Cited by 444Mitochondrial Function and PathologyEnzyme Structure and FunctionCoenzyme Q10 studies and effects

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Mitochondrial Respiratory Complex I: Structure, Function and Implication in Human Diseases

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Sharma, Lokendra, Lu, Jianxin, Bai, Yidong·2009·Current Medicinal Chemistry

DOI 10.2174/092986709787846578PMC PMC4706149

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Abstract

Mitochondria are ubiquitous organelles in eukaryotic cells whose primary function is to generate energy supplies in the form of ATP through oxidative phosphorylation. As the entry point for most electrons into the respiratory chain, NADH:ubiquinone oxidoreductase, or complex I, is the largest and least understood component of the mitochondrial oxidative phosphorylation system. Substantial progress has been made in recent years in understanding its subunit composition, its assembly, the interaction among complex I and other respiratory components, and its role in oxidative stress and apoptosis. This review provides an updated overview of the structure of complex I, as well as its cellular functions, and discusses the implication of complex I dysfunction in various human diseases.

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Sequence and organization of the human mitochondrial genome
Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,740
Parkinson's Disease
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
Chronic Parkinsonism in Humans Due to a Product of Meperidine-Analog Synthesis
Langston, J. W., Ballard, P., Tetrud, J. W., & Irwin, I. (1983) · Science · doi:10.1126/science.6823561 · Cited by 4,914
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,777
Mitochondrial control of cell death
Kroemer, G., & Reed, J. C. (2000) · Nature Medicine · doi:10.1038/74994 · Cited by 3,103
Mitochondrial DNA mutation associated with Leber’s hereditary optic neuropathy
Wallace, D. C., Singh, G., Lott, M. T., Hodge, J. A., Schurr, T. G., Lezza, A. M. S., Elsas, L. J., & Nikoskelainen, E. K. (1988) · Science · doi:10.1126/science.3201231 · Cited by 2,440
Untitled work
(2001) · PubMed · Cited by 2,381
Mitochondrial Complex I Deficiency in Parkinson's Disease
Schapira, A. H. V., Cooper, J. M., Dexter, D., Clark, J. B., Jenner, P., & Marsden, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb02325.x · Cited by 2,283
Mitochondria, oxidative stress and cell death
Ott, M., Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0756-2 · Cited by 2,020
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994

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Authors: Sharma, L., Lu, J., & Bai, Y.
Affiliations: The University of Texas at San Antonio Health Science Center (US)
ORCID: Sharma, Lokendra
Bai, Yidong
Venue: Current Medicinal Chemistry
Publisher: Bentham Science Publishers Ltd.
Published: 2009-04-01
Volume: 16
Issue: 10
Pages: 1266-1277
ISSN: 0929-8673 (ISSN-L)
DOI: 10.2174/092986709787846578
PMC: PMC4706149
OpenAlex: W2126962886
Cited by: 438
References: 161
Citations by year: 2026: 41 · 2025: 51 · 2024: 69 · 2023: 52 · 2022: 48 · 2021: 50 · 2020: 42 · 2019: 22 · 2018: 16 · 2017: 15 · 2016: 2 · 2015: 2 · 2014: 1 · 2013: 7 · 2012: 8
FWCI: 0.51
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Current Medicinal Chemistry (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute on Aging (R01AG025223)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Keywords: mitochondrial complex I, complex I, mitochondrial respiratory chain, oxidative phosphorylation, complex I assembly, subunit composition, oxidative stress, apoptosis, complex I dysfunction, human disease
MeSH terms: Animals, Disease, Humans, Apoptosis, Reactive Oxygen Species, Electron Transport Complex I

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Mitochondrial Respiratory Complex I: Structure, Function and Implication in Human Diseases

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