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

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

Genetics - 31 Mar 2021

Hohrman Kaitlyn, Gonçalves Davi, Morano Kevin A, Johnson Jill L

Abstract excerpt

The protein molecular chaperone Hsp90 (Heat shock protein, 90 kilodalton) plays multiple roles in the biogenesis and regulation of client proteins impacting myriad aspects of cellular physiology. Amino acid alterations located throughout Saccharomyces cerevisiae Hsp90 have been shown to result in reduced client activity and temperature-sensitive growth defects. Although some Hsp90 mutants have been shown to...

Read the complete abstract on PubMed

Topics

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

Share to DNA Helicases
Share to Heat-Shock Proteins

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

Share to HSP70 Heat-Shock Proteins

Share to HSP90 Heat-Shock Proteins

Share to Molecular Chaperones

Share to Protein Folding

Share to Saccharomyces cerevisiae Proteins

Share to Transcription Factor TFIIH

Source

Open in PubMed Open full text

Identifiers

PMID: 33789348
DOI: 10.1093/genetics/iyab009
PMCID: PMC8045699

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

Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.PMID 33789348Read ↗

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Semantic proximity Read ↗

Functional and physical interaction between yeast Hsp90 and Hsp70.Semantic proximity Read ↗

Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function.Semantic proximity Read ↗

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.Semantic proximity Read ↗

Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome.Semantic proximity Read ↗

Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast.Semantic proximity Read ↗

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

Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions.Semantic proximity Read ↗

Identification of an Hsp90 mutation that selectively disrupts cAMP/PKA signaling in Saccharomyces cerevisiae.Semantic proximity Read ↗

Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth.Semantic proximity Read ↗

Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity.Semantic proximity Read ↗

Mechanistic Asymmetry in Hsp90 Dimers.Semantic proximity Read ↗

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