Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase
about
Uracil-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.Active DNA demethylation in post-mitotic neurons: a reason for optimismSpecificity and catalytic mechanism in family 5 uracil DNA glycosylaseBCR-ABL1 kinase inhibits uracil DNA glycosylase UNG2 to enhance oxidative DNA damage and stimulate genomic instability.Recognition of oxidized thymine base on the single-stranded DNA by replication protein A.Regulatory mechanisms of RNA function: emerging roles of DNA repair enzymes.Epigenetic regulation of adult neural stem cells: implications for Alzheimer's disease.C --> T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylasesGermline ablation of SMUG1 DNA glycosylase causes loss of 5-hydroxymethyluracil- and UNG-backup uracil-excision activities and increases cancer predisposition of Ung-/-Msh2-/- mice.Vertebrate POLQ and POLbeta cooperate in base excision repair of oxidative DNA damage.Base excision repair, aging and health span.Mechanisms of base selection by human single-stranded selective monofunctional uracil-DNA glycosylaseRole of Base Excision "Repair" Enzymes in Erasing Epigenetic Marks from DNAOxanine DNA glycosylase activities in mammalian systems.Mechanisms of base selection by the Escherichia coli mispaired uracil glycosylase.Base excision repair and the role of MUTYHOpposite-base dependent excision of 5-formyluracil from DNA by hSMUG1.Pre-steady-state kinetic analysis of damage recognition by human single-strand selective monofunctional uracil-DNA glycosylase SMUG1.Identification of a prototypical single-stranded uracil DNA glycosylase from Listeria innocua.
P2860
Q24672089-A0F69366-2FF6-407C-B925-DBCC177C89FEQ24797132-4BE7B4C4-B33C-4E94-A3C6-D3168502339DQ26829515-D4CAF0BD-695B-487F-9342-982683110DDEQ28770317-C21ABA03-D8C6-4F03-A054-3EBD64D3A8E2Q30537656-B3DE59C1-ACBB-4E56-8C47-357EB440520CQ33250054-D81D11DB-7DCD-4449-8D86-D360EAA77460Q33749402-E4DC1F4F-2CA8-4DB8-B767-54541120BA29Q33841944-2AE1B26A-7F21-428C-9B2D-5E4EDBF140A5Q33854159-9EA5807F-C6C6-4FDF-95CE-28A5A65496D9Q34263614-E9E1F6CC-FFD7-404D-A5AD-58E7B13396E0Q35792481-7AC18332-37FA-48B1-A9DE-BA1843806D1AQ36853499-9206AA8E-449F-455A-900E-343F3836A2F1Q37257364-9E3FEF06-483E-4103-8951-C660D1F9545AQ38921717-0023F884-9D71-43A6-A188-28C9B75F5341Q41957575-8FA12DBD-B86F-456B-A69B-76DB22B07723Q42182897-4C00FA3A-F959-458D-91FB-8993EE4EF5E8Q42230093-C3CDB898-DF62-444B-8C4E-27F8BEFF663EQ46051706-C46251EB-D03E-402E-9551-B637DD4ECBD4Q47756226-1848FC2A-9547-42A6-8EFA-A5A30F7AC0C3Q50883819-A14FBC54-42EA-4409-8725-49103513F01C
P2860
Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase
description
2004 nî lūn-bûn
@nan
2004 թուականին հրատարակուած գիտական յօդուած
@hyw
2004 թվականին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@ast
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@en
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@nl
type
label
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@ast
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@en
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@nl
prefLabel
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@ast
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@en
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@nl
P2093
P2860
P356
P1476
Mutational analysis of the dam ...... of human SMUG1 DNA glycosylase
@en
P2093
Eiji Ohmae
Hiroaki Terato
Hiroshi Ide
Katsuo Katayanagi
Mayumi Matsubara
Shunsuke Izumi
Tamon Tanaka
P2860
P304
P356
10.1093/NAR/GKH859
P407
P577
2004-01-01T00:00:00Z