Zobrazeno 1 - 10 of 81 pro vyhledávání: '"John J. Baldwin"'
3
Drug discovery and development 2014: Returning toward the norm?
Autor: John J Baldwin
Publikováno v: Future medicinal chemistry. 7(7)
2014 was a banner year for new drug approvals with the US FDA announcing a total of 41 new chemical entities (NCE). This number far exceeded the most recent 10-year average of 24. Significant among the breakthrough therapeutics were Keytruda (Merck)
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::add21d89502a0befdffc96c5c8f065b1
https://pubmed.ncbi.nlm.nih.gov/26061103
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5
Design, syntheses, and activity of new 3-[(sulfonylaryl)-amino]-1,4-benzodiazepin-2-one derivatives as α-thrombin inhibitors
Autor: John J. Baldwin, S. Dale Lewis, D. Dumas, Adel M. Naylor-Olsen, Gérard Leclerc, Murcko Mark A
Publikováno v: European Journal of Medicinal Chemistry. 33:471-488
Thrombin plays a central role in thrombosis. Because of the medical need for novel antithrombotic drugs, a search for structurally novel thrombin inhibitors was undertaken. In the absence of a crystal structure, a class was designed based on a modeli
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ca02e0f8d329b72e146f64efdf003ee6
https://doi.org/10.1016/s0223-5234(98)80048-2
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9
Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors
Autor: Richard S. Alexander, William C. Randall, Graham M. Smith, James P. Springer, Brian M. McKeever, David W. Christianson, Charles N. Habecker, John J. Baldwin, Gerald S. Ponticello
Publikováno v: Protein Science. 3:118-125
The 3-dimensional structure of human carbonic anhydrase II (HCAII; EC 4.2.1.1) complexed with 3 structurally related inhibitors, 1a, 1b, and 1c, has been determined by X-ray crystallographic methods. The 3 inhibitors (1a = C8H12N2O4S3) vary only in t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::111801c085a16909f1a3035d0a460b1f
https://doi.org/10.1002/pro.5560030115
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10
Inhibition of thrombin and other trypsin-like serine proteinases by cyclotheonamide A
Autor: S. D. Lewis, John J. Baldwin, Nobuhiro Fusetani, Adel M. Naylor, Jules A. Shafer, Assunta S. Ng
Publikováno v: Thrombosis Research. 70:173-190
Cyclotheonamide A (CA), a cyclic peptide isolated from the marine sponge of the genus Theonella was shown to be a slow-binding inhibitor of several trypsin-like serine proteinases. Values of 4.6 x 10(4), 4.8 x 10(4), 9.3 x 10(3), 2.1 x 10(3) and 2.7
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdeff7e6b939a106d9d186066b881946
https://doi.org/10.1016/0049-3848(93)90158-k
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