Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
thymidylate synthase inhibition leads to UDG-dependent cell death
malfunction
-
enzyme deficiency enhances translesion polymerase recruitment and inhibits S-S synapse formation during class switch recombination
malfunction
-
enzyme inhibition enhances APOBEC3G-induced hypermutation of hepatitis B virus nucleocapsid-associated DNA
malfunction
-
enzyme knockdown in the zebrafish embryo increases global DNA methylation level, inhibits transcription, and causes embryonic lethality
malfunction
-
inhibition of endogenous isoform UNG2 does not affect reverse transcription, permits integration of uracilated viruses but does not rescue viral protein expression
malfunction
-
human immunodeficiency virus-1 infectivity and replication in peripheral blood mononuclear cells and monocyte-derived macrophages as well as the efficiency of the viral DNA synthesis are significantly reduced when viruses are produced from cells depleted of endogenous enzyme
metabolism
UDG encoded by the At3g18 630 locus might be the first enzyme of the mitochondrial short-patch base excision repair pathway in Arabidopsis thaliana, overview
metabolism
-
UNG2 is a major determinant of the uracil base excision repair pathway, that undergoes rapid proteasome-dependent degradation following HIV-1 infection
metabolism
uracil DNA glycosylase initiates the uracil excision repair pathway
metabolism
the enzyme removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway
metabolism
-
the enzyme removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway
-
physiological function
-
base excision repair is required to maintain genome stability as a means to counter the accumulation of unusual bases and to protect from the loss of DNA bases
physiological function
-
involvement but dispensability of UNG in DNA cleavage in class switch recombination
physiological function
-
UdgB from Mycobacterium smegmatis protects this organism against mutagenesis associated with deamination of both cytosine and adenine. Together with Ung-type uracil glycosylase, UdgB also helps attenuate the cytotoxicity of the antimicrobial agent 5-fluorouracil
physiological function
-
UNG-1 contributes to repair of ionizing radiation-induced DNA base damage in vivo
physiological function
-
uracil DNA glycosylase 2 negatively regulates HIV-1 LTR transcription, and shows antiviral activity at the transcriptional level requiring the integrity of its catalytic domain, depletion of endogenous UNG2 promotes Tat-mediated LTR transcription, molecular mechanisms, overview
physiological function
the enzyme is essential for maintaining genomic integrity
physiological function
-
hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA
physiological function
-
hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA
physiological function
-
hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA
physiological function
-
hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA
physiological function
-
hyperthermophiles exist in conditions which present an increased threat to the informational integrity of their DNA, particularly by hydrolytic damage. One of the most common hydrolytic damage events is the deamination of cytosine to uracil. The enzyme excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Thus it restores and protects the template function of DNA
physiological function
-
isoform UNG2 initiates degradation of HIV-1 cDNA containing misincorporated dUTP and prevents viral integration
physiological function
-
one of the most important base excision repair enzymes responsible for the exclusion of uracil from cellular DNA
physiological function
-
the DNA base excision repair enzyme is essential for class switch recombination
physiological function
-
the noncanonical function of the enzyme regulates the steps after activation-induced cytidine deaminase-induced DNA cleavage: errorprone repair suppression in S region somatic hypermutation and end-joining promotion in class switch recombination
physiological function
-
uracil DNA glycosylase is a base excision repair enzyme that removes uracil residues from DNA following dUTP misincorporations or cytosine deaminations. The enzyme is also essential for class-switch recombination and somatic hypermutation
physiological function
-
uracil-DNA glycosylase is involved in postfertilization genomic DNA demethylation and zygotic gene transcription and is required for normal embryonic development in the zebrafish embryo. Enzyme-mediated DNA demethylation facilitates histone modifications of chromatin in zebrafish embryos
physiological function
-
isoform UNG1 supports antibody class switching and repairs genomic uracil in the cell nucleus
physiological function
isoform UNG1 supports antibody class switching and repairs genomic uracil in the cell nucleus
physiological function
-
the DNA repair enzyme excises uracil from U/A and U/G base pairs and initiates the process of uracil base excision repair
physiological function
-
the enzyme interacts with the p32 subunit of the replication protein A complex to modulate human immunodeficiency virus-1 reverse transcription for optimal virus dissemination
physiological function
the enzyme is involved in base excision repair of uracil
physiological function
-
the enzyme regulates transcription of a series of virulence factor genes involved in microsclerotial formation and pathogenesis of Verticilliumxa0dahliae
physiological function
-
the enzyme is involved in base excision repair of uracil
-