Modulation of Akt kinase activity by binding to Hsp90.
By Saori Sato, N. Fujita, T. Tsuruo. Proceedings of the National Academy of Sciences of the United States of America, 2000
1,005 citations recorded by the source corpus.
Subfields: Cell Biology, Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e4810c77d267bd6b0dda74bcbc40bf3f416ef242
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Citations in the corpus
- Apoptosis and Molecular Targeting Therapy in Cancer (2014, background): “Conflict of Interests The authors declare that there is no conflict of interests regarding the publication of this paper.”
- The phosphatidylinositol 3-Kinase–AKT pathway in human cancer (2002, background): “An additional level of AKT regulation is provided by its association with the chaperone protein heat-shock protein 90 (HSP90), which protects AKT from dephosphorylation by the general phosphatase PP2”
- Apoptosis defects and chemotherapy resistance: molecular interaction maps and networks (2004, background): “Thus, besides PI3K and AKT, PDK1 and PDK1-interacting proteins (e.g. HSP90 (Sato et al., 2000), PRK2 (Vanhaesebroeck and Alessi, 2000), 14-3-3 proteins (Sato et al., 2002b), the proto-oncogene TCL1 (Kunstle et al., 2002), CTMP (Maira et al., 2001)) are promising new targets for tumors with enhanced…”
- Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. (2002, background): “Hsp90 has been found in association with many components and regulators of the Ras/Raf-1 pathway, including Raf-1, Ksr1, Akt and Src (Kolch, 2000; Sato et al., 2000; Stewart et al., 1999; Whitesell et al., 1994).”
- PKB/Akt: a key mediator of cell proliferation, survival and insulin responses? (2001, background): “PKB has also recently been shown to interact with heat shock protein 90 (HSP90) and this has been proposed to play a role in maintaining PKB in a phosphorylated and active form by preventing its dephosphorylation and inactivation by protein phosphatase 2A (PP2A; Sato et al., 2000), a phosphatase pre”
- Human Host Factors Required for Influenza Virus Replication (2010, positive): “Consistent with these observations, we found that small molecule inhibition of two identified AKT pathway regulators, mTOR (FRAP1) and HSP90AA1, as well as microtubule assembly (TUBB), resulted in a dose-dependent inhibition of influenza virus replication (Supplementary Figure S3)15, 16.”