ReviewBiopolymers2010
Hsp90 and co-chaperones twist the functions of diverse client proteins.
Review in Biopolymers, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT01581541 (Phase I Study of the Hsp90 Inhibitor, PU-H71, in Patients With Refractory Solid Tumors and Low-Grade Non-Hodgkin's Lymphoma), which is not on this map. Cited by 146 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Phase I Study of the Hsp90 Inhibitor, PU-H71, in Patients With Refractory Solid Tumors and Low-Grade Non-Hodgkin's Lymphoma
Who cites it
146 citing papers in PubMed, 249 citations in OpenAlex.
- A phase 2 clinical trial of the heat shock protein 90 (HSP 90) inhibitor ganetespib in patients with refractory advanced esophagogastric cancer.Investigational new drugs · 2020Trial
- Polyploidy and plant resilience to environmental stresses: Molecular mechanisms and future applications.Plant communications · 2026Review
- Embracing diversity: Post-translational modifications, the chaperone code, and the emergence of new chaperone entities.Cell stress & chaperones · 2026Review
- The GHKL ATPase Family as a Paradigm for MutL Homolog Function in DNA Mismatch Repair.International journal of molecular sciences · 2025Review
- Hsp90 and associates shaping parasite biology.mSphere · 2025Review
- Beyond Folding: Expanding the Functional Landscape of Hsp90 Chaperone Machinery in Health and Disease.International journal of molecular sciences · 2025Review
- Identification of thePlants (Basel, Switzerland) · 2025Article
- Benzbromarone interferes with the interaction between Hsp90 and Aha1 by interacting with both of them.Communications biology · 2025Article
- Peptide Fraction fromAntioxidants (Basel, Switzerland) · 2025Article
- Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria.Genome biology and evolution · 2025Review
- Insects in agricultural greenhouses: a metagenomic analysis of microbes inFrontiers in plant science · 2025Article
- Genome-wide identification and characterization ofFrontiers in plant science · 2025Article
- Exploring the Molecular Targets and Therapeutic Potential of Coptisine in Colon Cancer: A Network Pharmacology Approach.Current medicinal chemistry · 2025Article
- Geldanamycins: Potent Hsp90 Inhibitors with Significant Potential in Cancer Therapy.International journal of molecular sciences · 2024Review
- Evolution of the conformational dynamics of the molecular chaperone Hsp90.Nature communications · 2024Article
- Misfolding and aggregation in neurodegenerative diseases: protein quality control machinery as potential therapeutic clearance pathways.Cell communication and signaling : CCS · 2024Review
- A novel nanodrug for the sensitization of photothermal chemotherapy for breast cancerRSC advances · 2024Article
- Review
- Climate Stressors and Physiological Dysregulations: Mechanistic Connections to Pathologies.International journal of environmental research and public health · 2023Review
- Structural and functional complexity of HSP90 in cellular homeostasis and disease.Nature reviews. Molecular cell biology · 2023Review
86 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 1 institution in 1 country.
Funding
Abstract
Hsp90 molecular chaperones are required for the stability and activity of a diverse range of client proteins that have critical roles in signal transduction, cellular trafficking, chromatin remodeling, cell growth, differentiation, and reproduction. Mammalian cells contain three types of Hsp90s: cytosolic Hsp90, mitochondrial Trap-1, and Grp94 of the endoplasmic reticulum. Each of the Hsp90s, as well as the bacterial homolog, HtpG, hydrolyze ATP and undergo similar conformational changes. Unlike the other forms of Hsp90, cytosolic Hsp90 function is dependent on a battery of co-chaperone proteins that regulate the ATPase activity of Hsp90 or direct Hsp90 to interact with specific client proteins. This review will summarize what is known about Hsp90's ability to mediate the folding and activation of diverse client proteins that contribute to human diseases, such as cancer and fungal and viral infections.
Indexed as
Identifiers
What OpenQuestion holds
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.