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

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

The Journal of biological chemistry - 6 Aug 2004

Bowman Emma Jean, Graham Laurie A, Stevens Tom H, Bowman Barry J

Abstract excerpt

The vacuolar H+-ATPase is inhibited with high specificity and potency by bafilomycin and concanamycin, macrolide antibiotics with similar structures. We previously reported that mutation at three residues in subunit c of the vacuolar ATPase from Neurospora crassa conferred strong resistance to bafilomycin but little or no resistance to concanamycin (Bowman, B. J., and Bowman, E. J. (2002) J. Biol. Chem. 277,...

Read the complete abstract on PubMed

Topics

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

Share to Antifungal Agents
Share to Drug Resistance, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Macrolides

Share to Mutagenesis, Site-Directed

Share to Neurospora crassa

Share to Protein Structure, Secondary

Share to Saccharomyces cerevisiae

Share to Vacuolar Proton-Translocating ATPases

Source

Identifiers

PMID: 15180988
DOI: 10.1074/jbc.M404638200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae.PMID 15180988Read ↗

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

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

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

Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase.Semantic proximity Read ↗

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

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

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

Identification of a new chondropsin class of antitumor compound that selectively inhibits V-ATPases.Semantic proximity Read ↗

The binding site of the V-ATPase inhibitor apicularen is in the vicinity of those for bafilomycin and archazolid.Semantic proximity Read ↗

Crystal structure and mechanism of the Staphylococcus cohnii virginiamycin B lyase (Vgb).Semantic proximity Read ↗

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