Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1
about
Enzymes of the cyclooxygenase pathways of prostanoid biosynthesisA Radical Transfer Pathway in Spore Photoproduct LyaseAsymmetric acetylation of the cyclooxygenase-2 homodimer by aspirin and its effects on the oxygenation of arachidonic, eicosapentaenoic, and docosahexaenoic acids.Decreased cyclooxygenase inhibition by aspirin in polymorphic variants of human prostaglandin H synthase-1.Pulsed Dipolar Spectroscopy Reveals That Tyrosyl Radicals Are Generated in Both Monomers of the Cyclooxygenase-2 DimerProstaglandin H synthase: resolved and unresolved mechanistic issues.Structural comparisons of arachidonic acid-induced radicals formed by prostaglandin H synthase-1 and -2.Cyclooxygenase reaction mechanism of PGHS--evidence for a reversible transition between a pentadienyl radical and a new tyrosyl radical by nitric oxide trapping.Cyclooxygenase competitive inhibitors alter tyrosyl radical dynamics in prostaglandin H synthase-2.
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Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 17 April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1
@en
Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1.
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type
label
Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1
@en
Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1.
@nl
prefLabel
Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1
@en
Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1.
@nl
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P2860
P1476
Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1
@en
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Ah-Lim Tsai
Corina E Rogge
Richard J Kulmacz
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P304
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10.1016/J.JINORGBIO.2009.04.002
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2009-04-17T00:00:00Z