Zobrazeno 1 - 4 of 4 pro vyhledávání: '"Dagart Allison"'
1
Crystal Structures of mPGES-1 Inhibitor Complexes Form a Basis for the Rational Design of Potent Analgesic and Anti-Inflammatory Therapeutics
Autor: Kuklish Steven Lee, Dagart Allison, Bradley Condon, Aiping Zhang, Anita K. Harvey, Ashley V. Sloan, Xiao-Peng Yu, Ryan Thomas Backer, Matthew R. Lee, John G. Luz, Marijane Russell, Srinivasan Chandrasekhar, Matthew Fisher, Shawn Chang, Stephen Antonysamy
Publikováno v: Journal of Medicinal Chemistry. 58:4727-4737
Microsomal prostaglandin E synthase 1 (mPGES-1) is an α-helical homotrimeric integral membrane inducible enzyme that catalyzes the formation of prostaglandin E2 (PGE2) from prostaglandin H2 (PGH2). Inhibition of mPGES-1 has been proposed as a therap
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52f51d736c36586dd49c583231b9633f
https://doi.org/10.1021/acs.jmedchem.5b00330
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2
The 2.5 Å Crystal Structure of the SIRT1 Catalytic Domain Bound to Nicotinamide Adenine Dinucleotide (NAD+) and an Indole (EX527 Analogue) Reveals a Novel Mechanism of Histone Deacetylase Inhibition
Autor: Aiping Zhang, Yuewei Qian, Feiyu Zhang, Dagart Allison, Bradley Condon, Xun Zhao, James A. Jamison, Sheela Ashok, Tarun Gheyi, Marijane Russell, John G. Luz, Iain MacEwan
Publikováno v: Journal of Medicinal Chemistry. 56:963-969
The sirtuin SIRT1 is a NAD(+)-dependent histone deacetylase, a Sir2 family member, and one of seven human sirtuins. Sirtuins are conserved from archaea to mammals and regulate transcription, genome stability, longevity, and metabolism. SIRT1 regulate
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b78d0a61c4026702dc3228580a78fbc
https://doi.org/10.1021/jm301431y
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