Chaperonins [chaperoniny]
- Terms
-
bílkoviny teplotního šoku
chaperonin
chaperonové komplexy
chaperonový komplex
chaperony
-
Chaperonin
Chaperonin Complex
Chaperonin Complexes
Chaperonin Family
Chaperonin Protein Complex
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.
- Annotation
- general or unspecified; prefer specifics
- všeobecné nebo nevymezené, dej přednost přesnějšímu deskriptoru
- DUI
- D018833 MeSH Browser
- CUI
- M0028187
- Previous indexing
- Heat-Shock Proteins (1989-1994); Proteins (1989-1994)
- History note
- 95; was CHAPERONIN FAMILY (NM) 1989-94
- Online note
- use CHAPERONINS (NM) to search CHAPERONIN FAMILY 1989-94
- Public note
- 95; CHAPERONIN FAMILY was indexed under PROTEINS 1989-94
Allowable subheadings
- AD
- administration & dosage
- AE
- adverse effects
- AG
- agonists
- AN
- analysis
- AI
- antagonists & inhibitors
- BI
- biosynthesis
- BL
- blood
- CF
- cerebrospinal fluid
- CS
- chemical synthesis
- CH
- chemistry
- CL
- classification 1
- DF
- deficiency
- DE
- drug effects
- EC
- economics
- GE
- genetics
- HI
- history
- IM
- immunology 2
- IP
- isolation & purification
- ME
- metabolism 1
- PK
- pharmacokinetics
- PD
- pharmacology
- PH
- physiology 2
- PO
- poisoning
- RE
- radiation effects
- ST
- standards
- SD
- supply & distribution
- TU
- therapeutic use 1
- TO
- toxicity
- UL
- ultrastructure
- UR
- urine
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TpCCTeta protein, Tetrahymena pyriformis Chemical MeSH Browser
chaperonin cofactor A Chemical MeSH Browser
htrE protein, E coli Chemical MeSH Browser