The role of mitochondria in inherited neurodegenerative diseases

Kwong, Jennifer Q.; Beal, M. Flint; Manfredi, Giovanni

doi:10.1111/j.1471-4159.2006.03990.x

Cited by 180Mitochondrial Function and PathologyHereditary Neurological DisordersParkinson's Disease Mechanisms and Treatments

The role of mitochondria in inherited neurodegenerative diseases

Kwong, Jennifer Q., Beal, M. Flint, Manfredi, Giovanni·2006·Journal of Neurochemistry

DOI 10.1111/j.1471-4159.2006.03990.x

Open this paper in CoChat — free account

Abstract

In the past decade, the genetic causes underlying familial forms of many neurodegenerative disorders, such as Huntington's disease, Parkinson's disease, Alzheimer's disease, amyotrophic lateral sclerosis, Friedreich ataxia, hereditary spastic paraplegia, dominant optic atrophy, Charcot‐Marie‐Tooth type 2A, neuropathy ataxia and retinitis pigmentosa, and Leber's hereditary optic atrophy have been elucidated. However, the common pathogenic mechanisms of neuronal death are still largely unknown. Recently, mitochondrial dysfunction has emerged as a potential ‘lowest common denominator’ linking these disorders. In this review, we discuss the body of evidence supporting the role of mitochondria in the pathogenesis of hereditary neurodegenerative diseases. We summarize the principal features of genetic diseases caused by abnormalities of mitochondrial proteins encoded by the mitochondrial or the nuclear genomes. We then address genetic diseases where mutant proteins are localized in multiple cell compartments, including mitochondria and where mitochondrial defects are likely to be directly caused by the mutant proteins. Finally, we describe examples of neurodegenerative disorders where mitochondrial dysfunction may be ‘secondary’ and probably concomitant with degenerative events in other cell organelles, but may still play an important role in the neuronal decay. Understanding the contribution of mitochondrial dysfunction to neurodegeneration and its pathophysiological basis will significantly impact our ability to develop more effective therapies for neurodegenerative diseases.

Integrity signals

Registry

Crossref · 10.1111/j.1471-4159.2006.03990.x

Cites

202 of 202 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Pathogenic mutations in several genes including α-synuclein, parkin, UCHL-1, DJ-1, PINK-1, LRRK-2, NURR-1, tau, and HtrA2 directly or indirectly implicate a role of mitochondrial dysfunction in familial PD pathogenesis.
“In addition to mtDNA mutations, pathogenic mutations in several genes including α–synuclein, parkin, UCHL-1, DJ-1, PINK-1, LRRK-2, NURR-1, tau, and HtrA2 also directly or indirectly implicate a role of mitochondrial dysfunction in familial PD pathogenesis3, 28, 29.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [3]
Mitochondrial dysfunction plays a role in the pathophysiology of Parkinson's disease.
“Much evidence suggests a role for mitochondrial dysfunction in the pathophysiology of PD, a common age-associated neurodegenerative disease characterized by progressive degeneration of the nigrostriatal dopamine (DA) pathway and presence of the intraneuronal protein inclusions (Lewy bodies)1-3.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [3]

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
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366 · see citing works
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240 · see citing works
Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · 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
Cell Death
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651 · 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
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group.
Shah, M. A., Datson, N. A., Srinidhi, L., Stanton, V. P., MacDonald, M. E., Allard, M. W., Youngman, S., Am, F., Mott, R., Draths, K., et al. (1993) · Cell · Cited by 3,055 · see citing works
Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology
Zimprich, A. A., Biskup, S., Leitner, P., Lichtner, P., Farrer, M. J., Lincoln, S., Kachergus, J. M., Hulihan, M., Uitti, R. J., Calne, D. B., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.11.005 · Cited by 3,024 · see citing works
Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism
Bonifati, V., Rizzu, P., van Baren, M. J., Schaap, O., Breedveld, G. J., Krieger, E., Dekker, M. C. J., Squitieri, F., Ibáñez, P., Joosse, M., et al. (2003) · Science · doi:10.1126/science.1077209 · Cited by 2,800 · see citing works
Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786 · 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
Peroxisome Proliferator-Activated Receptor-γ Coactivator 1α (PGC-1α): Transcriptional Coactivator and Metabolic Regulator
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076 · see citing works
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · see citing works
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885 · see citing works
The ubiquitin pathway in Parkinson's disease
Leroy, E., Boyer, R., Auburger, G. W. J., Leube, B., Ulm, G., Mezey, É., Harta, G., Brownstein, M., Jonnalagada, S., Chernova, T., et al. (1998) · Nature · doi:10.1038/26652 · Cited by 1,572 · see citing works
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works
High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease
Bender, A., Krishnan, K. J., Morris, C. M., Taylor, G. A., Reeve, A. K., Perry, R. H., Jaros, E., Hersheson, J. S., Betts, J., Klopstock, T., et al. (2006) · Nature Genetics · doi:10.1038/ng1769 · Cited by 1,570 · see citing works
The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
Li, Z., Okamoto, K.-I., Hayashi, Y., & Sheng, M. (2004) · Cell · doi:10.1016/j.cell.2004.11.003 · Cited by 1,498 · see citing works
Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446 · see citing works
An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
Wong, P. C., Pardo, C. A., Borchelt, D., Lee, M. K., Copeland, N. G., Jenkins, N. A., Sisodia, S. S., Cleveland, D. W., & Price, D. L. (1995) · Neuron · doi:10.1016/0896-6273(95)90259-7 · Cited by 1,439 · see citing works
Alpha-synuclein and neurodegenerative diseases
Goedert, M. (2001) · Nature reviews. Neuroscience · doi:10.1038/35081564 · Cited by 1,402 · see citing works
OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330 · see citing works
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303 · see citing works
Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
Nicklas, W. J., Vyas, I. L., & Heikkila, R. E. (1985) · Life Sciences · doi:10.1016/0024-3205(85)90146-8 · Cited by 1,266 · see citing works
Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
Kelly, D. P., & Scarpulla, R. C. (2004) · Genes & Development · doi:10.1101/gad.1177604 · Cited by 1,243 · see citing works
Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
West, A. B., Moore, D. J., Biskup, S., Bugayenko, A., Smith, W. W., Ross, C. A., Dawson, V. L., & Dawson, T. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507360102 · Cited by 1,228 · see citing works
Axonopathy and Transport Deficits Early in the Pathogenesis of Alzheimer’s Disease
Stokin, G. B., Lillo, C., Falzone, T. L., Brusch, R. G., Rockenstein, E., Mount, S. L., Raman, R., Davies, P., Masliah, E., Williams, D. S., et al. (2005) · Science · doi:10.1126/science.1105681 · Cited by 1,214 · see citing works
Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants
Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737556100 · Cited by 1,203 · see citing works
Defects in Adaptive Energy Metabolism with CNS-Linked Hyperactivity in PGC-1α Null Mice
Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., Zhang, C.-Y., Mootha, V. K., Jäger, S., Vianna, C. R., Reznick, R. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.013 · Cited by 1,162 · see citing works
A Serine Protease, HtrA2, Is Released from the Mitochondria and Interacts with XIAP, Inducing Cell Death
Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K., & Takahashi, R. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00341-0 · Cited by 1,116 · see citing works
The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization
Canet-Aviles, R., Wilson, M. A., Miller, D. W., Ahmad, R., McLendon, C., Bandyopadhyay, S., Baptista, M. J., Ringe, D., Petsko, G. A., & Cookson, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402959101 · Cited by 1,115 · see citing works
Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · see citing works
Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice
Zhu, S., Stavrovskaya, I. G., Drozda, M., Kim, B. Y. S., Ona, V. O., Li, M., Sarang, S. S., Liu, A. S., Hartley, D. M., Wu, D. C., et al. (2002) · Nature · doi:10.1038/417074a · Cited by 1,071 · see citing works
Clinical and Genetic Abnormalities in Patients with Friedreich's Ataxia
Dürr, A., Cossee, M., Agid, Y., Campuzano, V., Mignard, C., Penet, C., Mandel, J.-L., Brice, A., & Koenig, M. (1996) · New England Journal of Medicine · doi:10.1056/nejm199610173351601 · Cited by 1,071 · see citing works
Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
Panov, A. V., Gutekunst, C.-A., Leavitt, B. R., Hayden, M. R., Burke, J. R., Strittmatter, W. J., & Greenamyre, J. T. (2002) · Nature Neuroscience · doi:10.1038/nn884 · Cited by 1,030 · see citing works
Subcellular Distribution of Superoxide Dismutases (SOD) in Rat Liver
Okado‐Matsumoto, A., & Fridovich, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105395200 · Cited by 1,013 · see citing works
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012 · see citing works
A new mitochondrial disease associated with mitochondrial DNA heteroplasmy.
Holt, I. J., Harding, A. E., Petty, R., & MORGAN-HUGHES, J. A. (1990) · PubMed · Cited by 996 · see citing works
Mitochondrial Dysfunction and Oxidative Damage in parkin-deficient Mice
Palacino, J. J., Sagi, D., Goldberg, M. S., Krauss, S., Motz, C., Wacker, M., Klose, J., & Shen, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401135200 · Cited by 995 · see citing works
FRIEDREICH'S ATAXIA: A CLINICAL AND GENETIC STUDY OF 90 FAMILIES WITH AN ANALYSIS OF EARLY DIAGNOSTIC CRITERIA AND INTRAFAMILIAL CLUSTERING OF CLINICAL FEATURES
Harding, A. E. (1981) · Brain · doi:10.1093/brain/104.3.589 · Cited by 929 · see citing works
Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921 · see citing works
Superoxide Dismutase
Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43969-0 · Cited by 895 · see citing works
Mitochondrial DNA deletions in human brain: regional variability and increase with advanced age
Corral-Debrinski, M., Horton, T., Lott, M. T., Shoffner, J. M., Flint Beal, M., & Wallace, D. C. (1992) · Nature Genetics · doi:10.1038/ng1292-324 · Cited by 890 · see citing works
Oxidative damage and metabolic dysfunction in Huntington's disease: Selective vulnerability of the basal ganglia
Browne, S. E., Bowling, A. C., Macgarvey, U., Baik, M. J., Berger, S. C., Muquit, M. M. K., Bird, E. D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410514 · Cited by 885 · see citing works
Self-citation
Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons
Kraytsberg, Y., Kudryavtseva, E., McKee, A. C., Geula, C., Kowall, N. W., & Khrapko, K. (2006) · Nature Genetics · doi:10.1038/ng1778 · Cited by 884 · see citing works
Reconstitution of γ-secretase activity
Edbauer, D., Winkler, E., Regula, J. T., Pesold, B., Steiner, H., & Haass, C. (2003) · Nature Cell Biology · doi:10.1038/ncb960 · Cited by 882 · see citing works
DJ‐1 has a role in antioxidative stress to prevent cell death
Taira, T., Saito, Y., Niki, T., Iguchi‐Ariga, S. M. M., Takahashi, K., & Ariga, H. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400074 · Cited by 852 · see citing works
Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832 · cited 2× · see citing works
“…and Fuller 2001), is defective in a hereditary form of progressive axonal sensory polyneuropathy, known as Charcot-Marie-Tooth type 2A (Zuchner et al. 2004). mitofusin 2 defects result in a hyper-fragmented mitochondrial network and mitochondrial dysfunction (Bach et al. 2003; Honda et al. 2005).”
Background
Spastic Paraplegia and OXPHOS Impairment Caused by Mutations in Paraplegin, a Nuclear-Encoded Mitochondrial Metalloprotease
Casari, G., Fusco, M. D., Ciarmatori, S., Zeviani, M., Mora, M., Fernández‐Silva, P., Michele, G. D., Filla, A., Cocozza, S., Marconi, R., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81203-9 · Cited by 826 · see citing works
SUBACUTE NECROTIZING ENCEPHALOMYELOPATHY IN AN INFANT
Leigh, D. (1951) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.14.3.216 · Cited by 795 · see citing works
Frataxin is Reduced in Friedreich Ataxia Patients and is Associated with Mitochondrial Membranes
Campuzano, V., Montermini, L., Lutz, Y., Cova, L., Hindelang, C., Jiralerspong, S., Trottier, Y., Kish, S. J., Faucheux, B. A., Trouillas, P., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.11.1771 · Cited by 739 · see citing works
Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., & Koenig, M. (2001) · Nature Genetics · doi:10.1038/84818 · Cited by 738 · see citing works
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738 · see citing works
Massive Mitochondrial Degeneration in Motor Neurons Triggers the Onset of Amyotrophic Lateral Sclerosis in Mice Expressing a Mutant SOD1
Kong, J., & Xu, Z. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-09-03241.1998 · Cited by 723 · see citing works
A Fraction of Yeast Cu,Zn-Superoxide Dismutase and Its Metallochaperone, CCS, Localize to the Intermembrane Space of Mitochondria
Sturtz, L. A., Diekert, K., Jensen, L. T., Lill, R., & Culotta, V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105296200 · Cited by 719 · see citing works
Functional Role of Caspase-1 and Caspase-3 in an ALS Transgenic Mouse Model
Li, M., Ona, V. O., Guégan, C., Chen, M., Jackson-Lewis, V. R., Andrews, L. J., Olszewski, A. J., Stieg, P. E., Lee, J.-P., Przedborski, S., et al. (2000) · Science · doi:10.1126/science.288.5464.335 · Cited by 717 · see citing works
α-Synuclein Promotes Mitochondrial Deficit and Oxidative Stress
Hsu, L. J., Sagara, Y., Arroyo, A., Rockenstein, E. M., Sisk, A., Mallory, M. E., Wong, J., Takenouchi, T., Hashimoto, M., & Masliah, E. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64553-1 · Cited by 716 · see citing works
Sp1 and TAFII130 Transcriptional Activity Disrupted in Early Huntington's Disease
Dunah, A. W., Jeong, H., Griffin, A. M., Kim, Y., Standaert, D. G., Hersch, S. M., Mouradian, M. M., Young, A. B., Tanese, N., & Krainc, D. (2002) · Science · doi:10.1126/science.1072613 · Cited by 708 · see citing works
Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress
Kim, R. H., Smith, P. D., Aleyasin, H., Hayley, S. P., Mount, M. P., Pownall, S., Wakeham, A. C., You-Ten, A. J., Kalia, S. K., Horne, P., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501282102 · Cited by 697 · see citing works
Parkinson's Disease α-Synuclein Transgenic Mice Develop Neuronal Mitochondrial Degeneration and Cell Death
Martin, L. J., Pan, Y., Price, A. C., Sterling, W., Copeland, N. G., Jenkins, N. A., Price, D. L., & Lee, M. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4308-05.2006 · Cited by 684 · see citing works
Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
Bubber, P., Haroutunian, V., Fisch, G., Blass, J. P., & Gibson, G. E. (2005) · Annals of Neurology · doi:10.1002/ana.20474 · Cited by 622 · see citing works
Mutated Human SOD1 Causes Dysfunction of Oxidative Phosphorylation in Mitochondria of Transgenic Mice
Mattiazzi, M., D’Aurelio, M., Gajewski, C. D., Martushova, K., Kiaei, M., Beal, M. F., & Manfredi, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203065200 · Cited by 616 · see citing works
Self-citation
Resistance of α-synuclein null mice to the parkinsonian neurotoxin MPTP
Dauer, W. T., Kholodilov, N. G., Vila, M., Trillat, A., Goodchild, R. E., Larsen, K. E., Staal, R. G. W., Tieu, K., Schmitz, Y., Yuan, C. A., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172514599 · Cited by 580 · see citing works
Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207030 · Cited by 571 · see citing works
Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease
Strauss, K. M., Martins, L. M., Plun‐Favreau, H., Marx, F. P., Kautzmann, S., Berg, D., Gasser, T., Wszolek, Z., Müller, T. H., Bornemann, A., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi215 · Cited by 569 · see citing works
Parkinsonism, premature menopause, and mitochondrial DNA polymerase γ mutations: clinical and molecular genetic study
Luoma, P., Melberg, A., Rinne, J. O., Kaukonen, J. A., Nupponen, N. N., Chalmers, R. M., Oldfors, A., Rautakorpi, I., Peltonen, L., Majamaa, K., et al. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16983-3 · Cited by 548 · see citing works
Emerging functions of mammalian mitochondrial fusion and fission
Chen, H., & Chan, D. C. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi270 · Cited by 538 · see citing works
Brain cytochrome oxidase in Alzheimer's disease
Kish, S. J., Bergeron, C., Rajput, A., Dozic, S., Mastrogiacomo, F., Chang, L., Wilson, J. M., DiStefano, L. M., & Nobrega, J. N. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09439.x · Cited by 537 · see citing works
Mitochondrial Polymorphisms Significantly Reduce the Risk of Parkinson Disease
van der Walt, J. M., Nicodemus, K. K., Martin, E. R., Scott, W. K., NANCE, M. A., Watts, R. L., Hubble, J. P., Haines, J. L., Koller, W. C., Lyons, K. E., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/373937 · Cited by 537 · see citing works
Cortical Cytochrome Oxidase Activity Is Reduced in Alzheimer's Disease
Mutisya, E. M., Bowling, A. C., & Beal, M. F. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63062179.x · Cited by 531 · see citing works
Self-citation
Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
Choo, Y. S. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh162 · Cited by 515 · see citing works
Toxicity of Familial ALS-Linked SOD1 Mutants from Selective Recruitment to Spinal Mitochondria
Liu, J., Lillo, C., Jonsson, P. A., Velde, C. V., Ward, C. M., Miller, T. M., Subramaniam, J. R., Rothstein, J. D., Marklund, S. L., Andersen, P. M., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.016 · Cited by 506 · see citing works
Amyotrophic Lateral Sclerosis-Associated SOD1 Mutant Proteins Bind and Aggregate with Bcl-2 in Spinal Cord Mitochondria
Pasinelli, P., Belford, M. E., Lennon, N. J., Bacskai, B. J., Hyman, B. T., Trotti, D., & Brown, R. H. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.021 · Cited by 506 · see citing works
β‐Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
Casley, C. S., Canevari, L., Land, J. M., Clark, J. B., & Sharpe, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00681.x · Cited by 485 · see citing works
Vesicle Permeabilization by Protofibrillar α-Synuclein Is Sensitive to Parkinson's Disease-Linked Mutations and Occurs by a Pore-like Mechanism
Volles, M. J., & Lansbury, P. T. (2002) · Biochemistry · doi:10.1021/bi0121353 · Cited by 485 · see citing works
3-Nitropropionic Acid - Exogenous Animal Neurotoxin and Possible Human Striatal Toxin
Ludolph, A. C., He, F., Spencer, P. S., Hammerstad, J. P., & Sabri, M. I. (1991) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100032212 · Cited by 484 · see citing works
Heteroplasmic mtDNA mutation (T----G) at 8993 can cause Leigh disease when the percentage of abnormal mtDNA is high.
Tatuch, Y., Christodoulou, J., Feigenbaum, A., Clarke, J. T. R., Wherret, J., Smith, C., Rudd, N., Petrova-Benedict, R., & Robinson, B. H. (1992) · PubMed · Cited by 483 · see citing works
p53 Mediates Cellular Dysfunction and Behavioral Abnormalities in Huntington’s Disease
Bae, B.-I., Xu, H., Igarashi, S., Fujimuro, M., Agrawal, N., Taya, Y., Hayward, S. D., Moran, T. H., Montell, C., Ross, C. A., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.005 · Cited by 480 · see citing works
Evidence for irnnairment of energy metabofism in vivo in Huntington's disease using localized 1H NMR spectroscopy
Jenkins, B. G., Koroshetz, W. J., Beal, M. F., & Rosen, B. R. (1993) · Neurology · doi:10.1212/wnl.43.12.2689 · Cited by 479 · see citing works
Self-citation
Bcl-2: Prolonging Life in a Transgenic Mouse Model of Familial Amyotrophic Lateral Sclerosis
Kostić, V., Jackson-Lewis, V. R., de Bilbao, F., Dubois‐Dauphin, M., & Przedborski, S. (1997) · Science · doi:10.1126/science.277.5325.559 · Cited by 477 · see citing works
Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
Silvestri, L., Caputo, V., Bellacchio, E., Atorino, L., Dallapiccola, B., Valente, E. M., & Casari, G. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi377 · Cited by 449 · see citing works
Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
Pesah, Y., Pham, T., Burgess, H., Middlebrooks, B. W., Verstreken, P., Zhou, Y., Harding, M. J., Bellen, H. J., & Mardon, G. (2004) · Development · doi:10.1242/dev.01095 · Cited by 441 · see citing works
The human dynamin‐related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter‐membrane space
Olichon, A., Emorine, L. J., Descoins, E., Pelloquin, L., Brichese, L., Gas, N., Guillou, E., Delettre, C., Valette, A., Hamel, C., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02985-x · Cited by 430 · see citing works
Increased glutathione S -transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease
Whitworth, A. J., Theodore, D. A., Greene, J. C., Beneš, H., Wes, P. D., & Pallanck, L. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501078102 · Cited by 421 · see citing works
Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration
Smith, W. W., Pei, Z., Jiang, H., Moore, D. J., Liang, Y., West, A. B., Dawson, V. L., Dawson, T. M., & Ross, C. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508052102 · Cited by 420 · see citing works
Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis
Zhang, L., Shimoji, M., Thomas, B., Moore, D. J., Yu, S.-W., Marupudi, N. I., Torp, R., Torgner, I. A., Ottersen, O. P., Dawson, T. M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi211 · Cited by 418 · see citing works
Haplotype and phylogenetic analyses suggest that one European-specific mtDNA background plays a role in the expression of Leber hereditary optic neuropathy by increasing the penetrance of the primary mutations 11778 and 14484.
Torroni, A., Petrozzi, M., D'Urbano, L., Sellitto, D., Zeviani, M., Carrara, F., Carducci, C., Leuzzi, V., Carelli, V., Barboni, P., et al. (1997) · Europe PMC (PubMed Central) · Cited by 417 · see citing works
Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain
Soong, N. W., Hinton, D. R., Cortopassi, G. A., & Arnheim, N. (1992) · Nature Genetics · doi:10.1038/ng1292-318 · Cited by 414 · see citing works
Energy metabolism defects in Huntington's disease and effects of coenzyme Q10
Koroshetz, W. J., Jenkins, B. G., Rosen, B. R., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410206 · Cited by 405 · see citing works
Self-citation
Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
Darios, F. D. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg044 · Cited by 401 · see citing works
Leber hereditary optic neuropathy: identification of the same mitochondrial ND1 mutation in six pedigrees.
Howell, N., Bindoff, L. A., McCullough, D. A., Kubacka, I., Poulton, J., Mackey, D. A., Taylor, L., & Turnbull, D. M. (1991) · PubMed · Cited by 400 · see citing works
The m-AAA Protease Defective in Hereditary Spastic Paraplegia Controls Ribosome Assembly in Mitochondria
Nolden, M., Ehses, S., Koppen, M., Bernacchia, A., Rugarli, E. I., & Langer, T. (2005) · Cell · doi:10.1016/j.cell.2005.08.003 · Cited by 398 · see citing works
Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis.
Canto, M. C. D., & Gurney, M. E. (1994) · PubMed · Cited by 395 · see citing works
Neuroprotective Role of the Reaper-Related Serine Protease HtrA2/Omi Revealed by Targeted Deletion in Mice
Martins, L. M., Morrison, A., Klupsch, K., Fedele, V., Moisoi, N., Teismann, P., Abuin, A., Grau, E., Geppert, M., Livi, G. P., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.22.9848-9862.2004 · Cited by 395 · see citing works
Altered Metabolism of the Amyloid β Precursor Protein Is Associated with Mitochondrial Dysfunction in Down's Syndrome
Busciglio, J., Pelsman, A., Wong, C., Pigino, G., Yuan, M., Mori, H., & Yankner, B. A. (2002) · Neuron · doi:10.1016/s0896-6273(02)00604-9 · Cited by 387 · see citing works
An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease
Du Yan, S., Fu, J., Soto, C., Chen, X., Zhu, H., Al-Mohanna, F., Collison, K., Zhu, A., Stern, E., Saido, T., et al. (1997) · Nature · doi:10.1038/39522 · Cited by 379 · see citing works
Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
Foury, F., & Cazzalini, O. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00734-5 · Cited by 378 · see citing works
The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
Wong, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.3.425 · Cited by 374 · see citing works
Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture
Cooper, J. K. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.5.783 · Cited by 374 · see citing works
Hereditary Spastic Paraplegia SPG13 Is Associated with a Mutation in the Gene Encoding the Mitochondrial Chaperonin Hsp60
Hansen, J. J., Dürr, A., Cournu‐Rebeix, I., Georgopoulos, C. P., Ang, D., Nielsen, M. N., Davoine, C.-S., Brice, A., Fontaine, B., Gregersen, N., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/339935 · Cited by 373 · see citing works
Frataxin Acts as an Iron Chaperone Protein to Modulate Mitochondrial Aconitase Activity
Bulteau, A.-L., O’Neill, H. A., Kennedy, M. C., Ikeda‐Saito, M., Isaya, G., & Szweda, L. I. (2004) · Science · doi:10.1126/science.1098991 · Cited by 372 · see citing works
High aggregate burden of somatic mtDNA point mutations in aging and Alzheimer's disease brain
Lin, M. T. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.2.133 · Cited by 366 · see citing works
Huntington aggregates may not predict neuronal death in Huntington's disease.
Kuemmerle, S., Gutekunst, C., Klein, A., Li, X. J., Li, S. H., Beal, M. F., Hersch, S. M., & Ferrante, R. J. (1999) · PubMed · Cited by 362 · see citing works
Self-citation
Axonal neuropathy with optic atrophy is caused by mutations in mitofusin 2
Zuchner, S. L., Jonghe, P. D., Jordanova, A., Claeys, K. G., Guergueltcheva, V., Cherninkova, S., Hamilton, S. R., Stavern, G. P. V., Krajewski, K. M., Stajich, J. M., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20797 · Cited by 357 · see citing works
Effect of idebenone on cardiomyopathy in Friedreich's ataxia: a preliminary study
Rustin, P., von Kleist-Retzow, J., Chantrel-Groussard, K., Sidi, D., Münnich, A., & Rötig, A. (1999) · The Lancet · doi:10.1016/s0140-6736(99)01341-0 · Cited by 348 · see citing works
Interaction of Huntington Disease Protein with Transcriptional Activator Sp1
Li, S.-H., Cheng, A. L., Zhou, H., Lam, S., Rao, M., He, L., & Li, X. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1277-1287.2002 · Cited by 343 · see citing works
Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling
Yang, Y., Gehrke, S., Haque, M. E., Imai, Y., Kosek, J. C., Yang, L., Beal, M. F., Nishimura, I., Wakamatsu, K., Ito, S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504610102 · Cited by 338 · see citing works
Self-citation
Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells.
Rabizadeh, S., Gralla, E. B., Borchelt, D., Gwinn, R. P., Valentine, J. S., Sisodia, S., Wong, P., Lee, M. K., Hahn, H., & Bredesen, D. E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.3024 · Cited by 335 · see citing works
The victorin‐induced mitochondrial permeability transition precedes cell shrinkage and biochemical markers of cell death, and shrinkage occurs without loss of membrane integrity
Curtis, M. J., & Wolpert, T. (2004) · The Plant Journal · doi:10.1111/j.1365-313x.2004.02040.x · Cited by 334 · see citing works
Wild-type PINK1 Prevents Basal and Induced Neuronal Apoptosis, a Protective Effect Abrogated by Parkinson Disease-related Mutations
Petit-Paitel, A., Kawarai, T., Paitel, E., Sanjo, N., Maj, M. C., Scheid, M. P., Chen, F., Gu, Y., Hasegawa, H., Salehi‐Rad, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505143200 · Cited by 329 · see citing works
Copper-Dependent Inhibition of Human CytochromecOxidase by a Dimeric Conformer of Amyloid-β1-42
Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327 · see citing works
Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis
Shirane, M., & Nakayama, K. I. (2002) · Nature Cell Biology · doi:10.1038/ncb894 · Cited by 319 · see citing works
Sticky DNA
Sakamoto, N., Chastain, P. D., Parniewski, P., Ohshima, K., Pandolfo, M., Griffith, J. D., & Wells, R. D. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80474-8 · Cited by 313 · see citing works
Oxidative stress in patients with Friedreich ataxia
Schulz, J. B., Dehmer, T., Schöls, L. J., Mende, H. E., Hardt, C., Vorgerd, M., Bürk, K., Matson, W. R., DICHGANS, J., Beal, M. F., et al. (2000) · Neurology · doi:10.1212/wnl.55.11.1719 · Cited by 305 · see citing works
Self-citation
Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
Chang, D. T. W., Rintoul, G. L., Pandipati, S., & Reynolds, I. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.12.007 · Cited by 299 · see citing works
Age‐Dependent Striatal Excitotoxic Lesions Produced by the Endogenous Mitochondrial Inhibitor Malonate
Beal, M. F., Brouillet, E., Jenkins, B. G., Henshaw, R., Rosen, B. R., & Hyman, B. T. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03633.x · Cited by 297 · see citing works
Self-citation
Enhanced substantia nigra mitochondrial pathology in human α-synuclein transgenic mice after treatment with MPTP111-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine.
Song, D. D., Shults, C. W., Sisk, A., Rockenstein, E. M., & Masliah, E. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00342-x · Cited by 294 · see citing works
HD CAG repeat implicates a dominant property of huntingtin in mitochondrial energy metabolism
Seong, I. S., Ivanova, E. V., Lee, J., Choo, Y. S., Fossale, E., Anderson, M., Gusella, J. F., Laramie, J. M., Myers, R. H., Lesort, M. J., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi319 · Cited by 291 · see citing works
DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin
Mitsumoto, A., & Nakagawa, Y. (2001) · Free Radical Research · doi:10.1080/10715760100301381 · Cited by 285 · see citing works
Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
Atorino, L., Silvestri, L., Koppen, M., Cassina, L., Ballabio, A., Marconi, R., Langer, T., & Casari, G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304112 · Cited by 283 · see citing works
Mitochondrial dysfunction in a cell culture model of familial amyotrophic lateral sclerosis
Menzies, F. M. (2002) · Brain · doi:10.1093/brain/awf167 · Cited by 279 · see citing works
ALS-Linked Cu/Zn–SOD Mutation Increases Vulnerability of Motor Neurons to Excitotoxicity by a Mechanism Involving Increased Oxidative Stress and Perturbed Calcium Homeostasis
Kruman, I. I., Pedersen, W. A., Springer, J. E., & Mattson, M. P. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7190 · Cited by 268 · see citing works
Parkin enhances mitochondrial biogenesis in proliferating cells
Kuroda, Y., Mitsui, T., Kunishige, M., Shono, M., Akaike, M., Azuma, H., & Matsumoto, T. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl006 · Cited by 268 · see citing works
ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes
Higgins, C. M. J., Jung, C., & Xu, Z. (2003) · BMC Neuroscience · doi:10.1186/1471-2202-4-16 · Cited by 262 · see citing works
Crystal Structure of Human DJ-1, a Protein Associated with Early Onset Parkinson's Disease
Tao, X., & Tong, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304221200 · Cited by 256 · see citing works
Nicastrin, Presenilin, APH-1, and PEN-2 Form Active γ-Secretase Complexes in Mitochondria
Hansson, C. A., Frykman, S., Farmery, M. R., Tjernberg, L. O., Nilsberth, C., Pursglove, S. E., Ito, A., Winblad, B., Cowburn, R. F., Thyberg, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404500200 · Cited by 256 · see citing works
ABAD enhances Aβ‐induced cell stress via mitochondrial dysfunction
Takuma, K., Yao, J., Huang, J., Xu, H., Chen, X., Luddy, J. S., Trillat, A., Stern, D. M., Arancio, O., & Yan, S. S. (2005) · The FASEB Journal · doi:10.1096/fj.04-2582fje · Cited by 254 · see citing works
Mutant Superoxide Dismutase 1 Forms Aggregates in the Brain Mitochondrial Matrix of Amyotrophic Lateral Sclerosis Mice
Vijayvergiya, C., Beal, M. F., Buck, J., & Manfredi, G. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4385-04.2005 · Cited by 251 · see citing works
Self-citation
Idebenone and reduced cardiac hypertrophy in Friedreich's ataxia
HAUSSE, A., Aggoun, Y., Bonnet, D., Sidi, D., Münnich, A., Rötig, A., & Rustin, P. (2002) · Heart · doi:10.1136/heart.87.4.346 · Cited by 251 · see citing works
Neural mitochondrial Ca 2+ capacity impairment precedes the onset of motor symptoms in G93A Cu/Zn‐superoxide dismutase mutant mice
Damiano, M. G., Starkov, A. A., Petri, S., Kipiani, K., Kiaei, M., Mattiazzi, M., Beal, M. F., & Manfredi, G. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03619.x · Cited by 247 · see citing works
Self-citation
Amyotrophic lateral sclerosis: A proposed mechanism
Okado‐Matsumoto, A., & Fridovich, I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132260399 · Cited by 247 · see citing works
Ubiquitin–proteasome system and Parkinson's diseases
Betarbet, R. S., Sherer, T., & Greenamyre, J. T. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.08.021 · Cited by 245 · see citing works
Accumulation of deletions in human mitochondrial DNA during normal aging: analysis by quantitative PCR
Simonetti, S., Chen, X., DiMauro, S., & Schon, E. A. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(92)90059-v · Cited by 241 · see citing works
Mutant Cu, Zn Superoxide Dismutase that Causes Motoneuron Degeneration Is Present in Mitochondria in the CNS
Higgins, C. M. J., Jung, C., Ding, H., & Xu, Z. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-06-j0001.2002 · Cited by 239 · see citing works
Mitochondrial complex I and IV activities in leukocytes from patients with parkin mutations
Müftüoğlu, M., Elibol, B., Dalmızrak, Ö., Ercan, A., Kulaksiz-Erkmen, G., Öğüş, İ. H., Dalkara, T., & Özer, N. (2003) · Movement Disorders · doi:10.1002/mds.10695 · Cited by 237 · see citing works
Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH‐SY5Y cells
Carrı̀, M. T., Ferri, A., Battistoni, A., Famhy, L., Gabbianelli, R., Poccia, F., & Rotilio, G. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01051-x · Cited by 221 · see citing works
The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants
Mattiazzi, M. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh103 · Cited by 221 · see citing works
Friedreich ataxia: the oxidative stress paradox
Seznec, H., Simon, D., Bouton, C., Reutenauer, L., Hertzog, A., Golik, P., Procaccio, V., Patel, M., Drapier, J.-C., Koenig, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi042 · Cited by 219 · see citing works
The role of mtDNA background in disease expression: a new primary LHON mutation associated with Western Eurasian haplogroup J
Brown, M. D., Starikovskaya, E. B., Derbeneva, O. A., Hosseini, S., Allen, J. C., Mikhailovskaya, I. E., Sukernik, R. I., & Wallace, D. C. (2002) · Human Genetics · doi:10.1007/s00439-001-0660-8 · Cited by 215 · see citing works
Mice lacking alpha-synuclein are resistant to mitochondrial toxins
Klivènyi, P., Siwek, D. F., Gardian, G., Yang, L., Starkov, A. A., Cléren, C., Ferrante, R. J., Kowall, N. W., Abeliovich, A., & Beal, M. F. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.08.018 · Cited by 213 · see citing works
Self-citation
Mitochondrial Cyclic AMP Response Element-binding Protein (CREB) Mediates Mitochondrial Gene Expression and Neuronal Survival
Lee, J.-H., Kim, C., Simon, D. K., Aminova, L. R., Andreyev, A. Y., Kushnareva, Y. E., Murphy, A. N., Lonze, B. E., Kim, K. S., Ginty, D. D., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500140200 · Cited by 213 · see citing works
Friedreich Ataxia Mouse Models with Progressive Cerebellar and Sensory Ataxia Reveal Autophagic Neurodegeneration in Dorsal Root Ganglia
Simon, D., Seznec, H., Gansmuller, A., Carelle, N., Weber, P., Metzger, D., Rustin, P., Koenig, M., & Puccio, H. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4549-03.2004 · Cited by 205 · see citing works
Adult-derived neural precursors transplanted into multiple regions in the adult brain
Herrera, D. G., García‐Verdugo, J. M., & Álvarez-Buylla, A. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199912)46:6 · Cited by 204 · see citing works
The GAATTC triplet repeat expanded in Friedreich's ataxia impedes transcription elongation by T7 RNA polymerase in a length and supercoil dependent manner
Grabczyk, E. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.14.2815 · Cited by 203 · see citing works
Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosis
Jung, C., Higgins, C. M. J., & Xu, Z. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01112.x · Cited by 202 · see citing works
Mutant Cu/Zn-Superoxide Dismutase Proteins Have Altered Solubility and Interact with Heat Shock/Stress Proteins in Models of Amyotrophic Lateral Sclerosis
Shinder, G. A., Lacourse, M.-C., Minotti, S., & Durham, H. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010759200 · Cited by 202 · see citing works
CytochromecAssociation with the Inner Mitochondrial Membrane Is Impaired in the CNS of G93A-SOD1 Mice
Kirkinezos, I. G., Bacman, S. R., Hernandez, D., Oca‐Cossio, J., Arias, L. J., Pérez‐Pinzón, M. A., Bradley, W. G., & Moraes, C. T. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3829-04.2005 · Cited by 200 · see citing works
Reduced platelet cytochrome c oxidase activity in Alzheimer's disease
Parker, W. D., Mahr, N., Filley, C. M., Parks, J. K., Hughes, D., Young, D. A., & Cullum, C. M. (1994) · Neurology · doi:10.1212/wnl.44.6.1086 · Cited by 199 · see citing works
Mutant Superoxide Dismutase-1-Linked Familial Amyotrophic Lateral Sclerosis: Molecular Mechanisms of Neuronal Death and Protection
Ghadge, G. D., Lee, J. P., Bindokas, V. P., Jordán, J., Ma, L., Miller, R. J., & Roos, R. P. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-22-08756.1997 · Cited by 195 · see citing works
Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis
Greene, J. C., Whitworth, A. J., Andrews, L. A., Parker, T. J., & Pallanck, L. J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi074 · Cited by 194 · see citing works
Cytoplasmic transfer of the mtDNA nt 8993 T-->G (ATP6) point mutation associated with Leigh syndrome into mtDNA-less cells demonstrates cosegregation with a decrease in state III respiration and ADP/O ratio.
Trounce, I. A., Neill, S. G., & Wallace, D. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8334 · Cited by 190 · see citing works
Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
Gakh, O., Park, S., Liu, G., Macomber, L., Imlay, J. A., Ferreira, G. C., & Isaya, G. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi461 · Cited by 184 · see citing works
Mitochondrial DNA haplogroup cluster UKJT reduces the risk of PD
Pyle, A., Foltynie, T., Tiangyou, W., Lambert, C., Keers, S. M., Allcock, L. M., Davison, J., Lewis, S. J. G., Perry, R. H., Barker, R. A., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20417 · Cited by 176 · see citing works
Excitotoxicity hypothesis
Rothstein, J. D. (1996) · Neurology · doi:10.1212/wnl.47.4_suppl_2.19s · Cited by 172 · see citing works
Population Genetics and Disease Susceptibility: Characterization of Central European Haplogroups By mtDNA Gene Mutations, Correlation with D Loop Variants and Association With Disease
Hofmann, S., Jaksch, M., Bezold, R., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.11.1835 · Cited by 170 · see citing works
The mitochondrial ND6 gene is a hot spot for mutations that cause Leber's hereditary optic neuropathy
Chinnery, P. F., Brown, D. T., Andrews, R. M., Kler, R. S., Riordan‐Eva, P., Lindley, J., Applegarth, D. A., Turnbull, D. M., & Howell, N. (2001) · Brain · doi:10.1093/brain/124.1.209 · Cited by 166 · see citing works
Mitochondrial encephalomyopathies: an update
DiMauro, S., & Hirano, M. (2005) · Neuromuscular Disorders · doi:10.1016/j.nmd.2004.12.008 · Cited by 162 · see citing works
The Hereditary Spastic Paraplegias
Fink, J. K. (2003) · Archives of Neurology · doi:10.1001/archneur.60.8.1045 · Cited by 154 · see citing works
Mitochondrial Localization of Mutant Superoxide Dismutase 1 Triggers Caspase-dependent Cell Death in a Cellular Model of Familial Amyotrophic Lateral Sclerosis*
Takeuchi, H., Kobayashi, Y., Ishigaki, S., Doyu, M., & Sobue, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209356200 · Cited by 154 · see citing works
Membrane protein degradation by AAA proteases in mitochondria
Arnold, I., & Langer, T. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00267-7 · Cited by 150 · see citing works
The mitochondrial DNA mutation at 8993 associated with NARP slows the rate of ATP synthesis in isolated lymphoblast mitochondria.
Tatuch, Y., & Robinson, B. H. (1993) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1006/bbrc.1993.1390 · Cited by 142 · see citing works
Pathogenic expression of homoplasmic mtDNA mutations needs a complex nuclear–mitochondrial interaction
Carelli, V., Giordano, C., & d’Amati, G. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00072-6 · Cited by 142 · see citing works
Familial multisystem degeneration with parkinsonism associated with the 11778 mitochondrial DNA mutation
Simon, D. K., Pulst, S. M., Sutton, J. P., Browne, S. E., Beal, M. F., & Johns, D. R. (1999) · Neurology · doi:10.1212/wnl.53.8.1787 · Cited by 141 · see citing works
Self-citation
Frataxin deficiency in pancreatic islets causes diabetes due to loss of β cell mass
Ristow, M., Mulder, H., Pomplun, D., Schulz, T. J., Schmehl, K., Krause, A., Fex, M., Puccio, H. M., Müller, J., Isken, F., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18107 · Cited by 131 · see citing works
Targeted disruption of hepatic frataxin expression causes impaired mitochondrial function, decreased life span and tumor growth in mice
Thierbach, R., Schulz, T. J., Isken, F., Voigt, A., Mietzner, B., Drewes, G., von Kleist-Retzow, J.-C., Wiesner, R. J., Magnuson, M. A., Puccio, H., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi410 · Cited by 127 · see citing works
Mitochondrial DNA polymorphisms as risk factors for Parkinson?s disease and Parkinson?s disease dementia
Finnil�, S., Autere, J. M., Moilanen, J. S., Soininen, H. S., Mannermaa, A., Hartikainen, P., Hallikainen, M., & Majamaa, K. (2004) · Human Genetics · doi:10.1007/s00439-004-1123-9 · Cited by 120 · see citing works
Leber hereditary optic neuropathy mtDNA mutations disrupt glutamate transport in cybrid cell lines
Beretta, S. (2004) · Brain · doi:10.1093/brain/awh258 · Cited by 120 · 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
Mutant huntingtin represses CBP, but not p300, by binding and protein degradation
Cong, S., Pepers, B. A., Evert, B. O., Rubinsztein, D. C., Roos, R. A. C., van Ommen, G. B., & Dorsman, J. C. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.05.003 · Cited by 116 · see citing works
Cellular localization and development of neuronal intranuclear inclusions in striatal and cortical neurons in R6/2 transgenic mice
Meade, C. A., Deng, Y., Fusco, F. R., Mar, N. D., Hersch, S. M., Goldowitz, D., & Reiner, A. J. (2002) · The Journal of Comparative Neurology · doi:10.1002/cne.10295 · Cited by 111 · see citing works
UCHL‐1 is not a Parkinson's disease susceptibility gene
Healy, D. G., Abou‐Sleiman, P. M., Casas, J. P., Ahmadi, K. R., Lynch, T., Gandhi, S., Muqit, M. M. K., Foltynie, T., Barker, R. A., Bhatia, K. P., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20757 · Cited by 109 · see citing works
Interactions between mitochondrial bioenergetics and cytoplasmic calcium in cultured cerebellar granule cells
Nicholls, D. G., Vesce, S., Kirk, L., & Chalmers, S. (2003) · Cell Calcium · doi:10.1016/s0143-4160(03)00144-1 · Cited by 108 · see citing works
Juvenile Huntington chorea
Goebel, H. H., Heipertz, R., Scholz, W. W., Iqbal, K., & Tellez-Nagel, I. (1978) · Neurology · doi:10.1212/wnl.28.1.23 · Cited by 108 · see citing works
Prolongation of the Normal Life Span by Radiation Protection Chemicals
Harman, D. (1957) · Journal of Gerontology · doi:10.1093/geronj/12.3.257 · Cited by 108 · see citing works
Antioxidant defences in cybrids harboring mtDNA mutations associated with Leber's hereditary optic neuropathy
Floreani, M., Napoli, E., Martinuzzi, A., Pantano, G., Riva, V., Trevisan, R., Bisetto, E., Valente, L., Carelli, V., & Dabbeni‐Sala, F. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2004.04542.x · Cited by 106 · see citing works
Mitochondrial DNA mutations in complex I and tRNA genes in Parkinson’s disease
Simon, D. K., Mayeux, R. P., Marder, K. S., Kowall, N. W., Beal, M. F., & Johns, D. R. (2000) · Neurology · doi:10.1212/wnl.54.3.703 · Cited by 106 · see citing works
Self-citation
The crucial role of caspase‐9 in the disease progression of a transgenic ALS mouse model
Inoue, H., Tsukita, K., Iwasato, T., Suzuki, Y., Tomioka, M., Tateno, M., Nagao, M., Kawata, A., Saido, T. C., Miura, M., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg634 · Cited by 106 · see citing works
Altered properties of mitochondrial ATP-synthase in patients with a T → G mutation in the ATPase 6 (subunit a) gene at position 8993 of mtDNA
Houštěk, J., Klement, P., Heřmanská, J., Houšt'ková, H., Hansíková, H., den Bogert, C. V., & Zeman, J. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00063-a · Cited by 105 · see citing works
Smoking as an aetiological factor in a pedigree with Leber's hereditary optic neuropathy
Tsao, K., Aitken, P. A., & Johns, D. R. (1999) · British Journal of Ophthalmology · doi:10.1136/bjo.83.5.577 · Cited by 105 · see citing works
Oligomycin Induces a Decrease in the Cellular Content of a Pathogenic Mutation in the Human Mitochondrial ATPase 6 Gene
Manfredi, G., Gupta, N., Vazquez-Memije, M. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9386 · Cited by 105 · see citing works
Self-citation
Interaction of presenilins with FKBP38 promotes apoptosis by reducing mitochondrial Bcl-2
Wang, H.-Q., Nakaya, Y., Du, Z., Yamane, T., Shirane, M., Kudo, T., Takeda, M., Takebayashi, K., Noda, Y., Nakayama, K. I., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi195 · Cited by 86 · see citing works
Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with amyotrophic lateral sclerosis is reversed by N-acetylcysteine
Beretta, S., Sala, G., Mattavelli, L., Ceresa, C., Casciati, A., Ferri, A., Carrı̀, M. T., & Ferrarese, C. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00043-3 · Cited by 81 · see citing works
Functional integrity of mitochondrial genomes in human platelets and autopsied brain tissues from elderly patients with Alzheimer’s disease
Ito, S., Ohta, S., Nishimaki, K., Kagawa, Y., Soma, R., Kuno, S., Komatsuzaki, Y., Mizusawa, H., & Hayashi, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2099 · Cited by 80 · see citing works
Sequence Analysis of the Entire Mitochondrial Genome in Parkinson's Disease
Vives-Bauzá, C., Andreu, A. L., Manfredi, G., Beal, M. F., Janetzky, B., Gruenewald, T. H., & Lin, M. T. S. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6388 · Cited by 73 · see citing works
Self-citation
Effects of Wild‐Type and Mutated Copper/Zinc Superoxide Dismutase on Neuronal Survival and l ‐DOPA‐Induced Toxicity in Postnatal Midbrain Culture
Mena, M. A., Khan, U., Togasaki, D. M., Sulzer, D. L., Epstein, C. J., & Przedborski, S. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69010021.x · Cited by 64 · see citing works
Presenilin-1 is located in rat mitochondria
Ankarcrona, M., & Hultenby, K. R. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00735-0 · Cited by 63 · see citing works
Abundant type 10 17β-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer’s disease model
He, X., Wen, G. Y., Merz, G., Lin, D., Yang, Y.-Z., Mehta, P., Schulz, H., & Yang, S.-Y. (2002) · Molecular Brain Research · doi:10.1016/s0169-328x(02)00102-x · Cited by 62 · see citing works
Inhibition of the α-ketoglutarate dehydrogenase complex alters mitochondrial function and cellular calcium regulation
Huang, H.-M., Zhang, H., Xu, H., & Gibson, G. E. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(02)00222-3 · Cited by 61 · see citing works
Comparative biochemical studies in fibroblasts from patients with different forms of Leigh syndrome
Vázquez-Memije, M. E., Shanske, S., Santorelli, F. M., et al. (1995) · Journal of Inherited Metabolic Disease · doi:10.1007/bf01799347 · Cited by 58 · see citing works
Endogenous oxidative stress in sporadic Alzheimer’s disease neuronal cybrids reduces viability by increasing apoptosis through pro-death signaling pathways and is mimicked by oxidant exposure of control cybrids
Onyango, I. G., Bennett, J. P., & Tuttle, J. B. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.01.026 · Cited by 56 · see citing works
Mutational analysis of action of mitochondrial fusion factor mitofusin-2
Honda, S., Aihara, T., Hontani, M., Okubo, K., & Hirose, S. (2005) · Journal of Cell Science · doi:10.1242/jcs.02449 · Cited by 53 · see citing works
Altered distribution of mitochondria impairs calcium homeostasis in rat hippocampal neurons in culture
Wang, G. J., Jackson, J. G., & Thayer, S. A. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01970.x · Cited by 49 · see citing works
Regulators of membrane trafficking andMycobacterium tuberculosis phagosome maturation block
Fratti, R. A., Vergne, I., Chua, J., Skidmore, J. M., & Deretic, V. P. (2000) · Electrophoresis · doi:10.1002/1522-2683(20001001)21:16 · Cited by 43 · see citing works
Rapid Aggregate Formation of the Huntingtin N-Terminal Fragment Carrying an Expanded Polyglutamine Tract
Hazeki, N., Nakamura, K., Goto, J., & Kanazawa, I. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0337 · Cited by 35 · see citing works
Motor Neuron Disease: Epidemiologic Studies
Mulder, D. W., & Kurland, L. T. (1987) · Amyotrophic Lateral Sclerosis · doi:10.1007/978-1-4684-5302-7_49 · Cited by 31 · see citing works
No mitochondrial haplotype was found to increase risk for alzheimer’s disease
Zsurka, G., Kalman, J. L., Juhász, A., Császár, A., Raskó, I., Janka, Z., & Venetianer, P. (1998) · Biological Psychiatry · doi:10.1016/s0006-3223(97)00461-7 · Cited by 28 · see citing works
Comparison of pathological alterations in ALS and a murine transgenic model: pathogenetic implications.
Canto, M. C. D. (1997) · PubMed · Cited by 16 · see citing works

Flagged first, then by citations

Sorted by citations

Neuroinflammation and regulation of glial glutamate uptake in neurological disorders
Tilleux, S., & Hermans, E. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21325 · Cited by 381 · see citing works
Mitochondrial Approaches for Neuroprotection
Chaturvedi, R. K., & Beal, M. F. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.027 · Cited by 294 · see citing works
Self-citation
Recent advances in our understanding of neurodegeneration
Jellinger, K. A. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0240-y · Cited by 274 · see citing works
Mitochondrial Medicine for Aging and Neurodegenerative Diseases
Reddy, P. H. (2008) · NeuroMolecular Medicine · doi:10.1007/s12017-008-8044-z · Cited by 230 · see citing works
Pathogenesis of ataxia-telangiectasia: the next generation of ATM functions
Ambrose, M., & Gatti, R. A. (2013) · Blood · doi:10.1182/blood-2012-09-456897 · Cited by 196 · see citing works
Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission
Liu, W., Acín-Peréz, R., Geghman, K. D., Manfredi, G., Lu, B., & Li, C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107332108 · Cited by 190 · see citing works
Self-citation
The Age Lipid A2E and Mitochondrial Dysfunction Synergistically Impair Phagocytosis by Retinal Pigment Epithelial Cells
Vives-Bauza, C., Anand, M., Shirazi, A. K., Magrane, J., Gao, J., Vollmer-Snarr, H. R., Manfredi, G., & Finnemann, S. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800706200 · Cited by 155 · see citing works
Self-citation
Inhibition of TFG function causes hereditary axon degeneration by impairing endoplasmic reticulum structure
Beetz, C., Johnson, A., Schuh, A. L., Thakur, S., Varga, R.-E., Fothergill, T., Hertel, N., Bomba-Warczak, E., Thiele, H., Nürnberg, G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217197110 · Cited by 106 · see citing works
C. elegans as a model organism for human mitochondrial associated disorders
Maglioni, S., & Ventura, N. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.02.003 · Cited by 54 · see citing works
Mitochondrial Genome Analysis of Primary Open Angle Glaucoma Patients
Banerjee, D., Banerjee, A., Mookherjee, S., Vishal, M., Mukhopadhyay, A., Sen, A., Basu, A., & Ray, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070760 · Cited by 48 · see citing works
Collaboration between mitochondria and the nucleus is key to long life in Caenorhabditis elegans
Chang, H.-W., Shtessel, L., & Lee, S. S. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.576 · Cited by 15 · see citing works

Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
Cavadini, P. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.3.217 · Cited by 197 · see citing works
Variations of frataxin protein levels in normal individuals
Boehm, T., Scheiber‐Mojdehkar, B., Kluge, B., et al. (2010) · Neurological Sciences · doi:10.1007/s10072-010-0326-1 · Cited by 17 · see citing works
Oligomerization of human and bacterial frataxin : Structural and functional studies
Abdalkhalik, M. (2017) · Lund University Publications (Lund University)
Extra-mitochondrial mouse frataxin and its implications for mouse models of Friedreich’s ataxia
Weng, L., Laboureur, L., Wang, Q., Guo, L., Xu, P. J., Gottlieb, L., Lynch, D. R., Mesaros, C., & Blair, I. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-72884-w · Cited by 20 · see citing works
Liquid Chromatography–Mass Spectrometry Analysis of Frataxin Proteoforms in Whole Blood as Biomarkers of the Genetic Disease Friedreich’s Ataxia
Rojsajjakul, T., Wu, L., Grady, C. B., Hwang, W., Mesaros, C., Lynch, D. R., & Blair, I. A. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00091 · Cited by 19 · see citing works

Authors: Kwong, J. Q., Beal, M. F., & Manfredi, G.
Affiliations: Cornell University (US)
ORCID: Kwong, Jennifer Q.
Manfredi, Giovanni
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2006-06
Volume: 97
Issue: 6
Pages: 1659-1675
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/j.1471-4159.2006.03990.x
OpenAlex: W2007815419
Cited by: 180
References: 202
Citations by year: 2026: 4 · 2025: 2 · 2024: 5 · 2023: 6 · 2022: 3 · 2021: 5 · 2019: 3 · 2018: 5 · 2017: 7 · 2016: 4 · 2015: 12 · 2014: 9 · 2013: 15 · 2012: 9
FWCI: 1.64
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 18 d)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Neurological Disorders and Stroke (P01NS011766)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Keywords: mitochondria, mitochondrial dysfunction, inherited neurodegenerative disorders, neuronal cell death, Huntington's disease, Parkinson's disease, Alzheimer's disease, amyotrophic lateral sclerosis, Friedreich's ataxia, hereditary spastic paraplegia, autosomal dominant optic atrophy, Charcot-Marie-Tooth disease type 2A, mitochondrial DNA mutations, nuclear-encoded mitochondrial proteins, pathogenesis
MeSH terms: Animals, Humans, Mitochondria, Heredodegenerative Disorders, Nervous System

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The role of mitochondria in inherited neurodegenerative diseases

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks