Chaperonin 60 [chaperon hsp60]
- Terms
-
chaperonin 60
GroEL
GroEL protein
heat shock protein 60
HSP-60
protein tepelného šoku hsp60
stresový chaperonin GroEL
-
GroEL Protein
GroEL Stress Protein
Heat-Shock Protein 60
Heat-Shock Proteins 60
hsp60 Family
hsp60 Protein
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.
- Annotation
- coordinate with MITOCHONDRIAL PROTEINS or BACTERIAL PROTEINS if pertinent
- DUI
- D018834 MeSH Browser
- CUI
- M0028189
- Previous indexing
- Heat-Shock Proteins (1989-1994); Bacterial Proteins (1989-1994)
- History note
- 1995(1989)
- Public note
- 1995; CHAPERONIN 60 was indexed under BACTERIAL PROTEINS & HEAT-SHOCK PROTEINS 1989-1994; HEAT-SHOCK PROTEIN 60 was indexed under HEAT-SHOCK PROTEINS 1993-1994; HSP60 PROTEIN was indexed under HEAT-SHOCK PROTEINS 1989-1994; for GROEL PROTEIN see GROEL PROTEIN 1995-2009
Allowable subheadings
- AD
- administration & dosage 1
- AE
- adverse effects
- AG
- agonists
- AN
- analysis 2
- AI
- antagonists & inhibitors 1
- BI
- biosynthesis
- BL
- blood
- CF
- cerebrospinal fluid
- CS
- chemical synthesis
- CH
- chemistry 2
- CL
- classification
- DF
- deficiency
- DE
- drug effects
- EC
- economics
- GE
- genetics 13
- HI
- history
- IM
- immunology 6
- IP
- isolation & purification
- ME
- metabolism 11
- PK
- pharmacokinetics
- PD
- pharmacology
- PH
- physiology 2
- PO
- poisoning
- RE
- radiation effects
- ST
- standards
- SD
- supply & distribution
- TU
- therapeutic use
- TO
- toxicity
- UL
- ultrastructure
- UR
- urine
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