Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Christopher R, Lopez"'
Autor:
Christopher R Lopez, Albert Ribes-Zamora, Sandra M Indiviglio, Christopher L Williams, Svasti Haricharan, Alison A Bertuch
Publikováno v:
PLoS Genetics, Vol 7, Iss 8, p e1002233 (2011)
The Ku heterodimer associates with the Saccharomyces cerevisiae telomere, where it impacts several aspects of telomere structure and function. Although Ku avidly binds DNA ends via a preformed channel, its ability to associate with telomeres via this
Externí odkaz:
https://doaj.org/article/96f0b3a85efb44979158bc1924f4785e
Publikováno v:
DNA repair. 55
Abasic or AP sites generated by spontaneous DNA damage accumulate at a higher rate in actively transcribed regions of the genome in S. cerevisiae and are primarily repaired by base excision repair (BER) pathway. We have demonstrated that transcriptio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbf8e92389a7869ae4b589862923d749
https://pubmed.ncbi.nlm.nih.gov/28521214
https://pubmed.ncbi.nlm.nih.gov/28521214
Autor:
Nayun Kim, Christopher R. Lopez, Shashank Hambarde, Kevin D. Raney, Jun Gao, Wezley C. Griffin, Yang Yu, Shubeena Chib, Grzegorz Ira, Shivani Singh
Publikováno v:
Nucleic Acids Research
G-quadruplex or G4 DNA is a non-B secondary DNA structure consisting of a stacked array of guanine-quartets that can disrupt critical cellular functions such as replication and transcription. When sequences that can adopt Non-B structures including G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::798db52701ea00230f4ea9786de623d5
https://pubmed.ncbi.nlm.nih.gov/28369605
https://pubmed.ncbi.nlm.nih.gov/28369605
Publikováno v:
Proceedings of the National Academy of Sciences. 103:2386-2391
Previously, we found that the quorum sensing transcription factor SdiA up-regulates AcrAB. Others found that a 4-quinolone was a quorum-sensing signal in Pseudomonas aeruginosa . In Escherichia coli , there are at least three multidrug transporters (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7691729f6bdcd4a853e1ccddabf184a
https://doi.org/10.1073/pnas.0502890102
https://doi.org/10.1073/pnas.0502890102
Autor:
Russell J. DiGate, P. J. Hastings, Richard W. Deibler, Jeanine M. Pennington, Christopher R. Lopez, Starlight A. Ray, Shirley Yang, Susan M. Rosenberg, Lynn Zechiedrich
Publikováno v:
Molecular Microbiology. 58:80-101
The physiological role of topoisomerase III is unclear for any organism. We show here that the removal of topoisomerase III in temperature sensitive topoisomerase IV mutants in Escherichia coli results in inviability at the permissive temperature. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e05156bcbd512ecd8c0cd7ff9aaebe95
https://doi.org/10.1111/j.1365-2958.2005.04812.x
https://doi.org/10.1111/j.1365-2958.2005.04812.x
Autor:
Alison A. Bertuch, Christopher R. Lopez, Inn Chung, Jaime M. Williams, Lei Wei, Xiaolan Zhao, Lisa E. Hang, Xianpeng Liu
The Ku70-Ku80 ring complex encloses DNA ends to facilitate telomere maintenance and DNA break repair. Many studies focus on the ring-forming regions of subunits Ku70 and Ku80. Less is known about the Ku70 C-terminal tail, which lies outside the ring.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c55339d133e8abdfb37b9d52d5cde0c9
https://europepmc.org/articles/PMC4036155/
https://europepmc.org/articles/PMC4036155/
Autor:
Alison A. Bertuch, Christopher L. Williams, Christopher R. Lopez, Sandra M. Indiviglio, Svasti Haricharan, Albert Ribes-Zamora
Publikováno v:
PLoS Genetics, Vol 7, Iss 8, p e1002233 (2011)
PLoS Genetics
PLoS Genetics
The Ku heterodimer associates with the Saccharomyces cerevisiae telomere, where it impacts several aspects of telomere structure and function. Although Ku avidly binds DNA ends via a preformed channel, its ability to associate with telomeres via this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3ad6275e0fddbdc42d7683acc22c514
http://europepmc.org/articles/PMC3154960?pdf=render
http://europepmc.org/articles/PMC3154960?pdf=render
Autor:
Christopher R, Lopez, Shirley, Yang, Richard W, Deibler, Starlight A, Ray, Jeanine M, Pennington, Russell J, Digate, P J, Hastings, Susan M, Rosenberg, E Lynn, Zechiedrich
Publikováno v:
Molecular microbiology. 58(1)
The physiological role of topoisomerase III is unclear for any organism. We show here that the removal of topoisomerase III in temperature sensitive topoisomerase IV mutants in Escherichia coli results in inviability at the permissive temperature. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::39e41df14d4b199ab7cb9d6e45404f7d
https://pubmed.ncbi.nlm.nih.gov/16164551
https://pubmed.ncbi.nlm.nih.gov/16164551