Structure, regulation and function of PKB/AKT--a major therapeutic target.
By M. Hanada, Jianhua Feng, B. Hemmings. Biochimica et Biophysica Acta, 2004
779 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/f1106359e61448e7f5456ba9da22ff23d2eef35f
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Citations in the corpus
- Autophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis. (2006, background): “Indeed, AKT synergizes with antiapoptotic BCL-xL to promote leukemogenesis (Karnauskas et al., 2003) and has prominent roles in regulating cell growth and metabolism that contribute to tumorigenesis (Hanada et al., 2004).”
- Regulation of Dendritic Morphogenesis by Ras–PI3K–Akt–mTOR and Ras–MAPK Signaling Pathways (2005, background): “In a simplified scheme, it can be generalized that PI3K–Akt via mTOR plays a central role in growth control by controlling ribosomal biogenesis and activity of the translation machinery, whereas other downstream effectors play dominant roles in cell survival through phosphorylation of the cytoskelet”
- PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. (2005, background): “Much progress has been made in the past decade in elucidating the mechanisms that lead to Akt phosphorylation and activation (Hanada et al., 2004).”
- Defining the role of mTOR in cancer. (2007, background): “In mammals, there are three AKT isoforms, each encoded by a unique gene (Hanada et al., 2004).”
- Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1. (2006, background): “Thus, mTORC2-dependent phosphorylation of Akt/PKB at S473 is required for its in vitro activity. rictor and mLST8 Are Required to Maintain PKCa Phosphorylation and Expression, but Not Cytoskeletal Integrity Akt/PKB, S6K1, and SGK belong to the AGC family of kinases, which also includes RSK and PKCa ”