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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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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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Hsp90 and Developmental Networks
2007The most abundant cytoplasmic chaperone of eukaryotic cells, Hsp90 is a hub in developmental regulatory networks and the first example described of the phenomenon of molecular buffering. As a chaperone for many different signaling proteins, Hsp90 maintains the clarity and strength of communication within and between cells, concealing developmental and ...
Suzannah, Rutherford +2 more
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Assays for HSP90 and Inhibitors
2003The molecular chaperone HSP90 is currently under investigation as a promising target for anticancer drug discovery. It constitutes 1–2% of total cellular protein and is present in the cell as a dimer in association with a number of other proteins (1).
Wynne, Aherne +9 more
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2012
Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways. It is important for the cell's response to stress and is a key player in maintaining cellular homeostasis. In the last ten years, it has become a major
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Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways. It is important for the cell's response to stress and is a key player in maintaining cellular homeostasis. In the last ten years, it has become a major
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Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90
Experimental Cell Research, 2006p23 is a component of the Hsp90 molecular chaperone machine. It binds and stabilizes the ATP-bound dimeric form of Hsp90. Since Hsp90 binds protein substrates in the ATP conformation, p23 has been proposed to stabilize Hsp90-substrate complexes. In addition, p23 can also function as a molecular chaperone by itself and even possesses an unrelated ...
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Structural and functional complexity of HSP90 in cellular homeostasis and disease
Nature Reviews Molecular Cell Biology, 2023Gabriela Chiosis +2 more
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