ArticleChemical science2024
Hsp90α forms condensate engaging client proteins with RG motif repeats.
Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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
3 citing papers in PubMed.
- Inherent MS-cleavability of diazirine photo-cross-links enables residue-level structural analysis.Nature communications · 2026Article
- Plasma heat shock protein 90α shows a concentration-dependent, threshold association with pulmonary nodules in asymptomatic males >40 years undergoing low-dose computed tomography.The Journal of international medical research · 2026Article
- Exogenous plastic stress: polypropylene-induced phenotypic alterations and oxidative stress adaptation in Pseudomonas aeruginosa.Antonie van Leeuwenhoek · 2025Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp90α, a pivotal canonical chaperone, is renowned for its broad interaction with numerous protein clients to maintain protein homeostasis, chromatin remodeling, and cell growth. Recent studies indicate its role in modifying various components of membraneless organelles (MLOs) such as stress granules and processing bodies, suggesting its participation in the regulation of protein condensates. In this study, we found that Hsp90α possesses an inherent ability to form dynamic condensates
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Registered trials
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