Investigation of NADH binding, hydride transfer, and NAD(+) dissociation during NADH oxidation by mitochondrial complex I using modified nicotinamide nucleotides.
about
Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex IArginine starvation impairs mitochondrial respiratory function in ASS1-deficient breast cancer cells.Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NAD+ dissociationElemental step thermodynamics of various analogues of indazolium alkaloids to obtaining hydride in acetonitrile.Mechanism-Informed Refinement Reveals Altered Substrate-Binding Mode for Catalytically Competent Nitroreductase.
P2860
Investigation of NADH binding, hydride transfer, and NAD(+) dissociation during NADH oxidation by mitochondrial complex I using modified nicotinamide nucleotides.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
@zh-my
2013年学术文章
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2013年學術文章
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name
Investigation of NADH binding, ...... fied nicotinamide nucleotides.
@en
Investigation of NADH binding, ...... fied nicotinamide nucleotides.
@nl
type
label
Investigation of NADH binding, ...... fied nicotinamide nucleotides.
@en
Investigation of NADH binding, ...... fied nicotinamide nucleotides.
@nl
prefLabel
Investigation of NADH binding, ...... fied nicotinamide nucleotides.
@en
Investigation of NADH binding, ...... fied nicotinamide nucleotides.
@nl
P2860
P356
P1433
P1476
Investigation of NADH binding, ...... fied nicotinamide nucleotides.
@en
P2093
James A Birrell
P2860
P304
P356
10.1021/BI3016873
P407
P50
P577
2013-05-30T00:00:00Z