Abstract
Complex I deficiency is difficult to treat because of the size and complexity of the multi-subunit enzyme complex. Mutations or deletions in the mitochondrial genome are not amenable to gene therapy. However, animal studies have shown that yeast-derived internal NADH quinone oxidoreductase (Ndi1) can be delivered as a cell-permeable recombinant protein (Tat-Ndi1) that can functionally replace complex I damaged by ischemia/reperfusion. Current and future treatment of disorders affecting complex I are discussed, including the use of Tat-Ndi1.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Cell-Penetrating Peptides / genetics
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Cell-Penetrating Peptides / therapeutic use*
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Electron Transport Complex I / genetics
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Electron Transport Complex I / therapeutic use*
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Humans
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Mitochondrial Diseases / drug therapy*
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Mitochondrial Diseases / enzymology
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Mitochondrial Diseases / genetics
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / therapeutic use*
Substances
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Cell-Penetrating Peptides
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Ndi1 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Electron Transport Complex I