Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Amy Y. Mak"'
Publikováno v:
Journal of Biological Chemistry. 273:5801-5807
Prostaglandin H synthases (PGHSs) catalyze the conversion of arachidonic acid to prostaglandins. In this report, we describe the effect of a PGHS2 Y355F mutation on the dynamics of PGHS2 catalysis and inhibition. Tyr355 is part of a hydrogen-bonding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b40d957816c756fbd9372e2acd421537
https://doi.org/10.1074/jbc.273.10.5801
https://doi.org/10.1074/jbc.273.10.5801
Publikováno v:
Journal of Biological Chemistry. 272:12393-12398
Prostaglandins are synthesized by prostaglandin H synthase (PGHS) 1 and 2. PGHS2 is regulated through inducible expression. We report here the regulation of PGHS1 activity by substrate-dependent cooperative activation. The cooperativity is characteri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7e96f27cfdce24918e25adfecab23f6
https://doi.org/10.1074/jbc.272.19.12393
https://doi.org/10.1074/jbc.272.19.12393
Publikováno v:
Methods in enzymology. 399
Little is known about the kinetic mechanism of E3 ubiquitin ligases. This work describes basic methodology to investigate the kinetic mechanism of E3 ubiquitin ligases. The method used steady state, bi-substrate kinetic analysis of an E3 ligase-catal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eb3e9a8ebc1244c0df10a1c16c8c2e40
https://pubmed.ncbi.nlm.nih.gov/16338366
https://pubmed.ncbi.nlm.nih.gov/16338366
Little is known about the kinetic mechanism of E3 ubiquitin ligases. This work describes basic methodology to investigate the kinetic mechanism of E3 ubiquitin ligases. The method used steady state, bi‐substrate kinetic analysis of an E3 ligase–c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::54085621f11f6ef2d31cd403eeef3df2
https://doi.org/10.1016/s0076-6879(05)99022-8
https://doi.org/10.1016/s0076-6879(05)99022-8
Autor:
Pamela Volkel, Yi-Zheng Xu, Martin Huber, Teresa Biegel, Chakkodabylu S. Ramesha, Simon W. Lee, Marie Dinh, Liliana E. Scarafia, Jim W. Barnett, Qing-Fen Gan, Amy Y. Mak, Stacie A. Dalrymple, On-Yee So, James Patrick Dunn, Mary Mulkins, David C. Swinney, Ina Lee
Publikováno v:
The Journal of biological chemistry. 277(26)
A small molecule inhibitor of NF-kappaB-dependent cytokine expression was discovered that blocked tumor necrosis factor (TNF) alpha-induced IkappaB(alpha) degradation in MM6 cells but not the degradation of beta-catenin in Jurkat cells. Ro106-9920 bl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa26b171203043d8e1aa00e897eed2ae
https://pubmed.ncbi.nlm.nih.gov/11950839
https://pubmed.ncbi.nlm.nih.gov/11950839
Autor:
Amy Y. Mak, David C. Swinney
Publikováno v:
Biochemistry. 33(8)
CYP17 catalyzes the cleavage of the C-17 side chain of progesterone to form androstenedione. The two-step reaction involves an initial 17 alpha-hydroxylation catalyzed by oxene chemistry followed by cleavage of the C-17 side chain. We have recently s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88c1e24b338cea1f78cd0df440a83db7
https://pubmed.ncbi.nlm.nih.gov/8117675
https://pubmed.ncbi.nlm.nih.gov/8117675
Autor:
Amy Y. Mak, David C. Swinney
Publikováno v:
Journal of the American Chemical Society. 114:8309-8310
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::676a213612b4e041353cfcb04433d2e9
https://doi.org/10.1021/ja00047a063
https://doi.org/10.1021/ja00047a063