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 human papillomavirus type 16 E5 protein alters vacuolar H(+)-ATPase function and stability in Saccharomyces cerevisiae.

Virology - 15 Feb 2001

Briggs M W, Adam J L, McCance D J

Abstract excerpt

The human papillomavirus 16 (HPV-16) E5 oncoprotein is a small integral membrane protein that binds to the 16-kDa subunit of the vacuolar H(+)-ATPase (v-ATPase). Conservation within the family of v-ATPases prompted us to look to Saccharomyces cerevisiae as a potential model organism for E5 study. The E5 open reading frame, driven by a galactose-inducible promoter, was integrated into the yeast genome, and the...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Stability
Share to Mutagenesis
Share to Oncogene Proteins, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Papillomaviridae

Share to Protein Conformation

Share to Proton-Translocating ATPases

Share to Saccharomyces cerevisiae

Share to Vacuolar Proton-Translocating ATPases

Source

Identifiers

PMID: 11162831
DOI: 10.1006/viro.2000.0783

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The human papillomavirus type 16 E5 protein alters vacuolar H(+)-ATPase function and stability in Saccharomyces cerevisiae.PMID 11162831Read ↗

Vacuolar H(+)-ATPase mutants transform cells and define a binding site for the papillomavirus E5 oncoprotein.Semantic proximity Read ↗

Bap31 Is a Novel Target of the Human Papillomavirus E5 ProteinSemantic proximity Read ↗

High-Risk Human Papillomavirus E5 Oncoprotein Displays Channel-Forming Activity Sensitive to Small-Molecule InhibitorsSemantic proximity Read ↗

VMA8 encodes a 32-kDa V1 subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase required for function and assembly of the enzyme complex.Semantic proximity Read ↗

Oligomerization of the E5 protein of human papillomavirus type 16 occurs through multiple hydrophobic regions.Semantic proximity Read ↗

The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase.Semantic proximity Read ↗

The HPV-16 E5 protein represses expression of stress pathway genes XBP-1 and COX-2 in genital keratinocytes.Semantic proximity Read ↗

The human papillomavirus type 6 and 16 E5 proteins are membrane-associated proteins which associate with the 16-kilodalton pore-forming proteinSemantic proximity Read ↗

Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity.Semantic proximity Read ↗

Golgi alkalinization by the papillomavirus E5 oncoprotein.Semantic proximity Read ↗

Close-up and genomic views of the yeast vacuolar H+-ATPase.Semantic proximity Read ↗

Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant.Semantic proximity Read ↗

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