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Human Complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect
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“The second enzyme is located near the mitochondrial inner membrane. This is a SOD that binds manganese in its catalytic centre (SOD2 or Mn-SOD) [71,72].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [71]
Citations
Cites
The Metabolic and Molecular Bases of Inherited Disease
Scriver, R. C. (1995) · Medical Entomology and Zoology · Cited by 12,101
The Metabolic Basis of Inherited Disease.
(1988) · Annals of Internal Medicine · doi:10.7326/0003-4819-108-3-503_7 · Cited by 7,807
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913
Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
Hockenbery, D., Nuñez, G., Milliman, C., Schreiber, R. D., & Korsmeyer, S. J. (1990) · Nature · doi:10.1038/348334a0 · Cited by 3,720
Bcl-2 functions in an antioxidant pathway to prevent apoptosis
Hockenbery, D. M., Oltvai, Z. N., Yin, X., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,402
Zou, H., Henzel, W. J., Liu, X., Lutschg, A., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80501-2 · Cited by 3,145
MERRITT, A. D. (2011) · Springer eBooks · doi:10.1007/springerreference_33432 · Cited by 2,522
Goto, Y.-I., Nonaka, I., & Horai, S. (1990) · Nature · doi:10.1038/348651a0 · Cited by 2,070
THE MITOCHONDRIAL ELECTRON TRANSPORT AND OXIDATIVE PHOSPHORYLATION SYSTEM
Hatefi, Y. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.005055 · Cited by 1,650
Shoffner, J. M., Lott, M. T., Lezza, A. M. S., Seibel, P., Ballinger, S. W., & Wallace, D. C. (1990) · Cell · doi:10.1016/0092-8674(90)90059-n · Cited by 1,476
Research works printed but not linked: 6
- Robinson, 1994, Lacticacidemia, Biochim. Biophys. Acta, 1182, 237
- Sardanelli, 1995, Phosphorylation of an 18 kDa subunit of bovine heart complex I by a cAMP dependent kinase, FEBS Lett., 377, 470
- Chomyn, 1988, The site of synthesis of the iron–sulfur subunits of the flavoprotein and iron protein factions of human NADH dehydrogenase, J. Biol. Chem., 31, 16395, 10.1016/S0021-9258(18)37606-3 · DOI
- De Vries, 1996, Genetic and biochemical impairment of mitochondrial complex I activity in a family with Leber Hereditary Optic Neuropathy and Hereditary Spastic Dystonia, Am. J. Hum. Genet., 58, 703
- Jun, 1994, A mitochondrial DNA mutation at nucleotide pair 14 459 of the NADH dehydrogenase subunit 6 gene associated with maternally inherited Leber Hereditary Optic Neuropathy and Dystonia, Proc. Natl. Acad. Sci. U.S.A., 91, 6206, 10.1073/pnas.91.13.6206 · DOI
- Beyer, 1991, An analysis of the role of coenzyme Q in free radical generation and as an oxidant, Biochem. Cell. Biol., 70, 343
Cited by
Sorted by citations
Items 101–200 of 223
Ahlers, P. M., Garofano, A., Kerscher, S., & Brandt, U. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00160-2 · Cited by 51
Exploring the Catalytic Core of Complex I by Yarrowia lipolytica Yeast Genetics
Kerscher, S., Kashani‐Poor, N., Zwicker, K., Zickermann, V., & Brandt, U. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1010726818165 · Cited by 51
Tsukada, H., Nishiyama, S., Ohba, H., Kanazawa, M., Kakiuchi, T., & Harada, N. (2014) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-014-2821-8 · Cited by 49
The energy-transducing NADH: quinone oxidoreductase, complex I
Yano, T. (2002) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(02)00011-0 · Cited by 47
Roles of reactive oxygen species and selected antioxidants in regulation of cellular metabolism.
Stańczyk, M. B., Gromadzińska, J., & Wąsowicz, W. (2005) · PubMed · Cited by 44
Ma, Y., Mehta, S. L., Lu, B., & Li, P. A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.06.019 · Cited by 43
Someya, S., Yamasoba, T., Prolla, T. A., & Tanokura, M. (2007) · Brain Research · doi:10.1016/j.brainres.2007.08.090 · Cited by 43
Clauzure, M., Valdivieso, Á. G., Massip-Copiz, M. M., Schulman, G., Teiber, M. L., & Santa-Coloma, T. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099257 · Cited by 44
Siriwardena, K., MacKay, N., Levandovskiy, V., Blasér, S., Raiman, J., Kantor, P. F., Ackerley, C. A., Robinson, B. H., Schulze, A., & Cameron, J. M. (2012) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2012.11.282 · Cited by 41
Self-citationFolbergrová, J., Ješina, P., Kubová, H., & Otáhal, J. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0924-0 · Cited by 42
Kerscher, S., Grgic, L., Garofano, A., & Brandt, U. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.07.006 · Cited by 41
Grad, L. I., Sayles, L. C., & Lemire, B. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506939102 · Cited by 41
DeCorby, A., Gášková, D., Sayles, L. C., & Lemire, B. D. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.07.003 · Cited by 40
Complex I and the cAMP Cascade in Human Physiopathology
Papa, S., Scacco, S., Sardanelli, A. M., Petruzzella, V., Vergari, R., Signorile, A., & Technikova-Dobrova, Z. (2002) · Bioscience Reports · doi:10.1023/a:1016004921277 · Cited by 40
A novel mutation in NDUFS4 causes Leigh syndrome in an Ashkenazi Jewish family
Anderson, S. L., Chung, W. K., Frezzo, J. A., Papp, J., Ekstein, J., DiMauro, S., & Rubin, B. Y. (2008) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-008-1049-9 · Cited by 39
On Complex I and Other NADH:Ubiquinone Reductases of Neurospora crassa Mitochondria
Videira, A., & Duarte, M. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1010778802236 · Cited by 38
Procaccio, V., Mousson, B., Beugnot, R., Duborjal, H., Feillet, F., Putet, G., Pignot‐Paintrand, I., Lombès, A., de Coo, I. F. M., Smeets, H. J. M., et al. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6184 · Cited by 36
The Effect of Coenzyme Q10 Therapy in Parkinson Disease Could Be Symptomatic
Horstink, M. W. I. M., & van Engelen, B. G. M. (2003) · Archives of Neurology · doi:10.1001/archneur.60.8.1170-b · Cited by 37
Valdivieso, Á. G., Dugour, A. V., Sotomayor, V., Clauzure, M., Figueroa, J. M., & Santa-Coloma, T. A. (2018) · Redox Biology · doi:10.1016/j.redox.2018.03.006 · Cited by 37
Edmunds, L. R., Sharma, L., Wang, H., Kang, A., D'Souza, S. S., Lu, J. L., McLaughlin, M., Dolezal, J. M., Gao, X., Weintraub, S. T., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134049 · Cited by 35
Rolandic Mitochondrial Encephalomyelopathy and MT-ND3 Mutations
Werner, K., Morel, C. F., Kirton, A., Benseler, S. M., Shoffner, J. M., Addis, J., Robinson, B. H., Burrowes, D. M., Blasér, S., Epstein, L. G., et al. (2009) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2009.02.010 · Cited by 35
Self-citation[Mitochondrial reactive oxygen species].
Nishikawa, T., Kukidome, D., & Araki, E. (2016) · PubMed · Cited by 38
Migliore, L. (2003) · Mutagenesis · doi:10.1093/mutage/geg036 · Cited by 34
Functional genetics of Yarrowia lipolytica
Barth, G., Beckerich, J.-M., Domínguez, Á., Kerscher, S., Ogrydziak, D. M., Titorenko, V. I., & Gaillardin, C. M. (2003) · Topics in current genetics · doi:10.1007/3-540-37003-x_8 · Cited by 34
Ali, M. Z., & Dholaniya, P. S. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105344 · Cited by 33
Mitochondrial fusion increases the mitochondrial DNA copy number in budding yeast
Hori, A., Yoshida, M., & Ling, F. (2011) · Genes to Cells · doi:10.1111/j.1365-2443.2011.01504.x · Cited by 32
Gu, Q., Xu, F., Orgil, B., Khuchua, Z. A., Munkhsaikhan, U., Johnson, J. N., Alberson, N. R., Pierre, J. F., Black, D. D., Dong, D., et al. (2021) · Physiological Genomics · doi:10.1152/physiolgenomics.00066.2021 · Cited by 32
The 24‐kDa iron–sulphur subunit of complex I is required for enzyme activity
Almeida, T., Duarte, M., Melo, A. M. P., & Videira, A. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00668.x · Cited by 32
Errores congénitos del metabolismo: ¿causa de estrés oxidativo?
Colomé, C., Sierra, C., & Vilaseca, M. A. (2000) · Medicina Clínica · doi:10.1016/s0025-7753(00)71479-5 · Cited by 31
Respiratory Complex I: Structure, Redox Components, and Possible Mechanisms of Energy Transduction
Vinogradov, A. D. (2001) · Biochemistry (Moscow) · doi:10.1023/a:1012476728710 · Cited by 32
Juo, S. H., Lu, M., Bai, R., Liao, Y., Trieu, R. B., Yu, M., & Wong, L. C. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.01.001 · Cited by 29
Mitochondrial Metabolism and Aging in Yeast
Baccolo, G., Stamerra, G., Pellegrino-Coppola, D., Orlandi, I., & Vai, M. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.001 · Cited by 33
The expanding spectrum of nuclear gene mutations in mitochondrial disorders
Zeviani, M. (2001) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.2001.0278 · Cited by 28
Agrochemicals, α-Synuclein, and Parkinson’s Disease
Silva, B. A., Breydo, L., Fink, A. L., & Uversky, V. N. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8333-2 · Cited by 28
Sala, G., Trombin, F., Beretta, S., Tremolizzo, L., Presutto, P., Montopoli, M., Fantin, M., Martinuzzi, A., Carelli, V., & Ferrarese, C. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21773 · Cited by 28
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el Azzouzi, H., van Oort, R. J., van der Nagel, R., Sluiter, W. J., Bergmann, M., & Windt, L. J. D. (2009) · European Journal of Heart Failure · doi:10.1093/eurjhf/hfp165 · Cited by 28
Mitrofanov, K. Y., Zhelankin, A. V., Shiganova, G. M., Sazonova, M. A., Bobryshev, Y. V., Postnov, A. Y., Sobenin, I. A., & Orekhov, A. N. (2015) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2015.12.003 · Cited by 29
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Kannan, K., & Jain, S. K. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/a:1024172525123 · Cited by 25
Kim, M. H., Lee, H. J., Lee, S., Lee, H., Huh, J., Bae, Y. C., & Lee, D. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00148-19 · Cited by 25
Baharudin, N. T., Jaafar, H., & Zainuddin, Z. (2012) · Europe PMC (PubMed Central) · Cited by 25
Paterson, A. W. J., Curtis, J. C., & MacLeod, N. K. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05123.x · Cited by 26
Zhou, Y., Li, L., Feng, F., Yuan, H. M., Gao, D., Fu, L.-A., & Zhou, F. G. (2013) · Journal of Surgical Research · doi:10.1016/j.jss.2013.06.044 · Cited by 23
Mitochondrial genome and human mitochondrial diseases
Mazunin, I., Volodko, N. V., Starikovskaya, E. B., & Sukernik, R. I. (2010) · Molecular Biology · doi:10.1134/s0026893310050018 · Cited by 23
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Bajracharya, R., Youngson, N. A., & Ballard, J. W. O. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081850 · Cited by 24
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Lukyanova, L. D. (2013) · Open Journal of Endocrine and Metabolic Diseases · doi:10.4236/ojemd.2013.32a004 · Cited by 22
Kanazawa, M., Ohba, H., Nishiyama, S., Kakiuchi, T., & Tsukada, H. (2017) · Journal of Nuclear Medicine · doi:10.2967/jnumed.116.189159 · Cited by 21
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Parihar, P., & Parihar, M. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9588-x · Cited by 16
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Piemonte, F., Casali, C., Carrozzo, R., Schägger, H., Patrono, C., Tessa, A., Tozzi, G., Cricchi, F., Capua, M. D., Siciliano, G., et al. (2001) · Neuromuscular Disorders · doi:10.1016/s0960-8966(01)00214-0 · Cited by 18
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Baghel, B., Kumari, B., Bhattacharjee, A., Sharma, S., & Roy, P. K. (2025) · 3 Biotech · doi:10.1007/s13205-025-04264-y · Cited by 3
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Urban, M. K. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4377-2787-6.00009-7 · Cited by 2
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Metadata
- Authors
- Robinson, B. H.
- Affiliations
- University of Toronto (CA)
- Corresponding author
- Robinson, Brian H
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 1998-05
- Volume
- 1364
- Issue
- 2
- Pages
- 271-286
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2067124266
- Cited by
- 223
- References
- 115
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 2 · 2022: 5 · 2021: 5 · 2020: 1 · 2019: 7 · 2018: 5 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 5 · 2013: 6 · 2012: 6
- FWCI
- 1.13
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Heart and Stroke Foundation of Canada
- Australian Government
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Keywords
- complex I deficiency, mitochondrial disease, clinical spectrum, oxygen free radicals, oxidative stress, lactic acidosis, optic neuropathy, exercise intolerance, mitochondrial DNA, nuclear DNA
- MeSH terms
- Free Radicals, Humans, Metabolism, Inborn Errors, NAD(P)H Dehydrogenase (Quinone)
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