XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage - Wikidata - wikimedia - TriplyDB

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

http://www.wikidata.org/entity/Q25257391

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Optimal function of the DNA repair enzyme TDP1 requires its phosphorylation by ATM and/or DNA-PK Base Excision Repair, a Pathway Regulated by Posttranslational Modifications ATM, ATR and DNA-PKcs expressions correlate to adverse clinical outcomes in epithelial ovarian cancers PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways X-ray repair cross complementing protein 1 in base excision repair.Differential recruitment of DNA Ligase I and III to DNA repair sites.XRCC1 and PCNA are loading platforms with distinct kinetic properties and different capacities to respond to multiple DNA lesions.Radiation cataracts: mechanisms involved in their long delayed occurrence but then rapid progression.Strategies for the evaluation of DNA damage and repair mechanisms in cancer.DNA repair genes polymorphisms and genetic susceptibility to Philadelphia-negative myeloproliferative neoplasms in a Portuguese population: The role of base excision repair genes polymorphisms.Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2).DNA-PKcs deficiency leads to persistence of oxidatively induced clustered DNA lesions in human tumor cells.Influence of XRCC1 Genetic Polymorphisms on Ionizing Radiation-Induced DNA Damage and Repair.Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition.Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells.HSP90 regulates DNA repair via the interaction between XRCC1 and DNA polymerase β Genetic polymorphisms in XRCC1 associated with radiation therapy in prostate cancer.Characterization of Halomonas sp. ZM3 isolated from the Zelazny Most post-flotation waste reservoir, with a special focus on its mobile DNA.The catalytic subunit of DNA-dependent protein kinase is required for cellular resistance to oxidative stress independent of DNA double-strand break repair.Choosing the right path: does DNA-PK help make the decision?Visual ModuleOrganizer: a graphical interface for the detection and comparative analysis of repeat DNA modules.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.Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of cysteines 93 and 310 XRCC1 and DNA polymerase beta in cellular protection against cytotoxic DNA single-strand breaks.Diversification of broad host range plasmids correlates with the presence of antibiotic resistance genes.A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification.DNA-PKcs and PARP1 Bind to Unresected Stalled DNA Replication Forks Where They Recruit XRCC1 to Mediate Repair Mutual regulation between DNA-PKcs and Snail1 leads to increased genomic instability and aggressive tumor characteristics.JWA regulates XRCC1 and functions as a novel base excision repair protein in oxidative-stress-induced DNA single-strand breaks.Mutagenesis is elevated in male germ cells obtained from DNA polymerase-beta heterozygous mice XRCC1 interacts with the p58 subunit of DNA Pol alpha-primase and may coordinate DNA repair and replication during S phase.Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining.TXNL1-XRCC1 pathway regulates cisplatin-induced cell death and contributes to resistance in human gastric cancer.E2F1 regulates the base excision repair gene XRCC1 and promotes DNA repair.p38 MAPK signaling and phosphorylations in the BRCT1 domain regulate XRCC1 recruitment to sites of DNA damage DNA-PK activity is associated with caspase-dependent myogenic differentiation.Near-infrared exposure changes cellular responses to ionizing radiation.Association of XRCC1 gene polymorphisms with chronic myeloid leukemia in the population of Andhra Pradesh, India.

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P2860

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

http://www.wikidata.org/entity/Q25257391

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@ast

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@en

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@nl

type

label

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@ast

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@en

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@nl

prefLabel

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@ast

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@en

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@nl

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Nucleic Acids Research

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XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage

@en

P2093

Adeline Martz

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

Anne Bresson

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

Catherine Spenlehauer

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

Gilbert de Murcia

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

Josiane Ménissier-de Murcia

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

Nicolas Lévy

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

P2860

Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure

The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4

Aprataxin, a novel protein that protects against genotoxic stress

XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage

Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor.

Autosomal recessive cerebellar ataxia with oculomotor apraxia (ataxia-telangiectasia-like syndrome) is linked to chromosome 9q34

XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions

Involvement of human polynucleotide kinase in double-strand break repair by non-homologous end joining

Ku recruits the XRCC4-ligase IV complex to DNA ends

Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein

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32-41

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scholarly article

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835434

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10.1093/NAR/GKJ409

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P433

1

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P478

34

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2006-01-05T00:00:00Z

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7374998

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16397295

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phosphorylation

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1325201

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