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Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock
Daniel H Craig
, Stephen K Chapman
, Simon Daff
Research output
:
Contribution to journal
›
Article
›
peer-review
100
Citations (Scopus)
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Dive into the research topics of 'Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock'. Together they form a unique fingerprint.
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INIS
electron transfer
100%
nitric oxide
100%
reductases
100%
calmodulin
100%
control
50%
reduction
50%
enzymes
33%
reaction kinetics
33%
oxygenases
33%
cytochromes
33%
electron acceptor
33%
kinases
16%
length
16%
synthesis
16%
oxidation
16%
ligands
16%
increasing
16%
in vivo
16%
steady-state conditions
16%
stimulation
16%
phosphorylation
16%
conformational changes
16%
nadp
16%
polypeptides
16%
Biochemistry, Genetics and Molecular Biology
Reductase
100%
Electron Transport
100%
Oxidoreductase
100%
Nitric Oxide Synthase
100%
Calmodulin
100%
Enzyme
33%
Oxygenase
33%
Cytochrome C
33%
Conformation
16%
Conformational Change
16%
Phosphotransferase
16%
Kinase
16%
Steady State
16%
Nitric Oxide
16%
C-Terminus
16%
Nicotinamide Adenine Dinucleotide Phosphate
16%