Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the Thr-2609 cluster upon DNA double strand break. - Wikidata - wikimedia - TriplyDB

Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the Thr-2609 cluster upon DNA double strand break.

Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the Thr-2609 cluster upon DNA double strand break.

http://www.wikidata.org/entity/Q53581072

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Hyperactivation of DNA-PK by double-strand break mimicking molecules disorganizes DNA damage response Phosphorylation: the molecular switch of double-strand break repair Regulation of DNA-dependent protein kinase by protein kinase CK2 in human glioblastoma cells The dynamics of Ku70/80 and DNA-PKcs at DSBs induced by ionizing radiation is dependent on the complexity of damage Essential role for DNA-PKcs in DNA double-strand break repair and apoptosis in ATM-deficient lymphocytes Ataxia telangiectasia mutated activation by transcription- and topoisomerase I-induced DNA double-strand breaks DNA damage response and prostate cancer: defects, regulation and therapeutic implications DNA-PK: a dynamic enzyme in a versatile DSB repair pathway Tyrosyl-DNA phosphodiesterase and the repair of 3'-phosphoglycolate-terminated DNA double-strand breaks.The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis TNKS1BP1 functions in DNA double-strand break repair though facilitating DNA-PKcs autophosphorylation dependent on PARP-1 MRNIP/C5orf45 Interacts with the MRN Complex and Contributes to the DNA Damage Response DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance Role of DNA-dependent protein kinase catalytic subunit in cancer development and treatment Targeting DNA-PKcs and ATM with miR-101 sensitizes tumors to radiation Establishment of a γ-H2AX foci-based assay to determine biological dose of radon to red bone marrow in rats ATM limits incorrect end utilization during non-homologous end joining of multiple chromosome breaks Identification of the DNA repair defects in a case of Dubowitz syndrome Functional intersection of ATM and DNA-dependent protein kinase catalytic subunit in coding end joining during V(D)J recombination PP6 regulatory subunit R1 is bidentate anchor for targeting protein phosphatase-6 to DNA-dependent protein kinase Improved ATM kinase inhibitor KU-60019 radiosensitizes glioma cells, compromises insulin, AKT and ERK prosurvival signaling, and inhibits migration and invasion DNA double-strand breaks induced by cavitational mechanical effects of ultrasound in cancer cell lines.Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks.Increased cancer risk of augmentation cystoplasty: possible role for hyperosmolal microenvironment on DNA damage recognition Radiation microbeams as spatial and temporal probes of subcellular and tissue response.Nonhomologous end joining: a good solution for bad ends A method for systematic mapping of protein lysine methylation identifies functions for HP1β in DNA damage response.The Ku-dependent non-homologous end-joining pathway contributes to low-dose radiation-stimulated cell survival.Non-homologous end joining: emerging themes and unanswered questions.DNA-PKcs deficiency leads to persistence of oxidatively induced clustered DNA lesions in human tumor cells.Genome-wide reinforcement of cohesin binding at pre-existing cohesin sites in response to ionizing radiation in human cells.miR-18a impairs DNA damage response through downregulation of ataxia telangiectasia mutated (ATM) kinase.More forks on the road to replication stress recovery Protein kinase CK2 localizes to sites of DNA double-strand break regulating the cellular response to DNA damage Akt: a double-edged sword in cell proliferation and genome stability.Selenium compounds activate ATM-dependent DNA damage response via the mismatch repair protein hMLH1 in colorectal cancer cells.TRIM28 regulates RNA polymerase II promoter-proximal pausing and pause release.BRCA1 modulates the autophosphorylation status of DNA-PKcs in S phase of the cell cycle.Ataxia telangiectasia mutated (Atm) and DNA-PKcs kinases have overlapping activities during chromosomal signal joint formation.Non-homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair process.

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Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the Thr-2609 cluster upon DNA double strand break.

http://www.wikidata.org/entity/Q53581072

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2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年學術文章

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Ataxia telangiectasia mutated ...... upon DNA double strand break.

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Ataxia telangiectasia mutated ...... upon DNA double strand break.

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Ataxia telangiectasia mutated ...... upon DNA double strand break.

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Journal of Biological Chemistry

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Ataxia telangiectasia mutated ...... upon DNA double strand break.

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Andrea Krempler

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Benjamin P C Chen

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David J Chen

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Hirohiko Yajima

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Junya Kobayashi

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Markus Löbrich

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Naoya Uematsu

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Yaniv Lerenthal

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Yosef Shiloh

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P2860

The BRCT domain is a phospho-protein binding domain

Evidence for a lack of DNA double-strand break repair in human cells exposed to very low x-ray doses

Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNA-dependent protein kinase.

Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks.

Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair.

A pathway of double-strand break rejoining dependent upon ATM, Artemis, and proteins locating to gamma-H2AX foci.

The DNA-dependent protein kinase catalytic subunit phosphorylation sites in human Artemis.

DNA-PK autophosphorylation facilitates Artemis endonuclease activity

Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae.

Substrate specificities and identification of putative substrates of ATM kinase family members

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6582-6587

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10.1074/JBC.M611605200

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9

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282

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17189255

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