A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

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A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

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A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

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A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

@en

A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

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A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

@en

A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.

@nl

P1476

A cross-domain charge interaction governs the activity of NO synthase

@en

P2093

Claire T Kenney

http://www.w3.org/2001/XMLSchema#string

Dennis J Stuehr

http://www.w3.org/2001/XMLSchema#string

Mekki Bayachou

http://www.w3.org/2001/XMLSchema#string

Mohammad Mahfuzul Haque

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P2860

Electrostatics of nanosystems: application to microtubules and the ribosome

Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase

"Bind and Crawl" Association Mechanism of Leishmania major Peroxidase and Cytochrome c Revealed by Brownian and Molecular Dynamics Simulations

The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase

A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism

Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase.

Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.

Enzymatic function of nitric oxide synthases.

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

P304

4545-4554

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P31

scholarly article

P356

10.1074/JBC.RA117.000635

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

293

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P50

J Tejero

P577

2018-02-02T00:00:00Z

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P698

29414777

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P932

5868255

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