Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space.
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Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein importStructural basis of yeast Tim40/Mia40 as an oxidative translocator in the mitochondrial intermembrane spaceMolecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALRIdentification and characterization of mitochondrial Mia40 as an iron-sulfur protein.The zinc-binding protein Hot13 promotes oxidation of the mitochondrial import receptor Mia40Atp23 biogenesis reveals a chaperone-like folding activity of Mia40 in the IMS of mitochondria.Oxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and diseaseCellular disulfide bond formation in bioactive peptides and proteinsImporting mitochondrial proteins: machineries and mechanismsRole of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane.From structure to redox: The diverse functional roles of disulfides and implications in disease.Redox regulation of protein folding in the mitochondrial intermembrane space.Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway.Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay systemMitochondrial translocation of APE1 relies on the MIA pathway.The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis.Role of twin Cys-Xaa9-Cys motif cysteines in mitochondrial import of the cytochrome C oxidase biogenesis factor Cmc1.In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins.The ubiquitin-proteasome system regulates mitochondrial intermembrane space proteins.Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidaseFolding and biogenesis of mitochondrial small Tim proteins.Mitochondrial biogenesis, switching the sorting pathway of the intermembrane space receptor Mia40.Reconstitution of the mia40-erv1 oxidative folding pathway for the small tim proteins.Augmenter of liver regeneration: substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space.The power of yeast to model diseases of the powerhouse of the cell.The coiled coil-helix-coiled coil-helix proteins may be redox proteins.Disulphide bond formation in the intermembrane space of mitochondria.Redox-regulation of protein import into chloroplasts and mitochondria: similarities and differences.Mechanisms of protein sorting in mitochondriaMitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles.Identification of the signal directing Tim9 and Tim10 into the intermembrane space of mitochondria.The rubella virus capsid protein inhibits mitochondrial import.Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria.Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins.Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40.Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space.Structural and functional roles of the conserved cysteine residues of the redox-regulated import receptor Mia40 in the intermembrane space of mitochondria.A single-cysteine mutant and chimeras of essential Leishmania Erv can complement the loss of Erv1 but not of Mia40 in yeast.Biogenesis of yeast Mia40 - uncoupling folding from import and atypical recognition features.
P2860
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P2860
Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Functional characterization of ...... chondrial intermembrane space.
@en
Functional characterization of ...... chondrial intermembrane space.
@nl
type
label
Functional characterization of ...... chondrial intermembrane space.
@en
Functional characterization of ...... chondrial intermembrane space.
@nl
prefLabel
Functional characterization of ...... chondrial intermembrane space.
@en
Functional characterization of ...... chondrial intermembrane space.
@nl
P2093
P2860
P356
P1476
Functional characterization of ...... chondrial intermembrane space.
@en
P2093
Barbara Grumbt
Lars Israel
Nadia Terziyska
Vincent Stroobant
P2860
P304
37461-37470
P356
10.1074/JBC.M707439200
P407
P577
2007-10-24T00:00:00Z