Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease. - Wikidata - awgldk - TriplyDB

Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease.

Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease.

http://www.wikidata.org/entity/Q31004989

about

Multiple ATR-Chk1 pathway proteins preferentially associate with checkpoint-inducing DNA substrates An alternative form of replication protein a expressed in normal human tissues supports DNA repair Human XPC-hHR23B interacts with XPA-RPA in the recognition of triplex-directed psoralen DNA interstrand crosslinks.Global-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo Modifiers Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation Nucleotide excision repair in eukaryotes Crystal Structure of the FeS Cluster–Containing Nucleotide Excision Repair Helicase XPD Fibroblasts from naked mole-rats are resistant to multiple forms of cell injury, but sensitive to peroxide, ultraviolet light, and endoplasmic reticulum stress Interactions of human replication protein A with single-stranded DNA adducts.Xeroderma pigmentosum complementation group E protein (XPE/DDB2): purification of various complexes of XPE and analyses of their damaged DNA binding and putative DNA repair properties.Recruitment of DNA damage checkpoint proteins to damage in transcribed and nontranscribed sequences.Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair.Repair of DNA-polypeptide crosslinks by human excision nuclease.A mathematical model for human nucleotide excision repair: damage recognition by random order assembly and kinetic proofreading.Physical and functional interaction between DDB and XPA in nucleotide excision repair.Regulation of nucleotide excision repair activity by transcriptional and post-transcriptional control of the XPA protein.RETRACTED: DDB2, an essential mediator of premature senescence Thymine dimer-induced structural changes to the DNA duplex examined with reactive probes (†).Role of interaction of XPF with RPA in nucleotide excision repair.Regulation of nucleotide excision repair by UV-DDB: prioritization of damage recognition to internucleosomal DNA Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase.NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites Complex formation with damage recognition protein Rad14 is essential for Saccharomyces cerevisiae Rad1-Rad10 nuclease to perform its function in nucleotide excision repair in vivo.DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA.GCN5 and E2F1 stimulate nucleotide excision repair by promoting H3K9 acetylation at sites of damage.Viral interference with DNA repair by targeting of the single-stranded DNA binding protein RPA.Genome-wide analysis of human global and transcription-coupled excision repair of UV damage at single-nucleotide resolution Xeroderma pigmentosum: from genetics to hopes and realities of cutaneous gene therapy.p21 cooperates with DDB2 protein in suppression of ultraviolet ray-induced skin malignancies.Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair.Mechanism of release and fate of excised oligonucleotides during nucleotide excision repair Molecular mechanisms of xeroderma pigmentosum (XP) proteins.Bringing It All Together: Coupling Excision Repair to the DNA Damage Checkpoint.Damaged DNA binding protein 2 in reactive oxygen species (ROS) regulation and premature senescence An Integrated Approach for Analysis of the DNA Damage Response in Mammalian Cells: NUCLEOTIDE EXCISION REPAIR, DNA DAMAGE CHECKPOINT, AND APOPTOSIS Functional analysis of Rad14p, a DNA damage recognition factor in nucleotide excision repair, in regulation of transcription in vivo Saccharomyces cerevisiae MutLalpha is a mismatch repair endonuclease DDB2 gene disruption leads to skin tumors and resistance to apoptosis after exposure to ultraviolet light but not a chemical carcinogen.Pre-steady-state binding of damaged DNA by XPC-hHR23B reveals a kinetic mechanism for damage discrimination.Genome-wide kinetics of DNA excision repair in relation to chromatin state and mutagenesis

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Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease.

http://www.wikidata.org/entity/Q31004989

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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Joyce T Reardon

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P2860

Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites

Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo

Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG

The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage

Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair

RPA involvement in the damage-recognition and incision steps of nucleotide excision repair

DDB, a putative DNA repair protein, can function as a transcriptional partner of E2F1.

Mutations specific to the xeroderma pigmentosum group E Ddb- phenotype

UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation

Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity

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10.1101/GAD.1131003

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