Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Sunbok Jang"'
Autor:
Emily C. Beckwitt, Sunbok Jang, Isadora Carnaval Detweiler, Jochen Kuper, Florian Sauer, Nina Simon, Johanna Bretzler, Simon C. Watkins, Thomas Carell, Caroline Kisker, Bennett Van Houten
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
It is not fully understood how XPA interacts with a DNA lesion during nucleotide excision repair. Here, the authors use single molecule analysis to study XPA–DNA interactions, including the DNA bend angle, protein stoichiometry, and diffusive prope
Externí odkaz:
https://doaj.org/article/cb2429af2c074e93843b6cd1c155ebba
Autor:
Sunbok Jang, Sripriya J Raja, Vera Roginskaya, Matthew A Schaich, Simon C Watkins, Bennett Van Houten
Publikováno v:
Nucleic Acids Research.
UV-damaged DNA-binding protein (UV-DDB) is a heterodimeric protein, consisting of DDB1 and DDB2 subunits, that works to recognize DNA lesions induced by UV damage during global genome nucleotide excision repair (GG-NER). Our laboratory previously dis
Autor:
Sunbok Jang, Namrata Kumar, Mathew A Schaich, Zhou Zhong, Barbara van Loon, Simon C Watkins, Bennett Van Houten
Publikováno v:
12856-12871
Nucleic Acids Research (NAR)
Nucleic Acids Research (NAR)
UV-DDB is a DNA damage recognition protein recently discovered to participate in the removal of 8-oxo-7,8-dihydro-2′-deoxyguanosine (8-oxoG) by stimulating multiple steps of base excision repair (BER). In this study, we examined whether UV-DDB has
Autor:
Hu Zhang, Alexander L. Marchetti, Sunbok Jang, Mu Wang, Haitao Guo, Xiaoyang Yu, Elena S. Kim
Publikováno v:
J Virol
Hepatitis B virus (HBV) utilizes host DNA repair mechanisms to convert viral relaxed circular DNA (rcDNA) into a persistent viral genome, the covalently closed circular DNA (cccDNA). To identify host factors involved in cccDNA formation, we developed
Autor:
Bennett Van Houten, Sheila S. David, Chandrima Majumdar, Cindy Khuu, Matthew A. Schaich, Brittani L Schnable, Sunbok Jang, Simon C. Watkins
Publikováno v:
Nucleic acids research, vol 49, iss 14
Nucleic Acids Research
Nucleic Acids Research
The oxidative base damage, 8-oxo-7,8-dihydroguanine (8-oxoG) is a highly mutagenic lesion because replicative DNA polymerases insert adenine (A) opposite 8-oxoG. In mammalian cells, the removal of A incorporated across from 8-oxoG is mediated by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdce6734987315aa70b2f26bec2dbeaa
https://escholarship.org/uc/item/7bs54080
https://escholarship.org/uc/item/7bs54080
Autor:
N.M. Hoitsma, Sunbok Jang, Bennett Van Houten, Bret D. Freudenthal, Emily C. Beckwitt, A.M. Whitaker, Pratul K Agarwal
Publikováno v:
Nucleic Acids Research
Base excision repair (BER) maintains genomic stability through the repair of DNA damage. Within BER, AP-endonuclease 1 (APE1) is a multifunctional enzyme that processes DNA intermediates through its backbone cleavage activity. To accomplish these rep
Autor:
Nina Simon, Florian Sauer, Bennett Van Houten, Thomas Carell, Isadora Carnaval Detweiler, Emily C. Beckwitt, Johanna Bretzler, Jochen Kuper, Caroline Kisker, Sunbok Jang, Simon C. Watkins
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications
Nature Communications
Nucleotide excision repair (NER) removes a wide range of DNA lesions, including UV-induced photoproducts and bulky base adducts. XPA is an essential protein in eukaryotic NER, although reports about its stoichiometry and role in damage recognition ar
Autor:
Namrata Kumar, Sunbok Jang, Cindy Khuu, Patricia L. Opresko, Muwen Kong, Bennett Van Houten, Elise Fouquerel, Emily C. Beckwitt, Simon C. Watkins, Sheila S. David, Chandrima Majumdar, Marcel P. Bruchez, Rajendra Prasad, Vesna Rapić-Otrin, Samuel H. Wilson
Publikováno v:
Nature structural & molecular biology, vol 26, iss 8
Nature structural & molecular biology
Nature structural & molecular biology
UV-DDB, a key protein in human global nucleotide excision repair (NER), binds avidly to abasic sites and 8-oxo-guanine (8-oxoG), suggesting a noncanonical role in base excision repair (BER). We investigated whether UV-DDB can stimulate BER for these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d4073e57005786b2de7cad2db34fbbf
https://escholarship.org/uc/item/55d5d9g6
https://escholarship.org/uc/item/55d5d9g6
Publikováno v:
DNA Repair (Amst)
UV-damaged DNA binding protein (UV-DDB) is a heterodimeric complex, composed of DDB1 and DDB2, and is involved in global genome nucleotide excision repair. Mutations in DDB2 are associated with xeroderma pigmentosum complementation group E. UV-DDB fo
Publikováno v:
Biochemistry. 55:5635-5646
Sterile alpha motif (SAM) and Histidine-Aspartate (HD)-domain containing protein 1 (SAMHD1) is a triphosphohydrolase that converts deoxyribonucleoside triphosphates (dNTPs) into deoxyribonucleosides and triphosphates. SAMHD1 exists in multiple states