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- W1998363973 abstract "The basic region:leucine zipper (bZIP) DNA-binding protein, C/EBPbeta is a key regulator of numerous cellular processes, but can also contribute to tumorigenesis and to viral diseases. It binds to specific DNA sites as homo- or hetero-dimers and interacts with other transcription factors to control transcription of a number of eukaryotic genes. Importantly, C/EBPbeta induces chromatin opening at several cell-type specific enhancers.C/EBPbeta is an intrinsically repressed protein that is activated in response to growth factors. This report discusses possible mechanisms modulating the biological activities of C/EBPbeta based on results from sequence analysis, molecular modeling, X-ray crystallography and mutagenesis studies. Analysis of primary structure indicated that C/EBPbeta is natively unstructured protein, which consists of regions with potential to fold upon binding to molecular partners and regions that retain irregular conformations independently of their environment. Conformational flexibility allows for the initial auto-inhibition via intramolecular interactions, and subsequently facilitates formation of transient intermolecular interactions that regulate C/EBPbeta's dimerization, nuclear translocation, DNA- binding and trans-activation activities in response to cellular signals." @default.
- W1998363973 created "2016-06-24" @default.
- W1998363973 creator A5022217525 @default.
- W1998363973 date "2015-01-01" @default.
- W1998363973 modified "2023-09-30" @default.
- W1998363973 title "C/EBPβ: Case Study for the Importance of Intrinsic Disorder for Protein Function" @default.
- W1998363973 doi "https://doi.org/10.1016/j.bpj.2014.11.2126" @default.
- W1998363973 hasPublicationYear "2015" @default.
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