Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Yang, Zhengguan"'
Autor:
Chen, Mengqian, Liang, Jiaxin, Ji, Hao, Yang, Zhengguan, Altilia, Serena, Hu, Bing, Schronce, Adam, McDermott, Martina S. J., Schools, Gary P., Lim, Chang-uk, Oliver, David, Shtutman, Michael S., Lu, Tao, Stark, George R., Porter, Donald C., Broude, Eugenia V., Roninson, Igor B.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2017 Sep . 114(38), 10208-10213.
Externí odkaz:
https://www.jstor.org/stable/26487964
Autor:
Zou, Yue, Ma, Huaxian, Minko, Irina G., Shell, Steven M., Yang, Zhengguan, Qu, Youxing, Xu, Ying, Geacintov, Nicholas E., Lloyd, R.
Publikováno v:
ETSU Faculty Works.
The DNA repair protein UvrB plays an indispensable role in the stepwise and sequential damage recognition of nucleotide excision repair in Escherichia coli. Our previous studies suggested that UvrB is responsible for the chemical damage recognition o
Externí odkaz:
https://dc.etsu.edu/etsu-works/18700
Autor:
Liu, Yiyong, Yang, Zhengguan, Utzat, Christopher D., Liu, Yu, Geacintov, Nicholas E., Basu, Ashis K., Zou, Yue
Publikováno v:
ETSU Faculty Works.
Human RPA (replication protein A), a single-stranded DNA-binding protein, is required for many cellular pathways including DNA repair, recombination and replication. However, the role of RPA in nucleotide excision repair remains elusive. In the prese
Externí odkaz:
https://dc.etsu.edu/etsu-works/18441
Autor:
Liu, Yu, Liu, Yiyong, Yang, Zhengguan, Utzat, Christopher, Wang, Guizhi, Basu, Ashis K., Zou, Yue
Publikováno v:
ETSU Faculty Works.
Human xeroderma pigmentosum group A (XPA) is an essential protein for nucleotide excision repair (NER). We have previously reported that XPA forms a homodimer in the absence of DNA. However, what oligomeric forms of XPA are involved in DNA damage rec
Externí odkaz:
https://dc.etsu.edu/etsu-works/18399
Publikováno v:
ETSU Faculty Works.
Nucleotide excision repair (NER) plays an important role in maintaining the integrity of DNA by removing various types of bulky or distorting DNA adducts in both prokaryotic and eukaryotic cells. In Escherichia coli, the excision repair proteins UvrA
Externí odkaz:
https://dc.etsu.edu/etsu-works/18364
Publikováno v:
ETSU Faculty Works.
RPA (replication protein A) is an essential factor for DNA DSB (double-strand break) repair and cell cycle checkpoint activation. The 32 kDa subunit of RPA undergoes hyperphosphorylation in response to cellular genotoxic insults. However, the potenti
Externí odkaz:
https://dc.etsu.edu/etsu-works/18339
Publikováno v:
ETSU Faculty Works.
DNA damage triggers complex cellular responses in eukaryotic cells, including initiation of DNA repair and activation of cell cycle checkpoints. In addition to inducing cell cycle arrest, checkpoint also has been suggested to modulate a variety of ot
Externí odkaz:
https://dc.etsu.edu/etsu-works/18067
Autor:
Yang, Zhengguan, Roginskaya, Marina, Colis, Laureen C., Basu, Ashis K., Shell, Steven M., Liu, Yiyong, Musich, Phillip R., Harris, Constance M., Harris, Thomas M., Zou, Yue
Publikováno v:
ETSU Faculty Works.
Human XPA is an important DNA damage recognition protein in nucleotide excision repair (NER). We previously observed that XPA binds to the DNA lesion as a homodimer [Liu, Y., Liu, Y., Yang, Z., Utzat, C., Wang, G., Basu, A. K., and Zou, Y. (2005) Bio
Externí odkaz:
https://dc.etsu.edu/etsu-works/18063
Publikováno v:
ETSU Faculty Works.
Nucleotide excision repair (NER) is a repair pathway that removes a variety of bulky DNA lesions in both prokaryotic and eukaryotic cells. The perturbation of DNA helix structure caused by the oxidative intrastrand lesions could render them good subs
Externí odkaz:
https://dc.etsu.edu/etsu-works/18062
Publikováno v:
ETSU Faculty Works.
Human replication protein A (RPA), a heterotrimer composed of RPA70, RPA32, and RPA14 subunits, contains four single-stranded DNA (ssDNA) binding domains (DBD): DBD-A, DBD-B, and DBD-C in RPA70 and DBD-D in RPA32. Although crystallographic or NMR str
Externí odkaz:
https://dc.etsu.edu/etsu-works/17795