Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR - Test2 - elhamkhani - TriplyDB

Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR

Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR

http://www.wikidata.org/entity/Q27667208

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Orphan proteins of unknown function in the mitochondrial intermembrane space proteome: New pathways and metabolic cross-talk Structure of Yeast Sulfhydryl Oxidase Erv1 Reveals Electron Transfer of the Disulfide Relay System in the Mitochondrial Intermembrane Space 77Se Enrichment of Proteins Expands the Biological NMR Toolbox Identification and characterization of mitochondrial Mia40 as an iron-sulfur protein.Mia40 is a trans-site receptor that drives protein import into the mitochondrial intermembrane space by hydrophobic substrate binding.Oxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and disease Cardiac Cell Senescence and Redox Signaling.A small molecule inhibitor of redox-regulated protein translocation into mitochondria Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway.Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space.A discrete pathway for the transfer of intermembrane space proteins across the outer membrane of mitochondria Combining phase information in reciprocal space for molecular replacement with partial models.Mitochondrial translocation of APE1 relies on the MIA pathway.Retro-translocation of mitochondrial intermembrane space proteins Role of twin Cys-Xaa9-Cys motif cysteines in mitochondrial import of the cytochrome C oxidase biogenesis factor Cmc1.The Oxidation Status of Mic19 Regulates MICOS Assembly In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins.Divergence of Erv1-associated mitochondrial import and export pathways in trypanosomes and anaerobic protists.The ubiquitin-proteasome system regulates mitochondrial intermembrane space proteins.Human augmenter of liver regeneration: probing the catalytic mechanism of a flavin-dependent sulfhydryl oxidase.Sulfhydryl oxidases: sources, properties, production and applications.Mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space.Mechanisms of protein sorting in mitochondria Common players in mitochondria biogenesis and neuronal protection against stress-induced apoptosis.The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond.Mechanisms and physiological impact of the dual localization of mitochondrial intermembrane space proteins.Liver-specific deletion of augmenter of liver regeneration accelerates development of steatohepatitis and hepatocellular carcinoma in mice.Oxidative folding: recent developments.Mitochondrial disulfide relay and its substrates: mechanisms in health and disease.Site-specific insertion of selenium into the redox-active disulfide of the flavoprotein augmenter of liver regeneration.Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space.Mitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles.Mia40 is a facile oxidant of unfolded reduced proteins but shows minimal isomerase activity.Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells.Divergent molecular evolution of the mitochondrial sulfhydryl:cytochrome C oxidoreductase Erv in opisthokonts and parasitic protists.Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria.Mia40 and MINOS act in parallel with Ccs1 in the biogenesis of mitochondrial Sod1.Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40.Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40.

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Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR

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2011 nî lūn-bûn

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Molecular recognition and subs ...... process between MIA40 and ALR

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Molecular recognition and subs ...... process between MIA40 and ALR

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Molecular recognition and subs ...... process between MIA40 and ALR

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

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Molecular recognition and subs ...... process between MIA40 and ALR

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Charalambos Pozidis

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Chiara Cefaro

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Eirini Lionaki

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Emmanouela Kallergi

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P2860

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

MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Protein structure prediction servers at University College London

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

Structure of the Human Sulfhydryl Oxidase Augmenter of Liver Regeneration and Characterization of a Human Mutation Causing an Autosomal Recessive Myopathy,

Protein secondary structure prediction based on position-specific scoring matrices

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase.

Novel mitochondrial intermembrane space proteins as substrates of the MIA import pathway.

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Simone Ciofi-Baffoni

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50304281

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