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• W1982254984 endingPage "2989" @default.
• W1982254984 startingPage "2981" @default.
• W1982254984 abstract "Apoptosis, an essential and basic biological phenomenon, is regulated in a complex manner by a multitude of factors. Myeloid cell leukemia 1 (Mcl-1), an anti-apoptotic member of the B-cell lymphoma 2 (Bcl-2) family of apoptosis-regulating proteins, exemplifies a number of the mechanisms by which a protein's contribution to cell fate may be modified. The N-terminus of Mcl-1 is unique amongst the Bcl-2 family, in that it is rich in experimentally confirmed and putative regulatory residues and motifs. These include sites for ubiquitination, cleavage and phosphorylation, which influence the protein's stability, localisation, dimerization and function. Here we review what is known about the regulation of Mcl-1 expression and function, with particular focus on post-translational modifications and how phosphorylation interconnects the complex molecular control of Mcl-1 with cellular state." @default.
• W1982254984 created "2016-06-24" @default.
• W1982254984 creator A5009481164 @default.
• W1982254984 creator A5015448519 @default.
• W1982254984 creator A5028356032 @default.
• W1982254984 date "2010-06-09" @default.
• W1982254984 modified "2023-09-29" @default.
• W1982254984 title "Mcl-1; the molecular regulation of protein function" @default.
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• W1982254984 doi "https://doi.org/10.1016/j.febslet.2010.05.061" @default.
• W1982254984 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20540941" @default.
• W1982254984 hasPublicationYear "2010" @default.
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