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Results demonstrated that MBD4 was downregulated, which lead to the overexpression and promoter hypomethylation of CD70 (show CD70 Proteins) in CD4 (show CD4 Proteins)+ T cells from patients from systemic lupus erythematosus (SLE). This study preliminarily revealed the role and mechanism of MBD4 in the pathogenesis of SLE.
a novel molecular mechanism by which MBD4 inhibits GITR (show TNFRSF18 Proteins) expression in a DNMT1 (show DNMT1 Proteins)-dependent manner
these data suggest that MBD4 inactivation may contribute to tumorigenesis, acting as a modifier of mismatch repair-deficient cancer phenotype.
MBD4 rs3138373 A>G and rs2005618 T>C single nucleotide polymorphisms were not associated with esophageal squamous cell carcinoma (ESCC) risk. rs3138355 GG genotype was associated with a decreased risk of ESCC among male patients and the elderly.
The ability of MBD4 to directly interact with and recruit USP7 (show USP7 Proteins) to chromocenters implicates it as an additional factor that can potentially regulate Dnmt1 (show DNMT1 Proteins) activity during cell proliferation.
Interaction between DNMT1 (show DNMT1 Proteins) and MBD4 is involved in controlling gene expression and responding to oxidative stress.
ERCC4 (show ERCC4 Proteins) rs1800124 and MBD4 rs10342 non-synonymous single nucleotide polymorphism variants were associated with DNA repair capacity.
the crystal structure of MBD4 bound to 5-hydroxymethylcytosine further demonstrates that MBDMBD4 is able to recognize a wide range of 5-methylcytosine modifications
MBD4 Glu346Lys polymorphism is associated with the risk of cervical cancer in a Chinese population.
Crystal structures of human MBD4(catalytic domain) reveal that MBD4 uses a base flipping mechanism to specifically recognize thymine and 5-hydroxymethyluracil.
Mbd4-/- mice displayed more severe symptoms, decreased survival, and a greater tumor burden than wild-type (WT) controls.
Mbd4 is a component of mismatch repair-directed DNA end processing.
A variant Mbd4 transcript spanning exons 1,6-8 is expressed in Mbd4 deficient B cells.
studies indicate that, although inactivation of Mbd4 does not by itself cause cancer predisposition in mice, it can alter the mutation spectrum in cancer cells and modify the cancer predisposition phenotype
structure and activity of the mismatch-specific thymine glycosylase domain of MBD4
Mbd4 glycosylase does not significantly contribute to mechanisms of antibody diversification, as analyzed by an in vitro switch assay and by in vivo immunizations in Mbd4-/- knockout mice.
results establish a novel functional role for MBD4 in the cellular response to DNA damage and may have implications for its role in suppressing neoplasia
MED1 has a role in cell cycle arrest and apoptosis induced by DNA damage
in the context of MMR (show MRC1 Proteins) deficiency, additional loss of Mbd4 does not alter spontaneous mutation frequency at the endogenous Dlb-1b locus, nor does it modify tumour onset, tumour spectrum or MSI (show EBP Proteins)
The protein encoded by this gene is a member of a family of nuclear proteins related by the presence of a methyl-CpG binding domain (MBD). These proteins are capable of binding specifically to methylated DNA, and some members can also repress transcription from methylated gene promoters. This protein contains an MBD domain at the N-terminus that functions both in binding to methylated DNA and in protein interactions and a C-terminal mismatch-specific glycosylase domain that is involved in DNA repair. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
, G/5-fluorouracil mismatch glycosylase with biphasic kinetics
, G/T mismatch glycosylase
, G/U mismatch glycosylase
, methyl-CpG-binding domain protein 4
, methyl-CpG-binding endonuclease 1
, methyl-CpG-binding protein MBD4
, mismatch-specific DNA N-glycosylase
, putative methyl-CpG binding protein