Mitochondrial respiratory complex I: Structure, function and implication in human diseases

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 9,640 · see citing works

Parkinson's Disease

Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469 · see citing works

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 · see citing works

Chronic systemic pesticide exposure reproduces features of Parkinson's disease

Betarbet, R., Sherer, T., Mackenzie, G., Garcia-Osuna, M., Panov, A., & Greenamyre, J. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,797 · see citing works

Mitochondrial control of cell death

Kroemer, G., & Reed, J. C. (2000) · Nature Medicine · doi:10.1038/74994 · Cited by 3,103 · see citing works

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 · see citing works

Untitled work

(2001) · PubMed · Cited by 2,381 · see citing works

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 · see citing works

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 · see citing works

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 1,976 · see citing works

Mitochondrial DNA mutations in human disease

Taylor, R. W., & Turnbull, D. M. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1606 · Cited by 1,866 · see citing works

MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE

Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757 · see citing works

Generation of reactive oxygen species by the mitochondrial electron transport chain

Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260 · see citing works

Mitochondrial reactive oxygen species in cell death signaling

Fleury, C., Mignotte, B., & Vayssière, J. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01369-x · Cited by 1,069 · see citing works

Somatic mutations of the mitochondrial genome in human colorectal tumours

Polyák, K., Li, Y., Zhu, H., Christoph Lengauer, C., Willson, J. K. V., Markowitz, S. D., Trush, M. A., Kinzler, K. W., & Vogelstein, B. (1998) · Nature Genetics · doi:10.1038/3108 · Cited by 834 · see citing works

mtDNA mutations increase tumorigenicity in prostate cancer

Petros, J. A., Baumann, A. K., Ruiz‐Pesini, E., Amin, M. B., Sun, C. Q., Hall, J., Lim, S.-D., Issa, M. M., Flanders, W. D., Hosseini, S. H., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408894102 · Cited by 834 · see citing works

Structure of the Hydrophilic Domain of Respiratory Complex I from <i>Thermus thermophilus</i>

Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763 · see citing works

Parkinson's Disease Brain Mitochondrial Complex I Has Oxidatively Damaged Subunits and Is Functionally Impaired and Misassembled

Keeney, P., Xie, J., Capaldi, R., & Bennett, J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0984-06.2006 · Cited by 757 · see citing works

AIF deficiency compromises oxidative phosphorylation

Vahsen, N., Candé, C., Brière, J.-J., Bénit, P., Joza, N. A., Larochette, N., Mastroberardino, P. G., Péquignot, M. O., Casares, N., Lazar, V., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600461 · Cited by 622 · see citing works

Disruption of Mitochondrial Function during Apoptosis Is Mediated by Caspase Cleavage of the p75 Subunit of Complex I of the Electron Transport Chain

Ricci, J., Muñoz‐Pinedo, C., FITZGERALD, P. J., Bailly‐Maitre, B., Perkins, G. A., Yadava, N., Scheffler, I. E., Ellisman, M. H., & Green, D. R. (2004) · Cell · doi:10.1016/j.cell.2004.05.008 · Cited by 602 · see citing works

Mitochondrial DNA mutations in human cancer

Chatterjee, A., Mambo, E., & Sidransky, D. (2006) · Oncogene · doi:10.1038/sj.onc.1209604 · Cited by 586 · see citing works

Complex I Is the Major Site of Mitochondrial Superoxide Production by Paraquat

Cochemé, H. M., & Murphy, M. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708597200 · Cited by 563 · see citing works

Mitochondria as all‐round players of the calcium game

Rizzuto, R., Bernardi, P., & Pozzan, T. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00037.x · Cited by 562 · see citing works

Targeting programmed cell death in neurodegenerative diseases

Vila, M., & Przedborski, S. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1100 · Cited by 545 · see citing works

Inhibitors of NADH–ubiquinone reductase: an overview

Esposti, M. D. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00029-2 · Cited by 530 · see citing works

Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase

Chomyn, A., Mariottini, P., Cleeter, M. W. J., RAGAN, C. I., Matsuno‐Yagi, A., Hatefi, Y., Doolittle, R. F., & Attardi, G. M. (1985) · Nature · doi:10.1038/314592a0 · Cited by 528 · see citing works

The respiratory‐chain NADH dehydrogenase (complex I) of mitochondria

Weiss, H., Friedrich, T., Hofhaus, G., & Preis, D. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15945.x · Cited by 498 · see citing works

Bovine Complex I Is a Complex of 45 Different Subunits

Carroll, J., Fearnley, I. M., Skehel, M. J., Shannon, R. J., Hirst, J., & Walker, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607135200 · Cited by 486 · see citing works

Respiratory Complex III Is Required to Maintain Complex I in Mammalian Mitochondria

Acín‐Pérez, R., Bayona‐Bafaluy, M. P., Fernández‐Silva, P., Moreno‐Loshuertos, R., Martos, A. P., Bruno, C., Moraes, C. T., & Enrı́quez, J. A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00124-8 · Cited by 475 · see citing works

Mitochondrial DNA mutations in human disease

DiMauro, S., & Schon, E. A. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1392 · Cited by 414 · see citing works

NADH Oxidase Activity of Mitochondrial Apoptosis-inducing Factor

Miramar, M. D., Costantini, P., Ravagnan, L., Saraiva, L. M., Haouzi, D., Brothers, G. M., Penninger, J. M., Peleato, M. L., Kroemer, G., & Susín, S. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010498200 · Cited by 388 · see citing works

The nuclear encoded subunits of complex I from bovine heart mitochondria

Hirst, J., Carroll, J., Fearnley, I. M., Shannon, R. J., & Walker, J. E. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(03)00059-8 · Cited by 384 · see citing works

Mitochondrial respiration defects in cancer cells cause activation of Akt survival pathway through a redox-mediated mechanism

Pelicano, H., Xu, R., Du, M., Feng, L., Sasaki, R., Carew, J. S., Hu, Y., Ramdas, L., Hu, L., Keating, M. J., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512100 · Cited by 382 · see citing works

Bax ablation prevents dopaminergic neurodegeneration in the 1-methyl- 4-phenyl-1,2,3,6-tetrahydropyridine mouse model of Parkinson's disease

Vila, M., Jackson-Lewis, V. R., Vukosavić, S., Djaldetti, R., Liberatore, G. T., Offen, D., Korsmeyer, S. J., & Przedborski, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051633998 · Cited by 372 · see citing works

Studies on the Electron Transfer System

Hatefi, Y., Haavik, A. G., & Griffiths, D. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83761-4 · Cited by 370 · see citing works

Respiratory chain supercomplexes of mitochondria and bacteria

Schägger, H. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00271-2 · Cited by 363 · see citing works

URF6, Last Unidentified Reading Frame of Human mtDNA, Codes for an NADH Dehydrogenase Subunit

Chomyn, A., Cleeter, M. W. J., Ragan, C., Riley, M., Doolittle, R. F., & Attardi, G. M. (1986) · Science · doi:10.1126/science.3764430 · Cited by 348 · see citing works

Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 å in ice

Grigorieff, N. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1668 · Cited by 336 · see citing works

Mitochondrial DNA transmission of the mitochondrial defect in Parkinson's disease

Gu, M., Cooper, J. A. D., Taanman, J., & Schapira, A. H. V. (1998) · Annals of Neurology · doi:10.1002/ana.410440207 · Cited by 313 · see citing works

The production of reactive oxygen species by complex I

Hirst, J., King, M. S., & Pryde, K. R. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360976 · Cited by 312 · see citing works

Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins

Fearnley, I. M., & Walker, J. E. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(92)90001-i · Cited by 308 · see citing works

The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron–sulfur cluster N2

Genova, M. L., Ventura, B., Giuliano, G., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02850-2 · Cited by 297 · see citing works

Complex I Binding by a Virally Encoded RNA Regulates Mitochondria-Induced Cell Death

Reeves, M., Davies, A., Mcsharry, B. P., Wilkinson, G., & Sinclair, J. (2007) · Science · doi:10.1126/science.1142984 · Cited by 297 · see citing works

The 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model: a tool to explore the pathogenesis of Parkinson's disease.

Przedborski, S., & Vila, M. (2003) · PubMed · Cited by 286 · see citing works

A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy

Ogilvie, I. M. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26020 · Cited by 279 · see citing works

Clinical and molecular findings in children with complex I deficiency

Bugiani, M., Invernizzi, F., Alberio, S., Briem, E., Lamantea, E., Carrara, F., Moroni, I., Farina, L., Spada, M., Donati, M. A., et al. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.09.006 · Cited by 264 · see citing works

Analysis of the Assembly Profiles for Mitochondrial- and Nuclear-DNA-Encoded Subunits into Complex I

Lazarou, M., McKenzie, M., Ohtake, A., Thorburn, D. R., & Ryan, M. T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00074-07 · Cited by 254 · see citing works

GRIM-19, a Cell Death Regulatory Gene Product, Is a Subunit of Bovine Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I)

Fearnley, I. M., Carroll, J., Shannon, R. J., Runswick, M. J., Walker, J. E., & Hirst, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100444200 · Cited by 247 · see citing works

A heteroplasmic, not homoplasmic, mitochondrial DNA mutation promotes tumorigenesis via alteration in reactive oxygen species generation and apoptosis

Park, J. S., Sharma, L. K., Li, H., Xiang, R., Holstein, D. M., Wu, J., Lechleiter, J. D., Naylor, S. L., Deng, J. J., Lü, J., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp069 · Cited by 243 · see citing works

Dominant cell death induction by extramitochondrially targeted apoptosis‐inducing factor

Loeffler, M. W., Daugas, É., Susín, S. A., Zamzami, N., Métivier, D., Nieminen, A., Brothers, G. M., Penninger, J. M., & Kroemer, G. (2001) · The FASEB Journal · doi:10.1096/fj.00-0388com · Cited by 241 · see citing works

Cytochrome c Oxidase Is Required for the Assembly/Stability of Respiratory Complex I in Mouse Fibroblasts

Díaz, F., Fukui, H., García, S., & Moraes, C. T. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01767-05 · Cited by 236 · see citing works

Assembly of Respiratory Complexes I, III, and IV into NADH Oxidase Supercomplex Stabilizes Complex I in Paracoccus denitrificans

Stroh, A., Anderka, O., Pfeiffer, K., Yagi, T., Finel, M., Ludwig, B., & Schägger, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309505200 · Cited by 231 · see citing works

Mitochondrial DNA Alterations in Cancer

Copeland, W. C., Wachsman, J. T., Johnson, F. M., & Penta, J. S. (2002) · Cancer Investigation · doi:10.1081/cnv-120002155 · Cited by 230 · see citing works

Tracing the Evolution of a Large Protein Complex in the Eukaryotes, NADH:Ubiquinone Oxidoreductase (Complex I)

Gabaldón, T., Rainey, D. Y., & Huynen, M. A. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.067 · Cited by 224 · see citing works

Defective Oxidative Phosphorylation in Thyroid Oncocytic Carcinoma Is Associated with Pathogenic Mitochondrial DNA Mutations Affecting Complexes I and III

Bonora, E., Porcelli, A. M., Gasparre, G., Biondi, A., Ghelli, A. M., Carelli, V., Baracca, A., Tallini, G., Martinuzzi, A., Lenaz, G., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0171 · Cited by 224 · see citing works

Mitochondrial DNA in Aging and Disease

Wallace, D. C. (1997) · Scientific American · doi:10.1038/scientificamerican0897-40 · Cited by 222 · see citing works

Why do mitochondria synthesize fatty acids? Evidence for involvement in lipoic acid production

Wada, H., Shintani, D. K., & Ohlrogge, J. B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.4.1591 · Cited by 220 · see citing works

Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency

Ugalde, C. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh071 · Cited by 216 · see citing works

Somatic and germline mutation in GRIM-19, a dual function gene involved in mitochondrial metabolism and cell death, is linked to mitochondrion-rich (Hürthle cell) tumours of the thyroid

Máximo, V., Botelho, T. O., Capela, J., Soares, P., Lima, J. P., Taveira, A., Amaro, T., Barbosa, A. P., Preto, A., Harach, H. R., et al. (2005) · British Journal of Cancer · doi:10.1038/sj.bjc.6602547 · Cited by 212 · see citing works

Assembly of mitochondrial complex I and defects in disease

Lazarou, M., Thorburn, D. R., Ryan, M. T., & McKenzie, M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.04.015 · Cited by 212 · see citing works

Granzyme A Cleaves a Mitochondrial Complex I Protein to Initiate Caspase-Independent Cell Death

Martinvalet, D., Dykxhoorn, D. M., Ferrini, R., & Lieberman, J. (2008) · Cell · doi:10.1016/j.cell.2008.03.032 · Cited by 208 · see citing works

Phosphorylation of the 6-Phosphofructo-2-Kinase/Fructose 2,6-Bisphosphatase/PFKFB3 Family of Glycolytic Regulators in Human Cancer

Bando, H., Atsumi, T., Nishio, T., Niwa, H., Mishima, S., Shimizu, C., Yoshioka, N., Bucala, R., & Koike, T. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-0149 · Cited by 208 · see citing works

Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction

Brandt, U. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(96)00141-7 · Cited by 206 · see citing works

GRIM-19, a Cell Death Regulatory Protein, Is Essential for Assembly and Function of Mitochondrial Complex I

Huang, G., Lu, H., Hao, A., Ng, D. C. H., Ponniah, S., Guo, K., Lufei, C., Zeng, Q., & Cao, X. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8447-8456.2004 · Cited by 202 · see citing works

Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assemblyPreprint

Vogel, R. O., Janssen, R. J. R. J., van den Brand, M. A. M., Dieteren, C. E. J., Verkaart, S., Koopman, W. J. H., Willems, P. H. G. M., Pluk, W., van den Heuvel, L. P. W. J., Smeitink, J. A. M., et al. (2007) · Genes & Development · doi:10.1101/gad.408407 · Cited by 195 · see citing works

Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (Complex I)

Hofhaus, G., Weiss, H., & Leonard, K. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)80190-6 · Cited by 193 · see citing works

Oxidative stress and cell death

Rumora, L., Petrik, J., & Žanić‐Grubišić, T. (2003) · Cited by 192 · see citing works

Human CIA30 is involved in the early assembly of mitochondrial complex I and mutations in its gene cause disease

Dunning, C. J. R., McKenzie, M., Sugiana, C., Lazarou, M., Silke, J., Connelly, A. A., Fletcher, J., Kirby, D. M., Thorburn, D. R., & Ryan, M. T. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601748 · Cited by 191 · see citing works

NDUFS6 mutations are a novel cause of lethal neonatal mitochondrial complex I deficiency

Kirby, D. M., Salemi, R., Sugiana, C., Ohtake, A., Parry, L., Bell, K. M., Kirk, E. P., Boneh, A., Taylor, R. W., Dahl, H. M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20683 · Cited by 191 · see citing works

Respiratory chain complex I deficiency

Triepels, R. H., van den Heuvel, L. P., Trijbels, J. M. F., & Smeitink, J. A. M. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1397 · Cited by 191 · see citing works

The mtDNA‐encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme

Bai, Y., & Attardi, G. M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4848 · Cited by 188 · see citing works

Mitochondrial oversight of cellular Ca2+ signaling

Babcock, D. F., & Hille, B. (1998) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(98)80067-6 · Cited by 186 · see citing works

De novo mutations in the mitochondrial ND3 gene as a cause of infantile mitochondrial encephalopathy and complex I deficiency

McFarland, R., Kirby, D. M., Fowler, K. J., Ohtake, A., Ryan, M. T., Amor, D. J., Fletcher, J. M., Dixon, J. W., Collins, F. A., Turnbull, D. M., et al. (2003) · Annals of Neurology · doi:10.1002/ana.10787 · Cited by 180 · see citing works

Mutations of the mitochondrial ND1 gene as a cause of MELAS

Kirby, D. M., McFarland, R., Ohtake, A., Dunning, C. J. R., Ryan, M. T., Wilson, C. J., Ketteridge, D., Turnbull, D. M., Thorburn, D. R., & Taylor, R. W. (2004) · Journal of Medical Genetics · doi:10.1136/jmg.2004.020537 · Cited by 179 · see citing works

Mutation of C20orf7 Disrupts Complex I Assembly and Causes Lethal Neonatal Mitochondrial Disease

Sugiana, C., Pagliarini, D. J., McKenzie, M., Kirby, D. M., Salemi, R., Abu‐Amero, K. K., Dahl, H. M., Hutchison, W. M., Vascotto, K. A., Smith, S. M., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.09.009 · Cited by 178 · see citing works

Mitochondrial dysfunction in Parkinson's disease

Schapira, A. H. V. (2007) · Cell Death &amp; Differentiation · doi:10.1038/sj.cdd.4402160 · Cited by 175 · see citing works

Identification and Characterization of a Common Set of Complex I Assembly Intermediates in Mitochondria from Patients with Complex I Deficiency

Antonická, H., Ogilvie, I. M., Taivassalo, T., Anitori, R. P., Haller, R. G., Vissing, J., Kennaway, N. G., & Shoubridge, E. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304998200 · Cited by 174 · see citing works

Resolution of the Membrane Domain of Bovine Complex I into Subcomplexes: Implications for the Structural Organization of the Enzyme

Sazanov, L. A., Peak‐Chew, S., Fearnley, I. M., & Walker, J. E. (2000) · Biochemistry · doi:10.1021/bi000335t · Cited by 171 · see citing works

The mitochondrial complex i inhibitor annonacin is toxic to mesencephalic dopaminergic neurons by impairment of energy metabolism

Lannuzel, A., Michel, P. P., Höglinger, G. U., Champy, P., Jousset, A. B., Medja, F., Lombès, A., Darios, F. D., Gleye, C., Laurens, A., et al. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00441-x · Cited by 168 · see citing works

Mutant NDUFV2 subunit of mitochondrial complex I causes early onset hypertrophic cardiomyopathy and encephalopathy

Bénit, P., Beugnot, R., Chrétien, D., Giurgea, I., de Lonlay, P., Issartel, J., Corral‐Debrinski, M., Kerscher, S., Rustin, P., Rötig, A., et al. (2003) · Human Mutation · doi:10.1002/humu.10225 · Cited by 163 · see citing works

Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae

Brody, S., Oh, C., Hoja, U., & Schweizer, E. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00428-6 · Cited by 160 · see citing works

C6ORF66 Is an Assembly Factor of Mitochondrial Complex I

Saada, A., Edvardson, S., Rapoport, M., Shaag, A., Amry, K., Miller, C., Lorberboum‐Galski, H., & Elpeleg, O. N. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2007.08.003 · Cited by 159 · see citing works

A New Metabolic Link

Jordan, S. W., & Cronan, J. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.17903 · Cited by 156 · see citing works

Definition of the Nuclear Encoded Protein Composition of Bovine Heart Mitochondrial Complex I

Carroll, J., Shannon, R. J., Fearnley, I. M., Walker, J. E., & Hirst, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209166200 · Cited by 155 · see citing works

Localization of the Site of Oxygen Radical Generation inside the Complex I of Heart and Nonsynaptic Brain Mammalian Mitochondria

Herrero, A., & Barja, G. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005626712319 · Cited by 149 · see citing works

Mitochondrial defects and anesthetic sensitivity

Morgan, P. G., Hoppel, C. L., & Sedensky, M. M. (2002) · Anesthesiology · doi:10.1097/00000542-200205000-00036 · Cited by 148 · see citing works

Identification of Mitochondrial Complex I Assembly Intermediates by Tracing Tagged NDUFS3 Demonstrates the Entry Point of Mitochondrial Subunits

Vogel, R. O., Dieteren, C. E. J., van den Heuvel, L. P. W. J., Willems, P. H. G. M., Smeitink, J. A. M., Koopman, W. J. H., & Nijtmans, L. G. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609410200 · Cited by 145 · see citing works

The mitochondrial respiratory chain is a modulator of apoptosis

Kwong, J. Q., Henning, M. S., Starkov, A. A., & Manfredi, G. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704059 · Cited by 145 · see citing works

The reduction of NADH

Kim, S. H., Vlkolinský, R., Cairns, N. J., Fountoulakis, M., & Lübec, G. (2001) · Life Sciences · doi:10.1016/s0024-3205(01)01074-8 · Cited by 144 · see citing works

An Assembled Complex IV Maintains the Stability and Activity of Complex I in Mammalian Mitochondria

Li, Y.-F., D’Aurelio, M., Deng, J., Park, J.-S., Manfredi, G., Hu, P., Lü, J., & Bai, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701056200 · Cited by 140 · see citing works

Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme

Finel, M., Skehel, M. J., Albracht, S. P. J., Fearnley, I. M., & Walker, J. E. (1992) · Biochemistry · doi:10.1021/bi00161a022 · Cited by 139 · see citing works

Novel Role for Mitochondria: Protein Kinase Cθ-Dependent Oxidative Signaling Organelles in Activation-Induced T-Cell Death

Kamiński, M. M., Kießling, M. K., Süss, D., Krammer, P. H., & Gülow, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02295-06 · Cited by 139 · see citing works

Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin

Bourges, I., Ramus, C., de Camaret, B. M., Beugnot, R., Remacle, C., Cardol, P., Hofhaus, G., & Issartel, J. (2004) · Biochemical Journal · doi:10.1042/bj20040256 · Cited by 133 · see citing works

Mitochondria, from cell death to proliferation

Rustin, P. (2002) · Nature Genetics · doi:10.1038/ng0402-352 · Cited by 132 · see citing works

Mitochondrial complex I mutations in Caenorhabditis elegans produce cytochrome c oxidase deficiency, oxidative stress and vitamin-responsive lactic acidosis

Grad, L. I. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddh027 · Cited by 130 · see citing works

Assembly of NADH: Ubiquinone reductase (complex I) in Neurospora mitochondria

Tuschen, G., Sackmann, U., Nehls, U., Haiker, H., Buse, G., & Weiss, H. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80268-2 · Cited by 121 · see citing works

Bioenergetics shapes cellular death pathways in Leber's hereditary optic neuropathy: a model of mitochondrial neurodegeneration

Carelli, V., Rugolo, M., Sgarbi, G., Ghelli, A. M., Zanna, C., Baracca, A., Lenaz, G., Napoli, E., Martinuzzi, A., & Solaini, G. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.05.009 · Cited by 119 · see citing works

The Mutant Human ND4 Subunit of Complex I Induces Optic Neuropathy in the Mouse

Qi, X., Sun, L., Lewin, A. S., Hauswirth, W. W., & Guy, J. R. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.06-0789 · Cited by 118 · see citing works

Obligatory Role for Complex I Inhibition in the Dopaminergic Neurotoxicity of 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

Richardson, J. R., Caudle, W. M., Guillot, T. S., Watson, J. L., Nakamaru‐Ogiso, E., Seo, B. B., Sherer, T., Greenamyre, J. T., Yagi, T., Matsuno‐Yagi, A., et al. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl133 · Cited by 117 · see citing works

Different respiratory-defective phenotypes of Neurospora crassa and Saccharomyces cerevisiae after inactivation of the gene encoding the mitochondrial acyl carrier protein

Schneider, R., Massow, M., Lisowsky, T., & Weiss, H. (1995) · Current Genetics · doi:10.1007/bf00313188 · Cited by 117 · see citing works

Protection by the NDI1 gene against neurodegeneration in a rotenone rat model of Parkinson's disease

Marella, M., Seo, B. B., Nakamaru-Ogiso, E., Greenamyre, J. T., Matsuno-Yagi, A., & Yagi, T. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001433 · Cited by 116 · see citing works

Impaired complex I assembly in a Leigh syndrome patient with a novel missense mutation in the ND6 gene

Ugalde, C., Triepels, R. H., Coenen, M. J. H., van den Heuvel, L. P., Smeets, R., Uusimaa, J., Briones, P., Campistol, J., Majamaa, K., Smeitink, J. A. M., et al. (2003) · Annals of Neurology · doi:10.1002/ana.10734 · Cited by 115 · see citing works

Mitochondrial DNA 3644T→C mutation associated with bipolar disorder

Munakata, K., Tanaka, M., Mori, K., Washizuka, S., Yoneda, M., Tajima, O., Akiyama, T., Nanko, S., Kunugi, H., Tadokoro, K., et al. (2004) · Genomics · doi:10.1016/j.ygeno.2004.08.015 · Cited by 113 · see citing works

Mitochondrial ND5 mutations in idiopathic Parkinson’s disease

Parker, W. D., & Parks, J. K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.11.093 · Cited by 108 · see citing works

Lack of assembly of mitochondrial DNA‐encoded subunits of respiratory NADH dehydrogenase and loss of enzyme activity in a human cell mutant lacking the mitochondrial ND4 gene product.

Hofhaus, G., & Attardi, G. M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05973.x · Cited by 104 · see citing works

[4] Resolution of complex I and isolation of NADH dehydrogenase and an iron-sulfur protein

Galante, Y. M., & Hatefi, Y. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)53007-3 · Cited by 104 · see citing works

Structure–activity relationships of some complex I inhibitors

Miyoshi, H. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00030-9 · Cited by 104 · see citing works

Complex I from the fungus Neurospora crassa

Videira, A. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00020-6 · Cited by 103 · see citing works

Analysis of mitochondrial subunit assembly into respiratory chain complexes using Blue Native polyacrylamide gel electrophoresis

McKenzie, M., Lazarou, M., Thorburn, D. R., & Ryan, M. T. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.02.022 · Cited by 101 · see citing works

Mitochondrial Dysfunction, Oxidative Stress, and Apoptosis Revealed by Proteomic and Transcriptomic Analyses of the Striata in Two Mouse Models of Parkinson’s Disease

Chin, M. H., Qian, W., Wang, H., Petyuk, V., Bloom, J. S., Sforza, D., Laćan, G., Liu, D., Khan, A. H., Cantor, R. M., et al. (2008) · Journal of Proteome Research · doi:10.1021/pr070546l · Cited by 101 · see citing works

Efficient Selection and Characterization of Mutants of a Human Cell Line Which are Defective in Mitochondrial DNA-Encoded Subunits of Respiratory NADH Dehydrogenase

Hofhaus, G., & Attardi, G. M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.964 · Cited by 101 · see citing works

Involvement of two novel chaperones in the assembly of mitochondrial NADH:ubiquinone oxidoreductase (complex I) 1 1Edited by A. R. Fersht

Küffner, R., Rohr, A., Schmiede, A., Krüll, C., & Schulte, U. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2114 · Cited by 99 · see citing works

Mitochondrial DNA damage in non-melanoma skin cancer

Durham, S. E., Krishnan, K. J., Betts, J., & Birch‐Machin, M. A. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6600773 · Cited by 95 · see citing works

From NADH to ubiquinone in Neurospora mitochondria

Videira, A., & Duarte, M. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00276-1 · Cited by 92 · see citing works

Substrate-induced Conformational Change in Bacterial Complex I

Mamedova, A. A., Holt, P. J., Carroll, J., & Sazanov, L. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401539200 · Cited by 89 · see citing works

LHON and Other Optic Nerve Atrophies: The Mitochondrial Connection

Howell, N. (2003) · KARGER eBooks · doi:10.1159/000072041 · Cited by 88 · see citing works

Characterization of assembly intermediates of NADH: Ubiquinone oxidoreductase (complex I) accumulated in Neurospora mitochondria by gene disruption

Nehls, U., Friedrich, T., Schmiede, A., Ohnishi, T., & Weiss, H. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90519-p · Cited by 84 · see citing works

GRIM-19 Is Essential for Maintenance of Mitochondrial Membrane Potential

Lu, H., & Cao, X. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-07-0683 · Cited by 84 · see citing works

Suppression of complex I gene expression induces optic neuropathy

Qi, X., Lewin, A. S., Hauswirth, W. W., & Guy, J. R. (2003) · Annals of Neurology · doi:10.1002/ana.10426 · Cited by 82 · see citing works

Mutated ND2 impairs mitochondrial complex I assembly and leads to Leigh Syndrome

Ugalde, C., Hinttala, R., Timal, S., Smeets, R., Rodenburg, R. J., Uusimaa, J., van den Heuvel, L. P., Nijtmans, L. G. J., Majamaa, K., & Smeitink, J. A. M. (2006) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2006.08.003 · Cited by 82 · see citing works

An analysis of the polypeptide composition of bovine heart mitochondrial NADH-ubiquinone oxidoreductase by two-dimensional polyacrylamide-gel electrophoresis

Heron, C., Smith, S. K., & RAGAN, C. I. (1979) · Biochemical Journal · doi:10.1042/bj1810435 · Cited by 81 · see citing works

Functional Implications from an Unexpected Position of the 49-kDa Subunit of NADH:Ubiquinone Oxidoreductase

Zickermann, V., Bostina, M., Hunte, C., Ruíz, T., Radermacher, M., & Brandt, U. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302713200 · Cited by 80 · see citing works

Mitochondrial complex I activity is impaired during HIV-1-induced T-cell apoptosis

Ladha, J., Tripathy, M. K., & Mitra, D. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401668 · Cited by 80 · see citing works

Generation of Reactive Oxygen Species by Mitochondrial Complex I: Implications in Neurodegeneration

Fato, R., Bergamini, C., Leoni, S., Strocchi, P., & Lenaz, G. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9747-0 · Cited by 79 · see citing works

The mechanism of proton and electron transport in mitochondrial complex I

Esposti, M. D., & Ghelli, A. M. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90095-7 · Cited by 79 · see citing works

Oxidative Phosphorylation Enzymes in Normal and Neoplastic Cell Growth

Capuano, F., GUERRIERI, F., & Papa, S. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022402915431 · Cited by 78 · see citing works

Mitochondrial complex I function modulates volatile anesthetic sensitivity in C. elegans

Falk, M. J., Kayser, E.-B., Morgan, P. G., & Sedensky, M. M. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.072 · Cited by 69 · see citing works

Mitochondrial fatty acid synthesis: a relic of endosymbiontic origin and a specialized means for respiration

Schneider, R., Brors, B., Massow, M., & Weiss, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00360-8 · Cited by 69 · see citing works

Development and Characterization of a Conditional Mitochondrial Complex I Assembly System

Yadava, N., Houchens, T., Potluri, P., & Scheffler, I. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313588200 · Cited by 68 · see citing works

Biogenesis of Respiratory Complex I

Schulte, U. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1010730919074 · Cited by 68 · see citing works

Species-specific and Mutant MWFE Proteins

Yadava, N., Potluri, P., Smith, E. N., Bisevac, A., & Scheffler, I. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202016200 · Cited by 64 · see citing works

NADH dehydrogenases: from basic science to biomedicine

Yagi, T., Seo, B. B., Bernardo, S. D., Nakamaru-Ogiso, E., Kao, M.-C., & Matsuno-Yagi, A. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1010787004053 · Cited by 63 · see citing works

In vivo dissection of the mitochondrial respiratory NADH:ubiquinone oxidoreductase (complex I)

Schulte, U., Fecke, W., Krüll, C., Nehls, U., Schmiede, A., Schneider, R., Ohnishi, T., & Weiss, H. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90096-5 · Cited by 57 · see citing works

Yeast NDI1 improves oxidative phosphorylation capacity and increases protection against oxidative stress and cell death in cells carrying a Leber's hereditary optic neuropathy mutation

Park, J. S., Li, Y.-F., & Bai, Y. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.01.009 · Cited by 47 · see citing works

Genetic and Functional Analysis of Mitochondrial DNA‐Encoded Complex I Genes

Bai, Y., Hu, P., Park, J. S., Deng, J., Song, X., Chomyn, A., Yagi, T., & Attardi, G. M. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1293.026 · Cited by 43 · see citing works

Mitochondrial Complex I Function Affects Halothane Sensitivity in Caenorhabditis elegans

Kayser, E., Morgan, P. G., & Sedensky, M. M. (2004) · Anesthesiology · doi:10.1097/00000542-200408000-00017 · Cited by 40 · see citing works

GRIM-19 associates with the serine protease HtrA2 for promoting cell death

Ma, X., Kalakonda, S., Srinivasula, S. M., Reddy, S. P., Platanias, L. C., & Kalvakolanu, D. V. (2007) · Oncogene · doi:10.1038/sj.onc.1210287 · Cited by 39 · see citing works

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 · see citing works

Free radicals‐mediated damage in transmitochondrial cells harboring the T14487C mutation in the ND6 gene of mtDNA

Gonzalo, R., García‐Arumí, E., Lligé, D., Martí, R., Solano, A., Montoya, J., Arenas, J., & Andreu, A. L. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.034 · Cited by 37 · see citing works

Attempts to define distinct parts of NADH: Ubiquinone oxidoreductase (complex I)

Friedrich, T., Weidner, U., Nehls, U., Fecke, W., Schneider, R., & Weiss, H. (1993) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762458 · Cited by 37 · see citing works

Maintenance of the Metabolic Homeostasis of the Heart

Balaban, R. S. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1380.013 · Cited by 35 · see citing works

A Novel Myc-target Gene, mimitin, That Is Involved in Cell Proliferation of Esophageal Squamous Cell Carcinoma

Tsuneoka, M., Teye, K., Arima, N., Soejima, M., Otera, H., Ohashi, K., Koga, Y., Fujita, H., Shirouzu, K., Kimurâ, H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501231200 · Cited by 34 · see citing works

Nuclear Suppression of Mitochondrial Defects in Cells without the ND6 Subunit

Deng, J., Li, Y.-F., Park, J. S., Wu, J., Hu, P., Lechleiter, J. D., & Bai, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.3.1077-1086.2006 · Cited by 33 · see citing works

Escherichia coli NADH dehydrogenase I, a minimal form of the mitochondrial complex I

Leif, H., Weidner, U., Berger, A., Spehr, V., Braun, M., van Heek, P., Friedrich, T., Ohnishi, T., & Weiss, H. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210998 · Cited by 31 · see citing works

Molecular genetic studies of complex I inNeurospora crassa, Aspergillus niger andEscherichia coli

Weidner, U., Nehls, U., Schneider, R., Fecke, W., Leif, H., Schmiede, A., Friedrich, T., Zensen, R., Schulte, U., Ohnishi, T., et al. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(92)90218-q · Cited by 30 · see citing works

The respiratory-chain NADH dehydrogenase (complex I) of mitochondria

Weiss, H., Friedrich, T., Hofhaus, G., & Preis, D. (1991) · Springer eBooks · doi:10.1007/978-3-642-77200-9_5 · Cited by 30 · see citing works

Mitochondrial Complex I: structure, function, and implications in neurodegeneration.

Lenaz, G., Baracca, A., Fato, R., Genova, M. L., & Solaini, G. (2006) · PubMed · Cited by 22 · see citing works

Oxidation of reduced cytosolic nicotinamide adenine dinucleotide by the malate-aspartate shuttle in the K-562 human leukemia cell line.

López‐Alarcón, L., & Eboli, M. L. (1986) · PubMed · Cited by 19 · see citing works

HRPAP20: a novel calmodulin-binding protein that increases breast cancer cell invasion

Karp, C. M., Shukla, M. N., Buckley, D. J., & Buckley, A. R. (2006) · Oncogene · doi:10.1038/sj.onc.1209980 · Cited by 19 · see citing works

Altered hepatic gluconeogenesis during L-alanine infusion in weight-losing lung cancer patients as observed by phosphorus magnetic resonance spectroscopy and turnover measurements.

Leij‐Halfwerk, S., van den Berg, J. W. O., Sijens, P. E., Wilson, J. H. P., Oudkerk, M., & Dagnelie, P. C. (2000) · PubMed · Cited by 19 · see citing works

A common ancestor for a subunit in the mitochondrial proton-translocating NADH:ubiquinone oxidoreductase (complex I) and short-chain dehydrogenases/reductases

Baker, M. E., Grundy, W. N., & Elkan, C. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050301 · Cited by 15 · see citing works

Restoration of Mitochondrial Function in Cells with Complex I Deficiency

Bai, Y., Park, J. S., Deng, J., Li, Y.-F., & Hu, P. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1338.003 · Cited by 14 · see citing works

Mitochondrial DNA mutations in the D-loop region may not be frequent in cervical cancer: a discussion on pitfalls in mitochondrial DNA studies

Fang, H., Lü, J., Wei, J., Shen, L.-J., Ding, Z., Li, H., & Bai, Y. (2009) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-008-0542-8 · Cited by 13 · see citing works

De novo mutations in the mitochondrial ND3 gene as a cause of infantile mitochondrial encephalopathy and complex I deficiency.

McFarland, R., Kirby, D., Fowler, K., Ohtake, A., Ryan, M., Amor, D., Fletcher, J., Dixon, J., Collins, F., Turnbull, D., et al. (n.d.) · University of Groningen research database (University of Groningen / Centre for Information Technology) · Cited by 13 · see citing works

Genetic and Functional Analysis of Mitochondrial DNA-Encoded Complex I Genes

Bai, Y., Hu, P., Park, J. S., Deng, J., Song, X., Chomyn, A., Yagi, T., & Attardi, G. M. (2004) · Springer eBooks · doi:10.1007/978-3-662-41088-2_26 · Cited by 9 · see citing works

Role for peroxisome proliferator-activated receptor-gamma in Alzheimer's disease.

van Geel (2001) · Open Repository and Bibliography (University of Luxembourg) · doi:10.1002/1531-8249(20010201)49:2 · Cited by 7 · see citing works

Species-specific and mutant MWFE proteins. Their effect on the assembly of a functional mammalian mitochondrial complex I.

Yadava, N., Potluri, P., Smith, E. N., Bisevac, A., & Scheffler, I. E. (2002) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)71961-9 · Cited by 2 · see citing works

The sites and topology of mitochondrial superoxide production

Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217 · see citing works

Reactive Oxygen Species: A Key Hallmark of Cardiovascular Disease

Panth, N., Paudel, K. R., & Parajuli, K. (2016) · Advances in Medicine · doi:10.1155/2016/9152732 · Cited by 405 · see citing works

Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity

Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works

The Roles of ROS in Cancer Heterogeneity and Therapy

Júnior, P. L. D. S., Câmara, D. A. D., Porcacchia, A. S., Fonseca, P. M. M., Jorge, S. D., Araldi, R. P., & Ferreira, A. K. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2467940 · Cited by 289 · see citing works

Proteomic analysis reveals ginsenoside Rb1 attenuates myocardial ischemia/reperfusion injury through inhibiting ROS production from mitochondrial complex I

Jiang, L., Yin, X., Chen, Y., Chen, Y., Jiang, W., Zheng, H., Huang, F., Liu, B., Zhou, W., Qi, L., et al. (2020) · Theranostics · doi:10.7150/thno.43895 · Cited by 217 · see citing works

Mitochondrial Localized Stat3 Promotes Breast Cancer Growth via Phosphorylation of Serine 727

Zhang, Q., Raje, V., Yakovlev, V. A., Yacoub, A., Szczepanek, K., Meier, J. A., Derecka, M., Chen, Q., Hu, Y., Sisler, J. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.505057 · Cited by 188 · see citing works

Why All the Fuss about Oxidative Phosphorylation (OXPHOS)?

Xu, Y., Xue, D., Bankhead, A., & Neamati, N. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01013 · Cited by 161 · see citing works

Mitochondrial respiratory complex I dysfunction promotes tumorigenesis through ROS alteration and AKT activation

Sharma, L. K., Fang, H., Liu, J., Vartak, R. S., Deng, J., & Bai, Y. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr395 · Cited by 157 · see citing works

Cytosine-5 RNA methylation links protein synthesis to cell metabolism

Gkatza, N. A., Castro, C., Harvey, R. F., Heiß, M., Popis, M. C., Blanco, S., Bornelöv, S., Sajini, A. A., Gleeson, J. G., Griffin, J. L., et al. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000297 · Cited by 136 · see citing works

Rotenone: from modelling to implication in Parkinson’s disease

Radad, K., Al-Shraim, M. M., Al‐Emam, A., Wang, F., Kranner, B., Rausch, W., & Moldzio, R. (2019) · Folia Neuropathologica · doi:10.5114/fn.2019.89857 · Cited by 133 · see citing works

An adverse outcome pathway for parkinsonian motor deficits associated with mitochondrial complex I inhibition

Members, E. W. E., Terron, A., Bal-Price, A., Paini, A., Monnet-Tschudi, F., Bennekou, S. H., Leist, M., & Schildknecht, S. (2018) · Archives of Toxicology · doi:10.1007/s00204-017-2133-4 · Cited by 124 · see citing works

Breast milk alkylglycerols sustain beige adipocytes through adipose tissue macrophages

Yu, H., Dilbaz, S., Coßmann, J., Hoang, A. C., Diedrich, V., Herwig, A., Harauma, A., Hoshi, Y., Moriguchi, T., Landgraf, K., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci125646 · Cited by 123 · see citing works

Mitochondrial DNA and TLR9 activation contribute to SARS-CoV-2-induced endothelial cell damage

Costa, T. J. D., Potje, S. R., Fraga‐Silva, T. F. D. C., da Silva-Neto, J. A., Barros, P. R., Rodrigues, D., Machado, M. R., Júnior, R. B. M., Eichler, R. A. D. S., Benatti, M. N., et al. (2021) · Vascular Pharmacology · doi:10.1016/j.vph.2021.106946 · Cited by 121 · see citing works

Carcinogenesis and Reactive Oxygen Species Signaling: Interaction of the NADPH Oxidase NOX1–5 and Superoxide Dismutase 1–3 Signal Transduction Pathways

Parascandolo, A., & Laukkanen, M. O. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7268 · Cited by 117 · see citing works

Chronic pro-oxidative state and mitochondrial dysfunctions are more pronounced in fibroblasts from Down syndrome foeti with congenital heart defects

Piccoli, C., Izzo, A., Scrima, R., Bonfiglio, F., Manco, R., Negri, R., Quarato, G., Cela, O., Ripoli, M. C., Prisco, M., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds529 · Cited by 96 · see citing works

A lethal mitonuclear incompatibility in complex I of natural hybrids

Moran, B. M., Payne, C. Y., Powell, D. L., Iverson, E. N. K., Donny, A. E., Banerjee, S. M., Langdon, Q. K., Gunn, T. R., Rodriguez-Soto, R. A., Madero, A. M., et al. (2024) · Nature · doi:10.1038/s41586-023-06895-8 · Cited by 87 · see citing works

A Highly Selective In Vitro JNK3 Inhibitor, FMU200, Restores Mitochondrial Membrane Potential and Reduces Oxidative Stress and Apoptosis in SH-SY5Y Cells

Rehfeldt, S. C. H., Laufer, S., & Goettert, M. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073701 · Cited by 85 · see citing works

ALS/FTD-associated protein FUS induces mitochondrial dysfunction by preferentially sequestering respiratory chain complex mRNAsPreprint

Tsai, Y.-L., Coady, T. H., Lü, L., Zheng, D., Alland, I., Tian, B., Shneider, N. A., & Manley, J. L. (2020) · Genes & Development · doi:10.1101/gad.335836.119 · Cited by 84 · see citing works

Diagnosis of mitochondrial disorders by concomitant next-generation sequencing of the exome and mitochondrial genome

Dinwiddie, D. L., Smith, L. D., Miller, N., Atherton, A. M., Farrow, E., Strenk, M. E., Soden, S. E., Saunders, C., & Kingsmore, S. F. (2013) · Genomics · doi:10.1016/j.ygeno.2013.04.013 · Cited by 80 · see citing works

p113 isoform encoded by CUX1 circular RNA drives tumor progression via facilitating ZRF1/BRD4 transactivation

Yang, F., Hu, A., Guo, Y., Wang, J., Li, D., Wang, X., Jin, S., Yuan, B., Cai, S., Zhou, Y., et al. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01421-8 · Cited by 79 · see citing works

Blackout in the powerhouse: clinical phenotypes associated with defects in the assembly of OXPHOS complexes and the mitoribosome

Hock, D. H., Robinson, D. R. L., & Stroud, D. A. (2020) · Biochemical Journal · doi:10.1042/bcj20190767 · Cited by 70 · see citing works

Loss of Caspase-2-dependent Apoptosis Induces Autophagy after Mitochondrial Oxidative Stress in Primary Cultures of Young Adult Cortical Neurons

Tiwari, M., Lopez‐Cruzan, M., MORGAN, W. W., & Herman, B. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163824 · Cited by 71 · see citing works

Mitochondrial DNA mutations in renal disease: an overview

Govers, L. P., Toka, H. R., Hariri, A., Walsh, S. B., & Böckenhauer, D. (2020) · Pediatric Nephrology · doi:10.1007/s00467-019-04404-6 · Cited by 70 · see citing works

Survival-Associated Metabolic Genes in Human Papillomavirus-Positive Head and Neck Cancers

Prusinkiewicz, M. A., Gameiro, S. F., Ghasemi, F., Dodge, M. J., Zeng, P. Y., Maekebay, H., Barrett, J. W., Nichols, A. C., & Mymryk, J. S. (2020) · Cancers · doi:10.3390/cancers12010253 · Cited by 70 · see citing works

Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function

Han, J., Park, H.-J., Maharana, C., Gwon, A., Park, J., Baek, S. H., Bae, H., Cho, Y., Kim, H. K., Sul, J. H., et al. (2021) · Theranostics · doi:10.7150/thno.59776 · Cited by 70 · see citing works

Metformin Improves Ovarian Cancer Sensitivity to Paclitaxel and Platinum-Based Drugs: A Review of In Vitro Findings

Tossetta, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112893 · Cited by 67 · see citing works

Chemotherapeutic induction of mitochondrial oxidative stress activates GSK-3α/β and Bax, leading to permeability transition pore opening and tumor cell death

Chiara, F., Gambalunga, A., Sciacovelli, M., Nicolli, A., Ronconi, L., Fregona, D., Bernardi, P., Rasola, A., & Trevisan, A. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.184 · Cited by 68 · see citing works

Mitochondrial integrity in neurodegeneration

Cowan, K., Anichtchik, O. V., & Luo, S. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13105 · Cited by 65 · see citing works

Mitochondrial DNA: Inherent Complexities Relevant to Genetic Analyses

Ferreira, T., & Rodrı́guez, S. (2024) · Genes · doi:10.3390/genes15050617 · Cited by 70 · see citing works

scTenifoldNet: A Machine Learning Workflow for Constructing and Comparing Transcriptome-wide Gene Regulatory Networks from Single-Cell Data

Osorio, D., Zhong, Y., Li, G., Huang, J. Z., & Cai, J. J. (2020) · Patterns · doi:10.1016/j.patter.2020.100139 · Cited by 65 · see citing works

Plasma mitochondrial DNA and metabolomic alterations in severe critical illness

Johansson, P. I., Nakahira, K., Rogers, A. J., McGeachie, M. J., Baron, R. M., Fredenburgh, L. E., Harrington, J. S., Choi, A. M. K., & Christopher, K. B. (2018) · Critical Care · doi:10.1186/s13054-018-2275-7 · Cited by 64 · see citing works

Maternal nutrition modulates fetal development by inducing placental efficiency changes in gilts

Che, L., Yang, Z., Xu, M., Xu, S., Che, L., Lin, Y., Fang, Z., Feng, B., Li, J., Chen, D., et al. (2017) · BMC Genomics · doi:10.1186/s12864-017-3601-1 · Cited by 65 · see citing works

SERPINB3 protects from oxidative damage by chemotherapeutics through inhibition of mitochondrial respiratory complex I

Ciscato, F., Sciacovelli, M., Villano, G., Turato, C., Bernardi, P., Rasola, A., & Pontisso, P. (2013) · Oncotarget · doi:10.18632/oncotarget.1411 · Cited by 62 · see citing works

SLC25A10 biallelic mutations in intractable epileptic encephalopathy with complex I deficiency

Punzi, G., Porcelli, V., Ruggiu, M., Hossain, M. F., Menga, A., Scarcia, P., Castegna, A., Gorgoglione, R., Pierri, C. L., Laera, L., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx419 · Cited by 56 · see citing works

Mitochondrial Dysfunction in Parkinson’s Disease: Focus on Mitochondrial DNA

Бунеева, О. А., Fedchenko, V. I., Kopylov, A. T., & Medvedev, A. E. (2020) · Biomedicines · doi:10.3390/biomedicines8120591 · Cited by 56 · see citing works

Mitochondrial dysfunction induces radioresistance in colorectal cancer by activating [Ca2+]m-PDP1-PDH-histone acetylation retrograde signaling

Shi, Y., Wang, Y., Jiang, H., Sun, X., Xu, H., Xue, W., Yan, W., Xiao, G., Song, Z., & Zhou, F. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03984-2 · Cited by 55 · see citing works

Lipophilic antioxidants in neurodegenerative diseases

Chang, K., Cheng, M., Chiang, M.-C., & Chen, C. (2018) · Clinica Chimica Acta · doi:10.1016/j.cca.2018.06.031 · Cited by 55 · see citing works

The mitochondrial unfolded protein response and its diverse roles in cellular stress

Smyrnias, I. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.105934 · Cited by 53 · see citing works

Proteomic analysis of cPKCβII‐interacting proteins involved in HPC‐induced neuroprotection against cerebral ischemia of mice

Bu, X., Zhang, N., Yang, X., Liu, Y., Du, J., Liang, J. L., Xu, Q., & Li, J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07209.x · Cited by 53 · see citing works

The Dictyostelium model for mitochondrial disease

Francione, L. M., Annesley, S. J., Carilla-Latorre, S., Escalante, R., & Fisher, P. R. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.11.004 · Cited by 53 · see citing works

Activation of Class I histone deacetylases contributes to mitochondrial dysfunction in cardiomyocytes with altered complex activities

Lkhagva, B., Kao, Y., Lee, T.-I., Lee, T., Cheng, W., & Chen, Y. (2018) · Epigenetics · doi:10.1080/15592294.2018.1460032 · Cited by 53 · see citing works

Status of Mitochondrial Oxidative Phosphorylation during the Development of Heart Failure

Bhullar, S. K., & Dhalla, N. S. (2023) · Antioxidants · doi:10.3390/antiox12111941 · Cited by 55 · see citing works

Testosterone Upregulates the Expression of Mitochondrial ND1 and ND4 and Alleviates the Oxidative Damage to the Nigrostriatal Dopaminergic System in Orchiectomized Rats

Yan, W., Kang, Y., Ji, X., Li, S., Li, Y., Zhang, G., Cui, H., & Shi, G. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/1202459 · Cited by 51 · see citing works

Limonene, a Monoterpene, Mitigates Rotenone-Induced Dopaminergic Neurodegeneration by Modulating Neuroinflammation, Hippo Signaling and Apoptosis in Rats

Eddin, L. B., Azimullah, S., Jha, N. K., Meeran, M. F. N., Beiram, R., & Ojha, S. K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065222 · Cited by 50 · see citing works

Sulforaphane Potentiates Anticancer Effects of Doxorubicin and Cisplatin and Mitigates Their Toxic Effects

Calcabrini, C., Maffei, F., Turrini, E., & Fimognari, C. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00567 · Cited by 50 · see citing works

Mitochondrial Complex I as a Pathologic and Therapeutic Target for Parkinson’s Disease

Tryphena, K. P., Uppala, S. N., Pinjala, P., Srivastava, S., Singh, S. B., & Khatri, D. K. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00819 · Cited by 49 · see citing works

Behavioral Improvement after Chronic Administration of Coenzyme Q10 in P301S Transgenic Mice

Elipenahli, C., Stack, C., Jainuddin, S., Gerges, M., Yang, L., Starkov, A. A., Beal, M. F., & Dumont, M. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111190 · Cited by 48 · see citing works

Structural Contribution of C-terminal Segments of NuoL (ND5) and NuoM (ND4) Subunits of Complex I from Escherichia coli

Torres‐Bacete, J., Sinha, P. K., Matsuno‐Yagi, A., & Yagi, T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.260968 · Cited by 48 · see citing works

Implication of SPARC in the modulation of the extracellular matrix and mitochondrial function in muscle cells

Melouane, A., Carbonell, A., Yoshioka, M., Puymirat, J., & St‐Amand, J. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192714 · Cited by 48 · see citing works

Elucidating Conserved Transcriptional Networks Underlying Pesticide Exposure and Parkinson's Disease: A Focus on Chemicals of Epidemiological Relevance

Cao, F., Souders, C. L., Perez‐Rodriguez, V., & Martyniuk, C. J. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2018.00701 · Cited by 48 · see citing works

Mitochondrial defects in the respiratory complex I contribute to impaired translational initiation via ROS and energy homeostasis in SMA motor neurons

Thelen, M. P., Wirth, B., & Kye, M. J. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01101-6 · Cited by 48 · see citing works

Association of Immunosuppressant-Induced Protein Changes in the Rat Kidney with Changes in Urine Metabolite Patterns: A Proteo-Metabonomic Study

Klawitter, J., Klawitter, J., Kushner, E. J., Jonscher, K. R., Bendrick‐Peart, J., Leibfritz, D., Christians, U., & Schmitz, V. (2009) · Journal of Proteome Research · doi:10.1021/pr900761m · Cited by 47 · see citing works

Physical exercise protects against mitochondria alterations in the 6-hidroxydopamine rat model of Parkinson’s disease

Ferreira, A. F. F., Binda, K. H., Singulani, M. P., Pereira, C. P. M., Ferrari, G. D., Alberici, L. C., Real, C. C., & Britto, L. R. (2020) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.112607 · Cited by 46 · see citing works

Potassium Channels in Parkinson’s Disease: Potential Roles in Its Pathogenesis and Innovative Molecular Targets for Treatment

Chen, X., Feng, Y., Quinn, R. J., Pountney, D. L., Richardson, D. R., Mellick, G. D., & Ma, L. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000743 · Cited by 44 · see citing works

Emerging model systems and treatment approaches for Leber's hereditary optic neuropathy: Challenges and opportunities

Bahr, T. A., Welburn, K., Donnelly, J., & Bai, Y. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165743 · Cited by 45 · see citing works

A Mutation in Hnrnph1 That Decreases Methamphetamine-Induced Reinforcement, Reward, and Dopamine Release and Increases Synaptosomal hnRNP H and Mitochondrial Proteins

Ruan, Q. T., Yazdani, N., Blum, B. C., Beierle, J. A., Lin, W., Coelho, M. A., Fultz, E. K., Healy, A. F., Shahin, J. R., Kandola, A. K., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1808-19.2019 · Cited by 42 · see citing works

Non-Histone Protein Methylation: Biological Significance and Bioengineering Potential

Blasi, R. D., Blyuss, O. B., Timms, J. F., Conole, D., Ceroni, F., & Whitwell, H. J. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.0c00771 · Cited by 44 · see citing works

The road to the structure of the mitochondrial respiratory chain supercomplex

Caruana, N. J., & Stroud, D. A. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190930 · Cited by 39 · see citing works

Reactive oxygen species (ROS)-mediated regulation of muscle texture in grass carp fed with dietary oxidants

Chen, L., Kaneko, G., Li, Y., Xie, J., Wang, G., Li, Z., Tian, J., Zhang, K., Gong, W., Xia, Y. L., et al. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.737150 · Cited by 41 · see citing works

Proteomic profile of sex-sorted bull sperm evaluated by SWATH-MS analysis

Scott, C., de Souza, F. F., Aristizábal, V. H. V., Hethrington, L., Krisp, C., Molloy, M. P., Baker, M. A., & Dell’Aqua, J. A. (2018) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2018.09.010 · Cited by 41 · see citing works

Micronutrients/miRs/ATP networking in mitochondria: Clinical intervention with ferroptosis, cuproptosis, and calcium burden

Panda, S. P., & Kesharwani, A. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.05.003 · Cited by 40 · see citing works

Electron transfer in biological systems

Marques, H. M. (2024) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-024-02076-8 · Cited by 40 · see citing works

Role of glycogen synthase kinase following myocardial infarction and ischemia–reperfusion

Ghaderi, S., Alidadiani, N., Dilaver, N., Heidari, H. R., Parvizi, R., Rahbarghazi‬, R., Soleimanirad, J., & Baradaran, B. (2017) · APOPTOSIS · doi:10.1007/s10495-017-1376-0 · Cited by 39 · see citing works

Lower oxygen consumption and Complex I activity in mitochondria isolated from skeletal muscle of fetal sheep with intrauterine growth restriction

Pendleton, A. L., Antolic, A. T., Kelly, A. C., Davis, M. A., Camacho, L. E., Doubleday, K., Anderson, M. J., Langlais, P. R., Lynch, R. M., & Limesand, S. W. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00057.2020 · Cited by 39 · see citing works

Novel insights into the mechanism of electron transfer in mitochondrial cytochrome c

Pérez‐Mejías, G., Dı́az-Quintana, A., Guerra‐Castellano, A., Díaz‐Moreno, I., & la Rosa, M. Á. D. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214233 · Cited by 37 · see citing works

Tissue- and substrate-dependent mitochondrial responses to acute hypoxia–reoxygenation stress in a marine bivalve (Crassostrea gigas )

Adzigbli, L., Sokolov, E. P., Ponsuksili, S., & Sokolova, I. M. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.243304 · Cited by 37 · see citing works

IGF1R Deficiency Modulates Brain Signaling Pathways and Disturbs Mitochondria and Redox Homeostasis

Cardoso, S., López, I. P., Piñeiro‐Hermida, S., Pichel, J. G., & Moreira, P. I. (2021) · Biomedicines · doi:10.3390/biomedicines9020158 · Cited by 36 · see citing works

Mitochondrial Modulators: The Defender

Makinde, E. A., Ma, L., Mellick, G. D., & Feng, Y. (2023) · Biomolecules · doi:10.3390/biom13020226 · Cited by 36 · see citing works

Epigenetically dysregulated genes and pathways implicated in the pathogenesis of non-syndromic high myopia

Vishweswaraiah, S., Swierkowska, J., Ratnamala, U., Mishra, N. K., Guda, C., Chettiar, S. S., Johar, K., Mrugacz, M., Karolak, J. A., Gajęcka, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40299-x · Cited by 36 · see citing works

Detection of biomarkers to differentiate endocrine disruption from hepatotoxicity in zebrafish (Danio rerio) using proteomics

Ayobahan, S. U., Eilebrecht, S., Baumann, L., Teigeler, M., Hollert, H., Kalkhof, S., Eilebrecht, E., & Schäfers, C. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.124970 · Cited by 36 · see citing works

The crosstalk between mitochondrial dysfunction and fatty acid metabolism in heart failure: mechanisms and therapeutic strategies

Wang, M., Zhu, Z., He, X., Dai, S., Liu, R., & Liu, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1679085 · Cited by 35 · see citing works

SCAP knockdown in vascular smooth muscle cells alleviates atherosclerosis plaque formation via up‐regulating autophagy in ApoE −/− mice

Li, D., Chen, A., Lan, T., Zou, Y., Zhao, L., Yang, P., Qu, H., Li, W., Varghese, Z., Moorhead, J. F., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800975rrr · Cited by 34 · see citing works

Mitochondria: one of the vital hubs for molecular hydrogen’s biological functions

Zhang, X., Xie, F., Ma, S., Ma, C., Jiang, X., Yang, Y., Song, Y., Liu, M., Zhao, P., & Ma, X. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1283820 · Cited by 33 · see citing works

Mouse models of mitochondrial complex I dysfunction

Irwin, M. H., Parameshwaran, K., & Pinkert, C. A. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.08.009 · Cited by 33 · see citing works

Mitochondrial complex I and cell death: a semi-automatic shotgun model

González‐Halphen, D., Ghelli, A. M., Iommarini, L., Carelli, V., & Esposti, M. D. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.107 · Cited by 33 · see citing works

Mapping the protein phosphorylation sites in human mitochondrial complex I (NADH: Ubiquinone oxidoreductase): A bioinformatics study with implications for brain aging and neurodegeneration

Gowthami, N., Sunitha, B., Kumar, M., Prasad, T. S. K., Gayathri, N., Padmanabhan, B., & Bharath, M. M. S. (2018) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2018.02.004 · Cited by 33 · see citing works

TRIM32 regulates mitochondrial mediated ROS levels and sensitizes the oxidative stress induced cell death

Prajapati, P., Gohel, D., Shinde, A., Roy, M., Singh, K., & Singh, R. K. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109777 · Cited by 33 · see citing works

Multiparameter Optimization of Oxidative Phosphorylation Inhibitors for the Treatment of Pancreatic Cancer

Xue, D., Xu, Y., Kyani, A., Roy, J., Dai, L., Sun, D., & Neamati, N. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01934 · Cited by 33 · see citing works

Discovery of a Potent and Oral Available Complex I OXPHOS Inhibitor That Abrogates Tumor Growth and Circumvents MEKi Resistance

He, P., Feng, J., Xia, X., Sun, Y., He, J., Guan, T., Peng, Y., Zhang, X., Liu, M., Pang, X., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01844 · Cited by 32 · see citing works

Inhibition of ERAD synergizes with FTS to eradicate pancreatic cancer cells

Du, R., Sullivan, D. K., Azizian, N. G., Liu, Y., & Li, Y. (2021) · BMC Cancer · doi:10.1186/s12885-021-07967-6 · Cited by 32 · see citing works

Curcumin induces mitochondrial biogenesis by increasing cyclic AMP levels via phosphodiesterase 4A inhibition in skeletal muscle

Ray, H. R. D., Shibaguchi, T., Yamada, T., Koma, R., Ishizawa, R., Saito, Y., Hosoi, T., & Masuda, K. (2021) · British Journal Of Nutrition · doi:10.1017/s0007114521000490 · Cited by 32 · see citing works

MicroRNAs as Regulators of Cancer Cell Energy Metabolism

Natarajaseenivasan, S. M., Velusamy, P., Mercy, C. S. A., Langford, D., Natarajaseenivasan, K., & Shanmughapriya, S. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12081329 · Cited by 33 · see citing works

Differential requirements for mitochondrial electron transport chain components in the adult murine liver

Lesner, N. P., Wang, X., Chen, Z., Frank, A. R., Menezes, C. J., House, S., Shelton, S. D., Lemoff, A. S., McFadden, D. G., Wansapura, J. P., et al. (2022) · eLife · doi:10.7554/elife.80919 · Cited by 32 · see citing works

A Systematic Review of the Impact of Mitochondrial Variations on Male Infertility

Amor, H., & Hammadeh, M. E. (2022) · Genes · doi:10.3390/genes13071182 · Cited by 31 · see citing works

Athyrium multidentatum (Doll.) Ching extract induce apoptosis via mitochondrial dysfunction and oxidative stress in HepG2 cells

Qi, G., Liu, Z., Fan, R., Yin, Z., Mi, Y., Ren, B., & Liu, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-02573-8 · Cited by 31 · see citing works

The mechanism of coupling between oxido‐reduction and proton translocation in respiratory chain enzymes

Papa, S., Capitanio, G., & Papa, F. (2017) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12347 · Cited by 31 · see citing works

Association between glaucoma susceptibility with combined defects in mitochondrial oxidative phosphorylation and fatty acid beta oxidation

Ulhaq, Z. S., Bittencourt, G. B., Soraya, G. V., Istifiani, L. A., Pamungkas, S. A., Ogino, Y., Nurputra, D. K., & Tse, W. K. F. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2023.101238 · Cited by 30 · see citing works

YAP1 preserves tubular mitochondrial quality control to mitigate diabetic kidney disease

Ye, S., Zhang, M., Zheng, X., Li, S., Fan, Y., Wang, Y., Peng, H., Chen, S., Yang, J., Li, Y., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103435 · Cited by 30 · see citing works

Ubiquitin-Proteasome-System and Enzymes of Energy Metabolism in Skeletal Muscle of Patients with HFpEF and HFrEF

Adams, V., Wunderlich, S., Mangner, N., Hommel, J., Esefeld, K., Gielen, S., Halle, M., Ellingsen, Ø., Craenenbroeck, E. M. V., Wisløff, U., et al. (2021) · ESC Heart Failure · doi:10.1002/ehf2.13405 · Cited by 28 · see citing works

Protection by an antioxidant of rotenone-induced neuromotor decline, reactive oxygen species generation and cellular stress in mouse brain

Parameshwaran, K., Irwin, M. H., Steliou, K., & Pinkert, C. A. (2012) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2012.02.011 · Cited by 28 · see citing works

Energy Transducing Roles of Antiporter-like Subunits in Escherichia coli NDH-1 with Main Focus on Subunit NuoN (ND2)

Sato, M., Sinha, P. K., Torres‐Bacete, J., Matsuno‐Yagi, A., & Yagi, T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482968 · Cited by 28 · see citing works

Piceatannol promotes hepatic and renal AMPK/SIRT1/PGC-1α mitochondrial pathway in rats exposed to reserpine or gamma-radiation

Moustafa, E. M., Rashed, E. R., Rashed, R. R., & Omar, N. N. (2021) · International Journal of Immunopathology and Pharmacology · doi:10.1177/20587384211016194 · Cited by 27 · see citing works

Should the standard model of cellular energy metabolism be reconsidered? Possible coupling between the pentose phosphate pathway, glycolysis and extra-mitochondrial oxidative phosphorylation

Morelli, A. M., & Scholkmann, F. (2024) · Biochimie · doi:10.1016/j.biochi.2024.01.018 · Cited by 27 · see citing works

Combining Photodynamic Therapy and Targeted Drug Delivery Systems: Enhancing Mitochondrial Toxicity for Improved Cancer Outcomes

Merlin, J. P. J., Crous, A., & Abrahamse, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910796 · Cited by 25 · see citing works

Thermal sensitivity links to cellular cardiac decline in three spiny lobsters

Oellermann, M., Hickey, A. J., Fitzgibbon, Q. P., & Smith, G. G. (2020) · Scientific Reports · doi:10.1038/s41598-019-56794-0 · Cited by 27 · see citing works

Intermediary metabolism: An intricate network at the crossroads of cell fate and function

Ferreira, L. M. R., Li, A. M., Serafim, T. L., Sobral, M. C. M., Alpoim, M. C., & Urbano, A. M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165887 · Cited by 26 · see citing works

Mitochondria and Peroxisome Remodeling across Cytomegalovirus Infection Time Viewed through the Lens of Inter-ViSTA

Federspiel, J. D., Cook, K. C., Kennedy, M. A., Venkatesh, S. S., Otter, C. J., Hofstadter, W. A., Beltran, P. M. J., & Cristea, I. M. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107943 · Cited by 26 · see citing works

The Anti-Aging Hormone Klotho Promotes Retinal Pigment Epithelium Cell Viability and Metabolism by Activating the AMPK/PGC-1α Pathway

Zhou, S., Hum, J., Taskintuna, K., Olaya, S., Steinman, J., Ma, J., & Golestaneh, N. (2023) · Antioxidants · doi:10.3390/antiox12020385 · Cited by 26 · see citing works

Loss of Cardiac Splicing Regulator RBM20 Is Associated With Early-Onset Atrial Fibrillation

Vad, O. B., Angeli, E., Liss, M., Ahlberg, G., Andreasen, L., Christophersen, I. E., Hansen, C. C., Møller, S., Hellsten, Y., Haunsøe, S., et al. (2023) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2023.08.008 · Cited by 26 · see citing works

DJ-1 mediates paraquat-induced dopaminergic neuronal cell death

Kwon, H. J., Heo, J. Y., Shim, J. H., Park, J. H., Seo, K. S., Ryu, M. J., Han, J., Shong, M., Son, J. H., & Kweon, G. R. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.01.018 · Cited by 26 · see citing works

Structure of Respiratory Complex I: “Minimal” Bacterial and “De luxe” Mammalian Versions

Sazanov, L. A. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781788010405-00025 · Cited by 3 · see citing works

Complex I of mitochondrial respiratory chain a its disorders.

Rodinová, M. (2010) · Digital Repository (National Repository of Grey Literature)

Structure and function of mitochondrial complex I

Wirth, C., Brandt, U., Hunte, C., & Zickermann, V. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.02.013 · Cited by 328 · see citing works

Gaining mass: the structure of respiratory complex I—from bacterial towards mitochondrial versions

Letts, J. A., & Sazanov, L. A. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.08.008 · Cited by 38 · see citing works

Mitochondrial complex I: structure, function and pathology

Janssen, R. J. R. J., Nijtmans, L. G., Heuvel, L. P. V. D., & Smeitink, J. A. M. (2006) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-006-0362-4 · Cited by 276 · see citing works