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CCR4 (zeige CCR4 Proteine) and CAF1, the two deadenylases in the CCR4 (zeige CCR4 Proteine)-NOT complex, can remove 3' terminal non-A residues in an exonucleolytic manner.
CAF1-p180 (zeige RRBP1 Proteine) and CAF1-p75 (zeige HNRNPM Proteine) subunits mediate assembly of two different forms of chromatin.
CAF-1 promotes Notch (zeige NOTCH1 Proteine) signaling through epigenetic control of target gene expression during Drosophila development.
these studies suggest that p55 is not crucial for PRC2-mediated gene silencing in vivo, and the vital function of p55 is probably not dependent on its interaction with histone H4.
Chromatin-modifying complex component Nurf55/p55 associates with histones H3 and H4 and polycomb (zeige CBX2 Proteine) repressive complex 2 subunit Su(z)12 through partially overlapping binding sites.
analysis of Caf1 mutant tissue suggests that Caf1 plays important roles in cell survival and segment identity, and loss of Caf1 is associated with a reduction in the Polycomb (zeige CBX2 Proteine) Repressive Complex 2 (PRC2)-specific histone methylation mark H3K27me3
spreading of heterochromatin is compromised in flies that have reduced CAF-1 p180 (zeige RRBP1 Proteine). Furthermore, reduced CAF-1 p180 (zeige RRBP1 Proteine) causes a defect in the dynamics of heterochromatic markers in early Drosophila embryos.
sliding model in which the position-specific tethering of NURF forces a translocating ISWI ATPase to pump a DNA distortion over the histone octamer, thereby changing the translational position of the nucleosome.
Data show that removal of p55 deregulated the expression of E2F targets that are normally repressed by dE2F2/RBF-1 and -2 complexes in a cell cycle-independent manner but had no effect on the expression of targets normally coupled with cell proliferation.
The nucleosome-binding subunits Su(z)12 and Nurf55 anchor the E(z) enzyme on chromatin substrates, an essential process in maintaining HOX (zeige MSH2 Proteine) gene silencing during development.
The MTA1 (zeige MTA1 Proteine) subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/RBBP7 (zeige RBBP7 Proteine).
RbAp48 is likely to act as a potent antiretroviral defense.
The crystal structure reveals an extensive interface between MTA1 (zeige MTA1 Proteine) and RBBP4.
RBBP4 interacts with ep300 (zeige EP300 Proteine) protein to form a complex that drives the expression of methylguanine-DNA-methyltransferase (zeige MGMT Proteine) , RAD51 (zeige RAD51 Proteine), and other selected DNA repair genes through histone acetylation.
RbAp48 was identified as critical in the proliferation of hypopharyngeal carcinoma in both in vitro and in vivo experiments.
RBBP4 functions as a novel regulatory factor to increase the efficiency of importin alpha/beta-mediated nuclear import
Our RBBP4-PHF6 (zeige PHF6 Proteine) complex structure provides insights into the molecular basis of PHF6 (zeige PHF6 Proteine)-NuRD complex interaction and implicates a role for PHF6 (zeige PHF6 Proteine) in chromatin structure modulation and gene regulation.
Our results reveal that the protein structure does not affect ligand binding, and the top three TCM candidates Bittersweet alkaloid II, Eicosandioic acid, and Perivine might resolve the instability of the RbAp48-FOG1 (zeige ZFPM1 Proteine) complex
RbAp48 recognizes MTA1 (zeige MTA1 Proteine) using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46 (zeige RBBP7 Proteine)/48 interactions with histones.
The most significant change was an age-related decline in RbAp48, a histone-binding protein that modifies histone acetylation.
RBBP4 is a regulator of histone deacetylation during oocyte maturation and deacetylation is required for bipolar spindle assembly through Aurora kinase C (zeige AURKC Proteine)
Studies indicate that estrogen deficiency initiates tissue-specific apoptosis in the exocrine gland cells through RbAp48 overexpression.
Estrogen deficiency initiates p53 (zeige TP53 Proteine)-mediated apoptosis in the exocrine glands through Rbbp4 overexpression.
Results report that transgenic expression of RbAp48 resulted in the development of autoimmune exocrinopathy resembling Sjogren's syndrome.
This gene encodes a ubiquitously expressed nuclear protein which belongs to a highly conserved subfamily of WD-repeat proteins. It is present in protein complexes involved in histone acetylation and chromatin assembly. It is part of the Mi-2 complex which has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. This encoded protein is also part of co-repressor complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to retinoblastoma protein to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of E2F-responsive genes. Three transcript variants encoding different isoforms have been found for this gene.
histone-binding protein RBBP4
, nucleosome-remodeling factor subunit RBAP48
, retinoblastoma-binding protein 4
, histone-binding protein RBBP4-A
, retinoblastoma A associated protein
, retinoblastoma-binding protein 4-A
, retinoblastoma-binding protein p48-A
, chromatin assembly Factor-1
, chromatin assembly factor 1
, chromatin assembly factor 1 subunit
, chromatin associated factor-1 subunit
, nucleosome remodeling factor
, nucleosome remodeling factor - 55kD
, retinoblastoma binding protein 4
, CAF-1 subunit C
, CAF-I 48 kDa subunit
, CAF-I p48
, MSI1 protein homolog
, chromatin assembly factor 1 subunit C
, chromatin assembly factor I p48 subunit
, chromatin assembly factor/CAF-1 p48 subunit
, retinoblastoma-binding protein p48
, CAF-1 p48 subunit
, chCAF-1 p48
, chromatin assembly factor 1 p48 subunit