Kelly S. Trego, Ph.D.

Affiliations: 
2003 Ohio State University, Columbus, Columbus, OH 
Area:
Molecular Biology, Genetics
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"Kelly Trego"
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Deborah S. Parris grad student 2003 Ohio State
 (Functional significance of the physical interaction between the herpes simplex virus type 1 origin-binding protein, UL9, and the DNA polymerase processivity factor, UL42.)
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Publications

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Tsutakawa SE, Sarker AH, Ng C, et al. (2020) 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
Sarker AH, Trego KS, Zhang W, et al. (2020) Thirdhand Smoke Exposure Causes Replication Stress and Impaired Transcription in Human Lung Cells. Environmental and Molecular Mutagenesis
Limpose KL, Trego KS, Li Z, et al. (2018) Overexpression of the base excision repair NTHL1 glycosylase causes genomic instability and early cellular hallmarks of cancer. Nucleic Acids Research
Trego KS, Groesser T, Davalos AR, et al. (2016) Non-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologous Recombination and Genome Stability. Molecular Cell
Trego KS, Chernikova SB, Davalos AR, et al. (2011) The DNA repair endonuclease XPG interacts directly and functionally with the WRN helicase defective in Werner syndrome. Cell Cycle (Georgetown, Tex.). 10: 1998-2007
Trego KS, Turchi JJ. (2006) Pre-steady-state binding of damaged DNA by XPC-hHR23B reveals a kinetic mechanism for damage discrimination. Biochemistry. 45: 1961-9
Boeckman HJ, Trego KS, Turchi JJ. (2005) Cisplatin sensitizes cancer cells to ionizing radiation via inhibition of nonhomologous end joining. Molecular Cancer Research : McR. 3: 277-85
Trego KS, Zhu Y, Parris DS. (2005) 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
Trego KS, Parris DS. (2003) 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
Zhu Y, Trego KS, Song L, et al. (2003) 3' to 5' exonuclease activity of herpes simplex virus type 1 DNA polymerase modulates its strand displacement activity. Journal of Virology. 77: 10147-53
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