Structure of the active site of prostaglandin synthase from studies of depsides: An alternate view

J. M. Gerrard; D. A. Peterson

doi:10.1016/0262-1746(84)90003-9

Structure of the active site of prostaglandin synthase from studies of depsides: An alternate view

J. M. Gerrard
, D. A. Peterson

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Evaluation of the structure of the lichen depside, 4-0-methylcryptochlorophaeic acid, the most potent inhibitor of prostaglandin synthesis known, and its potential interaction with heme supports a model of the active site of prostaglandin synthase initially suggested by studies of arachidonic acid-heme interaction.

Original language	English (US)
Pages (from-to)	139-142
Number of pages	4
Journal	Prostaglandins Leukotrienes and Medicine
Volume	13
Issue number	2
DOIs	https://doi.org/10.1016/0262-1746(84)90003-9
State	Published - Feb 1984
Externally published	Yes

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10.1016/0262-1746(84)90003-9

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title = "Structure of the active site of prostaglandin synthase from studies of depsides: An alternate view",

abstract = "Evaluation of the structure of the lichen depside, 4-0-methylcryptochlorophaeic acid, the most potent inhibitor of prostaglandin synthesis known, and its potential interaction with heme supports a model of the active site of prostaglandin synthase initially suggested by studies of arachidonic acid-heme interaction.",

author = "Gerrard, \{J. M.\} and Peterson, \{D. A.\}",

year = "1984",

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language = "English (US)",

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journal = "Prostaglandins Leukotrienes and Medicine",

issn = "0262-1746",

publisher = "Churchill Livingstone",

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T1 - Structure of the active site of prostaglandin synthase from studies of depsides

T2 - An alternate view

AU - Gerrard, J. M.

AU - Peterson, D. A.

PY - 1984/2

Y1 - 1984/2

N2 - Evaluation of the structure of the lichen depside, 4-0-methylcryptochlorophaeic acid, the most potent inhibitor of prostaglandin synthesis known, and its potential interaction with heme supports a model of the active site of prostaglandin synthase initially suggested by studies of arachidonic acid-heme interaction.

AB - Evaluation of the structure of the lichen depside, 4-0-methylcryptochlorophaeic acid, the most potent inhibitor of prostaglandin synthesis known, and its potential interaction with heme supports a model of the active site of prostaglandin synthase initially suggested by studies of arachidonic acid-heme interaction.

UR - https://www.scopus.com/pages/publications/0021321658

UR - https://www.scopus.com/pages/publications/0021321658#tab=citedBy

U2 - 10.1016/0262-1746(84)90003-9

DO - 10.1016/0262-1746(84)90003-9

M3 - Article

C2 - 6425861

AN - SCOPUS:0021321658

SN - 0262-1746

VL - 13

SP - 139

EP - 142

JO - Prostaglandins Leukotrienes and Medicine

JF - Prostaglandins Leukotrienes and Medicine

IS - 2

ER -

Structure of the active site of prostaglandin synthase from studies of depsides: An alternate view

Abstract

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