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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Basic helix-loop-helix family, member e40

DEC1, Stra13, BHLHB2, SHARP-2
This gene encodes a basic helix-loop-helix protein expressed in various tissues. Expression in the chondrocytes is responsive to the addition of Bt2cAMP. The encoded protein is believed to be involved in the control of cell differentiation. [provided by RefSeq, Aug 2008] (from NCBI)
Papers on DEC1
DEC1 binding to the proximal promoter of CYP3A4 ascribes to the downregulation of CYP3A4 expression by IL-6 in primary human hepatocytes.
GeneRIF
Yan et al., Nanjing, China. In Biochem Pharmacol, 2012
findings suggest that the repression of CYP3A4 by IL-6 is achieved through increasing the DEC1 expression in human hepatocytes, the increased DEC1 binds to the CCCTGC sequence in the promoter of CYP3A4 to form CCCTGC-DEC1 complex
Differentiated embryo-chondrocyte expressed gene 1 regulates p53-dependent cell survival versus cell death through macrophage inhibitory cytokine-1.
GeneRIF
Chen et al., Davis, United States. In Proc Natl Acad Sci U S A, 2012
DEC1 controls the response of p53-dependent cell survival vs. cell death to a stress signal through MIC-1
Differentiated embryo chondrocyte 1 (DEC1) represses PPARγ2 gene through interacting with CCAAT/enhancer binding protein β (C/EBPβ).
GeneRIF
Park et al., Seoul, South Korea. In Mol Cells, 2012
DEC1 is one of the mediators that reset the pattern of PPARgamma2 expression in response to hypoxia.
Clonal B cells of HCV-associated mixed cryoglobulinemia patients contain exhausted marginal zone-like and CD21 low cells overexpressing Stra13.
GeneRIF
Fiorilli et al., Roma, Italy. In Eur J Immunol, 2012
Marginal zone B cells activated by hepatitis C virus undergo functional exhaustion associated with BCR signaling defects and overexpression of a key antiproliferative gene, and may subsequently become terminally spent CD21(low) B cells.
The structure of the FANCM-MHF complex reveals physical features for functional assembly.
GeneRIF
Teng et al., Hefei, China. In Nat Commun, 2011
MHF1 and MHF2 form a compact tetramer to which FANCM-F binds through a 'dual-V' shaped structure.
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