ArticleCell chemical biology2016
In Vivo Conformational Dynamics of Hsp90 and Its Interactors.
Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 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.
The trial behind it
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Who cites it
56 citing papers in PubMed, 84 citations in OpenAlex.
- On the Feasibility of Clinical Studies with Cross-Linking Mass Spectrometry.Journal of proteome research · 2026Article
- An integrated multiscale computational study of nephrotoxicity mechanism of citrinin and its metabolites (CIMs)：density functional theory, network toxicology, and molecular dynamics simulation.Mycotoxin research · 2025Article
- Investigation of a cryptic ligand binding site on Plasmodium falciparum Hsp90.Bioorganic & medicinal chemistry · 2025Article
- Two sides of the same coin: heat shock proteins as biomarkers and therapeutic targets for some complex diseases.Frontiers in molecular biosciences · 2025Review
- Progress, Challenges and Opportunities of NMR and XL-MS for Cellular Structural Biology.JACS Au · 2024Review
- Multidimensional Cross-Linking and Real-Time Informatics for Multiprotein Interaction Studies.Journal of proteome research · 2024Article
- Structural and functional complexity of HSP90 in cellular homeostasis and disease.Nature reviews. Molecular cell biology · 2023Review
- Integrated Analysis of Cross-Links and Dead-End Peptides for Enhanced Interpretation of Quantitative XL-MS.Journal of proteome research · 2023Article
- Studying Protein-Ligand Interactions by Protein Denaturation and Quantitative Cross-Linking Mass Spectrometry.Analytical chemistry · 2023Article
- Protein complexes in cells by AI-assisted structural proteomics.Molecular systems biology · 2023Article
- Cross-linking mass spectrometry for mapping protein complex topologies in situ.Essays in biochemistry · 2023Article
- Unique interface and dynamics of the complex of HSP90 with a specialized cochaperone AIPL1.Structure (London, England : 1993) · 2023Article
- Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.PLoS biology · 2022Article
- Mitochondrial interactome quantitation reveals structural changes in metabolic machinery in the failing murine heart.Nature cardiovascular research · 2022Article
- Characterizing Endogenous Protein Complexes with Biological Mass Spectrometry.Chemical reviews · 2022Review
- In-Cell Labeling and Mass Spectrometry for Systems-Level Structural Biology.Chemical reviews · 2022Review
- Applications and advancements of FT-ICR-MS for interactome studies.Mass spectrometry reviews · 2022Review
- Multiplexed Isobaric Quantitative Cross-Linking Reveals Drug-Induced Interactome Changes in Breast Cancer Cells.Analytical chemistry · 2022Article
- Multiplexed Cross-Linking with Isobaric Quantitative Protein Interaction Reporter Technology.Analytical chemistry · 2021Article
- Protein interaction landscapes revealed by advanced in vivo cross-linking-mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Hsp90 belongs to a family of some of the most highly expressed heat shock proteins that function as molecular chaperones to protect the proteome not only from the heat shock but also from other misfolding events. As many client proteins of Hsp90 are involved in oncogenesis, this chaperone has been the focus of intense research efforts. Yet, we lack structural information for how Hsp90 interacts with co-chaperones and client proteins. Here, we developed a mass-spectrometry-based approach that allowed quantitative measurements of in vitro and in vivo effects of small-molecule inhibitors on Hsp90 conformation, and interaction with co-chaperones and client proteins. From this analysis, we were able to derive structural models for how Hsp90 engages its interaction partners in vivo, and how different drugs affect these structures. In addition, the methodology described here offers a new approach to probe the effects of virtually any inhibitor treatment on the proteome level.
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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.