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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.

The small heat shock proteins (sHSPs) recently have been reported to have molecular chaperone activity in vitro; however, the mechanism of this activity is poorly defined. We found that HSP18.1, a dodecameric sHSP from pea, prevented the aggregation of malate dehydrogenase (MDH) and glyceraldehyde-3...

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Autores principales: Lee, G J, Roseman, A M, Saibil, H R, Vierling, E
Formato: Artigo
Lenguaje:Inglês
Publicado: 1997
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1169668/
https://ncbi.nlm.nih.gov/pubmed/9034347
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/16.3.659
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