Uracil in DNA and its processing by different DNA glycosylases - Wikidata - awgldk - TriplyDB

Uracil in DNA and its processing by different DNA glycosylases

Uracil in DNA and its processing by different DNA glycosylases

http://www.wikidata.org/entity/Q34600267

about

Molecular mechanisms of the whole DNA repair system: a comparison of bacterial and eukaryotic systems Overview of base excision repair biochemistry Base excision repair and cancer Uracil-containing DNA in Drosophila: stability, stage-specific accumulation, and developmental involvement Structural and biophysical analysis of interactions between cod and human uracil-DNAN-glycosylase (UNG) and UNG inhibitor (Ugi)Structure and enzymatic mechanism of a moonlighting dUTPase Hypermutation in human cancer genomes: footprints and mechanisms Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition Molecular characterization of Plasmodium falciparum uracil-DNA glycosylase and its potential as a new anti-malarial drug target BCR-ABL1 kinase inhibits uracil DNA glycosylase UNG2 to enhance oxidative DNA damage and stimulate genomic instability.Targets of somatic hypermutation within immunoglobulin light chain genes in zebrafish.Differential control of dNTP biosynthesis and genome integrity maintenance by the dUTPase superfamily enzymes.Human base excision repair creates a bias toward -1 frameshift mutations Uracil-DNA glycosylase is involved in DNA demethylation and required for embryonic development in the zebrafish embryo Uracil excision by endogenous SMUG1 glycosylase promotes efficient Ig class switching and impacts on A:T substitutions during somatic mutation Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) deficiency is linked to aggressive breast cancer and predicts response to adjuvant therapy.VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase.Reactive species and DNA damage in chronic inflammation: reconciling chemical mechanisms and biological fates.Deoxyinosine repair in nuclear extracts of human cells.UNG shapes the specificity of AID-induced somatic hypermutation.Whole-genome sequencing reveals activation-induced cytidine deaminase signatures during indolent chronic lymphocytic leukaemia evolution Detection of uracil within DNA using a sensitive labeling method for in vitro and cellular applications.Non-canonical uracil processing in DNA gives rise to double-strand breaks and deletions: relevance to class switch recombination Should autism be considered a canary bird telling that Homo sapiens may be on its way to extinction?Plant mitochondria possess a short-patch base excision DNA repair pathway.Life without dUTPase.Single nucleotide polymorphisms in uracil-processing genes, intake of one-carbon nutrients and breast cancer risk DNA base repair--recognition and initiation of catalysis.Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.AID: a riddle wrapped in a mystery inside an enigma.Recognition of damaged DNA: structure and dynamic markers.MBD4 Facilitates Immunoglobulin Class Switch Recombination.Base excision DNA repair in the embryonic development of the sea urchin, Strongylocentrotus intermedius.Expanding the DNA alphabet in the fruit fly: uracil enrichment in genomic DNA.A novel class of chemicals that react with abasic sites in DNA and specifically kill B cell cancers.Pms2 and uracil-DNA glycosylases act jointly in the mismatch repair pathway to generate Ig gene mutations at A-T base pairs.Non-coding cancer driver candidates identified with a sample- and position-specific model of the somatic mutation rate.Deep sequencing of HIV-1 reverse transcripts reveals the multifaceted antiviral functions of APOBEC3G.Differential role of base excision repair proteins in mediating cisplatin cytotoxicity.

P2860

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P2860

Uracil in DNA and its processing by different DNA glycosylases

http://www.wikidata.org/entity/Q34600267

description

2009 nî lūn-bûn

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2009 թուականի Մարտին հրատարակուած գիտական յօդուած

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2009 թվականի մարտին հրատարակված գիտական հոդված

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2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

name

Uracil in DNA and its processing by different DNA glycosylases

@ast

Uracil in DNA and its processing by different DNA glycosylases

@en

Uracil in DNA and its processing by different DNA glycosylases

@nl

type

label

Uracil in DNA and its processing by different DNA glycosylases

@ast

Uracil in DNA and its processing by different DNA glycosylases

@en

Uracil in DNA and its processing by different DNA glycosylases

@nl

prefLabel

Uracil in DNA and its processing by different DNA glycosylases

@ast

Uracil in DNA and its processing by different DNA glycosylases

@en

Uracil in DNA and its processing by different DNA glycosylases

@nl

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Philosophical Transactions of the Royal Society B

P1476

Uracil in DNA and its processing by different DNA glycosylases

@en

P2093

Berit Doseth

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

Bodil Kavli

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

Henrik Sahlin Pettersen

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

Lars Hagen

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

Mansour Akbari

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

Mirta M L Sousa

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

Torkild Visnes

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

P2860

Identification and characterization of a family of mammalian methyl-CpG binding proteins

Instability and decay of the primary structure of DNA

hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup

Post-replicative base excision repair in replication foci

Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms

The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites

Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase

Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells

Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA.

P304

563-568

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scholarly article

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10.1098/RSTB.2008.0186

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P407

P433

1517

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P478

364

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P50

Hans Einar Krokan

P577

2009-03-01T00:00:00Z

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23472581

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19008197

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2660913

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