Cysteine-200 Of Human Inducible Nitric Oxide Synthase Is Essential For Dimerization Of Haem Domains And For Binding Of Haem, Nitroarginine And Tetrahydrobiopterin

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dc.contributor.author Cubberley, R
dc.contributor.author Alderton, W
dc.contributor.author Boyhan, A
dc.contributor.author Charles, IG
dc.contributor.author Lowe, P
dc.contributor.author Old, R
dc.date.accessioned 2011-02-07T06:20:18Z
dc.date.issued 1997-01
dc.identifier.citation Biochemical Journal, 1997, 323 (1), pp. 141 - 146
dc.identifier.issn 0264-6021
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/13267
dc.description.abstract Nitric oxide synthase (EC 1.14.13.39) is a homodimer. Limited proteolysis has previously shown that it consists of two major domains. The C-terminal or reductase domain binds FMN, FAD and NADPH. The N-terminal or oxygenase domain is known to bind arginin
dc.format Scott McWhirter
dc.publisher Portland Press
dc.title Cysteine-200 Of Human Inducible Nitric Oxide Synthase Is Essential For Dimerization Of Haem Domains And For Binding Of Haem, Nitroarginine And Tetrahydrobiopterin
dc.type Journal Article
dc.parent Biochemical Journal
dc.journal.volume 1
dc.journal.volume 323
dc.journal.number 1 en_US
dc.publocation London, UK en_US
dc.identifier.startpage 141 en_US
dc.identifier.endpage 146 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 0601 Biochemistry and Cell Biology
dc.personcode 109028
dc.percentage 100 en_US
dc.classification.name Biochemistry and Cell Biology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity ISI:A1997WR48800020 en_US
dc.location.activity ISI:A1997WR48800020
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - i3
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc false
utslib.collection.history Closed (ID: 3)


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