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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 ...
Florian H. Schopf +2 more
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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 ...
Florian H. Schopf +2 more
semanticscholar +3 more sources
Targeting the HSP90–CDC37–kinase chaperone cycle: A promising therapeutic strategy for cancer
Medicinal research reviews (Print), 2021Heat shock protein 90 (HSP90) is an indispensable molecular chaperone that facilitates the maturation of numerous oncoproteins in cancer cells, including protein kinases, ribonucleoproteins, steroid hormone receptors, and transcription factors.
Lei Wang, Qiuyue Zhang, Q. You
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Journal of Medicinal Chemistry, 2020
Hsp90 is one of the most important chaperones involved in regulating the maturation of more than 300 client proteins, many of which are closely associated with refractory diseases, including cancer, neurodegenerative diseases and viral infections ...
Li Li, Lei Wang, Q. You, Xiao-li Xu
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Hsp90 is one of the most important chaperones involved in regulating the maturation of more than 300 client proteins, many of which are closely associated with refractory diseases, including cancer, neurodegenerative diseases and viral infections ...
Li Li, Lei Wang, Q. You, Xiao-li Xu
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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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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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Spotlight on 17‐AAG as an Hsp90 inhibitor for molecular targeted cancer treatment
Chemical Biology and Drug Design, 2019Hsp90 is a ubiquitous chaperone with important roles in the organization and maturation of client proteins that are involved in the progression and survival of cancer cells.
Sona Talaei +5 more
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2021
Aim. Chaperones HSP90 have been considered as a mechanism for buffering and accumulating genetic changes which could be important for developmental networks. An analysis of polymorphic Arabidopsis thaliana seeds was carried out to test this hypothesis. Methods.
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Aim. Chaperones HSP90 have been considered as a mechanism for buffering and accumulating genetic changes which could be important for developmental networks. An analysis of polymorphic Arabidopsis thaliana seeds was carried out to test this hypothesis. Methods.
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1997
Abstract The alternative names of members of the Hsp90 family correspond to their apparent molecular weight on SDS-PAGE, depend on the context in which they have been identified: Hsp84/Hsp86 (mouse; Moore et al., 1989), Hsp85 (L929-cells; Lanks, 1989), Hsp89/Hsp90 (HeLa cells; Welch, Feramisco, 1982).
U Jakob, J Buchner
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Abstract The alternative names of members of the Hsp90 family correspond to their apparent molecular weight on SDS-PAGE, depend on the context in which they have been identified: Hsp84/Hsp86 (mouse; Moore et al., 1989), Hsp85 (L929-cells; Lanks, 1989), Hsp89/Hsp90 (HeLa cells; Welch, Feramisco, 1982).
U Jakob, J Buchner
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Current Oncology Reports, 2010
Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the trafficking of proteins in the cell. Under stressful conditions, Hsp90 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Disruption of Hsp90 leads to client protein degradation and often cell death.
Jeffrey M, Holzbeierlein +2 more
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Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the trafficking of proteins in the cell. Under stressful conditions, Hsp90 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Disruption of Hsp90 leads to client protein degradation and often cell death.
Jeffrey M, Holzbeierlein +2 more
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Hsp90: the vulnerable chaperone
Drug Discovery Today, 2004The molecular chaperone Hsp90 has emerged as an important target in cancer treatment because of its roles in maintaining transformation and regulating the function of proteins involved in apoptotic, survival and growth pathways. Many Hsp90 inhibitors function by binding to the N-terminal ATP pocket, but the chaperone has many other vulnerable points ...
Gabriela, Chiosis +3 more
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