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10.1074/jbc.R115.692020

http://scihub22266oqcxt.onion/10.1074/jbc.R115.692020
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suck abstract from ncbi


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pmid26851278
      J+Biol+Chem 2016 ; 291 (13 ): 6714-22
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  • Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300 #MMPMID26851278
  • Dyson HJ ; Wright PE
  • J Biol Chem 2016[Mar]; 291 (13 ): 6714-22 PMID26851278 show ga
  • The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a particularly rich set of interactions with disordered and partly ordered partners, as a part of their ubiquitous role in facilitating transcription of genes. CBP and p300 contain a number of small structured domains that provide scaffolds for the interaction of disordered transactivation domains from a wide variety of partners, including p53, hypoxia-inducible factor 1? (HIF-1?), NF-?B, and STAT proteins, and are the targets for the interactions of disordered viral proteins that compete with cellular factors to disrupt signaling and subvert the cell cycle. The functional diversity of the CBP/p300 interactome provides an excellent example of the power of intrinsic disorder to facilitate the complexity of living systems.
  • |CREB-Binding Protein/*chemistry/genetics/metabolism [MESH]
  • |E1A-Associated p300 Protein/*chemistry/genetics/metabolism [MESH]
  • |Humans [MESH]
  • |Hypoxia-Inducible Factor 1, alpha Subunit/chemistry/genetics/metabolism [MESH]
  • |Intrinsically Disordered Proteins/*chemistry/genetics/metabolism [MESH]
  • |Models, Molecular [MESH]
  • |NF-kappa B/chemistry/genetics/metabolism [MESH]
  • |Protein Binding [MESH]
  • |Protein Folding [MESH]
  • |Protein Interaction Domains and Motifs [MESH]
  • |Protein Structure, Secondary [MESH]
  • |STAT Transcription Factors/chemistry/genetics/metabolism [MESH]
  • |Transcription, Genetic [MESH]
  • |Tumor Suppressor Protein p53/chemistry/genetics/metabolism [MESH]


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