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CENPB product is a highly conserved protein that facilitates centromere formation. De plus, nous expédions Centromere Protein B Anticorps (44) et Centromere Protein B Protéines (7) et beaucoup plus de produits pour cette protéine.
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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
Upon cross-linking, the entire CENPA (Montrer CENPA Kits ELISA)/CENPB/CENPC (Montrer CENPC1 Kits ELISA)/CENPT (Montrer CENPT Kits ELISA) complex is nuclease-protected over an alpha-satellite dimer that comprises the fundamental unit of centromeric chromatin. We conclude that CENPA/CENPC (Montrer CENPA Kits ELISA) and CENPT (Montrer CENPT Kits ELISA) pathways for kinetochore assembly are physically integrated over young alpha-satellite dimers.
Findings indicate that expression of the scleroderma autoantigens IFI-16 (Montrer IFI16 Kits ELISA) and CENPs (Montrer APITD1 Kits ELISA), 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.
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.
CENP-B directly binds both CENP-A's amino-terminal tail and CENP-C (Montrer CENPC1 Kits ELISA), a key nucleator of kinetochore assembly
The results revealed that CENP-B binding in the vicinity of the CENP-A (Montrer CENPA Kits ELISA) nucleosome substantially stabilizes the CENP-A (Montrer CENPA Kits ELISA) nucleosome on alphoid DNA in human cells.
Centromere protein B (CENP-B) as a novel interacting partner of HBZ.
INMAP as a model regulator of CENP-B
N-terminal methylation is required for CENP-B's binding to the CENP-B box.
Human Nap1 (Montrer IL8 Kits ELISA), 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.
demonstrate a novel ADA3 interaction with CENP-B-centromere that may account for its previously known function in mitosis
Cenpa (Montrer CENPA Kits ELISA), Cenpb, and Bub3, but not Cenpc (Montrer CENPC1 Kits ELISA), interacted with PARP-1 (Montrer PARP1 Kits ELISA)
This study shows that ICP0 induces the proteasomal-dependent degradation of the centromeric protein CENP-B in infected as well as ICP0-expressing cells.
Propose that CENP-B plays a dual role in centromere formation, ensuring de novo formation on DNA lacking a functional centromere but preventing the formation of excess centromeres on chromosomes.
This gene product is a highly conserved protein that facilitates centromere formation. It is a DNA-binding protein that is derived from transposases of the pogo DNA transposon family. It contains a helix-loop-helix DNA binding motif at the N-terminus, and a dimerization domain at the C-terminus. The DNA binding domain recognizes and binds a 17-bp sequence (CENP-B box) in the centromeric alpha satellite DNA. This protein is proposed to play an important role in the assembly of specific centromere structures in interphase nuclei and on mitotic chromosomes. It is also considered a major centromere autoantigen recognized by sera from patients with anti-centromere antibodies.
, centromere autoantigen B
, major centromere autoantigen B
, CENP-B protein
, centromere protein B
, Major centromere autoantigen B
, centromere autoantigen protein B
, centromere protein B, 80kDa
, LOW QUALITY PROTEIN: major centromere autoantigen B