Zobrazeno 1 - 8
of 8
pro vyhledávání: '"James C. Mao"'
Publikováno v:
Journal of Medicinal Chemistry. 28:1371-1375
A series of ristocetin analogues with modifications (OH, C=O, C=NOH, NCOCH3) at the C-1' amino group was synthesized and found to possess antibacterial activity against gram-positive bacteria and to bind to Ac2-Lys-D-Ala-D-Ala, a model for the antibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d423484b19e239148ef9ad5255907fea
https://doi.org/10.1021/jm00147a047
https://doi.org/10.1021/jm00147a047
Autor:
Paul Kurath, Andre G. Pernet, Paul A. Lartey, Prabhavathi B. Fernandes, Larry L. Klein, Clinton M. Yeung, James C. Mao
Publikováno v:
Journal of Medicinal Chemistry. 32:151-160
Several series of pseudomonic acid analogues have been prepared that incorporate modified functionalities in place of the C1-C3 alpha,beta-unsaturated ester group. The inhibition of isoleucyl-tRNA synthetase and the in vitro activity of these compoun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e32a480ef958b7239392de040fa05e84
https://doi.org/10.1021/jm00121a028
https://doi.org/10.1021/jm00121a028
Autor:
Mary A. Marovich, Andre G. Pernet, Linus L. Shen, Prabhavathi B. Fernandes, Terry Rosen, James C. Mao
Publikováno v:
Journal of Medicinal Chemistry. 32:1062-1069
Streptolydigin (1) and tirandamycin A (2) are typical members of the naturally occurring class of 3-dienoyl tetramic acids. These compounds, which possess potent antibacterial activity particularly against anaerobes, have been shown to inhibit bacter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7164f2fd5f7e90b98a054f0a22701ad
https://doi.org/10.1021/jm00125a022
https://doi.org/10.1021/jm00125a022
Publikováno v:
Journal of Medicinal Chemistry. 32:84-93
Quantitative structure-activity relationships (QSAR) of N-Ac amino acids, N-Ac dipeptides, and N-Ac tripeptides in inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cell wall have been developed to probe the details of the binding b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea6a3a625e4d52217bcca1acc562b844
https://doi.org/10.1021/jm00121a018
https://doi.org/10.1021/jm00121a018
Publikováno v:
Circulation research. 35(1)
The effect of prolonged administration of alcohol on calcium binding and uptake by sarcoplasmic reticulum and mitochondria and on respiratory function of mitochondria was investigated in heart muscle of dogs. Dogs were paired and maintained with and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f8b7ad9b18cb1f0d16d666b5aa5fd93
https://pubmed.ncbi.nlm.nih.gov/4366862
https://pubmed.ncbi.nlm.nih.gov/4366862
Publikováno v:
Chemischer Informationsdienst. 16
A series of ristocetin analogues with modifications (OH, C=O, C=NOH, NCOCH3) at the C-1' amino group was synthesized and found to possess antibacterial activity against gram-positive bacteria and to bind to Ac2-Lys-D-Ala-D-Ala, a model for the antibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ebbaa7ed9234da6d7cfa35d3f46e4d52
https://doi.org/10.1002/chin.198552321
https://doi.org/10.1002/chin.198552321
Autor:
Paul Kurath, Larry L. Klein, Paul A. Lartey, Prabhavathi B. Fernandes, James C. Mao, Clinton M. Yeung, Andre G. Pernet
Publikováno v:
ChemInform. 20
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7546e4db654f4a99f4f30915546ecd6
https://doi.org/10.1002/chin.198925306
https://doi.org/10.1002/chin.198925306
Publikováno v:
The Journal of clinical investigation. 52(11)
The effect of prolonged administration of alcohol on mitochondrial function and high-energy phosphate (ATP) of heart muscle was investigated in dogs. Animals were divided into two groups, a control group and a group that received alcohol. In the expe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99e50b407d2ff64ae13f0af03429b3b3
https://pubmed.ncbi.nlm.nih.gov/4748507
https://pubmed.ncbi.nlm.nih.gov/4748507