Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol.

Molecular biology of the cell - 1 Oct 2011

Klöppel Christine, Suzuki Yutaka, Kojer Kerstin, Petrungaro Carmelina, Longen Sebastian, Fiedler Sebastian, Keller Sandro, Riemer Jan

Abstract excerpt

Superoxide dismutase 1 (Sod1) is an important antioxidative enzyme that converts superoxide anions to hydrogen peroxide and water. Active Sod1 is a homodimer containing one zinc ion, one copper ion, and one disulfide bond per subunit. Maturation of Sod1 depends on its copper chaperone (Ccs1). Sod1 and Ccs1 are dually localized proteins that reside in the cytosol and in the intermembrane space of mitochondria. The...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytosol
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Membranes

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Superoxide Dismutase-1

Share to Transduction, Genetic

Share to Transformation, Bacterial

Source

Open in PubMed Open full text

Identifiers

PMID: 21865594
DOI: 10.1091/mbc.E11-04-0293
PMCID: PMC3192855

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol.PMID 21865594Read ↗

Import, maturation, and function of SOD1 and its copper chaperone CCS in the mitochondrial intermembrane space.Semantic proximity Read ↗

Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system.Semantic proximity Read ↗

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.Semantic proximity Read ↗

Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria.Semantic proximity Read ↗

Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria.Semantic proximity Read ↗

The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase.Semantic proximity Read ↗

Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Semantic proximity Read ↗

Structural and functional roles of the conserved cysteine residues of the redox-regulated import receptor Mia40 in the intermembrane space of mitochondria.Semantic proximity Read ↗

Conserved and novel functions for Arabidopsis thaliana MIA40 in assembly of proteins in mitochondria and peroxisomes.Semantic proximity Read ↗

The right to choose: multiple pathways for activating copper,zinc superoxide dismutase.Semantic proximity Read ↗

Cmc1p is a conserved mitochondrial twin CX9C protein involved in cytochrome c oxidase biogenesis.Semantic proximity Read ↗

Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.