Thr 163 Phosphorylation Causes Mcl-1 Stabilization when Degradation Is Independent of the Adjacent GSK3-Targeted Phosphodegron, Promoting Drug Resistance in Cancer - Nifoussi, Shanna K.; Vrana, Julie A.; Domina, Aaron M.; De Biasio, Alfredo; Gui, Jingang; Gregory, Mark A.; Hann, Stephen R.; Craig, Ruth W. (PloS one, 2012)
Keywords: Acetic acid; Activation; Animals; Antineoplastic Agents - pharmacology; Apoptosis; Apoptosis - drug effects; Apoptosis - genetics; Bcl-2 protein; Biology; Blotting, Western; Burkitt's lymphoma; Cancer; Cell cycle; Cell death; Cell Line, Tumor; Chemotherapy; CHO Cells; Cisplatin; Cisplatin - pharmacology; Cotton, Norris; Cricetinae; Cytarabine - pharmacology; Degradation; Drug resistance; Drug Resistance, Neoplasm - genetics; Drug therapy; Etoposide; Etoposide - pharmacology; Extracellular signal-regulated kinase; Fibroblasts; Flow Cytometry; Glutamic acid; Glycogen; Glycogen synthase kinase 3; Glycogen Synthase Kinase 3 - genetics; Glycogen Synthase Kinase 3 - metabolism; Glycogen synthesis; Humans; Kinases; Laboratories; Leukemia; Lymphoma; Lymphomas; Mcl-1 protein; Medicine; MicroRNAs; Mutation; Myeloid Cell Leukemia Sequence 1 Protein; Organic acids; Pests; Phosphorylation; Proline; Protein Stability; Proteins; Proto-Oncogene Proteins c-bcl-2 - metabolism; Sequences; Serine; Signal transduction; Stabilization; Threonine; Threonine - metabolism; Toxicology; Vinblastine; Vinblastine - pharmacology; Lebanon; United States--US; New Hampshire