Mia40 targets cysteines in a hydrophobic environment to direct oxidative protein folding in the mitochondria

Nature Communications

Volumn 5, Issue , 2014, Pages

  Koch, Johanna R ^a   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; MITOCHONDRIAL IMPORT AND ASSEMBLY 40 PROTEIN; THIOL OXIDASE; UNCLASSIFIED DRUG; CARRIER PROTEIN; CATION TRANSPORT PROTEIN; CHAPERONE; COX17 PROTEIN, S CEREVISIAE; DISULFIDE; MIA40 PROTEIN, S CEREVISIAE; MITOCHONDRIAL PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

CATALYSIS; CHEMICAL BINDING; HYDROPHOBICITY; MITOCHONDRION; PROTEIN; SULFIDE;

ARTICLE; BINDING KINETICS; BINDING SITE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; DISULFIDE BOND; ENVIRONMENTAL FACTOR; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; MITOCHONDRION; OXIDATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN TARGETING; AMINO ACID SEQUENCE; ANIMAL; BIOLOGICAL MODEL; CHEMICAL PHENOMENA; CHEMISTRY; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PHYSIOLOGY;

AMINO ACID SEQUENCE; ANIMALS; CATION TRANSPORT PROTEINS; CYSTEINE; DISULFIDES; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MITOCHONDRIA; MITOCHONDRIAL MEMBRANE TRANSPORT PROTEINS; MITOCHONDRIAL PROTEINS; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84892184637     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4041     Document Type: Article

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