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

p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity.

Molecular and cellular biology - 1 May 2008

Forafonov Fedor, Toogun Oyetunji A, Grad Iwona, Suslova Elena, Freeman Brian C, Picard Didier

Abstract excerpt

The molecular chaperone Hsp90 assists a subset of cellular proteins and is essential in eukaryotes. A cohort of cochaperones contributes to and regulates the multicomponent Hsp90 machine. Unlike the biochemical activities of the cochaperone p23, its in vivo functions and the structure-function relationship remain poorly understood, even in the genetically tractable model organism Saccharomyces cerevisiae. The...

Read the complete abstract on PubMed

Topics

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

Share to DNA, Fungal
Share to Genes, Fungal
Share to Genetic Complementation Test

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP90 Heat-Shock Proteins

Share to Intramolecular Oxidoreductases

Share to Molecular Chaperones

Share to Mutagenesis, Site-Directed

Share to Sequence Deletion

Source

Open in PubMed Open full text

Identifiers

PMID: 18362168
DOI: 10.1128/MCB.02246-07
PMCID: PMC2423160

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity.PMID 18362168Read ↗

Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling.Semantic proximity Read ↗

Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins.Semantic proximity Read ↗

The complex evolutionary dynamics of Hsp70s: a genomic and functional perspective.Semantic proximity Read ↗

Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle.Semantic proximity Read ↗

The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation.Semantic proximity Read ↗

Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.Semantic proximity Read ↗

Molecular chaperones: Guardians of tumor suppressor stability and function.Semantic proximity Read ↗

Gedunin inactivates the co-chaperone p23 protein causing cancer cell death by apoptosis.Semantic proximity Read ↗

The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.Semantic proximity Read ↗

The Hsp70/Hsp90 Co-Chaperone Hop/Stip1 Shifts the Proteostatic Balance from Folding Towards DegradationSemantic proximity Read ↗

Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.Semantic proximity Read ↗

Network of general and specialty J protein chaperones of the yeast cytosol.Semantic proximity Read ↗

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