Human recombinant mutated forms of the mitochondrial COX assembly Sco2 protein differ from wild-type in physical state and copper binding capacity (Q47198282)

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scientific article published in March 2004

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English	Human recombinant mutated forms of the mitochondrial COX assembly Sco2 protein differ from wild-type in physical state and copper binding capacity	scientific article published in March 2004

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scholarly article

1 reference

Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

Human recombinant mutated forms of the mitochondrial COX assembly Sco2 protein differ from wild-type in physical state and copper binding capacity (English)

1 reference

Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

author name string

Parthena F Foltopoulou

1

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Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

George A Zachariadis

2

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Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

Anastasia S Politou

3

1 reference

Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

Asterios S Tsiftsoglou

4

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Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

Lefkothea C Papadopoulou

5

1 reference

Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

publication date

1 March 2004

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Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

Molecular Genetics and Metabolism

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Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

81

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11 January 2018

http://europepmc.org/abstract/MED/14972329

3

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11 January 2018

http://europepmc.org/abstract/MED/14972329

225-236

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11 January 2018

http://europepmc.org/abstract/MED/14972329

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Mitochondrial respiratory chain diseases and mutations in nuclear DNA: a promising start?

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Oxidative phosphorylation at the fin de siècle

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Cytochrome oxidase in health and disease.

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Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A.

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A new mutation associated with MELAS is located in a mitochondrial DNA polypeptide-coding gene.

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A microdeletion in cytochrome c oxidase (COX) subunit III associated with COX deficiency and recurrent myoglobinuria

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Molecular analysis of cytochrome c oxidase deficiency in Leigh's syndrome.

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A systematic mutation screen of 10 nuclear and 25 mitochondrial candidate genes in 21 patients with cytochrome c oxidase (COX) deficiency shows tRNA(Ser)(UCN) mutations in a subgroup with syndromal encephalopathy

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SURF1, encoding a factor involved in the biogenesis of cytochrome c oxidase, is mutated in Leigh syndrome

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Fatal infantile cardioencephalomyopathy with COX deficiency and mutations in SCO2, a COX assembly gene

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A mutation in the human heme A:farnesyltransferase gene (COX10 ) causes cytochrome c oxidase deficiency

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Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic pathway, causing early-onset fatal hypertrophic cardiomyopathy

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Cytochrome c oxidase deficiency due to mutations in SCO2, encoding a mitochondrial copper-binding protein, is rescued by copper in human myoblasts

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Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein.

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Purification and characterization of yeast Sco1p, a mitochondrial copper protein

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SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae

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Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency.

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Mutagenesis reveals a specific role for Cox17p in copper transport to cytochrome oxidase.

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Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein.

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Characterization and localization of human COX17, a gene involved in mitochondrial copper transport

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Mutational analysis of the mitochondrial copper metallochaperone Cox17

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N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat.

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PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity.

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PHD: predicting one-dimensional protein structure by profile-based neural networks

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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Protein secondary structure prediction based on position-specific scoring matrices

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Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle

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The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex.

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Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes.

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ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling

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SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

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Predicting coiled coils from protein sequences

1 reference

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Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency

1 reference

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Mutation screening in patients with isolated cytochrome c oxidase deficiency

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Homozygosity (E140K) in SCO2 causes delayed infantile onset of cardiomyopathy and neuropathy

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Cytochrome c oxidase deficiency due to a novel SCO2 mutation mimics Werdnig-Hoffmann disease

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p

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Function, structure, and mechanism of intracellular copper trafficking proteins

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Regulated protein degradation in mitochondria

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Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations

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10.1016/J.YMGME.2003.11.006

1 reference

Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

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Europe PubMed Central

11 January 2018

http://europepmc.org/abstract/MED/14972329

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