Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1

By W. Pratt, D. Toft. Experimental biology and medicine, 2003

1,520 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0ad23bc6458ffb3c65ce22ac5241fa10bfafa4be

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In Computational Theory and Mathematics

M. Al-Whaibi

In Immunology

In Molecular Biology

Citations in the corpus

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. (2006, background): “p23, a cochaperone that can stabilize Hsp90-client interactions in the ATP state (Pratt and Toft, 2003), was found to be important to prevent destabilization and degradation of DF508.”
Progesterone receptors: form and function in brain. (2008, neutral): “The interaction of PRs with the chaperones is a prerequisite for hormone binding [218,219].”
Recognition and response in the plant immune system. (2003, background): “For instance, the formation of functional steroid receptors in mammals requires cytosolic HSP90 (117).”
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. (2005, background): “On the one hand, Hsp90 has a well-established ability to directly influence the folding of critical signaling proteins, protein kinases, and transcription factors (Pratt and Toft, 2003).”
The heat shock response: life on the verge of death. (2010, background): “This has been shown for the chaperonins and the Hsp70 system and for Hsp70 and Hsp90 during the processing of steroid hormone receptors (Pratt and Toft, 2003).”
Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications (2005, background): “These include Hsp10 and Hsp60 complexes that mediate protein folding and Hsp70- and Hsp90-containing complexes that are involved in both generic protein-folding pathways and in specific association with key regulatory proteins within the cell (Netzer and Hartl 1998; Pratt and Toft 2003).”
SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. (2014, background): “293T cells were co-transfected with a FLAGSMYD2 expression vector and four different lengths of HA-HSP90AB1 vectors ([1–724], [1–500], [250–724] and [500–724]).”
Plant heat-shock proteins: A mini review (2011, positive): “The class Hsp90 shares with other classes, the role being molecular chaperones as Hsp90 can bind Hsp70 in many chaperone complexes and has important role in signaling protein function and trafﬁcking (Pratt and Toft, 2003).”
Hsp70 and Hsp90--a relay team for protein folding. (2004, background): “These substrates include transcription factors such as steroid hormone receptors and some proto-oncogenic serine/threonine and tyrosine kinases like Raf and Src in higher eukaryotes (for reviews see Buchner 1999; Picard 2002; Pratt and Toft 2003).”