Heat-Shock Proteins
| Definition: |
Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions. |
| Notes: |
/biosyn /drug eff /physiol /ultrastruct permitted; do not use /analogs |
| Also Called: |
Heat-Shock Protein 27,Stress Protein 34,Stress Protein 71,Heat-Shock Protein Chlamydomonas |
| Previously Indexed: |
Heat (1966-1983),Proteins (1966-1983) |
Heat-Shock Proteins Categories.
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Chaperonins - A class of sequence-related MOLECULAR CHAPERONES found in bacteria, mitochondria, and plastids. Chaperonins are abundant constitutive proteins that increase in amount after stresses such as heat shock, bacterial infection of macrophages, and an increase in the cellular content of unfolded proteins. Bacterial chaperonins are major immunogens in human bacterial infections because of their accumulation during the stress of infection. Two members of this class of chaperones are CHAPERONIN 10 and CHAPERONIN 60. |
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Heat-Shock Proteins 70 - A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. There is evidence that these proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures. |
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Heat-Shock Proteins 90 - A class of MOLECULAR CHAPERONES whose members act in the mechanism of signal transduction by steroid receptors. |
Heat-Shock Proteins Definitions and Terms
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