The DOI matches its Crossref record; 40 of the 41 references it cites were found in a registry or an index.
Oxidative damage and metabolic dysfunction in Huntington's disease: Selective vulnerability of the basal ganglia
Abstract
The etiology of the selective neuronal death that occurs in Huntington's disease (HD) is unknown. Several lines of evidence implicate the involvement of energetic defects and oxidative damage in the disease process, including a recent study that demonstrated an interaction between huntingtin protein and the glycolytic enzyme glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH). Using spectrophotometric assays in postmortem brain tissue, we found evidence of impaired oxidative phosphorylation enzyme activities restricted to the basal ganglia in HD brain, while enzyme activities were unaltered in three regions relatively spared by HD pathology (frontal cortex, parietal cortex, and cerebellum). Citrate synthase‐corrected complex II‐III activity was markedly reduced in both HD caudate (−29%) and putamen (−67%), and complex IV activity was reduced in HD putamen (−62%). Complex I and GAPDH activities were unaltered in all regions examined. We also measured levels of the oxidative damage product 8‐hydroxydeoxyguanosine (OH 8 dG) in nuclear DNA, and superoxide dismutase (SOD) activity. OH 8 dG levels were significantly increased in HD caudate. Cytosolic SOD activity was slightly reduced in HD parietal cortex and cerebellum, whereas particulate SOD activity was unaltered in these regions. These results further support a role for metabolic dysfunction and oxidative damage in the pathogenesis of HD.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Biochemical studies revealed reduced activity of several key components of oxidative phosphorylation and the TCA cycle, including complexes II-III and aconitase, in advanced stage HD patients, while complex-I activity was unaltered40-43.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [42]
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366
Neuropathological Classification of Huntingtonʼs Disease
VONSATTEL, J.-P., MYERS, R. H., STEVENS, T. J., FERRANTE, R. J., BIRD, E. D., & RICHARDSON, E. P. (1985) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-198511000-00003 · Cited by 2,227
Self-citationBeal, M. F. (1992) · Annals of Neurology · doi:10.1002/ana.410310202 · Cited by 962
Self-citationNovelli, A., Reilly, J. A., Lysko, P. G., & Henneberry, R. C. (1988) · Brain Research · doi:10.1016/0006-8993(88)90765-2 · Cited by 961
Mitochondrial defect in Huntington's disease caudate nucleus
Gu, M., Gash, M. T., Mann, V. M., Javoy‐Agid, F., Cooper, J. M., & Schapira, A. H. V. (1996) · Annals of Neurology · doi:10.1002/ana.410390317 · Cited by 758
Oxidative damage to mitochondrial DNA shows marked age-dependent increases in human brain
Mecocci, P., MacGarvey, U., Kaufman, A. E., Koontz, D., Shoffner, J. M., Wallace, D. C., & Beal, M. F. (1993) · Annals of Neurology · doi:10.1002/ana.410340416 · Cited by 757
Self-citationHuntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
DiFiglia, M., Sapp, E., Chase, K., Schwarz, C., Meloni, A., Young, C., Martin, E., Vonsattel, J.-P., Carraway, R., Reeves, S. A., et al. (1995) · Neuron · doi:10.1016/0896-6273(95)90346-1 · Cited by 749
Bourgeron, T., Rustin, P., Chretien, D., Birch-Machin, M., Bourgeois, M., Viegas-Péquignot, E., Munnich, A., & Rötig, A. (1995) · Nature Genetics · doi:10.1038/ng1095-144 · Cited by 730
PURIFICATION OF AMINE OXIDASE FROM BEEF PLASMA
Tabor, C. W., Tabor, H., & Rosenthal, S. M. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65591-7 · Cited by 725
Research works printed but not linked: 1
- Tabor CW, 1954, Amine oxidases, J Biol Chem, 208, 645
Cited by
Sorted by citations
Items 601–700 of 883
RNA Aptamers Rescue Mitochondrial Dysfunction in a Yeast Model of Huntington’s Disease
Patel, K. A., Chaudhary, R. K., & Roy, I. (2018) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2018.04.010 · Cited by 16
Ciancia, M., Rataj-Baniowska, M., Zinter, N., Baldassarro, V. A., Fraulob, V., Charles, A., Álvarez, R., Muramatsu, S., de Lera, Á. R., Gény, B., et al. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102246 · Cited by 14
Molecular characterization of two CuZn-SOD family proteins in the Pacific oyster Crassostrea gigas
Ruan, Z., Liu, Y., Chang, G., Lin, Z., & Xue, Q. (2022) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2022.110736 · Cited by 15
Vanišová, M., Štufková, H., Kohoutová, M., Daňhelovská, T., Křížová, J., Klempíř, J., Ryšánková, I., Roth, J., Zeman, J., & Hansíková, H. (2022) · Ultrastructural Pathology · doi:10.1080/01913123.2022.2100951 · Cited by 15
VGF and striatal cell damage in in vitro and in vivo models of Huntington's disease
Noda, Y., Shimazawa, M., Tanaka, H., Tamura, S., Inoue, T., Tsuruma, K., & Hara, H. (2015) · Pharmacology Research & Perspectives · doi:10.1002/prp2.140 · Cited by 15
Martínez‐Lazcano, J. C., Montes, S., Sánchez-Mendoza, A., Rodríguez‐Páez, L., Pérez‐Neri, I., Boll, M., Campos-Arroyo, H. D., Rı́os, C., & Pérez‐Severiano, F. (2014) · Biological Trace Element Research · doi:10.1007/s12011-014-0127-0 · Cited by 15
Okada, N., Yako, T., Nakamura, S., Shimazawa, M., & Hara, H. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.09.001 · Cited by 16
Brocardo, P. S., McGinnis, E., Christie, B. R., & Gil‐Mohapel, J. (2015) · Rejuvenation Research · doi:10.1089/rej.2015.1736 · Cited by 15
CHOI, Y.-J., Kim, N. H., Lim, M. S., Lee, H. J., Kim, S. S., & Chun, W. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1747 · Cited by 15
The Drosophila Model: Exploring Novel Therapeutic Compounds against Neurodegenerative Diseases
Cha, S. J., Do, H., Choi, H., Lee, M., & Kim, K. (2019) · Antioxidants · doi:10.3390/antiox8120623 · Cited by 15
Centonze, D., Gubellini, P., Picconi, B., Saulle, E., Tolu, M., Bonsi, P., Giacomini, P., & Calabresi, P. (2001) · Neurological Sciences · doi:10.1007/s100720170047 · Cited by 15
Bypassing mitochondrial defects rescues Huntington's phenotypes in Drosophila
Campesan, S., Popolo, I. D., Marcou, K., Straatman-Iwanowska, A. A., Repici, M., Boytcheva, K. V., Cotton, V. E., Allcock, N., Rosato, E., Kyriacou, C. P., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106236 · Cited by 14
Rossi, S., Prosperetti, C., Picconi, B., Chiara, V. D., Mataluni, G., Bernardi, G., Calabresi, P., & Centonze, D. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.09.056 · Cited by 14
Restorative neuroscience: concepts and perspectives
Meyer, M., Ducray, A., & Widmer, H. (2008) · Swiss Medical Weekly · doi:10.4414/smw.2008.10387 · Cited by 14
The proposed mechanisms of radio frequency waves (RFWs) on nervous system functions impairment
Akbari, A., Jelodar, G., & Nazıfı, S. (2015) · Comparative Clinical Pathology · doi:10.1007/s00580-015-2096-x · Cited by 14
Increased expression of transglutaminase 2 drives glycolytic metabolism in renal carcinoma cells
Ku, B. M., Lee, C. H., Lee, S.-H., & Kim, S. (2014) · Amino Acids · doi:10.1007/s00726-014-1714-2 · Cited by 14
Skillings, E. A., & Morton, A. J. (2016) · Journal of Huntington s Disease · doi:10.3233/jhd-160189 · Cited by 14
Role of Phosphorylated Tau and Glucose Synthase Kinase 3 Beta in Huntington’s Disease Progression
Sawant, N. A., & Reddy, P. H. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190851 · Cited by 14
Study of Oxidative Damage and Antioxidant Systems in Two Huntington’s Disease Rodent Models
Pérez‐Severiano, F., Montes, S., Gerónimo‐Olvera, C., & Segovia, J. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-411-1_12 · Cited by 14
Vis, J. C., Huizen, R. D. B.-V., Verbeek, M. M., de Waal, R. M. W., ten Donkelaar, H. J., & Kremer, B. H. P. H. (2004) · Brain Research · doi:10.1016/j.brainres.2004.06.087 · Cited by 14
Jenkins, B. G., Chen, Y. I., Küestermann, E. H. G. K., Makris, N., Nguyen, T., Kraft, E., Brownell, A., Rosas, H. D., Kennedy, D. N., Rosen, B. R., et al. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07828.x · Cited by 14
Self-citationReactive Oxygen Species in the Induction of Toxicity
Lenaz, G., & Strocchi, P. (2009) · Wiley eBooks · doi:10.1002/9780470744307.gat024 · Cited by 15
DNA Damage and Chromatin Rearrangement Work Together to Promote Neurodegeneration
Sharma, H., Koirala, S., Chew, Y. L., & Konopka, A. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04331-0 · Cited by 14
Distinct molecular patterns in R6/2 HD mouse brain: Insights from spatiotemporal transcriptomics
Burns, M. S., Miramontes, R., Wu, J., Gulia, R., Saddala, M. S., Lau, A., Quach, T., Reidling, J. C., Swarup, V., Spada, A. R. L., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.05.014 · Cited by 14
Mitochondrial Biology and the Identification of Biomarkers of Huntington’s Disease
Neueder, A., & Orth, M. (2020) · Neurodegenerative Disease Management · doi:10.2217/nmt-2019-0033 · Cited by 13
Chhetri, G., Ke, Y., Wang, P., Usman, M., Li, Y., Sapp, E., Wang, J., Ghosh, A., Islam, M. A., Wang, X., et al. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202112073 · Cited by 12
Margolis, R. L., & Rudnicki, D. D. (2007) · Springer eBooks · doi:10.1007/978-3-540-71693-8_5 · Cited by 13
Sandhir, R., Mahajan, N., Mehrotra, A., Aggarwal, A., & Sunkaria, A. (2014) · Synapse · doi:10.1002/syn.21793 · Cited by 13
Huntington’s Disease Pathogenesis: Mechanisms and Pathways
Spada, A. R. L., Weydt, P., & Pineda, V. V. (2011) · Europe PMC (PubMed Central) · Cited by 13
Lithium carbonate and coenzyme Q10 reduce cell death in a cell model of Machado-Joseph disease
Lopes‐Ramos, C. M., Pereira, T. C., Dogini, D. B., Gilioli, R., & Lopes‐Cendes, Í. (2016) · Brazilian Journal of Medical and Biological Research · doi:10.1590/1414-431x20165805 · Cited by 13
Ruoppolo, M., Orrù, S., Francese, S., Caputo, I., & Esposito, C. (2003) · Protein Science · doi:10.1110/ps.0216103 · Cited by 13
Klapstein, G. J., & Levine, M. S. (2004) · Journal of Neurophysiology · doi:10.1152/jn.00483.2004 · Cited by 11
The neuroprotectant properties of glutamate antagonists and antiglutamatergic drugs
Pedersen, V., & Schmidt, W. (2000) · Neurotoxicity Research · doi:10.1007/bf03033793 · Cited by 14
Tallaksen‐Greene, S. J., Ordway, J. M., Crouse, A. B., Jackson, W. S., Detloff, P. J., & Albin, R. L. (2003) · The Journal of Comparative Neurology · doi:10.1002/cne.10855 · Cited by 13
Challenges of Huntington's disease and quest for therapeutic biomarkers
Kotrčová, E., Jarkovská, K., Valeková, I., Žižková, M. (., Motlík, J., Gadher, S. J., & Kovářová, H. (2014) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400073 · Cited by 12
Traa, A., Machiela, E., Rudich, P. D., Soo, S. K., Senchuk, M. M., & Raamsdonk, J. M. V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413447 · Cited by 13
Investigation of tRNALeu/Lys and ATPase 6 Genes Mutations in Huntington’s Disease
Kasraie, S., Houshmand, M., Banoei, M. M., Etemad, S., Panahi, M. S. S., Shariati, P., Bahar, M. A., & Moin, M. (2008) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-008-9261-6 · Cited by 12
Prospects for redox-based therapy in neurodegenerative diseases
Friedlich, A. L., & Beal, M. F. (2000) · Neurotoxicity Research · doi:10.1007/bf03033796 · Cited by 12
Self-citationNeuroprotective therapy for Huntington’s disease: new prospects and challenges
Hersch, S. M., & Rosas, H. D. (2001) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.1.1.111 · Cited by 12
Neuroprotective possibilities for Huntington’s disease
Emerich, D. F. (2001) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.1.3.467 · Cited by 12
Huntington's disease: The mystery unfolds?
Petersén, Å., & Brundin, P. (2002) · International review of neurobiology · doi:10.1016/s0074-7742(02)53012-9 · Cited by 12
Oxidative Stress in Huntington’s Disease
Jiménez‐Jiménez, F. J., Alonso‐Navarro, H., García‐Martín, E., Cárcamo-Fonfría, A., Caballero-Muñoz, M. D. M., & Agúndez, J. A. G. (2025) · Biomolecules · doi:10.3390/biom15040527 · Cited by 13
Melatonin reverses the oxidative stress and mitochondrial dysfunction caused by LETM1 silencing
Aral, C., Demirkesen, Ş., Bircan, R., & Şirin, D. Y. (2019) · Cell Biology International · doi:10.1002/cbin.11274 · Cited by 11
Vitamin E Status and Neurodegenerative Disease
Fryer, M. J. (1998) · Nutritional Neuroscience · doi:10.1080/1028415x.1998.11747243 · Cited by 11
Wieloch, T. W., Mattiasson, G., Hansson, M. J., & Elmér, E. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_25 · Cited by 11
Cantero-Téllez, A., Moreno‐Fierros, L., Gutiérrez‐Ospina, G., Santiago-Prieto, A. C., Juárez, I., Rodríguez‐Sosa, M., & Hernández, E. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04356-4 · Cited by 10
Mitochondrial Dynamics in Neurodegenerative Diseases
Pinnell, J. R., & Tieu, K. (2017) · Advances in neurotoxicology · doi:10.1016/bs.ant.2017.07.006 · Cited by 10
Surveying the Landscape of Huntington's Disease Mechanisms, Measurements, and Medicines
Crook, Z. R., & Housman, D. E. (2013) · Journal of Huntington s Disease · doi:10.3233/jhd-130072 · Cited by 11
Oxidative Damage in Huntington's Disease
Segovia, J., & Pérez‐Severiano, F. (2004) · Humana Press eBooks · doi:10.1385/1-59259-804-8:321 · Cited by 10
Altmann, S. M., Muryshev, A., Fossale, E., Maxwell, M. M., Norflus, F., Fox, J. H., Hersch, S. M., Young, A. B., MacDonald, M. E., Abagyan, R. A., et al. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.05.012 · Cited by 10
Nucleocytoplasmic transport of huntingtin and Huntington's disease
Truant, R. (2003) · Clinical Neuroscience Research · doi:10.1016/s1566-2772(03)00058-6 · Cited by 10
Mitochondria in neurodegeneration
Beal, M. F. (2002) · Springer eBooks · doi:10.1007/978-2-8178-0929-8_3 · Cited by 10
Self-citationThe Role of Impaired Mitochondrial Transport in the Development of Neurodegenerative Diseases
Blagov, A. V., Borisov, E. E., Grechko, A. V., Popov, M. A., Sukhorukov, V. N., & Orekhov, A. N. (2023) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2204086 · Cited by 9
Adhesion Regulating Molecule 1 Mediates HAP40 Overexpression-Induced Mitochondrial Defects
Huang, Z.-N., Chung, H. M., Fang, S., & Her, L. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.20742 · Cited by 9
Physiopathologie de la maladie de Huntington : état des connaissances
Roze, E. F., Bétuing, S., Deyts, C., Vidailhet, M., & Caboche, J. (2008) · Revue Neurologique · doi:10.1016/j.neurol.2008.03.006 · Cited by 11
Insulin and Insulin-Sensitizing Drugs in Neurodegeneration: Mitochondria as Therapeutic Targets
Cardoso, S., Santos, R. X., Correia, S. C., Carvalho, C., Zhu, X., Lee, H., Casadesús, G., Smith, M. A., Perry, G. L., & Moreira, P. I. (2009) · Pharmaceuticals · doi:10.3390/ph2030250 · Cited by 10
Translational research in Huntington’s disease: opening up for disease modifying treatment
Burgunder, J. (2013) · Translational Neurodegeneration · doi:10.1186/2047-9158-2-2 · Cited by 9
Choi, S., Choi, H. H., Choi, J.-H., Yoon, B.-H., You, H. J., Hyun, J., Kim, J., Ye, S., & Chung, M.-H. (2006) · Leukemia Research · doi:10.1016/j.leukres.2006.03.020 · Cited by 9
Fox, J. H., Lü, Z., & Barrows, L. F. (2016) · PLoS Currents · doi:10.1371/currents.hd.b966ec2eca8e2d89d2bb4d020be4351e · Cited by 9
Anglin, R., Rosebush, P. I., Noseworthy, M. D., Tarnopolsky, M. A., Weber, A. M., Soreni, N., & Mazurek, M. F. (2013) · CMAJ Open · doi:10.9778/cmajo.20120020 · Cited by 8
Promethazine protects against 3-nitropropionic acid-induced neurotoxicity
Cléren, C., Calingasan, N. Y., Starkov, A. A., Jacquard, C., Chen, J., Brouillet, E., & Beal, M. F. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.10.006 · Cited by 8
Self-citationFrancisconi, S., Codenotti, M., Ferrari‐Toninelli, G., Uberti, D. L., & Memo, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03864.x · Cited by 8
Seppet, E. K., Gizatullina, Z. Z., Trumbeckaitė, S., Zierz, S., Striggow, F., & Gellerich, F. N. (2007) · Wiley eBooks · doi:10.1002/9783527621095.ch15 · Cited by 8
Introduction: Immunosuppressants as Neuroprotective Agents
Keep, M. F., Uchino, H., & Elmér, E. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-315-6_1 · Cited by 8
Babu, A., & Urulangodi, M. (2023) · Genome Instability & Disease · doi:10.1007/s42764-023-00110-8 · Cited by 7
Louessard, M., Cailleret, M., Jarrige, M., Bigarreau, J., Lenoir, S., Dufour, N., Rey, M. J., Saudou, F., Déglon, N., & Perrier, A. L. (2024) · Journal of Huntington s Disease · doi:10.3233/jhd-231509 · Cited by 7
Nakabeppu, Y. (2016) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814719735_0015 · Cited by 7
Tu, Y., Li, X., Zhu, X., Liu, X., Guo, C., Jia, D., & Tang, T.-S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.619911 · Cited by 8
Transcriptomic analysis of human endometrial stromal cells during early embryo invasion
Han, S., Liu, M., Liu, S., & Li, Y. (2021) · Annals of Medicine · doi:10.1080/07853890.2021.1988139 · Cited by 7
Nascimento-Castro, C. D. P., Duarte, E. C. W., Mancini, G., Welter, P. G., Plácido, E., Farina, M., Gil‐Mohapel, J., Rodrigues, A. L. S., Bem, A. F. D., & Brocardo, P. S. (2022) · Biomedicines · doi:10.3390/biomedicines10061433 · Cited by 7
Jiang, A., You, L., Handley, R. R., Hawkins, V., Reid, S. J., Jacobsen, J. C., Patassini, S., Rudiger, S. R., McLaughlan, C. J., Kelly, J. M., et al. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae087 · Cited by 8
Babušíková, E., Evinová, A., Hatok, J., Dobrota, D., & Jurecekov, J. (2013) · InTech eBooks · doi:10.5772/54619 · Cited by 8
Gil‐Mohapel, J., & Rego, A. C. (2001) · Revista Neurociências · doi:10.34024/rnc.2011.v19.8332 · Cited by 7
Of mice and men: solving the molecular mysteries of Huntington's disease
Shelbourne, P. (2000) · Journal of Anatomy · doi:10.1046/j.1469-7580.2000.19640617.x · Cited by 7
Cunha‐Oliveira, T., Lusa, I., & Cristina, A. (2012) · InTech eBooks · doi:10.5772/32728 · Cited by 6
Fox, S. N., Savage, C. H., Amireddy, N., McMeekin, L. J., Crossman, D. K., Detloff, P. J., Gray, M., & Cowell, R. M. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106818 · Cited by 8
Role of mitochondria in neuronal function and survival in the enteric and central nervous systems
KURAL, İ., Mombeek, L. M. M., & Wilson, D. M. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-06053-5 · Cited by 8
The Essential Role of Astrocytes in Neurodegeneration and Neuroprotection
Couselo, F. L., Saba, J., Carniglia, L., Durand, D., Lasaga, M., & Caruso, C. M. (2023) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273269881231012062255 · Cited by 6
Pathophysiological Mechanisms of Huntington’s Disease
Ignácio, Z. M., Quevedo, J., & Réus, G. Z. (2018) · Springer eBooks · doi:10.1007/978-981-13-0944-1_5 · Cited by 6
Neural Transplantation in Huntington's Disease
Rosser, A., & Dunnett, S. B. (2007) · Elsevier eBooks · doi:10.1016/b978-012369415-7/50025-9 · Cited by 6
Adenosine Receptors in Huntington’s Disease
Blum, D. L., Martire, A., Burnouf, S., Sablonnière, B., Krystkowiak, P. C., Ledent, C. A., Lopes, L. V., & Popoli, P. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3903-5_20 · Cited by 6
Polyalanine and Polyglutamine Diseases: Possible Common Mechanisms?
Abu‐Baker, A., & Rouleau, G. A. (2006) · Elsevier eBooks · doi:10.1016/b978-012369462-1/50034-x · Cited by 6
Machado-Joseph Disease / Spinocerebellar Ataxia Type 3
Nbrega, C., & de Almei, L. P. (2012) · InTech eBooks · doi:10.5772/28576 · Cited by 7
The Use of the Mitochondrial Toxin 3-NP to Uncover Cellular Dysfunction in Huntington’s Disease
Hernández, E., la Rosa-Lpez, G. D., & Mendoza, E. (2012) · InTech eBooks · doi:10.5772/31284 · Cited by 6
8-OHdG: Its (Limited) Potential As a Biomarker For Huntington‘s Disease
Killoran, A., & Biglan, K. (2012) · Biomarkers in Medicine · doi:10.2217/bmm.12.84 · Cited by 6
Alleviating neurodegeneration in Drosophila models of PolyQ diseases
Long, Z., Tang, B., & Jiang, H. F. (2014) · Cerebellum & Ataxias · doi:10.1186/2053-8871-1-9 · Cited by 6
Traa, A., Machiela, E., Rudich, P. D., Soo, S. K., Senchuk, M. M., & Raamsdonk, J. M. V. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.19.465059 · Cited by 6
Bhatia, V., Bisht, G., Thakur, T., Thakur, H., & Ashawat, M. S. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02146-0 · Cited by 5
OSP-1 protects neurons from autophagic cell death induced by acute oxidative stress
Donato, A., Ritchie, F. K., Lu, L., Wadia, M., Martínez-Mármol, R., Kaulich, E., Sankorrakul, K., Lu, H., Coakley, S., Coulson, E. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55105-0 · Cited by 4
Campos, H. M., Pereira, R. M., Ferreira, P. Y. D. O., Uchenna, N., da Silva, C. R. B., Pruccoli, L., Lobón, G. S., Rodrigues, M. F., Vaz, B. G., Rivello, B. G., et al. (2024) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2024.111026 · Cited by 5
Toxin Induced Mitochondrial Dysfunction and Neurodegeneration
Sabri, M. I. (1998) · Springer eBooks · doi:10.1007/978-3-662-12509-0_14 · Cited by 5
Basal ganglia neuroprotection with anticonvulsants after energy stress: a comparative study
Arpin, S., Lagrue, E., Bodard, S., Chalon, S., & Castelnau, P. (2009) · Metabolic Brain Disease · doi:10.1007/s11011-009-9144-7 · Cited by 5
Duran‐Vilaregut, J., Manich, G., del Valle, J., Camins, A., Pallàs, M., Vilaplana, J., & Pelegrı́, C. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23060 · Cited by 5
The X-Linked Adrenoleukodystrophy (X-ALD) and Oxidative Stress
Al-Omar, M. A. (2006) · Journal of Herbal Pharmacotherapy · doi:10.1080/j157v06n03_07 · Cited by 5
Abada, Y.-S. K., & Ellenbroek, B. A. (2016) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000217 · Cited by 5
Jiang, X., Chen, M., Song, W., & Lin, G. N. (2021) · BMC Medical Genomics · doi:10.1186/s12920-021-00985-0 · Cited by 5
Churkina, A. S., Shakhov, A. S., Kotlobay, A. A., & Alieva, I. B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415533 · Cited by 5
Delorme, T., Najafi, M., & Nasr, P. (2012) · World Journal of Neuroscience · doi:10.4236/wjns.2012.24036 · Cited by 5
Role of Mitochondria in Neurodegenerative Diseases: The Dark Side of the “Energy Factory”
Correia, S. C., & Moreira, P. I. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_11 · Cited by 5
Huntington’s Disease: From the Physiological Function of Huntingtin to the Disease
Borgs, L., Juliette, D. L., Malgrange, B., & Nguye, L. (2012) · InTech eBooks · doi:10.5772/31789 · Cited by 4
Retracted
Metadata
- Authors
- Browne, S. E., Bowling, A. C., Macgarvey, U., Baik, M. J., Berger, S. C., Muquit, M. M. K., Bird, E. D., & Beal, M. F.
- Affiliations
- Harvard University (US)
- McLean Hospital (US)
- Corresponding author
- Beal, M. Flint
- Venue
- Annals of Neurology
- Publisher
- Wiley
- Published
- 1997-05
- Volume
- 41
- Issue
- 5
- Pages
- 646-653
- ISSN
- 0364-5134 (ISSN-L)
- 1531-8249
- OpenAlex
- W2102430316
- Cited by
- 885
- References
- 41
- Citations by year
- 2026: 14 · 2025: 12 · 2024: 18 · 2023: 17 · 2022: 25 · 2021: 33 · 2020: 22 · 2019: 18 · 2018: 31 · 2017: 13 · 2016: 47 · 2015: 31 · 2014: 41 · 2013: 37 · 2012: 46
- FWCI
- 10.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annals of Neurology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- Huntington's disease, oxidative damage, metabolic dysfunction, basal ganglia, selective neuronal vulnerability, oxidative phosphorylation, complex IV activity, complex I, glyceraldehyde-3-phosphate dehydrogenase, huntingtin, 8-hydroxy-2'-deoxyguanosine, superoxide dismutase, caudate nucleus, putamen, postmortem brain
- MeSH terms
- Basal Ganglia, Cerebellum, Cerebral Cortex, DNA, Glyceraldehyde-3-Phosphate Dehydrogenases, Humans, Huntington Disease, Mitochondria, Oxidation-Reduction, Reference Values, Spectrophotometry, Stress, Physiological, Superoxide Dismutase, NAD(P)H Dehydrogenase (Quinone), In Vitro Techniques
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