Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Laura M. S. Baker"'
Autor:
Steven R. Woodcock, Bruce P. Branchaud, Paul R. S. Baker, Rafael Radi, Franca Golin-Bisello, Bruce A. Freeman, Mitchell P. Fink, Francisco J. Schopfer, Laura M. S. Baker
Publikováno v:
Journal of Biological Chemistry. 282:31085-31093
Fatty acid nitration by nitric oxide-derived species yields electrophilic products that adduct protein thiols, inducing changes in protein function and distribution. Nitro-fatty acid adducts of protein and reduced glutathione (GSH) are detected in he
Autor:
Yuqing E. Chen, Francisco J. Schopfer, Scott Sweeney, Carlos Batthyány, Yiming Lin, Paul R. S. Baker, Alison L. Groeger, Karen E. Iles, Laura M. S. Baker, Marshall H. Long, Steven R. Woodcock, Bruce P. Branchaud, Bruce A. Freeman
Publikováno v:
Journal of Biological Chemistry. 280:42464-42475
Mass spectrometric analysis of human plasma and urine revealed abundant nitrated derivatives of all principal unsaturated fatty acids. Nitrated palmitoleic, oleic, linoleic, linolenic, arachidonic and eicosapentaenoic acids were detected in concert w
Autor:
Laura M. S. Baker, Leslie B. Poole
Publikováno v:
Journal of Biological Chemistry. 278:9203-9211
Escherichia coli thiol peroxidase (Tpx, p20, scavengase) is part of an oxidative stress defense system that uses reducing equivalents from thioredoxin (Trx1) and thioredoxin reductase to reduce alkyl hydroperoxides. Tpx contains three Cys residues, C
Publikováno v:
Journal of Bacteriology. 183:1961-1973
Helicobacter pylori , an oxygen-sensitive microaerophile, contains an alkyl hydroperoxide reductase homologue (AhpC, HP1563) that is more closely related to 2-Cys peroxiredoxins of higher organisms than to most other eubacterial AhpC proteins. Alleli
Autor:
Laura M S, Baker, Paul R S, Baker, Franca, Golin-Bisello, Francisco J, Schopfer, Mitchell, Fink, Steven R, Woodcock, Bruce P, Branchaud, Rafael, Radi, Bruce A, Freeman
Publikováno v:
The Journal of biological chemistry. 282(42)
Fatty acid nitration by nitric oxide-derived species yields electrophilic products that adduct protein thiols, inducing changes in protein function and distribution. Nitro-fatty acid adducts of protein and reduced glutathione (GSH) are detected in he
Publikováno v:
Redox Proteomics
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aacc68005fc6b2ac584a93fd60e9fb5e
https://doi.org/10.1002/0471973122.ch23
https://doi.org/10.1002/0471973122.ch23
Autor:
Francisco J. Schopfer, Bruce P. Branchaud, Bruce A. Freeman, Yingying Huang, Rosario Durán, Laura M. S. Baker, Carlos Cerveñansky, Paul R. S. Baker, Carlos Batthyány
Publikováno v:
The Journal of biological chemistry. 281(29)
Nitric oxide ((*)NO)-derived reactive species nitrate unsaturated fatty acids, yielding nitroalkene derivatives, including the clinically abundant nitrated oleic and linoleic acids. The olefinic nitro group renders these derivatives electrophilic at
Autor:
Paul R S, Baker, Yiming, Lin, Francisco J, Schopfer, Steven R, Woodcock, Alison L, Groeger, Carlos, Batthyany, Scott, Sweeney, Marshall H, Long, Karen E, Iles, Laura M S, Baker, Bruce P, Branchaud, Yuqing E, Chen, Bruce A, Freeman
Publikováno v:
The Journal of biological chemistry. 280(51)
Mass spectrometric analysis of human plasma and urine revealed abundant nitrated derivatives of all principal unsaturated fatty acids. Nitrated palmitoleic, oleic, linoleic, linolenic, arachidonic and eicosapentaenoic acids were detected in concert w
Autor:
Laura M S, Baker, Leslie B, Poole
Publikováno v:
The Journal of biological chemistry. 278(11)
Escherichia coli thiol peroxidase (Tpx, p20, scavengase) is part of an oxidative stress defense system that uses reducing equivalents from thioredoxin (Trx1) and thioredoxin reductase to reduce alkyl hydroperoxides. Tpx contains three Cys residues, C