Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2.
about
Radiochemistry on electrodes: Synthesis of an 18F-labelled and in vivo stable COX-2 inhibitor.Prokaryotic expression, purification and characterization of human cyclooxygenase-2.CD64 and Group II Secretory Phospholipase A2 (sPLA2-IIA) as Biomarkers for Distinguishing Adult Sepsis and Bacterial Infections in the Emergency Department.Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry.Interactions of 2-O-arachidonylglycerol ether and ibuprofen with the allosteric and catalytic subunits of human COX-2.Substrate-selective Inhibition of Cyclooxygeanse-2 by Fenamic Acid Derivatives Is Dependent on Peroxide ToneFatty Acid Binding to the Allosteric Subunit of Cyclooxygenase-2 Relieves a Tonic Inhibition of the Catalytic Subunit.Dual cyclooxygenase-fatty acid amide hydrolase inhibitor exploits novel binding interactions in the cyclooxygenase active site.
P2860
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P2860
Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2.
description
2015 nî lūn-bûn
@nan
2015年の論文
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2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
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2015年论文
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name
Action at a distance: mutation ...... t binders of cyclooxygenase-2.
@ast
Action at a distance: mutation ...... t binders of cyclooxygenase-2.
@en
type
label
Action at a distance: mutation ...... t binders of cyclooxygenase-2.
@ast
Action at a distance: mutation ...... t binders of cyclooxygenase-2.
@en
prefLabel
Action at a distance: mutation ...... t binders of cyclooxygenase-2.
@ast
Action at a distance: mutation ...... t binders of cyclooxygenase-2.
@en
P2093
P2860
P50
P356
P1476
Action at a distance: mutation ...... t binders of cyclooxygenase-2.
@en
P2093
Anna L Blobaum
Kebreab Ghebreselasie
Kelsey C Duggan
Lawrence J Marnett
Scott W Rowlinson
P2860
P304
12793-12803
P356
10.1074/JBC.M114.635987
P407
P577
2015-03-30T00:00:00Z