Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA
about
Excision of 5-hydroxymethyluracil and 5-carboxylcytosine by the thymine DNA glycosylase domain: its structural basis and implications for active DNA demethylationActivity and crystal structure of human thymine DNA glycosylase mutant N140A with 5-carboxylcytosine DNA at low pHStructural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residuesRole of base excision repair in maintaining the genetic and epigenetic integrity of CpG sitesMBD4 and TDG: multifaceted DNA glycosylases with ever expanding biological rolesVariations in brain DNAThymine DNA glycosylase exhibits negligible affinity for nucleobases that it removes from DNAE2-mediated small ubiquitin-like modifier (SUMO) modification of thymine DNA glycosylase is efficient but not selective for the enzyme-product complex.Recent advances in the structural mechanisms of DNA glycosylasesThe effect of a G:T mispair on the dynamics of DNADifferential stabilities and sequence-dependent base pair opening dynamics of Watson-Crick base pairs with 5-hydroxymethylcytosine, 5-formylcytosine, or 5-carboxylcytosine.Lesion search and recognition by thymine DNA glycosylase revealed by single molecule imaging.Mechanisms of glycosylase induced genomic instabilitySelective excision of 5-carboxylcytosine by a thymine DNA glycosylase mutant.Divergent mechanisms for enzymatic excision of 5-formylcytosine and 5-carboxylcytosine from DNA.Structural Basis for Excision of 5-Formylcytosine by Thymine DNA Glycosylase.Structural and mutation studies of two DNA demethylation related glycosylases: MBD4 and TDG.Role of Base Excision "Repair" Enzymes in Erasing Epigenetic Marks from DNAAberrant repair initiated by mismatch-specific thymine-DNA glycosylases provides a mechanism for the mutational bias observed in CpG islands.How a mismatch repair enzyme balances the needs for efficient lesion processing and minimal action on undamaged DNA.Structure of a DNA glycosylase that unhooks interstrand cross-links.Dynamics of the excised base release in thymine DNA glycosylase during DNA repair process.Base-flipping dynamics from an intrahelical to an extrahelical state exerted by thymine DNA glycosylase during DNA repair process.Defining the impact of sumoylation on substrate binding and catalysis by thymine DNA glycosylase.
P2860
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P2860
Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Lesion processing by a repair ...... rant activity on undamaged DNA
@ast
Lesion processing by a repair ...... rant activity on undamaged DNA
@en
Lesion processing by a repair ...... rant activity on undamaged DNA
@en-gb
Lesion processing by a repair ...... rant activity on undamaged DNA
@nl
type
label
Lesion processing by a repair ...... rant activity on undamaged DNA
@ast
Lesion processing by a repair ...... rant activity on undamaged DNA
@en
Lesion processing by a repair ...... rant activity on undamaged DNA
@en-gb
Lesion processing by a repair ...... rant activity on undamaged DNA
@nl
prefLabel
Lesion processing by a repair ...... rant activity on undamaged DNA
@ast
Lesion processing by a repair ...... rant activity on undamaged DNA
@en
Lesion processing by a repair ...... rant activity on undamaged DNA
@en-gb
Lesion processing by a repair ...... rant activity on undamaged DNA
@nl
P2860
P50
P3181
P356
P1476
Lesion processing by a repair ...... rant activity on undamaged DNA
@en
P2093
Muhammad S Noon
P2860
P304
P3181
P356
10.1073/PNAS.1201010109
P407
P577
2012-05-09T00:00:00Z