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OTUB1 leads to the phosphorylation of AKT. 2 / 2
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"Moreover, OTUB1 is found to inhibit K63-linked ubiquitination and the PIP3-binding function of AKT in a manner dependent on the catalytic residues Cys91 and Asp88, thereby decreasing AKT phosphorylati[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Following exogenous IL-2 addition, rapamycin did not inhibit phosphorylation of STAT5 or Akt but specifically inhibited mTOR activity as demonstrated by decreased phosphorylation of S6K1 and 4E-BP1, reduced Otub1 protein, and maintenance of GRAIL (XREF_FIG)."