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Given that CENP-B is the only centromere protein that binds centromere-specific DNA elements, our study provides a new link between centromere DNA and unique epigenetic landscape of centromere chromatin
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Upon cross-linking, the entire CENPA/CENPB/CENPC/CENPT complex is nuclease-protected over an alpha-satellite dimer that comprises the fundamental unit of centromeric chromatin. We conclude that CENPA/CENPC and CENPT pathways for kinetochore assembly are physically integrated over young alpha-satellite dimers.
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Findings indicate that expression of the scleroderma autoantigens IFI-16 and CENPs, which are associated with severe vascular disease, is increased in vascular progenitors and mature endothelial cells. High level, lineage-enriched expression of autoantigens may explain the striking association between clinical phenotypes and the immune targeting of specific autoantigens.
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The results indicated that CENPB boxes are highly conserved in Down syndrome (DS) patients and may not be responsible for Chr21 nondisjunction events. However, alphasatDNA in Chr21 is variable and deoxynucleotide deletions, mutations and polymorphisms may act as potential molecular diagnostic markers of DS.
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CENP-B directly binds both CENP-A's amino-terminal tail and CENP-C, a key nucleator of kinetochore assembly
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The results revealed that CENP-B binding in the vicinity of the CENP-A nucleosome substantially stabilizes the CENP-A nucleosome on alphoid DNA in human cells.
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Centromere protein B (CENP-B) as a novel interacting partner of HBZ.
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INMAP as a model regulator of CENP-B
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N-terminal methylation is required for CENP-B's binding to the CENP-B box.
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Human Nap1, an acidic histone chaperone, inhibited the non-specific binding of CENP-B to nucleosomes and apparently stimulated CENP-B binding to its cognate CENP-B box DNA.
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CENP-A and/or B status is predictive of the extent of skin involvement over time in systemic sclerosis.
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Anti-CENP-B autoantibodies in breast cancer patients prolong disease-free and overall survival.
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CENP-A, -B, and -C chromatin complex that contains the I-type alpha-satellite array constitutes the prekinetochore in HeLa cells
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crystal structure of its dimerization domain (CENP-B-(540-599)), another functional domain of CENP-B, at 1.65-A resolution
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the interaction between CENP-B and CENP-C may be involved in the correct assembly of CENP-C on alphoid DNA
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CENP-B for the CENP-B box DNA is reduced nearly to the level of nonspecific DNA binding by CpG methylation
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CENP-B may be a determinant for translational positioning of the centromere-specific nucleosomes through its binding to the nucleosomal CENP-B box
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This study shows that ICP0 induces the proteasomal-dependent degradation of the centromeric protein CENP-B in infected as well as ICP0-expressing cells.
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CENP-B was found to bind specifically to the surface of human pulmonary artery smooth muscle cells and not to fibroblasts or endothelial cells
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observation of FRET between CENP-A and CENP-B at centromere locations; this indicates that these proteins are in the molecular vicinity (<10 nm) of each other