ReviewCold Spring Harbor perspectives in biology2019
Structure, Function, and Regulation of the Hsp90 Machinery.
Review in Cold Spring Harbor perspectives in biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
164 citing papers in PubMed, 296 citations in OpenAlex.
- Comparative genomic and evolutionary analysis of the heat shock protein gene family in the chicken genome.Animal biotechnology · 2026Article
- Antifungal metallacarboranes modulate Hsp90 activity.Future medicinal chemistry · 2026Article
- Synergies and trade-offs in the heat shock response mechanism.PLoS computational biology · 2026Article
- Usp31 Promotes Cardiomyocyte Injury Under Ischemic Stress and Is Inhibited by Sodium Tanshinone IIA Sulfonate.Biomedicines · 2026Article
- Structural analysis ofbioRxiv : the preprint server for biology · 2026Article
- Recent progress in the development of HSP90 inhibitors: structure-activity relationship and biological evaluation studies.Molecular diversity · 2026Review
- Heat Shock Protein 90 in Sepsis-Induced Cardiomyopathy: Mechanistic Insights and Emerging Therapeutic Target.Shock (Augusta, Ga.) · 2026Review
- RPAP3: Structural evolution, chaperone networks, and disease implications of a transcriptional Co-chaperone.The Journal of biological chemistry · 2026Review
- Nucleotide-dependent domain interactions of Aha1-type co-chaperones with Hsp90 reveal evolutionarily conserved binding determinants.Cell stress & chaperones · 2026Review
- Rearrangement of the Cell Chaperone Machinery in Human Fibrosarcoma HT1080 Cells With the Knocked-Out HSP90AA1 Gene Encoding Hsp90α.Biology of the cell · 2026Article
- The evolution of heat shock protein 90 C-terminal inhibitors: From novobiocin to potential clinical candidates.Cell stress & chaperones · 2026Review
- Functional interplay between heat shock protein 90 (HSP90) and heat shock factors (HSFs).Cell stress & chaperones · 2026Review
- Beyond a Passive Tether: Structural Insights into the Disordered Tail of Hsp90.Journal of the American Chemical Society · 2026Article
- Amygdalin synergizes with the TNF-α monoclonal antibody infliximab to modulate HSP90 and related necro-inflammatory/oxidative stress pathways in a rat model of hepatic I/R.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Article
- Review
- Molecular Mechanisms and Therapeutic Potential of Degron-Mediated Proteostasis Regulation in Neurodegenerative Diseases.Cellular and molecular neurobiology · 2026Review
- Key roles of GAPDH, Hsp90, and NO in heme trafficking.Journal of inorganic biochemistry · 2026Review
- CUL5-mediated ubiquitination in cancer cell therapy: context-dependent roles, molecular networks, and emerging therapeutic avenues.Frontiers in medicine · 2026Review
- Inhibition ofFrontiers in parasitology · 2026Article
104 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a plethora of substrates ("clients"), including protein kinases, transcription factors, and E3 ubiquitin ligases, positioning Hsp90 as a central regulator of cellular proteostasis. Hsp90 undergoes large conformational changes during its ATPase cycle. The processing of clients by cytosolic Hsp90 is assisted by a cohort of cochaperones that affect client recruitment, Hsp90 ATPase function or conformational rearrangements in Hsp90. Because of the importance of Hsp90 in regulating central cellular pathways, strategies for the pharmacological inhibition of the Hsp90 machinery in diseases such as cancer and neurodegeneration are being developed. In this review, we summarize recent structural and mechanistic progress in defining the function of organelle-specific and cytosolic Hsp90, including the impact of individual cochaperones on the maturation of specific clients and complexes with clients as well as ways of exploiting Hsp90 as a drug target.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.