Descriptor English: | Endoplasmic Reticulum Chaperone BiP | ||||||
Descriptor Spanish: |
Chaperón BiP del Retículo Endoplásmico
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Descriptor Portuguese: | Chaperona BiP do Retículo Endoplasmático | ||||||
Descriptor French: | Chaperonne BiP du réticulum endoplasmique | ||||||
Entry term(s): |
BiP, Molecular Chaperone Binding immunoglobulin Protein Molecular Chaperone Binding-immunoglobulin Protein Molecular Chaperone GRP78, Molecular Chaperone Glucose Regulated Protein 78 kDa Grp78 HSPA5 Protein Heat Shock Protein 5 Heat-Shock Protein 5 Molecular Chaperone BiP Molecular Chaperone GRP78 Protein, HSPA5 |
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Tree number(s): |
D12.776.580.216.375.100 |
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RDF Unique Identifier: | https://id.nlm.nih.gov/mesh/D000091342 | ||||||
Scope note: | 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. |
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Allowable Qualifiers: |
AD administration & dosage AE adverse effects AG agonists AI antagonists & inhibitors AN analysis BI biosynthesis BL blood CF cerebrospinal fluid CH chemistry CL classification CS chemical synthesis DE drug effects DF deficiency EC economics GE genetics HI history IM immunology IP isolation & purification ME metabolism PD pharmacology PH physiology PK pharmacokinetics PO poisoning RE radiation effects SD supply & distribution ST standards TO toxicity TU therapeutic use UL ultrastructure UR urine |
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Public MeSH Note: | 2022; for MOLECULAR CHAPERONE GRP78 see under HEAT-SHOCK PROTEINS 2008-2021 |
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History Note: | 2022(2008) |
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DeCS ID: | 59863 | ||||||
Unique ID: | D000091342 | ||||||
Documents indexed in the Virtual Health Library (VHL): | Click here to access the VHL documents | ||||||
Date Established: | 2022/01/01 | ||||||
Date of Entry: | 2021/07/09 | ||||||
Revision Date: | 2021/06/30 |
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CHEMICALS AND DRUGS
Amino Acids, Peptides, and Proteins [D12]Amino Acids, Peptides, and Proteins
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Endoplasmic Reticulum Chaperone BiP
- Preferred
Concept UI |
M000748485 |
Scope note | 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. |
Preferred term | Endoplasmic Reticulum Chaperone BiP |
Entry term(s) |
BiP, Molecular Chaperone Binding immunoglobulin Protein Molecular Chaperone Binding-immunoglobulin Protein Molecular Chaperone GRP78, Molecular Chaperone Glucose Regulated Protein 78 kDa Grp78 HSPA5 Protein Heat Shock Protein 5 Heat-Shock Protein 5 Molecular Chaperone BiP Molecular Chaperone GRP78 Protein, HSPA5 |
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