Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain.
about
MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNAGut Microbiota Imbalance and Base Excision Repair Dynamics in Colon CancerBase excision repair and cancerA Structural Hinge in Eukaryotic MutY Homologues Mediates Catalytic Activity and Rad9–Rad1–Hus1 Checkpoint Complex InteractionsBase-excision repair of oxidative DNA damageInsights into the role of Val45 and Gln182 of Escherichia coli MutY in DNA substrate binding and specificity.Molecular cloning and functional analysis of the MutY homolog of Deinococcus radiodurans.Electrochemistry of the [4Fe4S] Cluster in Base Excision Repair Proteins: Tuning the Redox Potential with DNA.Protein-DNA charge transport: redox activation of a DNA repair protein by guanine radical.Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition.Electron trap for DNA-bound repair enzymes: a strategy for DNA-mediated signaling.MUTYH Associated Polyposis (MAP).The carboxy-terminal domain of ROS1 is essential for 5-methylcytosine DNA glycosylase activityProfiling base excision repair glycosylases with synthesized transition state analogsPhysical and functional interactions between Escherichia coli MutY glycosylase and mismatch repair protein MutSRole of a MutY DNA glycosylase in combating oxidative DNA damage in Helicobacter pylori.Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays.DNA-mediated charge transport for DNA repair.In vitro ligation of oligodeoxynucleotides containing C8-oxidized purine lesions using bacteriophage T4 DNA ligase.Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutY.Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer.Adenine release is fast in MutY-catalyzed hydrolysis of G:A and 8-Oxo-G:A DNA mismatches.Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe4S4] Site in EndoIII and MutY.Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Dispensability of the [4Fe-4S] cluster in novel homologues of adenine glycosylase MutY.Structure-Activity Relationships Reveal Key Features of 8-Oxoguanine: A Mismatch Detection by the MutY Glycosylase.Mutants of the base excision repair glycosylase, endonuclease III: DNA charge transport as a first step in lesion detection.Physical and functional interactions between Escherichia coli MutY and endonuclease VIIIBase excision repair and the role of MUTYHEscherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates.Flipping duplex DNA inside out: a double base-flipping reaction mechanism by Escherichia coli MutY adenine glycosylase.Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase.A role for Myh1 in DNA repair after treatment with strand-breaking and crosslinking chemotherapeutic agents.Hybrid QM/MM Simulations of Enzyme-Catalyzed DNA Repair Reactions
P2860
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P2860
Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին 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
Efficient recognition of subst ...... equires the C-terminal domain.
@ast
Efficient recognition of subst ...... equires the C-terminal domain.
@en
Efficient recognition of subst ...... equires the C-terminal domain.
@nl
type
label
Efficient recognition of subst ...... equires the C-terminal domain.
@ast
Efficient recognition of subst ...... equires the C-terminal domain.
@en
Efficient recognition of subst ...... equires the C-terminal domain.
@nl
prefLabel
Efficient recognition of subst ...... equires the C-terminal domain.
@ast
Efficient recognition of subst ...... equires the C-terminal domain.
@en
Efficient recognition of subst ...... equires the C-terminal domain.
@nl
P2093
P2860
P356
P1476
Efficient recognition of subst ...... equires the C-terminal domain.
@en
P2093
A W Francis
M P Golinelli
N H Chmiel
P2860
P304
P356
10.1093/NAR/29.2.553
P407
P577
2001-01-01T00:00:00Z