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These results suggest that different DDB1-CUL4 associated factors play distinct roles in human lung adenocarcinoma development.
The DDB1 is acetylated and acetylation promotes DDB1 binding to CUL4.
Results revealed a function independent of its transcriptional activity, as TTF-1 was found to interact with DDB1 and block its binding to CHK1, which in turn attenuated ubiquitylation and subsequent degradation of CHK1.
SIRT7 inhibits TR4 degradation by deacetylation of DDB1.
the c-Abl non-receptor kinase phosphorylates DDB1 at residue Tyr-316 to recruit a small regulatory protein, DDA1, leading to increased substrate ubiquitination
knockdown of DCAF7 reduced the degradation of DNA ligase I in response to inhibition of proliferation and replacement of ubiquitylated lysine residues reduced the in vitro ubiquitylation of DNA ligase I by Cul4-DDB1 and DCAF7. In contrast, a different E3 ubiquitin ligase regulates FEN-1 turnover.
This study presents the crystal structure of the DDB1-DCAF1-HIV-1-Vpr-uracil-DNA glycosylase (cyclin U) complex.
Our data are consistent with the idea that the CUL4A/B-DDB1-CRBN complex catalyses the polyubiquitination and thus controls the degradation of CLC-1 channels.
These results revealed a novel role of DDB in H3K56Ac deacetylation during early step of NER 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 cooperate to repress Bcl-2 transcription. DDB2 recognizes and binds to the Bcl-2 P1 promoter, and HDAC1 is recruited through the DDB1 subunit associated with DDB2 to deacetylate histone H3K9.
The study presents the crystal structure of human CRBN bound to DDB1 and the drug lenalidomide.
CUL4A-DDB1-Rbx1 E3 ligase controls the quality of the PTS2 receptor Pex7p.
structures of the DDB1-CRBN complex bound to thalidomide, lenalidomide and pomalidomide
In the three intrinsically IMiD-resistant cell lines that clearly express detectable levels of cereblon, the absence of CRBN and DDB1 mutations suggest that potential cereblon-independent mechanisms of resistance exist
UV-DDB examines sites on DNA in discrete steps before forming long-lived, nonmotile UV-DDB dimers (DDB1-DDB2)2 at sites of damage.
p73 interacts with the CDL4A complex by binding directly to DDB1. The CDL4A complex is able to monoubiquitylate p73, negatively affecting its transcriptional function.
As a molecular adaptor, Vpr enhanced the interaction between TERT and the VPRBP substrate receptor of the DYRK2-associated EDD-DDB1-VPRBP E3 ligase complex, resulting in increased ubiquitination of TERT.
Data indicate that Dyrk2 phosphorylates TERT protein, which is then associated with the EDD-DDB1-VprBP E3 ligase complex for subsequent ubiquitin-mediated TERT protein degradation.
Our findings suggest that DDB1 is a cellular substrate of NS3/4A required for Hepatitis c viurs replication.
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-DDB1-CDT2 E3 ligase that regulates molecular circadian behaviors via promoting ubiquitination-dependent degradation of CRY1
UCH-L1 disrupts a complex between the DDB1-CUL4 ubiquitin ligase complex.
In a constructive process, pM27 recruits DDB1 to exploit ubiquitin ligase complexes catalyzing the obstruction of the STAT2-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