Endoplasmic Reticulum Chaperone BiP [chaperon endoplazmatického retikula BiP]
- Terms
-
člen 5 rodiny Hsp70
glukózou regulovaný protein 78 kDa
Grp78
molekulární chaperon BiP
molekulární chaperon GRP78
protein HSPA5
protein vázající imunoglobuliny
-
Binding-immunoglobulin Protein Molecular Chaperone
Glucose Regulated Protein 78 kDa
Grp78
Heat-Shock Protein 5
HSPA5 Protein
Molecular Chaperone BiP
Molecular Chaperone GRP78
An ENDOPLASMIC RETICULUM specific chaperone of the HSP70 family. They are involved in folding and oligomerization of secreted and membrane proteins and ENDOPLASMIC RETICULUM STRESS related UNFOLDED PROTEIN RESPONSE.
- DUI
- D000091342 MeSH Browser
- CUI
- M000748485
- History note
- 2022(2008)
- Public note
- 2022; for MOLECULAR CHAPERONE GRP78 see under HEAT-SHOCK PROTEINS 2008-2021
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
- DF
- deficiency
- DE
- drug effects
- EC
- economics
- GE
- genetics
- HI
- history
- IM
- immunology
- IP
- isolation & purification
- ME
- metabolism 1
- PK
- pharmacokinetics
- PD
- pharmacology
- PH
- physiology
- PO
- poisoning
- RE
- radiation effects
- ST
- standards
- SD
- supply & distribution
- TU
- therapeutic use
- TO
- toxicity
- UL
- ultrastructure
- UR
- urine
GRP78 protein, rat Chemical MeSH Browser
HSPA5 protein, human Chemical MeSH Browser
Hspa5 protein, mouse Chemical MeSH Browser