Mitochondrial translocation of APE1 relies on the MIA pathway. - Test2 - elhamkhani - TriplyDB

Mitochondrial translocation of APE1 relies on the MIA pathway.

Mitochondrial translocation of APE1 relies on the MIA pathway.

http://www.wikidata.org/entity/Q35770659

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Dynamic Regulation of APE1/Ref-1 as a Therapeutic Target Protein Cardiac Cell Senescence and Redox Signaling.DNA damage related crosstalk between the nucleus and mitochondria.The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis.Tumor-associated APE1 variant exhibits reduced complementation efficiency but does not promote cancer cell phenotypes.POLB: A new role of DNA polymerase beta in mitochondrial base excision repair.Homologous recombination-mediated repair of DNA double-strand breaks operates in mammalian mitochondria.DNA polymerase β: A missing link of the base excision repair machinery in mammalian mitochondria.CUX1 Stimulates APE1 Enzymatic Activity and Increases the Resistance of Glioblastoma Cells to the Mono-Alkylating Agent, Temozolomide.Reactive oxygen species stress increases accumulation of tyrosyl-DNA phsosphodiesterase 1 within mitochondria.Placental aging and oxidation damage in a tissue micro-array model: an immunohistochemistry study.

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P2860

Mitochondrial translocation of APE1 relies on the MIA pathway.

http://www.wikidata.org/entity/Q35770659

description

2015 nî lūn-bûn

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2015年論文

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Mitochondrial translocation of APE1 relies on the MIA pathway.

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Mitochondrial translocation of APE1 relies on the MIA pathway.

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Mitochondrial translocation of APE1 relies on the MIA pathway.

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Mitochondrial translocation of APE1 relies on the MIA pathway.

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Mitochondrial translocation of APE1 relies on the MIA pathway.

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Mitochondrial translocation of APE1 relies on the MIA pathway.

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Nucleic Acids Research

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Mitochondrial translocation of APE1 relies on the MIA pathway.

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Michal Wasilewski

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P2860

An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR

Identification and characterization of mitochondrial targeting sequence of human apurinic/apyrimidinic endonuclease 1

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

Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space

Mitochondrial disulfide relay mediates translocation of p53 and partitions its subcellular activity

Normal oxidative damage to mitochondrial and nuclear DNA is extensive

Evolution of the redox function in mammalian apurinic/apyrimidinic endonuclease

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

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

Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins.

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5451-5464

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10.1093/NAR/GKV433

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11

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43

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Agnieszka Chacińska

Arianna Barchiesi

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2015-05-08T00:00:00Z

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276066302

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