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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Bromodomain adjacent to zinc finger domain, 2B

Top mentioned proteins: Histone, H4, CBP, WSTF, OUT
Papers on BAZ2B
Discovery and Characterization of GSK2801, a Selective Chemical Probe for the Bromodomains BAZ2A and BAZ2B.
Drewry et al., United States. In J Med Chem, May 2015
The two closely related bromodomain containing proteins BAZ2A and BAZ2B constitute the central scaffolding protein of the nucleolar remodeling complex (NoRC) that regulates the expression of noncoding RNAs.
Structure enabled design of BAZ2-ICR, a chemical probe targeting the bromodomains of BAZ2A and BAZ2B.
Hoelder et al., London, United Kingdom. In J Med Chem, Apr 2015
The bromodomain containing proteins BAZ2A/B play essential roles in chromatin remodeling and regulation of noncoding RNAs.
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC.
Ciulli et al., Cambridge, United Kingdom. In Structure, Feb 2015
Here, we report crystal structures of PHD zinc finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3 and/or H4 histones.
Binding hotspots of BAZ2B bromodomain: Histone interaction revealed by solution NMR driven docking.
Ciulli et al., Cambridge, United Kingdom. In Biochemistry, 2014
Effective targeting of the BAZ2B bromodomain by small molecule inhibitors has been recently reported, but no structural information is yet available on the interaction with its natural binding partner, acetylated histone H3K14ac.
Structured water molecules in the binding site of bromodomains can be displaced by cosolvent.
Caflisch et al., Zürich, Switzerland. In Chemmedchem, 2014
Here, explicit solvent molecular dynamics (MD) simulations of two bromodomains (BAZ2B and CREBBP) are used to analyze the water molecules that seem to be conserved at the bottom of the acetyl-lysine binding site in most crystal structures of bromodomains.
Targeting low-druggability bromodomains: fragment based screening and inhibitor design against the BAZ2B bromodomain.
Ciulli et al., Cambridge, United Kingdom. In J Med Chem, 2014
We describe successful targeting of the challenging BAZ2B bromodomain using biophysical fragment screening and structure-based optimization of high ligand-efficiency fragments into a novel series of low-micromolar inhibitors.
Does bromodomain flexibility influence histone recognition?
Caflisch et al., Zürich, Switzerland. In Febs Lett, 2013
Furthermore, for the BAZ2B and CREBBP bromodomains we observe occlusion of the binding site which is coupled to the displacement of the two aromatic residues.
Identification of a sudden cardiac death susceptibility locus at 2q24.2 through genome-wide association in European ancestry individuals.
Chugh et al., Baltimore, United States. In Plos Genet, 2011
We performed a genome-wide association meta-analysis in 1,283 SCD cases and >20,000 control individuals of European ancestry from 5 studies, with follow-up genotyping in up to 3,119 SCD cases and 11,146 controls from 11 European ancestry studies, and identify the BAZ2B locus as associated with SCD (P = 1.8×10(-10)).
A novel family of bromodomain genes.
Shimane et al., Ibaraki, Japan. In Genomics, 2000
The novel genes, termed BAZ1A, BAZ1B, BAZ2A, and BAZ2B, localize to chromosomes 14q12-q13, 7q11-q21, 12q24.3-qter,
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