Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Lauren E. Frick"'
Autor:
Nidhi Shrivastav, Bogdan I Fedeles, Deyu Li, James C Delaney, Lauren E Frick, James J Foti, Graham C Walker, John M Essigmann
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e94716 (2014)
DinB, the E. coli translesion synthesis polymerase, has been shown to bypass several N2-alkylguanine adducts in vitro, including N2-furfurylguanine, the structural analog of the DNA adduct formed by the antibacterial agent nitrofurazone. Recently, it
Externí odkaz:
https://doaj.org/article/b840c4fcffaf4a45bc97174bd5776e9a
Autor:
Morteza Razavi, William A. LaMarr, Matthew E. Pope, Christine A. Miller, N. Leigh Anderson, Lauren E. Frick, Terry W. Pearson
Publikováno v:
Journal of Proteome Research. 11:5642-5649
We investigated the utility of an SPE-MS/MS platform in combination with a modified SISCAPA workflow for chromatography-free MRM analysis of proteotypic peptides in digested human plasma. This combination of SISCAPA and SPE-MS/MS technology allows se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ba565363847d86c80f5e1c56f45d9e4
https://doi.org/10.1021/pr300652v
https://doi.org/10.1021/pr300652v
Publikováno v:
SLAS Discovery. 16:1217-1226
The sirtuin enzymes, a class of NAD(+)-dependent histone deacetylases, are a focal point of epigenetic research because of their roles in regulating gene expression and cellular differentiation by deacetylating histones and a host of transcription fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e63061510ba9a4ec107ec92af9bb8bf
https://doi.org/10.1177/1087057111420291
https://doi.org/10.1177/1087057111420291
Publikováno v:
SLAS Discovery. 16:1186-1195
Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from an acetyl-coenzyme A donor molecule to specific lysine residues within proteins. The acetylation state of proteins, particularly histones, is known to modulate their inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fd20ee03dbf34a4726db71cd68949fb
https://doi.org/10.1177/1087057111418653
https://doi.org/10.1177/1087057111418653
Publikováno v:
Proceedings of the National Academy of Sciences. 104:755-760
1, N 6 -ethanoadenine (EA) forms through the reaction of adenine in DNA with the antitumor agent 1,3-bis(2-chloroethyl)-1-nitrosourea, a chemotherapeutic used to combat various brain, head, and neck tumors. Previous studies of the toxic and mutagenic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6de3d5c4d8c828d9fe50992e18193cc4
https://doi.org/10.1073/pnas.0607377104
https://doi.org/10.1073/pnas.0607377104
Autor:
Cintyu Wong, Catherine L. Drennan, Leona D. Samson, Lauren E. Frick, Lisa Smeester, John M. Essigmann, Koli Taghizadeh, John S. Wishnok, James C. Delaney
Publikováno v:
Nature Structural & Molecular Biology. 12:855-860
Oxidative stress converts lipids into DNA-damaging agents. The genomic lesions formed include 1,N(6)-ethenoadenine (epsilonA) and 3,N(4)-ethenocytosine (epsilonC), in which two carbons of the lipid alkyl chain form an exocyclic adduct with a DNA base
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3293fbc847292ba7773699a870ddc039
https://doi.org/10.1038/nsmb996
https://doi.org/10.1038/nsmb996
Autor:
Bogdan I. Fedeles, Nidhi Shrivastav, John M. Essigmann, James J. Foti, Deyu Li, Lauren E. Frick, Graham C. Walker, James C. Delaney
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e94716 (2014)
Public Library of Science
PLoS ONE
Public Library of Science
PLoS ONE
DinB, the E. coli translesion synthesis polymerase, has been shown to bypass several N[superscript 2]-alkylguanine adducts in vitro, including N[superscript 2]-furfurylguanine, the structural analog of the DNA adduct formed by the antibacterial agent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be4c680eb9f4bc08d862134c054b1d8e
http://europepmc.org/articles/PMC3986394?pdf=render
http://europepmc.org/articles/PMC3986394?pdf=render
Autor:
Rebecca Turincio, Peter Thana, Yichin Liu, Erica VanderPorten, William A. LaMarr, Lauren E. Frick
Publikováno v:
Analytical biochemistry. 441(2)
Catalytic turnover of pyruvate to lactate by lactate dehydrogenase (LDH) is critical in maintaining an intracellular nicotinamide adenine dinucleotide (NAD⁺) pool for continuous fueling of the glycolytic pathway. In this article, we describe two la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf1c70def5a6733b746084a32c2b016d
https://pubmed.ncbi.nlm.nih.gov/23871998
https://pubmed.ncbi.nlm.nih.gov/23871998