HUS1 Antibody

1. These results suggest that p21(Waf1/CIP1) and Hus1 play crucial roles in the generation and transmission of bystander damage signals after low-dose alpha-particle irradiation. PMID: 26600172
2. adenine glycosylase activity, mismatch recognition properties and interaction with protein partners of MUTYH and 5 MAP variants were examined; P502L and R520Q had reduced affinity for PCNA; only Q324H was found to have reduced affinity for Hus1 PMID: 26377631
3. Intramolecular binding of the rad9 C-terminus in the checkpoint clamp Rad9-Hus1-Rad1 is closely linked with its DNA binding. PMID: 26088138
4. these pockets were not required for 9-1-1 chromatin localization or ATR-mediated CHK1 activation but were necessary for interactions between HUS1 and its binding partner MYH PMID: 25911100
5. Expression of cell cycle regulatory factors hus1, gadd45a, rb1, cdkn2a and mre11a correlates with expression of clock gene per2 in human colorectal carcinoma tissue. PMID: 24062075
6. HUS1 polymorphisms act as risk breast cancer modifiers in the group of non-carriers of BRCA1/2 mutations. PMID: 22926736
7. Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies. PMID: 22586102
8. The HUS1 is loaded to damaged sites where it serves as a platform for the selective recruitment of checkpoint and repair proteins. PMID: 21978893
9. The HUS1 protein interacts with casein kinase 2. PMID: 20545769
10. 9-1-1 complex is a component of the mismatch repair involved in MNNG-induced damage response. PMID: 20188637
11. Rad9-Rad1-Hus1 complex enhances in vitro activity of 8-oxoguanine DNA glycosylase. PMID: 19615952
12. downregulation by specific antisense oligonucleotides sensitizes human lung carcinoma cells to treatment with the DNA-damaging agent cisplatin PMID: 11920544
13. Rad9, Hus1, and Rad1 heterotrimeric complex chromatin binding is a proximal event in the checkpoint signaling cascade PMID: 12228248
14. HUS1 is an unstable protein that is actively degraded via the ubiquitin-proteasome pathway. Its expression can be stabilized by treating cells with proteasome-specific inhibitors. PMID: 15122316
15. The human Rad9/Rad1/Hus1 complex interacts with and stimulates DNA polymerase beta activity. PMID: 15314187
16. complex with rad1 and rad9 is a damage-specific activator of flap endonuclease 1 PMID: 15556996
17. The long-patch base excision machinery is an important target of the Rad9-Rad1-Hus1 complex, thus enhancing the quality control of DNA. PMID: 15871698
18. 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 PMID: 16216273
19. human DNA ligase I is stimulated by the Rad9-rad1-Hus1 checkpoint complex PMID: 16731526
20. 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. PMID: 16814252
21. Human NEIL1 DNA glycosylase activity is significantly stimulated by Hus1 and by the Rad9/Rad1/Hus1 heterotrimer. PMID: 17395641
22. 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. PMID: 17493829
23. Jab1 physically associates with the 9-1-1 complex (Rad1-Rad9-Hus1) PMID: 17583730
24. Human thymine DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately, and by the 9-1-1 complex. PMID: 17855402
25. Hus1 levels correlated significantly with the clinicopathologic factors of bad prognosis in epithelial ovarian tumors PMID: 18156970
26. Loss of HUS1 sensitizes cells to etopside-induced apoptosis by regulating BH3-only proteins. PMID: 18794804
27. 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). PMID: 19523882
28. The interdomain connecting loops (IDC loop) of hRad9, hHus1, and hRad1 are largely divergent and unique structural features of the 9-1-1 complex that are proposed to contribute to DNA damage recognition. PMID: 19535328
29. Functional study of the yeast homolog. PMID: 9524127

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HGNC: 5309

OMIM: 603760

KEGG: hsa:3364

STRING: 9606.ENSP00000258774

UniGene: Hs.152983