Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import

Cooperativity and protein folding rates

(2010) John J Portman   CURRENT OPINION IN STRUCTURAL BIOLOGY

Mitochondrial Disulfide Bond Formation Is Driven by Intersubunit Electron Transfer in Erv1 and Proofread by Glutathione

(2010) Melanie Bien et al.   MOLECULAR CELL

A novel intermembrane space–targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding

(2009) Dionisia P. Sideris et al.   JOURNAL OF CELL BIOLOGY

Identification of the Signal Directing Tim9 and Tim10 into the Intermembrane Space of Mitochondria

(2009) Dusanka Milenkovic et al.   MOLECULAR BIOLOGY OF THE CELL

MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria

(2009) Lucia Banci et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Structural basis of yeast Tim40/Mia40 as an oxidative translocator in the mitochondrial intermembrane space

(2009) S. Kawano et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Disulfide Formation in the ER and Mitochondria: Two Solutions to a Common Process

(2009) J. Riemer et al.   SCIENCE

Structural and Functional Roles of the Conserved Cysteine Residues of the Redox-regulated Import Receptor Mia40 in the Intermembrane Space of Mitochondria

(2008) Nadia Terziyska et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase

(2008) Diana Stojanovski et al.   JOURNAL OF CELL BIOLOGY