ArticleCell reports2016
Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function.
Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
51 citing papers in PubMed, 108 citations in OpenAlex.
- Overestimating zero-shot fitness prediction: Broad benchmarks mask local failures and practical limitations.bioRxiv : the preprint server for biology · 2026Article
- EZ-DMS - A Simple and Accessible Protocol and Software Package for Deep Mutational Scanning of Virus Proteins.bioRxiv : the preprint server for biology · 2026Article
- Protein structure shapes natural genetic variation andbioRxiv : the preprint server for biology · 2025Article
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- MaveDB 2024: a curated community database with over seven million variant effects from multiplexed functional assays.Genome biology · 2025Article
- MMRT: MultiMut Recursive Tree for predicting functional effects of high-order protein variants from low-order variants.Computational and structural biotechnology journal · 2025Article
- Dominant negative mutations in yeast Hsp90 indicate triage decision mechanism targeting client proteins for degradation.Molecular biology of the cell · 2025Article
- Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function.PLoS genetics · 2024Article
- Unsupervised evolution of protein and antibody complexes with a structure-informed language model.Science (New York, N.Y.) · 2024Article
- Functional effects of mutations in proteins can be predicted and interpreted by guided selection of sequence covariation information.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions.Genetics · 2024Article
- Structure-based network analysis predicts pathogenic variants in human proteins associated with inherited retinal disease.NPJ genomic medicine · 2024Article
- Dominant negative mutations in yeast Hsp90 reveal triage decision mechanism targeting client proteins for degradation.bioRxiv : the preprint server for biology · 2024Article
- Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024Review
- Inverse folding of protein complexes with a structure-informed language model enables unsupervised antibody evolution.bioRxiv : the preprint server for biology · 2023Article
- ProteinGym: Large-Scale Benchmarks for Protein Design and Fitness Prediction.bioRxiv : the preprint server for biology · 2023Article
- Infer global, predict local: Quantity-relevance trade-off in protein fitness predictions from sequence data.PLoS computational biology · 2023Article
- Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle.PLoS genetics · 2023Article
- Tenth International Symposium on the Hsp90 chaperone machine : Switzerland, October 19-23, 2022.Cell stress & chaperones · 2023Review
- Nucleotide exchange is sufficient for Hsp90 functions in vivo.Nature communications · 2023Article
Corrections and comments
- Commented on by
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
To probe the mechanism of the Hsp90 chaperone that is required for the maturation of many signaling proteins in eukaryotes, we analyzed the effects of all individual amino acid changes in the ATPase domain on yeast growth rate. The sensitivity of a position to mutation was strongly influenced by proximity to the phosphates of ATP, indicating that ATPase-driven conformational changes impose stringent physical constraints on Hsp90. To investigate how these constraints may vary for different clients, we performed biochemical analyses on a panel of Hsp90 mutants spanning the full range of observed fitness effects. We observed distinct effects of nine Hsp90 mutations on activation of v-src and glucocorticoid receptor (GR), indicating that different chaperone mechanisms can be utilized for these clients. These results provide a detailed guide for understanding Hsp90 mechanism and highlight the potential for inhibitors of Hsp90 that target a subset of clients.
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.