Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer.
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Base excision repair and cancerA Structural Hinge in Eukaryotic MutY Homologues Mediates Catalytic Activity and Rad9–Rad1–Hus1 Checkpoint Complex InteractionsAdenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancerFunctional Complementation Assay for 47 MUTYH Variants in a MutY-Disrupted Escherichia coli Strain.Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition.Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays.Surprising repair activities of nonpolar analogs of 8-oxoG expose features of recognition and catalysis by base excision repair glycosylases.Cancer-associated variants and a common polymorphism of MUTYH exhibit reduced repair of oxidative DNA damage using a GFP-based assay in mammalian cells.Understanding the role of the Q338H MUTYH variant in oxidative damage repairSteady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity.Distinct functional consequences of MUTYH variants associated with colorectal cancer: Damaged DNA affinity, glycosylase activity and interaction with PCNA and Hus1.DNA glycosylase encoded by MUTYH functions as a molecular switch for programmed cell death under oxidative stress to suppress tumorigenesis.Genetic instability in lymphoblastoid cell lines expressing biallelic and monoallelic variants in the human MUTYH gene.Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Impaired suppressive activities of human MUTYH variant proteins against oxidative mutagenesis.Loss of MUTYH function in human cells leads to accumulation of oxidative damage and genetic instability.Dispensability of the [4Fe-4S] cluster in novel homologues of adenine glycosylase MutY.A zinc linchpin motif in the MUTYH glycosylase interdomain connector is required for efficient repair of DNA damage.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.MUTYH-associated polyposis (MAP), the syndrome implicating base excision repair in inherited predisposition to colorectal tumors.Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanineDefective MUTYH substrate processingA human MUTYH variant linking colonic polyposis to redox degradation of the [4Fe4S] cluster
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Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on December 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Adenine removal activity and b ...... ciated with colorectal cancer.
@en
Adenine removal activity and b ...... ciated with colorectal cancer.
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type
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Adenine removal activity and b ...... ciated with colorectal cancer.
@en
Adenine removal activity and b ...... ciated with colorectal cancer.
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prefLabel
Adenine removal activity and b ...... ciated with colorectal cancer.
@en
Adenine removal activity and b ...... ciated with colorectal cancer.
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P2860
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Adenine removal activity and b ...... ciated with colorectal cancer.
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Alison L Livingston
Megan K Brinkmeyer
Sheila S David
Sucharita Kundu
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P304
P356
10.1016/J.DNAREP.2009.09.009
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2009-12-01T00:00:00Z