نتایج جستجو برای: molecular chaperone
تعداد نتایج: 644698 فیلتر نتایج به سال:
Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.
Background: Hsp110, an Hsp70 homolog, is highly efficient in preventing protein aggregation, but lacks the folding activity seen in Hsp70s. Result: In contrast to Hsp70s, Hsp110s exhibit distinct peptide substrate binding properties. Conclusion: The peptide substrate binding properties determine the chaperone activity differences between Hsp70s and Hsp110s. Significance: Our studies shed light ...
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