Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Nataline Meinhardt"'
Autor:
Kristine Wilhelm, Schuler, Meera I, Kodukulla, Charles I, Rosenblum, Nataline, Meinhardt, Rhyomi C, Sellnow, Todd, Parker
Publikováno v:
Current Medical Research and Opinion. 38:875-880
Recent increases in the practice of parallel publication, during which a peer-reviewed manuscript is published concurrently with the first dissemination of the same key data at a medical congress as a late-breaking abstract, have highlighted substant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da4c0403aff527b00bfeadd16127db4c
https://doi.org/10.1080/03007995.2022.2078102
https://doi.org/10.1080/03007995.2022.2078102
Publikováno v:
Journal of the American Chemical Society
Thioamide quenchers can be paired with compact fluorophores to design “turn-on” fluorescent protease substrates. We have used this method to study a variety of serine-, cysteine-, carboxyl-, and metallo-proteases, including trypsin, chymotrypsin,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d8836ed0302c17f304771d5046e1c9a
https://doi.org/10.1021/ja412297x
https://doi.org/10.1021/ja412297x
Autor:
Hyunil Jo, Swapnil J. Kulkarni, Kristin E. Low, William F. DeGrado, Xiaozhen Hu, Doron C. Greenbaum, Peter L. Davies, Nataline Meinhardt, Yibing Wu
Publikováno v:
Journal of the American Chemical Society. 134:17704-17713
We have designed a highly specific inhibitor of calpain by mimicking a natural protein-protein interaction between calpain and its endogenous inhibitor calpastatin. To enable this goal we established a new method of stabilizing an α-helix in a small
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::671f4f9b15fc2ed6bf727819bc946348
https://doi.org/10.1021/ja307599z
https://doi.org/10.1021/ja307599z
Autor:
Michael Klemba, Geetha Velmourougane, Seema Dalal, Doron C. Greenbaum, Nataline Meinhardt, Michael B. Harbut, Sheena McGowan, James C. Whisstock, Christine A Oellig
Publikováno v:
Journal of Medicinal Chemistry. 54:1655-1666
The malarial PfA-M1 metallo-aminopeptidase is considered a putative drug target. The natural product dipeptide mimetic, bestatin, is a potent inhibitor of PfA-M1. Herein we present a new, efficient, and high-yielding protocol for the synthesis of bes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de4cd1f54ccf6faec17095997b56f2e9
https://doi.org/10.1021/jm101227t
https://doi.org/10.1021/jm101227t
Autor:
Geetha Velmourougane, Michael B. Harbut, Seema Dalal, Sheena McGowan, Christine A. Oellig, Nataline Meinhardt, James C. Whisstock, Michael Klemba, Doron C. Greenbaum
Publikováno v:
Journal of Medicinal Chemistry; Mar2011, Vol. 54 Issue 6, p1655-1666, 12p