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- W2083144628 endingPage "365" @default.
- W2083144628 startingPage "341" @default.
- W2083144628 abstract "Chaperones/heat shock proteins (HSPs) of the HSP90 and HSP70 families show elevated levels in proliferating mammalian cells and a cell cycle-dependent expression. They transiently associate with key molecules of the cell cycle control system such as Cdk4, Wee-1, pRb, p53, p27/Kip1 and are involved in the nuclear localization of regulatory proteins. They also associate with viral oncoproteins such as SV40 super T, large T and small t antigen, polyoma large and middle S antigen and EpsteinBarr virus nuclear antigen. This association is based on a J-domain in the viral proteins and may assist their targeting to the pRb/E2F complex. Small HSPs and their state of phosphorylation and oligomerization also seem to be involved in proliferation and differentiation. Chaperones/HSPs thus play important roles within cell cycle processes. Their exact functioning, however, is still a matter of discussion. HSP90 in particular, but also HSP70 and other chaperones associate with proteins of the mitogen-activated signal cascade, particularly with the Src kinase, with tyrosine receptor kinases, with Raf and the MAP-kinase activating kinase (MEK). This apparently serves the folding and translocation of these proteins, but possibly also the formation of large immobilized complexes of signal transducing molecules (scaffolding function)." @default.
- W2083144628 created "2016-06-24" @default.
- W2083144628 creator A5026803267 @default.
- W2083144628 creator A5085333361 @default.
- W2083144628 creator A5091468044 @default.
- W2083144628 date "2000-12-01" @default.
- W2083144628 modified "2023-10-14" @default.
- W2083144628 title "Chaperones in cell cycle regulation and mitogenic signal transduction: a review" @default.
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