Results 211 to 220 of about 58,138 (243)
The ‘active life’ of Hsp90 complexes
Biochimica Et Biophysica Acta - Molecular Cell Research, 2012 Hsp90 forms a variety of complexes differing both in clientele and co-chaperones. Central to the role of co-chaperones in the formation of Hsp90 complexes is the delivery of client proteins and the regulation of the ATPase activity of Hsp90. Determining the mechanisms by which co-chaperones regulate Hsp90 is essential in understanding the assembly of ...
Chrisostomos Prodromou
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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 Inhibitors in the Clinic
2005Specific inhibitors of Hsp90 have recently entered human clinical trials. At the time of writing, trials have been initiated only in metastatic cancer, although a rationale exists for using these agents in a variety of human diseases where protein (mis)folding is involved in the disease pathophysiology.
S, Pacey +3 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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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 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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