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Dominant alleles of RAD51, TP53 and XRCC1 combined genotypes indicated a strong protective role against hereditary breast cancer.
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Intramolecular binding of the rad9 C-terminus in the checkpoint clamp Rad9-Hus1-Rad1 is closely linked with its DNA binding.
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Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies.
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The RAD1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins.
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CK2 plays a crucial role in the ATR-dependent checkpoint pathway through its ability to phosphorylate Ser-341 and Ser-387 of the Rad9 subunit of the Rad9-Hus1-Rad1 complex
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9-1-1 complex is a component of the mismatch repair involved in MNNG-induced damage response.
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Rad9-Rad1-Hus1 complex enhances in vitro activity of 8-oxoguanine DNA glycosylase.
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Rad9, Hus1, and Rad1 heterotrimeric complex chromatin binding is a proximal event in the checkpoint signaling cascade
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RAD1 is a potential intrinsic chaperone in the stabilization of HUS1 for the heterotrimeric (RAD9-RAD1-HUS1) checkpoint complex formation.
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The human Rad9/Rad1/Hus1 complex interacts with and stimulates DNA polymerase beta activity.
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complex with rad9 and hus1 is a damage-specific activator of flap endonuclease 1
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The long-patch base excision machinery is an important target of the Rad9-Rad1-Hus1 complex, thus enhancing the quality control of DNA.
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PCNA and the Rad9/Rad1/Hus1 complex can independently bind and activate Fen1; acetylation of Fen1 by p300-HAT abolished the stimulatory effect of the complex but not that of PCNA, suggesting a possible mechanism of regulation of this repair pathway
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human DNA ligase I is stimulated by the Rad9-rad1-Hus1 checkpoint complex
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These data provide in vivo evidence that the human 9-1-1 complex participates in DNA repair in addition to its previously described role in DNA damage sensing.
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Human NEIL1 DNA glycosylase activity is significantly stimulated by hRad1 and by the Rad9/Rad1/Hus1 heterotrimer.
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we report successful tri-cistronic cloning, overexpression and purification of a three-protein complex of Rad9, Rad1 and Hus1 using a single hexa-histidine tag.
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Jab1 physically associates with the 9-1-1 complex; this association is mediated through direct interaction between Jab1 and Rad1, one of the subunits of the 9-1-1 complex
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Human thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex.
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The DNA binding domain (DBD) within the hLigI catalytic fragment interacts with both PCNA and the heterotrimeric cell-cycle checkpoint clamp, hRad9-hRad1-hHus1 (9-1-1).
