ReviewCellular and molecular life sciences : CMLS2014
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.
Review in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 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.
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Who cites it
69 citing papers in PubMed, 122 citations in OpenAlex.
- Bacterial extracellular vesicles as emerging biostimulants in plant microbe signaling and stress tolerance.World journal of microbiology & biotechnology · 2026Review
- ATP modulates holdase activity of fungal and human 110-kilodalton heat shock proteins to promote protein folding.Protein science : a publication of the Protein Society · 2026Article
- Hypertension and Diabetes Cooperatively Drive HSP90 Activation, HSP70 Suppression, and Left Ventricular Interstitial Expansion: Relevance to Maladaptive Myocardial Remodeling.Pathophysiology : the official journal of the International Society for Pathophysiology · 2026Article
- Stimuli-Responsive Chemical Systems That Mimic Biological Dynamics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- How SecB maintains clients in a translocation competent state.Communications biology · 2025Article
- Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions.mSphere · 2025Article
- Review
- Cysteine string protein α and a link between rare and common neurodegenerative dementias.NPJ dementia · 2025Review
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- Elevated Temperature Effects on Protein Turnover Dynamics inInternational journal of molecular sciences · 2024Article
- Amphiphilic dendrons as supramolecular holdase chaperones.RSC chemical biology · 2023Article
- Chaperonin counteracts diet-induced non-alcoholic fatty liver disease by aiding sirtuin 3 in the control of fatty acid oxidation.Diabetologia · 2023Article
- Unique Structural Fold of LonBA Protease fromInternational journal of molecular sciences · 2022Article
- The expression of HSP70 in skeletal muscle is not associated with glycogen availability during recovery following prolonged exercise in elite endurance athletes.European journal of applied physiology · 2022Article
- Article
- Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance.Plant, cell & environment · 2021Article
- Mechanism of the small ATP-independent chaperone Spy is substrate specific.Nature communications · 2021Article
- Proteostasis in the Male and Female Germline: A New Outlook on the Maintenance of Reproductive Health.Frontiers in cell and developmental biology · 2021Review
9 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By virtue of their general ability to bind (hold) translocating or unfolding polypeptides otherwise doomed to aggregate, molecular chaperones are commonly dubbed "holdases". Yet, chaperones also carry physiological functions that do not necessitate prevention of aggregation, such as altering the native states of proteins, as in the disassembly of SNARE complexes and clathrin coats. To carry such physiological functions, major members of the Hsp70, Hsp110, Hsp100, and Hsp60/CCT chaperone families act as catalytic unfolding enzymes or unfoldases that drive iterative cycles of protein binding, unfolding/pulling, and release. One unfoldase chaperone may thus successively convert many misfolded or alternatively folded polypeptide substrates into transiently unfolded intermediates, which, once released, can spontaneously refold into low-affinity native products. Whereas during stress, a large excess of non-catalytic chaperones in holding mode may optimally prevent protein aggregation, after the stress, catalytic disaggregases and unfoldases may act as nanomachines that use the energy of ATP hydrolysis to repair proteins with compromised conformations. Thus, holding and catalytic unfolding chaperones can act as primary cellular defenses against the formation of early misfolded and aggregated proteotoxic conformers in order to avert or retard the onset of degenerative protein conformational diseases.
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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.