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anti-Human DDB1 Antibodies:
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Dog (Canine) Monoclonal DDB1 Primary Antibody for IF, WB - ABIN968852
Dualan, Brody, Keeney, Nichols, Admon, Linn: Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein. in Genomics 1996
Show all 4 Pubmed References
Human Polyclonal DDB1 Primary Antibody for ELISA, WB - ABIN262637
Malatesta, Peschiaroli, Memmi, Zhang, Antonov, Green, Barlev, Garabadgiu, Zhou, Melino, Bernassola: The Cul4A-DDB1 E3 ubiquitin ligase complex represses p73 transcriptional activity. in Oncogene 2013
Show all 2 Pubmed References
Human Polyclonal DDB1 Primary Antibody for ELISA, WB - ABIN184570
Li, Robert, van Breugel, Strubin, Zheng: A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery. in Nature structural & molecular biology 2010
Show all 2 Pubmed References
The DDB1 is acetylated and acetylation promotes DDB1 binding to CUL4.
Results revealed a function independent of its transcriptional activity, as TTF-1 (show NKX2-1 Antibodies) was found to interact with DDB1 and block its binding to CHK1 (show CHEK1 Antibodies), which in turn attenuated ubiquitylation and subsequent degradation of CHK1 (show CHEK1 Antibodies).
SIRT7 inhibits TR4 degradation by deacetylation of DDB1.
the c-Abl (show ABL1 Antibodies) non-receptor kinase phosphorylates DDB1 at residue Tyr (show TYR Antibodies)-316 to recruit a small regulatory protein, DDA1 (show DDA1 Antibodies), leading to increased substrate ubiquitination
knockdown of DCAF7 (show DCAF7 Antibodies) reduced the degradation of DNA ligase I (show LIG1 Antibodies) in response to inhibition of proliferation and replacement of ubiquitylated lysine residues reduced the in vitro ubiquitylation of DNA ligase I (show LIG1 Antibodies) by Cul4-DDB1 and DCAF7 (show DCAF7 Antibodies). In contrast, a different E3 ubiquitin ligase (show MUL1 Antibodies) regulates FEN-1 (show FEN1 Antibodies) turnover.
This study presents the crystal structure of the DDB1-DCAF1 (show VPRBP Antibodies)-HIV-1-Vpr-uracil-DNA glycosylase (show UNG Antibodies) (cyclin U (show CCNO Antibodies)) complex.
Our data are consistent with the idea that the CUL4A (show CUL4A Antibodies)/B-DDB1-CRBN (show CRBN Antibodies) complex catalyses the polyubiquitination and thus controls the degradation of CLC-1 (show CLCN1 Antibodies) channels.
These results revealed a novel role of DDB in H3K56Ac deacetylation during early step of NER (show NR1H2 Antibodies) and the existence of active functional cross-talk between DDB-mediated damage recognition and H3K56Ac deacetylation.
The identification of Vpr mutants which associate with DCAF1 but only poorly with DDB1 suggests that DCAF1 is necessary but is not sufficient for the Vpr association with DDB1-containing E3 ligase complex.
Data support a model wherein DDB1 and DDB2 (show DDB2 Antibodies) cooperate to repress Bcl-2 (show BCL2 Antibodies) transcription. DDB2 (show DDB2 Antibodies) recognizes and binds to the Bcl-2 (show BCL2 Antibodies) P1 promoter, and HDAC1 (show HDAC1 Antibodies) is recruited through the DDB1 subunit associated with DDB2 (show DDB2 Antibodies) to deacetylate histone H3K9.
Bovine herpesvirus-1 VP8 interacts with DDB1 and is monoubiquitinated during infection.
These studies identify CUL4-DDB1 complex as a novel post-translational regulator of stem and progenitor maintenance and differentiation.
uncovered a novel biological role for CUL4A (show CUL4A Antibodies)-DDB1-CDT2 E3 ligase that regulates molecular circadian behaviors via promoting ubiquitination-dependent degradation of CRY1 (show CRY1 Antibodies)
UCH-L1 disrupts a complex between the DDB1-CUL4 ubiquitin ligase complex.
In a constructive process, pM27 recruits DDB1 to exploit ubiquitin ligase (show RNF123 Antibodies) complexes catalyzing the obstruction of the STAT2 (show STAT2 Antibodies)-dependent antiviral state of cells to permit viral replication.
Hepatocyte-specific deletion of DDB1 induces liver regeneration and tumorigenesis.
These results indicate that DDB1 plays an essential role in maintaining viability and genomic integrity of dividing cells.
DDB1 plays an important role in development by controlling levels of cell cycle regulators and thereby maintaining genomic stability.
Caenorhabditis elegans DDB-1 is required for the degradation of CDT-1 during S phase. DDB-1 interacts specifically with CUL-4 but not with other C. elegans cullins.
Data show that SKN-1 protein levels, nuclear accumulation, and activity are repressed by the WD40 repeat protein WDR-23, which interacts with the CUL-4/DDB-1 ubiquitin ligase to presumably target the transcription factor for proteasomal degradation.
The protein encoded by this gene is the large subunit (p127) of the heterodimeric DNA damage-binding (DDB) complex while another protein (p48) forms the small subunit. This protein complex functions in nucleotide-excision repair and binds to DNA following UV damage. Defective activity of this complex causes the repair defect in patients with xeroderma pigmentosum complementation group E (XPE) - an autosomal recessive disorder characterized by photosensitivity and early onset of carcinomas. However, it remains for mutation analysis to demonstrate whether the defect in XPE patients is in this gene or the gene encoding the small subunit. In addition, Best vitelliform mascular dystrophy is mapped to the same region as this gene on 11q, but no sequence alternations of this gene are demonstrated in Best disease patients. The protein encoded by this gene also functions as an adaptor molecule for the cullin 4 (CUL4) ubiquitin E3 ligase complex by facilitating the binding of substrates to this complex and the ubiquitination of proteins.
DDB p127 subunit
, DNA damage-binding protein 1
, DNA damage-binding protein a
, HBV X-associated protein 1
, UV-DDB 1
, UV-damaged DNA-binding factor
, UV-damaged DNA-binding protein 1
, XPE-binding factor
, xeroderma pigmentosum group E-complementing protein
, damage-specific DNA-binding protein 1
, damage-specific DNA binding protein 1, 127kDa
, DNA damage-binding protein 1-like
, DNA repair protein
, damage-specific DNA-binding protein, DNA repair
, damaged-DNA recognition protein 1
, damage specific DNA binding protein 1