The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair - Wikidata - awgldk - TriplyDB

The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair

The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair

http://www.wikidata.org/entity/Q35618148

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The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery DNA polymerase family X: function, structure, and cellular roles Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex Conditional inactivation of the DNA damage response gene Hus1 in mouse testis reveals separable roles for components of the RAD9-RAD1-HUS1 complex in meiotic chromosome maintenance Structure and Functional Implications of the Human Rad9-Hus1-Rad1 Cell Cycle Checkpoint Complex The 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mutagenesis in Saccharomyces cerevisiae.DNA damage response genes and the development of cancer metastasis USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication Replication protein A directs loading of the DNA damage checkpoint clamp to 5'-DNA junctions.Stripped-down DNA repair in a highly reduced parasite.Rad9 modulates the P21WAF1 pathway by direct association with p53.TLK1B promotes repair of DSBs via its interaction with Rad9 and Asf1.Interaction between human mismatch repair recognition proteins and checkpoint sensor Rad9-Rad1-Hus1 Pol β associated complex and base excision repair factors in mouse fibroblasts.Visualization of the physical and functional interaction between hMYH and hRad9 by Dronpa bimolecular fluorescence complementation.The RAD9-RAD1-HUS1 (9.1.1) complex interacts with WRN and is crucial to regulate its response to replication fork stalling Rad9 is required for B cell proliferation and immunoglobulin class switch recombination Phosphorylation of Xenopus Rad1 and Hus1 defines a readout for ATR activation that is independent of Claspin and the Rad9 carboxy terminus Targeted deletion of Rad9 in mouse skin keratinocytes enhances genotoxin-induced tumor development.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.Need telomere maintenance? Call 911 Increased common fragile site expression, cell proliferation defects, and apoptosis following conditional inactivation of mouse Hus1 in primary cultured cells.Genome maintenance defects in cultured cells and mice following partial inactivation of the essential cell cycle checkpoint gene Hus1.Contributions of Rad9 to tumorigenesis.The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease 1 and DNA polymerase beta in long patch base excision repair The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylase Hypersensitivity phenotypes associated with genetic and synthetic inhibitor-induced base excision repair deficiency Microhomology-mediated DNA strand annealing and elongation by human DNA polymerases λ and β on normal and repetitive DNA sequences.The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase Bypass of a psoralen DNA interstrand cross-link by DNA polymerases β, ι, and κ in vitro.The role of DNA exonucleases in protecting genome stability and their impact on ageing.Multiple functions of rad9 for preserving genomic integrity Understanding the role of the Q338H MUTYH variant in oxidative damage repair Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1 Rad9 plays an important role in DNA mismatch repair through physical interaction with MLH1 The DNA damage checkpoint protein RAD9A is essential for male meiosis in the mouse.Phosphorylation of human DNA ligase I regulates its interaction with replication factor C and its participation in DNA replication and DNA repair A junction branch point adjacent to a DNA backbone nick directs substrate cleavage by Saccharomyces cerevisiae Mus81-Mms4.Alu-miRNA interactions modulate transcript isoform diversity in stress response and reveal signatures of positive selection.Jab1 mediates protein degradation of the Rad9-Rad1-Hus1 checkpoint complex

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The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair

http://www.wikidata.org/entity/Q35618148

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The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair

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The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair

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Nucleic Acids Research

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The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair

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Dorothee Funk

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Erica Friedrich-Heineken

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Giuseppe Villani

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Igor Shevelev

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Isabelle Frouin

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Magali Toueille

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Michael O Hottiger

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Nazim El-Andaloussi

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Raimundo Freire

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Ulrich Hübscher

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Eukaryotic DNA Polymerases

Analysis of Rad3 and Chk1 protein kinases defines different checkpoint responses.

Long-patch DNA repair synthesis during base excision repair in mammalian cells

Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro

Purification and characterization of human DNA damage checkpoint Rad complexes

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Replication protein A-mediated recruitment and activation of Rad17 complexes

Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin

Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5' recessed DNA

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

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3316-3324

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scholarly article

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10.1093/NAR/GKH652

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11

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32

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2004-06-22T00:00:00Z

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8397626

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15314187

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443528

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