartments within the inner ear.Semantic proximity Read ↗

The Na,K-ATPase alpha4 gene (Atp1a4) encodes a ouabain-resistant alpha subunit and is tightly linked to the alpha2 gene (Atp1a2) on mouse chromosome 1.Semantic proximity Read ↗

Urinary Sodium Wasting and Disrupted Collecting Duct Function in Mice with dRTA-Causing <i>SLC4A1</i> MutationsSemantic proximity Read ↗

Effects of human a3 and a4 mutations that result in osteopetrosis and distal renal tubular acidosis on yeast V-ATPase expression and activity.Semantic proximity Read ↗

Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits.Semantic proximity Read ↗

A Comprehensive Map of mRNAs and Their Isoforms across All 14 Renal Tubule Segments of MouseSemantic proximity Read ↗

Molecular physiology and genetics of Na+-independent SLC4 anion exchangersSemantic proximity Read ↗

Regulation of luminal acidification by the V-ATPase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.