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Cryo-EM structure of human mitochondrial trifunctional protein

Cryo-EM structure of human mitochondrial trifunctional protein

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Cryo-EM structure of human mitochondrial trifunctional protein

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article published in the Proce ...... f the United States of America

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article publié dans les Procee ...... f the United States of America

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im Juli 2018 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована в липні 2018

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Cryo-EM structure of human mitochondrial trifunctional protein

@en

Cryo-EM structure of human mitochondrial trifunctional protein

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Cryo-EM structure of human mitochondrial trifunctional protein

@en

Cryo-EM structure of human mitochondrial trifunctional protein

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Cryo-EM structure of human mitochondrial trifunctional protein

@en

Cryo-EM structure of human mitochondrial trifunctional protein

@nl

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PNAS.1801252115

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Proceedings of the National Academy of Sciences of the United States of America

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Cryo-EM structure of human mitochondrial trifunctional protein

@en

P2093

Kai Liang

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

Pulan Liu

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

Xiao Wang

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

Xiao-Wei Chen

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P2860

Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme

The thiolase reaction mechanism: the importance of Asn316 and His348 for stabilizing the enolate intermediate of the Claisen condensation

Structure of mycobacterial β-oxidation trifunctional enzyme reveals its altered assembly and putative substrate channeling pathway

UCSF Chimera--a visualization system for exploratory research and analysis

EMAN2: an extensible image processing suite for electron microscopy

Features and development of Coot

General mitochondrial trifunctional protein (TFP) deficiency as a result of either alpha- or beta-subunit mutations exhibits similar phenotypes because mutations in either subunit alter TFP complex expression and subunit turnover

Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations

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7039-7044

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scholarly article

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10.1073/PNAS.1801252115

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27

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115

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2018-06-18T00:00:00Z

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29915090

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protein structure

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6142257

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