(Q28190707)

Europe PubMed Central

PubMed publication ID

11677234

https://europepmc.org/article/MED/11677234

9 December 2020

1

C Schneider

1 reference

Europe PubMed Central

PubMed publication ID

11677234

https://europepmc.org/article/MED/11677234

9 December 2020

5

Lawrence J Marnett

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author name string

William E Boeglin

2

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Jeffery J Prusakiewicz

3

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Scott W Rowlinson

4

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Nigulas Samel

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

4 January 2002

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published in

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volume

277

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issue

1

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page(s)

478-85

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cites work

A single amino acid difference between cyclooxygenase-1 (COX-1) and -2 (COX-2) reverses the selectivity of COX-2 specific inhibitors.

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Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2

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Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents

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Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations

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Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition

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Involvement of arginine 120, glutamate 524, and tyrosine 355 in the binding of arachidonate and 2-phenylpropionic acid inhibitors to the cyclooxygenase active site of ovine prostaglandin endoperoxide H synthase-1.

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Mutation of serine-516 in human prostaglandin G/H synthase-2 to methionine or aspirin acetylation of this residue stimulates 15-R-HETE synthesis

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Analysis of hydroperoxide-induced tyrosyl radicals and lipoxygenase activity in aspirin-treated human prostaglandin H synthase-2

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Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products

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Arginine 120 of prostaglandin G/H synthase-1 is required for the inhibition by nonsteroidal anti-inflammatory drugs containing a carboxylic acid moiety

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Stereospecificity of hydrogen abstraction in the conversion of arachidonic acid to 15R-HETE by aspirin-treated cyclooxygenase-2. Implications for the alignment of substrate in the active site

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Vaccinia-T7 RNA polymerase expression system: evaluation for the expression cloning of plasma membrane transporters

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