Structured Summary
Abstract
A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.
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Classification
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MeSH Record
Synonyms
6 entry terms
- Chaperonin
- Chaperonin Family
- Chaperonin Complex
- Chaperonin Complexes
- Chaperonin Protein Complex
- Complex, Chaperonin
MeSH Record
Aspects Covered
30 allowable subheadings
Indexed with the subheadings administration & dosage, adverse effects, agonists, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.
MeSH Record
Indexing Annotation
general or unspecified; prefer specifics
MeSH Record
History Note
95; was CHAPERONIN FAMILY (NM) 1989-94
MeSH Record
Previous Indexing
- Heat-Shock Proteins (1989-1994)
- Proteins (1989-1994)
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NLM Classification
QU 55.6
AMA Style
References
- National Library of Medicine. Chaperonins. Medical Subject Headings (MeSH). 2026. Unique ID D018833. http://id.nlm.nih.gov/mesh/2026/D018833
- Chaperonins. In: Wikipedia. https://en.wikipedia.org/wiki/Chaperonin
- Chaperonins. In: Wikidata. https://www.wikidata.org/wiki/Q24771589