Nicole M. Okeley, Ph.D. - Publications
Affiliations: | 2002 | University of Illinois, Urbana-Champaign, Urbana-Champaign, IL |
Area:
organic chemistry and chemical biologyYear | Citation | Score | |||
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2003 | Okeley NM, Paul M, Stasser JP, Blackburn N, van der Donk WA. SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins. Biochemistry. 42: 13613-24. PMID 14622008 DOI: 10.1021/Bi0354942 | 0.655 | |||
2002 | Peng S, Okeley NM, Tsai AL, Wu G, Kulmacz RJ, van der Donk WA. Synthesis of isotopically labeled arachidonic acids to probe the reaction mechanism of prostaglandin H synthase. Journal of the American Chemical Society. 124: 10785-96. PMID 12207535 DOI: 10.1021/Ja026880U | 0.51 | |||
2002 | Tsai AL, Palmer G, Wu G, Peng S, Okeley NM, van der Donk WA, Kulmacz RJ. Structural characterization of arachidonyl radicals formed by aspirin-treated prostaglandin H synthase-2. The Journal of Biological Chemistry. 277: 38311-21. PMID 12167656 DOI: 10.1074/Jbc.M206961200 | 0.484 | |||
2002 | Xie L, Chatterjee C, Balsara R, Okeley NM, van der Donk WA. Heterologous expression and purification of SpaB involved in subtilin biosynthesis. Biochemical and Biophysical Research Communications. 295: 952-7. PMID 12127987 DOI: 10.1016/S0006-291X(02)00783-0 | 0.647 | |||
2001 | Peng S, Okeley NM, Tsai AL, Wu G, Kulmacz RJ, van der Donk WA. Structural characterization of a pentadienyl radical intermediate formed during catalysis by prostaglandin H synthase-2. Journal of the American Chemical Society. 123: 3609-10. PMID 11472139 DOI: 10.1021/Ja015599X | 0.48 | |||
2001 | Okeley NM, van der Donk WA. Corrigendum to: ‘Novel cofactors via post-translational modifications of enzyme active sites’ Chemistry & Biology. 8: 97. DOI: 10.1016/S1074-5521(00)00054-5 | 0.331 | |||
2000 | Okeley NM, Zhu Y, van Der Donk WA. Facile chemoselective synthesis of dehydroalanine-containing peptides. Organic Letters. 2: 3603-6. PMID 11073655 DOI: 10.1021/Ol006485D | 0.566 | |||
2000 | Okeley NM, van der Donk WA. Novel cofactors via post-translational modifications of enzyme active sites. Chemistry & Biology. 7: R159-71. PMID 10903941 DOI: 10.1016/S1074-5521(00)00140-X | 0.492 | |||
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