Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase
about
Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnoverUnique misinsertion specificity of poliota may decrease the mutagenic potential of deaminated cytosinesSMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repairMutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylaseHuman APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanismsRepair activity of base and nucleotide excision repair enzymes for guanine lesions induced by nitrosative stress.Human cytomegalovirus uracil DNA glycosylase associates with ppUL44 and accelerates the accumulation of viral DNA.The current state of eukaryotic DNA base damage and repairMismatch Repair in Methylated DNA: STRUCTURE AND ACTIVITY OF THE MISMATCH-SPECIFIC THYMINE GLYCOSYLASE DOMAIN OF METHYL-CpG-BINDING PROTEIN MBD4The main role of human thymine-DNA glycosylase is removal of thymine produced by deamination of 5-methylcytosine and not removal of ethenocytosineBCR-ABL1 kinase inhibits uracil DNA glycosylase UNG2 to enhance oxidative DNA damage and stimulate genomic instability.Mimicking damaged DNA with a small molecule inhibitor of human UNG2.Regulatory mechanisms of RNA function: emerging roles of DNA repair enzymes.C --> T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylasesUracil excision by endogenous SMUG1 glycosylase promotes efficient Ig class switching and impacts on A:T substitutions during somatic mutationGermline ablation of SMUG1 DNA glycosylase causes loss of 5-hydroxymethyluracil- and UNG-backup uracil-excision activities and increases cancer predisposition of Ung-/-Msh2-/- mice.Human DNA polymerase-eta, an A-T mutator in somatic hypermutation of rearranged immunoglobulin genes, is a reverse transcriptase.Increased postischemic brain injury in mice deficient in uracil-DNA glycosylase.Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) deficiency is linked to aggressive breast cancer and predicts response to adjuvant therapy.B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil.An interplay of the base excision repair and mismatch repair pathways in active DNA demethylation.Uracil in DNA and its processing by different DNA glycosylasesEffect of the thymidylate synthase inhibitors on dUTP and TTP pool levels and the activities of DNA repair glycosylases on uracil and 5-fluorouracil in DNA.The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs.Phylogenomic analysis of the uracil-DNA glycosylase superfamilyClass-switch recombination: after the dawn of AID.Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteinsOn the molecular mechanism of somatic hypermutation of rearranged immunoglobulin genes.UNG shapes the specificity of AID-induced somatic hypermutation.Somatic Genomics and Clinical Features of Lung Adenocarcinoma: A Retrospective Study.Evaluation of molecular models for the affinity maturation of antibodies: roles of cytosine deamination by AID and DNA repairNon-canonical uracil processing in DNA gives rise to double-strand breaks and deletions: relevance to class switch recombinationMonitoring eukaryotic and bacterial UDG repair activity with DNA-multifluorophore sensorsOrigin of endogenous DNA abasic sites in Saccharomyces cerevisiae5-hydroxymethylcytosine marks regions with reduced mutation frequency in human DNAMechanisms of base selection by human single-stranded selective monofunctional uracil-DNA glycosylaseSteady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity.DNA base repair--recognition and initiation of catalysis.
P2860
Q24291615-9728AC69-6C5C-41C1-BAA6-FA76906DA28DQ24534803-E047E55B-4867-4607-A0EC-A0AC0A88BA07Q24535948-9FAD306E-02FD-4D30-AC2E-DDAC1BF55E51Q24541386-63143BE2-9479-4E84-9111-3EBA049F6F0FQ24563901-19215182-A3A7-4F3B-BE61-296E62207974Q24655541-E7AC2F5E-629A-4F42-8BD3-C769F36C6718Q24672089-BF6218B8-B1B6-4EB5-9C60-91922036AC18Q24797132-15ECFF5E-4714-42AA-80FF-F86FAF37B74EQ24813107-C79380EA-9045-4E52-B277-8A8C78C1C1C1Q26777671-51C71CE1-52AB-46E3-B8A4-7D8E23921853Q27640047-C46369E6-82F8-4DF4-913B-9CDAA6F19DFFQ28218523-F6B56E38-9416-4112-9FBD-59BAE2E92FC0Q30537656-28893D2A-5CFB-4EE1-9C3C-80401B8A8F03Q33261442-3B3D3FE0-DB1B-4929-867E-3202D382DAFFQ33749402-2D4D7176-ADB7-463C-A479-140567F91200Q33854159-4461BA7B-713F-44A2-ABDB-256E5C0445DBQ34154230-523A48C2-BCE8-4CEF-8C50-BC7C65D5F787Q34263614-DCCF0588-15E7-41DB-AE7A-5FCB88088793Q34310763-C5FEB016-C6EC-4F68-A855-358AE0674CF1Q34380700-EB0F0918-D3B0-484D-916A-FE8CDB3B7755Q34386345-E4764D02-401A-4B66-AC28-47202CD9ECECQ34427857-69C59A6A-7B1E-4817-B440-08295FF990B5Q34512288-DDCBD6DE-A3A6-4A11-AB06-4F7A92050151Q34600267-B8B43E5E-8393-4BB5-A2CA-E03062DF2859Q34782000-507D3185-8F9F-4078-9745-466D5CEB5C9EQ34980538-5B039CED-4574-4EB8-8148-9B5A2F680F9FQ35023107-6514527E-0199-4927-A37B-6B7F0FF75A2AQ35084277-B8657661-2B9A-43C9-9378-A816B7C3879AQ35781797-AE767D8E-9AE5-441E-A61F-AA58EEA868EEQ35953749-4D804AE0-F87E-4F81-B7AC-BEBA3348CC3BQ36118300-47E9B60F-FF4A-4798-A974-0BA1780A44C0Q36214274-13E2233C-A8CB-417E-8293-46E1A91B8A63Q36389685-BADD3D57-8175-41CF-BC04-62BC50A237DEQ36775503-E02C03B5-72B4-4B30-979C-34A7E4FF47E4Q36963330-8A2871A3-3B39-4FC6-87C6-81BC8896895CQ37056372-5A32B102-F7F8-4465-BACD-9D7492F05AE5Q37062667-D04260FF-6B6B-4385-B0AB-E09B721A7C64Q37257364-7CD40BBC-88C5-4487-A36A-1F7587779BAAQ37375102-000AABD6-D94A-4BB2-9E0D-A468C3EA1213Q37573870-B2816798-11CF-4393-B0A3-C0857EAB9A0F
P2860
Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@ast
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@en
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@nl
type
label
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@ast
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@en
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@nl
prefLabel
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@ast
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@en
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@nl
P2093
P2860
P3181
P356
P1433
P1476
Excision of deaminated cytosin ...... e SMUG1 uracil-DNA glycosylase
@en
P2093
D E Barnes
G L Verdine
K A Haushalter
P2860
P304
P3181
P356
10.1093/EMBOJ/20.15.4278
P407
P577
2001-08-01T00:00:00Z