Identification of the Catalytic Residue of Rat Acyl-CoA Dehydrogenase 9 by Site-Directed Mutagenesis.

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Identification of the Catalytic Residue of Rat Acyl-CoA Dehydrogenase 9 by Site-Directed Mutagenesis.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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Identification of the Catalyti ...... by Site-Directed Mutagenesis.

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Identification of the Catalyti ...... by Site-Directed Mutagenesis.

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Identification of the Catalyti ...... by Site-Directed Mutagenesis.

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Identification of the Catalyti ...... by Site-Directed Mutagenesis.

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Identification of the Catalyti ...... by Site-Directed Mutagenesis.

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Identification of the Catalyti ...... by Site-Directed Mutagenesis.

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P1476

Identification of the Catalyti ...... by Site-Directed Mutagenesis.

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P2093

Jia Zeng

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

Senwen Deng

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

Yiping Wang

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P2860

Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I

Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase

A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Intrinsic isomerase activity of medium-chain acyl-CoA dehydrogenase

Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family.

Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids.

Exome sequencing identifies ACAD9 mutations as a cause of complex I deficiency.

Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain.

P2888

s12010-016-2392-1

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1198-1207

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scholarly article

P356

10.1007/S12010-016-2392-1

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P433

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P478

182

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P577

2017-01-13T00:00:00Z

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P698

28084602

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