Year |
Citation |
Score |
2020 |
Tsutakawa SE, Sarker AH, Ng C, Arvai AS, Shin DS, Shih B, Jiang S, Thwin AC, Tsai MS, Willcox A, Her MZ, Trego KS, Raetz AG, Rosenberg D, Bacolla A, et al. Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations. Proceedings of the National Academy of Sciences of the United States of America. PMID 32522879 DOI: 10.1073/Pnas.1921311117 |
0.494 |
|
2020 |
Sarker AH, Trego KS, Zhang W, Jacob P, Snijders A, Mao JH, Schick SF, Cooper PK, Hang B. Thirdhand Smoke Exposure Causes Replication Stress and Impaired Transcription in Human Lung Cells. Environmental and Molecular Mutagenesis. PMID 32267018 DOI: 10.1002/Em.22372 |
0.493 |
|
2018 |
Limpose KL, Trego KS, Li Z, Leung SW, Sarker AH, Shah JA, Ramalingam SS, Werner EM, Dynan WS, Cooper PK, Corbett AH, Doetsch PW. Overexpression of the base excision repair NTHL1 glycosylase causes genomic instability and early cellular hallmarks of cancer. Nucleic Acids Research. PMID 29522130 DOI: 10.1093/Nar/Gky162 |
0.588 |
|
2016 |
Trego KS, Groesser T, Davalos AR, Parplys AC, Zhao W, Nelson MR, Hlaing A, Shih B, Rydberg B, Pluth JM, Tsai MS, Hoeijmakers JH, Sung P, Wiese C, Campisi J, et al. Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologous Recombination and Genome Stability. Molecular Cell. PMID 26833090 DOI: 10.1016/J.Molcel.2015.12.026 |
0.459 |
|
2011 |
Trego KS, Chernikova SB, Davalos AR, Perry JJ, Finger LD, Ng C, Tsai MS, Yannone SM, Tainer JA, Campisi J, Cooper PK. The DNA repair endonuclease XPG interacts directly and functionally with the WRN helicase defective in Werner syndrome. Cell Cycle (Georgetown, Tex.). 10: 1998-2007. PMID 21558802 DOI: 10.4161/Cc.10.12.15878 |
0.509 |
|
2006 |
Trego KS, Turchi JJ. Pre-steady-state binding of damaged DNA by XPC-hHR23B reveals a kinetic mechanism for damage discrimination. Biochemistry. 45: 1961-9. PMID 16460043 DOI: 10.1021/Bi051936T |
0.682 |
|
2005 |
Boeckman HJ, Trego KS, Turchi JJ. Cisplatin sensitizes cancer cells to ionizing radiation via inhibition of nonhomologous end joining. Molecular Cancer Research : McR. 3: 277-85. PMID 15886299 DOI: 10.1158/1541-7786.Mcr-04-0032 |
0.602 |
|
2005 |
Trego KS, Zhu Y, Parris DS. The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA. Nucleic Acids Research. 33: 536-45. PMID 15673714 DOI: 10.1093/Nar/Gki196 |
0.69 |
|
2003 |
Trego KS, Parris DS. Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activity. Journal of Virology. 77: 12646-59. PMID 14610187 DOI: 10.1128/Jvi.77.23.12646-12659.2003 |
0.691 |
|
2003 |
Zhu Y, Trego KS, Song L, Parris DS. 3' to 5' exonuclease activity of herpes simplex virus type 1 DNA polymerase modulates its strand displacement activity. Journal of Virology. 77: 10147-53. PMID 12941927 DOI: 10.1128/Jvi.77.18.10147-10153.2003 |
0.607 |
|
Show low-probability matches. |