Substrate recognition by Escherichia coli MutY using substrate analogs
about
Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsAtomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylaseStructure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidasesRecent progress in the biology, chemistry and structural biology of DNA glycosylases.Competitive inhibition of uracil DNA glycosylase by a modified nucleotide whose triphosphate is a substrate for DNA polymerase.Phosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity.Effects of polyamines on the thermal stability and formation kinetics of DNA duplexes with abnormal structureSer 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition.Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain.Profiling base excision repair glycosylases with synthesized transition state analogsCatalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays.NEIL1 binding to DNA containing 2'-fluorothymidine glycol stereoisomers and the effect of editingDNA repair glycosylases with a [4Fe-4S] cluster: a redox cofactor for DNA-mediated charge transport?Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutY.Distinct functional consequences of MUTYH variants associated with colorectal cancer: Damaged DNA affinity, glycosylase activity and interaction with PCNA and Hus1.Structural Basis for Excision of 5-Formylcytosine by Thymine DNA Glycosylase.Adenine release is fast in MutY-catalyzed hydrolysis of G:A and 8-Oxo-G:A DNA mismatches.A dimeric mechanism for contextual target recognition by MutY glycosylase.Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe4S4] Site in EndoIII and MutY.Structure-Activity Relationships Reveal Key Features of 8-Oxoguanine: A Mismatch Detection by the MutY Glycosylase.Chemical reagents for investigating the major groove of DNA.Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates.
P2860
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P2860
Substrate recognition by Escherichia coli MutY using substrate analogs
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Substrate recognition by Escherichia coli MutY using substrate analogs
@ast
Substrate recognition by Escherichia coli MutY using substrate analogs
@en
Substrate recognition by Escherichia coli MutY using substrate analogs
@nl
type
label
Substrate recognition by Escherichia coli MutY using substrate analogs
@ast
Substrate recognition by Escherichia coli MutY using substrate analogs
@en
Substrate recognition by Escherichia coli MutY using substrate analogs
@nl
prefLabel
Substrate recognition by Escherichia coli MutY using substrate analogs
@ast
Substrate recognition by Escherichia coli MutY using substrate analogs
@en
Substrate recognition by Escherichia coli MutY using substrate analogs
@nl
P2093
P2860
P356
P1476
Substrate recognition by Escherichia coli MutY using substrate analogs
@en
P2093
C L Chepanoske
H Sugiyama
S L Porello
T Fujiwara
P2860
P304
P356
10.1093/NAR/27.15.3197
P407
P577
1999-08-01T00:00:00Z