Distinct dimer interaction and regulation in nitric-oxide synthase types I, II, and III. (Q44016910)

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9 November 2019

title

Distinct dimer interaction and regulation in nitric-oxide synthase types I, II, and III (English)

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9 November 2019

1

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9 November 2019

5

Elizabeth D Getzoff

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Dennis J Stuehr

6

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author name string

Robin J Rosenfeld

2

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9 November 2019

Sanjay Ghosh

3

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9 November 2019

Abigail L Meade

4

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9 November 2019

language of work or name

English

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publication date

4 June 2002

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Journal of Biological Chemistry

9 November 2019

number of pages

11

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based on heuristic

inferred from page(s)

published in

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9 November 2019

volume

277

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9 November 2019

issue

34

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page(s)

31020-31030

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The dual personality of NO.

9 November 2019

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Characterization of heme-deficient neuronal nitric-oxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin.

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Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction

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Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation

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Domains of macrophage N(O) synthase have divergent roles in forming and stabilizing the active dimeric enzyme

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Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer

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Heme iron reduction and catalysis by a nitric oxide synthase heterodimer containing one reductase and two oxygenase domains

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An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity

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Identification, characterization, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases

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Differences in three kinetic parameters underpin the unique catalytic profiles of nitric-oxide synthases I, II, and III.

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Chimeras of nitric-oxide synthase types I and III establish fundamental correlates between heme reduction, heme-NO complex formation, and catalytic activity

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M203749200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12048205%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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