Structural and functional complexity of HSP90 in cellular ... - Nature
2023年7月31日 · Heat shock protein 90 (HSP90) is a chaperone with vital roles in regulating proteostasis, long recognized for its function in protein folding and maturation. A view...
The HSP90 Family: Structure, Regulation, Function, and ...
HSP90 proteins take part in essential cellular processes and regulatory pathways like apoptosis, cell cycle control, cell viability, protein folding and degradation, and signalling events. In addition, they induce the adaptive immunity by activation of antigen presenting cells and dendritic cells.
Design, synthesis and biological studies of new isoxazole ... - Nature
1 天前 · Heat shock protein 90 (Hsp90), a molecular chaperone, contributes to the preservation of folding, structure, stability, and function proteins. In this study, novel compounds comprising isoxazole ...
Hsp90: a specialized but essential protein-folding tool - PMC
Recent advances in understanding the structure and function of Hsp90 now indicate that it uses a protein-folding strategy different from that of either Hsp70 or the chaperonins. Here, we discuss the distinct biochemical mechanisms by which Hsp90 handles its substrate polypeptides and the unique biological functions of this curious protein ...
The Hsp70–Hsp90 Chaperone Cascade in Protein Folding
2019年2月1日 · We describe three main routes for protein folding in the cell: (i) spontaneous folding, without the aid of any chaperone; (ii) folding assisted in cycles of Hsp70 binding and release; (iii) folding along the Hsp70–Hsp90 cascade (Figure 1).
The HSP90 chaperone machinery - Nature Reviews Molecular …
2017年4月21日 · The HSP90 machinery evolved to control protein function and activity by facilitating protein folding, the binding of ligands to their receptors or targets, or the assembly of multiprotein...
Molecular Interaction Network of the Hsp90 Chaperone System
Hsp90 is an essential and ubiquitous molecular chaperone that is required for the proper folding of a set of client proteins at a late stage in their folding process. In eukaryotes, cytoplasmic Hsp90 is absolutely essential for cell viability under all growth conditions.
Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System - Cell …
Here, we show that Hsp90 takes a key role in protein folding by breaking an Hsp70-inflicted folding block, empowering protein clients to fold on their own. At physiological concentrations, Hsp70 stalls productive folding by binding hydrophobic, core-forming segments. Hsp90 breaks this deadlock and restarts folding.
Heat shock protein 90: biological functions, diseases, and …
Heat shock protein 90 (Hsp90) is a predominant member among Heat shock proteins (HSPs), playing a central role in cellular protection and maintenance by aiding in the folding, stabilization, and modification of diverse protein substrates.
Hsp90 - Wikipedia
Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why …