Results 201 to 210 of about 58,138 (243)
Engineered protein nanoclusters reduce liver fibrosis and hepatocellular carcinoma in mice models. [PDF]
Bioact MaterSaxena T +12 more
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Heat shock protein Gp96 (Grp94) in malaria: functional insights at the host-parasite interface and therapeutic perspectives. [PDF]
Front Cell Dev BiolDjoumoi D +5 more
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Embracing diversity: Post-translational modifications, the chaperone code, and the emergence of new chaperone entities. [PDF]
Cell Stress ChaperonesDigwal CS, Wang S, Chiosis G.
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Journal of Cell Biology, 2001 Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.
Jason C Young +2 more
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International Journal of Molecular Sciences, 2021 HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein, it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits that consist of three main conserved domains known as the N-terminal domain, middle domain, and the C-terminal domain.
Chikezie O Madu
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DNA and Cell Biology, 2023
Heat shock protein 90 (HSP90) family is a class of proteins known as molecular chaperones that promote client protein folding and translocation in unstressed cells and regulate cellular homeostasis in the stress response. Noncoding RNAs (ncRNAs) are defined as RNAs that do not encode proteins.
Qing Xu +6 more
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Heat shock protein 90 (HSP90) family is a class of proteins known as molecular chaperones that promote client protein folding and translocation in unstressed cells and regulate cellular homeostasis in the stress response. Noncoding RNAs (ncRNAs) are defined as RNAs that do not encode proteins.
Qing Xu +6 more
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Nature Reviews Molecular Cell Biology, 2017
The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis under both physiological and stress conditions in eukaryotic cells. As HSP90 has several hundred protein substrates (or 'clients'), it is involved in many cellular processes beyond protein folding, which include DNA repair, development, the immune response and ...
Johannes Büchner, Büchner Johannes
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The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis under both physiological and stress conditions in eukaryotic cells. As HSP90 has several hundred protein substrates (or 'clients'), it is involved in many cellular processes beyond protein folding, which include DNA repair, development, the immune response and ...
Johannes Büchner, Büchner Johannes
exaly +3 more sources
Overview: Translating Hsp90 Biology into Hsp90 Drugs
Current Cancer Drug Targets, 2003The Hsp90 molecular chaperone has emerged as one of the most exciting targets for cancer drug development. Hsp90 is overexpressed in many malignancies, very likely as a result of the stress that is induced both by the hostile cancer microenvironment and also by the mutation and abberant expression of oncoproteins.
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