ReviewFrontiers in molecular biosciences2021
Redefining Molecular Chaperones as Chaotropes.
Review in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 25 citations in OpenAlex.
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- STIP1/HOP promotes the formation of cytotoxic α-synuclein oligomers.Molecular neurodegeneration advances · 2026Article
- Albumin: A Review of Market Trends, Purification Methods, and Biomedical Innovations.Current issues in molecular biology · 2025Review
- Protein misfolding involving entanglements providesa structural explanation for the origin of stretched-exponential refolding kinetics.Science advances · 2025Article
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Misfolding and aggregation in neurodegenerative diseases: protein quality control machinery as potential therapeutic clearance pathways.Cell communication and signaling : CCS · 2024Review
- There Are No Insurmountable Barriers: Passage of theMembranes · 2023Review
- Dissecting aggregation and seeding dynamics of α-Syn polymorphs using the phasor approach to FLIM.Communications biology · 2022Article
- A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Current trends in biopharmaceuticals production in Escherichia coli.Biotechnology letters · 2022Review
- Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad.Chemical science · 2022Article
- Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin.Nature communications · 2022Article
- Amyloid management by chaperones: The mystery underlying protein oligomers' dual functions.Current research in structural biology · 2022Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular chaperones are the key instruments of bacterial protein homeostasis. Chaperones not only facilitate folding of client proteins, but also transport them, prevent their aggregation, dissolve aggregates and resolve misfolded states. Despite this seemingly large variety, single chaperones can perform several of these functions even on multiple different clients, thus suggesting a single biophysical mechanism underlying. Numerous recently elucidated structures of bacterial chaperone-client complexes show that dynamic interactions between chaperones and their client proteins stabilize conformationally flexible non-native client states, which results in client protein denaturation. Based on these findings, we propose chaotropicity as a suitable biophysical concept to rationalize the generic activity of chaperones. We discuss the consequences of applying this concept in the context of ATP-dependent and -independent chaperones and their functional regulation.
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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.