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

Cellular role of the V-ATPase in Neurospora crassa: analysis of mutants resistant to concanamycin or lacking the catalytic subunit A.

The Journal of experimental biology - 1 Jan 2000

Bowman E J, Bowman B J

Abstract excerpt

Vacuolar ATPases (V-ATPases) are large complex enzymes that are structural and mechanistic relatives of F(1)F(o)-ATPases. They hydrolyze ATP and pump protons across membranes to hyperpolarize membranes and, often, to acidify cellular compartments. The proton gradients generated are used to drive the movement of various compounds across membranes. V-ATPases are found in membranes of archaebacteria and some...

Read the complete abstract on PubMed

Topics

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

Share to Anti-Bacterial Agents
Share to Drug Resistance, Microbial

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

Share to Macrolides

Share to Mutation

Share to Neurospora crassa

Share to Proton-Translocating ATPases

Share to Vacuolar Proton-Translocating ATPases

Source

Identifiers

PMID: 10600678
DOI: 10.1242/jeb.203.1.97

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

Cellular role of the V-ATPase in Neurospora crassa: analysis of mutants resistant to concanamycin or lacking the catalytic subunit A.PMID 10600678Read ↗

Analysis of strains with mutations in six genes encoding subunits of the V-ATPase: eukaryotes differ in the composition of the V0 sector of the enzyme.Semantic proximity Read ↗

Disruption of vma-1, the gene encoding the catalytic subunit of the vacuolar H(+)-ATPase, causes severe morphological changes in Neurospora crassa.Semantic proximity Read ↗

Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site.Semantic proximity Read ↗

Disruption of the gene encoding the V-ATPase subunit A results in inhibition of normal growth and abolished sporulation in Aspergillus nidulans.Semantic proximity Read ↗

The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae.Semantic proximity Read ↗

Vacuolar ATPase of Neurospora crassa: electron microscopy, gene characterization and gene inactivation/mutation.Semantic proximity Read ↗

The pmr gene, encoding a Ca2+-ATPase, is required for calcium and manganese homeostasis and normal development of hyphae and conidia in Neurospora crassa.Semantic proximity Read ↗

The phenotype of a phospholipase C (plc-1) mutant in a filamentous fungus, Neurospora crassa.Semantic proximity Read ↗

The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa.Semantic proximity Read ↗

Subunit a of the yeast V-ATPase participates in binding of bafilomycin.Semantic proximity Read ↗

Vacuolar H(+)-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger.Semantic proximity Read ↗

Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting.Semantic proximity Read ↗

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