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TRDMT1 encodes a protein responsible for the methylation of aspartic acid transfer RNA, specifically at the cytosine-38 residue in the anticodon loop. Additionally we are shipping tRNA Aspartic Acid Methyltransferase 1 Antibodies (150) and tRNA Aspartic Acid Methyltransferase 1 Proteins (10) and many more products for this protein.
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Data suggest that, upon HIV-1 infection, DNMT2 is re-localized from the nucleus to cytoplasmic stress granules where DNMT2 methylates HIV-1 messenger RNA; this methylation increases the stability of the HIV-1 RNA genome and up-regulates virus replication; thus, DNMT2 appears to facilitate HIV-1 infection.
The strong effect of some of the somatic cancer mutations on DNMT2 activity suggests that these mutations have a functional role in tumorigenesis.
DNMT1, DNMT2 and DNMT3A may play important roles in gastric cancer carcinogenesis.
Mapped is the tRNA binding site of DNMT2 by systematically mutating surface-exposed lysine and arginine residues to alanine and studying the tRNA methylation activity and binding of the corresponding variants.
the role of Dnmt2 in stress granules could represent a primitive cellular defense mechanism against viral infection.
The expression of DNMT1, DNMT2, DNMT3A and DNMT3B in pediatric acute lymphoblastic leukemia patients, was investigated.
Hepatitis B virus-induced overexpression of DNMTs leads to viral DNA methylation and decreased viral gene expression and also leads to methylation of host CpG islands.
identification of residual DNA-(cytosine-C5) methyltransferase activity
cDNA microarray analysis identified several genes involved in DNA methylation, such as DNMT2 and DNMT3a that were more highly expressed in LNCaP-r (an androgen sensitive prostate cancer cell line).
genetic and biochemical approach revealed that DNMT2 did not methylate DNA but instead methylated aspartic acid transfer RNA (tRNA(Asp)) and that DNMT2 specifically methylated cytosine 38 in the anticodon loop
An association study of 45 folate-related genes in spina bifida: Involvement of tRNA aspartic acid methyltransferase 1 (TRDMT1)
Dnmt2 may promote lifespan in the control conditions and survival during stress conditions in mouse fibroblasts.
Dnmt2 plays an unexpected role for regulation of cardiac growth by modulating activity of the P-TEFb complex.
Treatment of aged mice and their derived macrophages with methyltransferase inhibitor (2)-epigallocatechin-3-gallate (EGCG) or specific DNA methyltransferase 2 (DNMT2) siRNA restored the expression of Atg5 and LC3 in vivo and in vitro.
Dnmt2 plays an important role in haematopoiesis and define a novel function of C38 tRNA methylation in the discrimination of near-cognate codons, thereby ensuring accurate polypeptide synthesis.
these findings uncover a novel function of Dnmt2 in RNA-mediated epigenetic heredity
Dnmt2-dependent methylomes lack defined DNA methylation patterns.
Steady-state levels of unmethylated tRNAs were substantially reduced, and loss of Dnmt2 and NSun2 was further associated with reduced rates of overall protein synthesis.
This gene encodes a protein responsible for the methylation of aspartic acid transfer RNA, specifically at the cytosine-38 residue in the anticodon loop. This enzyme also possesses residual DNA-(cytosine-C5) methyltransferase activity. While similar in sequence and structure to DNA cytosine methyltransferases, this gene is distinct and highly conserved in its function among taxa.
tRNA aspartic acid methyltransferase 1
, DNA (cytosine-5)-methyltransferase-like protein 2
, DNA MTase homolog HsaIIP
, DNA methyltransferase-2
, tRNA (cytosine(38)-C(5))-methyltransferase
, tRNA (cytosine-5-)-methyltransferase
, DNA MTase homolog MmuIIP
, DNA methyltransferase 2
, DNA methyltransferase homolog MmuIIP
, DNA (cytosine-5-)-methyltransferase 2