Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers.
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منابع مشابه
Phosphorylation inhibits the DNA-binding activity of MyoD homodimers but not MyoD-E12 heterodimers.
MyoD is a member of the basic helix-loop-helix (bHLH) family of muscle gene regulatory proteins that includes myogenin, myf-5, and MRF4. These proteins have been shown to heterodimerize with E2A bHLH proteins, E12/E47, and to bind to a consensus sequence known as an E-box, CANNTG, the target for transcriptional activation by these myogenic regulators. MyoD is also a phosphorylated nuclear prote...
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متن کاملPhosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52.
FKBP52 (HSP56, p59, HBI) is the 59-kDa immunosuppressant FK506-binding protein and has peptidyl prolyl isomerase as well as a chaperone-like activity in vitro. FKBP52 associates with the heat shock protein HSP90 and is included in the steroid hormone receptor complexes in vivo. FKBP52 possesses a well conserved phosphorylation site for casein kinase II (CK2) that was previously shown to be asso...
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ژورنال
عنوان ژورنال: Genes & Development
سال: 1992
ISSN: 0890-9369
DOI: 10.1101/gad.6.2.166