Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Megan C. Branch"'
Autor:
Susan T Mashiyama, M Merced Malabanan, Eyal Akiva, Rahul Bhosle, Megan C Branch, Brandan Hillerich, Kevin Jagessar, Jungwook Kim, Yury Patskovsky, Ronald D Seidel, Mark Stead, Rafael Toro, Matthew W Vetting, Steven C Almo, Richard N Armstrong, Patricia C Babbitt
Publikováno v:
PLoS Biology, Vol 12, Iss 4, p e1001843 (2014)
The cytosolic glutathione transferase (cytGST) superfamily comprises more than 13,000 nonredundant sequences found throughout the biosphere. Their key roles in metabolism and defense against oxidative damage have led to thousands of studies over seve
Externí odkaz:
https://doaj.org/article/dd598339e1bd44de93570af2d943bd14
Autor:
Patricia C. Babbitt, Nir London, Guang Qiang Dong, Richard N. Armstrong, Chakrapani Kalyanaraman, Brian K. Shoichet, Hao Fan, Andrej Sali, Matthew P. Jacobson, Sara Calhoun, Megan C. Branch, Susan T. Mashiyama
Publikováno v:
Journal of Chemical Information and Modeling
Enzymes in the glutathione transferase (GST) superfamily catalyze the conjugation of glutathione (GSH) to electrophilic substrates. As a consequence they are involved in a number of key biological processes, including protection of cells against chem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c637de52d527a755138c526b542bb3e
https://doi.org/10.1021/ci5001554
https://doi.org/10.1021/ci5001554
Autor:
Jane E. Ladner, Richard N. Armstrong, Nina V. Stourman, Matthew R. Schaab, Joel M. Harp, Megan C. Branch
Publikováno v:
Biochemistry. 50:1274-1281
The crystal structure (1.50 Å resolution) and biochemical properties of the GSH transferase homologue, YghU, from Escherichia coli reveal that the protein is unusual in that it binds two molecules of GSH in each active site. The crystallographic obs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44b99e6d9b95e0bded8ac8448ca01b26
https://doi.org/10.1021/bi101861a
https://doi.org/10.1021/bi101861a
Publikováno v:
Biochemistry. 52:3191-3193
KijD3 is a flavin-dependent N-oxygenase implicated in the formation of the nitro-containing sugar d-kijanose, found attached to the antibiotic kijanimicin. For this investigation, the structure of KijD3 in complex with FMN and its dTDP-sugar substrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06d8c4fe72fb804b4c03705c8b222035
https://doi.org/10.1021/bi400407x
https://doi.org/10.1021/bi400407x
Autor:
Patricia C. Babbitt, B. Hillerich, Richard N. Armstrong, Mark Stead, Megan C. Branch, Rafael Toro, Yury Patskovsky, Steven C. Almo, Kevin L. Jagessar, Susan T. Mashiyama, M. Merced Malabanan, Jungwook Kim, R.D. Seidel, R. Bhosle, Eyal Akiva, Matthew W. Vetting
Publikováno v:
PLoS Biology, Vol 12, Iss 4, p e1001843 (2014)
PLoS Biology
PLoS Biology
Global networks of the cytosolic glutathione S-transferases illuminate sequence-structure-function relationships across more than 13,000 members of this superfamily, including experimental confirmation of enzymatic activity for 82 members and new cry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6381789866282cb77064971e6652979b
http://europepmc.org/articles/PMC3995644?pdf=render
http://europepmc.org/articles/PMC3995644?pdf=render