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Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

http://www.wikidata.org/entity/Q37459997

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The Response to Oxidative DNA Damage in Neurons: Mechanisms and Disease Continuous and periodic expansion of CAG repeats in Huntington's disease R6/1 mice APE1 incision activity at abasic sites in tandem repeat sequences Role of oxidative DNA damage in mitochondrial dysfunction and Huntington's disease pathogenesis Instability of CTG repeats is governed by the position of a DNA base lesion through base excision repair Stoichiometry of base excision repair proteins correlates with increased somatic CAG instability in striatum over cerebellum in Huntington's disease transgenic mice HMGB1: roles in base excision repair and related function.Modulation of trinucleotide repeat instability by DNA polymerase β polymorphic variant R137Q.Phosphate steering by Flap Endonuclease 1 promotes 5'-flap specificity and incision to prevent genome instability.Topoisomerase 1 and single-strand break repair modulate transcription-induced CAG repeat contraction in human cells.Functional regulation of FEN1 nuclease and its link to cancer HMGB1 in health and disease.A 5', 8-cyclo-2'-deoxypurine lesion induces trinucleotide repeat deletion via a unique lesion bypass by DNA polymerase β Mismatch repair genes Mlh1 and Mlh3 modify CAG instability in Huntington's disease mice: genome-wide and candidate approaches Incidence and persistence of 8-oxo-7,8-dihydroguanine within a hairpin intermediate exacerbates a toxic oxidation cycle associated with trinucleotide repeat expansion Base excision repair of chemotherapeutically-induced alkylated DNA damage predominantly causes contractions of expanded GAA repeats associated with Friedreich's ataxia.Mechanisms of trinucleotide repeat instability during human development DNA pol λ's extraordinary ability to stabilize misaligned DNA.New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Heterozygosity for a hypomorphic Polβ mutation reduces the expansion frequency in a mouse model of the Fragile X-related disorders.Premutation huntingtin allele adopts a non-B conformation and contains a hot spot for DNA damage.RECQ1 interacts with FEN-1 and promotes binding of FEN-1 to telomeric chromatin.Trinucleotide repeat DNA alters structure to minimize the thermodynamic impact of 8-oxo-7,8-dihydroguanine.Repeat instability during DNA repair: Insights from model systems AP endonuclease 1 prevents trinucleotide repeat expansion via a novel mechanism during base excision repair.Instability of (CTG)n•(CAG)n trinucleotide repeats and DNA synthesis DNA base excision repair: a mechanism of trinucleotide repeat expansion.Base excision repair and design of small molecule inhibitors of human DNA polymerase β.Base excision repair: contribution to tumorigenesis and target in anticancer treatment paradigms The nucleotide sequence, DNA damage location, and protein stoichiometry influence the base excision repair outcome at CAG/CTG repeats Rate-determining Step of Flap Endonuclease 1 (FEN1) Reflects a Kinetic Bias against Long Flaps and Trinucleotide Repeat Sequences.Microhomology-mediated DNA strand annealing and elongation by human DNA polymerases λ and β on normal and repetitive DNA sequences.Msh2-Msh3 interferes with Okazaki fragment processing to promote trinucleotide repeat expansions.Base excision repair in physiology and pathology of the central nervous system Trinucleotide repeat deletion via a unique hairpin bypass by DNA polymerase β and alternate flap cleavage by flap endonuclease 1.Trinucleotide repeat expansions catalyzed by human cell-free extracts Flap endonuclease 1.Oxidized dNTPs and the OGG1 and MUTYH DNA glycosylases combine to induce CAG/CTG repeat instability.Crosstalk between MSH2-MSH3 and polβ promotes trinucleotide repeat expansion during base excision repair.Abnormal base excision repair at trinucleotide repeats associated with diseases: a tissue-selective mechanism.

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Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

http://www.wikidata.org/entity/Q37459997

description

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 11 August 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

Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

@en

Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

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type

label

Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

@en

Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

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prefLabel

Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

@en

Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion.

@nl

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JBC.M109.050286

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Journal of Biological Chemistry

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Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion

@en

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Cynthia T McMurray

http://www.w3.org/2001/XMLSchema#string

Esther W Hou

http://www.w3.org/2001/XMLSchema#string

Julie K Horton

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Rajendra Prasad

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William A Beard

http://www.w3.org/2001/XMLSchema#string

Yuan Liu

http://www.w3.org/2001/XMLSchema#string

P2860

Free radicals and antioxidants in normal physiological functions and human disease

Functional and physical interaction between WRN helicase and human replication protein A

Werner syndrome protein interacts with human flap endonuclease 1 and stimulates its cleavage activity

HMGB1 is a cofactor in mammalian base excision repair

The characterization of a mammalian DNA structure-specific endonuclease

Assignment of the gene for human DNA polymerase alpha to the X chromosome

Advances in mechanisms of genetic instability related to hereditary neurological diseases.

Inhibition of FEN-1 processing by DNA secondary structure at trinucleotide repeats

Flap endonuclease 1: a central component of DNA metabolism

AP endonuclease-independent DNA base excision repair in human cells

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28352-28366

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scholarly article

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10.1074/JBC.M109.050286

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41

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Samuel H. Wilson

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2009-08-11T00:00:00Z

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19674974

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