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UnknownProteinaceous Transformers: Structural and Functional Variability of Human sHsps.
Not available
S-EPMC7432308 | biostudies-literature
Unknownα-Crystallin Domains of Five Human Small Heat Shock Proteins (sHsps) Differ in Dimer Stabilities and Ability to Incorporate Themselves into Oligomers of Full-Length sHsps.
Not available
S-EPMC9860685 | 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 
UnknownDifferential Roles of Three α-Crystallin Domain-Containing sHsps of Beauveria bassiana in Asexual Development, Multiple Stress Tolerance and Virulence.
Not available
S-EPMC9224193 | biostudies-literature
UnknownInvolvement of small heat shock proteins (sHsps) in developmental stages of fall armyworm, Spodoptera frugiperda and its expression pattern under abiotic stress condition.
Not available
S-EPMC8105634 | 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 | PXD030504 | Pride
Hsp-17 Cehsp17 Shsps C. elegans Chaperone Hsp17 Small heat shock protein 
UnknownSignificant influence of four highly conserved amino-acids in lipochaperon-active sHsps on the structure and functions of the Lo18 protein.
Not available
S-EPMC10624808 | biostudies-literature
UnknownDownregulation of the GhROD1 Gene Improves Cotton Fiber Fineness by Decreasing Acyl Pool Saturation, Stimulating Small Heat Shock Proteins (sHSPs), and Reducing H2O2 Production.
Not available
S-EPMC11509027 | biostudies-literature
ProteomicsStructural probing of Hsp26 activation and client binding by quantitative cross-linking mass spectrometry
Small heat-shock proteins (sHSP) are important members of the cellular stress response in all species. Their best described function is the binding of early unfolding states and the resulting prevention of protein aggregation. All sHSPs exist as oligomers but vary in size and subunit organization. S...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-08-13 | PXD026244 | Pride
Chaperones Hsp26 Shsps Ssa1 Qxl-ms Xl-ms Refolding complex Ydj1 
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 | PXD038019 | Pride
Molecular chaperone Protein structure Protein aggregation Small heat shock protein 
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