The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
CCAAT/enhancer-binding proteins: structure, function and regulation
Open accessAbstract
CCAAT/enhancer binding proteins (C/EBPs) are a family of transcription factors that all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. At least six members of the family have been isolated and characterized to date (C/EBPα—C/EBPζ), with further diversity produced by the generation of different sized polypeptides, predominantly by differential use of translation initiation sites, and extensive protein—protein interactions both within the family and with other transcription factors. The function of the C/EBPs has recently been investigated by a number of approaches, including studies on mice that lack specific members, and has identified pivotal roles of the family in the control of cellular proliferation and differentiation, metabolism, inflammation and numerous other responses, particularly in hepatocytes, adipocytes and haematopoietic cells. The expression of the C/EBPs is regulated at multiple levels during several physiological and pathophysiological conditions through the action of a range of factors, including hormones, mitogens, cytokines, nutrients and certain toxins. The mechanisms through which the C/EBP members are regulated during such conditions have also been the focus of several recent studies and have revealed an immense complexity with the potential existence of cell/tissue- and species-specific differences. This review deals with the structure, biological function and the regulation of the C/EBP family.
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Cites
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“Indeed, several C/EBPb isoforms (including LIP and LAP, which are generated by differential start site usage and proteolytic cleavage [ Ramji and Foka, 2002 ]), were upregulated during OIS (Figure 4B).”
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Metadata
- Authors
- RAMJI, D. P., & FOKA, P.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2002-08-01
- Volume
- 365
- Issue
- 3
- Pages
- 561-575
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2129011493
- Cited by
- 1,400
- References
- 16
- FWCI
- 18.57
- Type
- journal article
- Language
- en
- Open access
- green
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