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UnknownA novel mechanism for small heat shock proteins to function as molecular chaperones.
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S-EPMC4351549 | biostudies-literature
ProteomicsThe permanently chaperone-active small heat shock protein Hsp17 from C. elegans exhibits topological separation of its N-terminal regions
Small Heat shock proteins (sHsps) are a family of molecular chaperones that bind non-native proteins in an ATP-independent manner. C. elegans encodes 16 different sHsps, among them Hsp17, which is evolutionarily distinct from other sHsps in the nematode. The structure and mechanism of Hsp17 and how ...
ORGANISM(S): Caenorhabditis elegans 
2022-12-08 | PXD028080 | Pride
Hsp-17 Cehsp17 Shsps C. elegans Chaperone Hsp17 Small heat shock protein 
ProteomicsThe permanently chaperone-active small heat shock protein Hsp17 from C. elegans exhibits topological separation of its N-terminal regions
Small Heat shock proteins (sHsps) are a family of molecular chaperones that bind non-native proteins in an ATP-independent manner. C. elegans encodes 16 different sHsps, among them Hsp17, which is evolutionarily distinct from other sHsps in the nematode. The structure and mechanism of Hsp17 and how ...
ORGANISM(S): Caenorhabditis elegans 
2022-12-08 | PXD030504 | Pride
Hsp-17 Cehsp17 Shsps C. elegans Chaperone Hsp17 Small heat shock protein 
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