Structured Summary
Abstract
A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.
MeSH Record
Classification
Broader headings
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MeSH Record
Synonyms
8 entry terms
- Heat-Shock Protein 60
- Heat-Shock Proteins 60
- hsp60 Family
- hsp60 Protein
- Heat Shock Protein 60
- Heat Shock Proteins 60
- GroEL Protein
- GroEL Stress Protein
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
coordinate with MITOCHONDRIAL PROTEINS or BACTERIAL PROTEINS if pertinent
MeSH Record
History Note
1995(1989)
MeSH Record
Previous Indexing
- Bacterial Proteins (1989-1994)
- Heat-Shock Proteins (1989-1994)
MeSH Hierarchy
Tree Numbers
AMA Style
References
- National Library of Medicine. Chaperonin 60. Medical Subject Headings (MeSH). 2026. Unique ID D018834. http://id.nlm.nih.gov/mesh/2026/D018834
- Chaperonin 60. In: Wikidata. https://www.wikidata.org/wiki/Q3047550