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- W2019683899 abstract "The organization of eukaryotic chromatin into specific conformations that are associated with transcription, replication, repair and other nuclear processes are achieved via a series of DNA–protein interactions. These interactions are mediated by a range of DNA-binding domains or modules, such as the high mobility group 1 (HMG1) domain 1 Baxevanis A.D. Landsman D. The HMG-1 box protein family: classification and functional relationships. Nucleic Acids Res. 1995; 23: 1604-1613 Crossref PubMed Scopus (189) Google Scholar , the AT hook 2 Aravind L. Landsman D. AT-hook motifs identified in a wide variety of DNA-binding proteins. Nucleic Acids Res. 1998; 26: 4413-4421 Crossref PubMed Scopus (385) Google Scholar , the plant homeodomain (PHD) finger 3 Aasland R. et al. The PHD finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem Sci. 1995; 20: 56-59 Abstract Full Text PDF PubMed Scopus (759) Google Scholar , the Bright domain 4 Gregory S.L. et al. Characterization of the dead ringer gene identifies a novel, highly conserved family of sequence-specific DNA-binding proteins. Mol. Cell Biol. 1996; 16: 792-799 Crossref PubMed Scopus (137) Google Scholar and the Myb/SANT domain 5 Aasland R. et al. The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem Sci. 1996; 21: 87-88 Abstract Full Text PDF PubMed Scopus (294) Google Scholar . These domains typically bend DNA, recognize non-canonical DNA structures and organize chromatin structure. While analysing recently reported transcription and chromatin structure regulators, we discovered yet another potential DNA-binding motif that could perform a specific role in chromosomal organization and provide links between transcription, repair, RNA processing and apoptotic chromatin degradation." @default.
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- W2019683899 title "SAP – a putative DNA-binding motif involved in chromosomal organization" @default.
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- W2019683899 doi "https://doi.org/10.1016/s0968-0004(99)01537-6" @default.
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