Cited by 690Parkinson's Disease Mechanisms and TreatmentsMitochondrial Function and PathologyAutophagy in Disease and Therapy

The DOI matches its Crossref record; 325 of the 326 references it cites were found in a registry or an index.

Mitochondrial dysfunction in Parkinson's disease

Open access

Winklhofer, Konstanze F., Haass, Christian·2010·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

DOI 10.1016/j.bbadis.2009.08.013

Open this paper in CoChat — free account Open PDF

Abstract

Mitochondria are highly dynamic organelles which fulfill a plethora of functions. In addition to their prominent role in energy metabolism, mitochondria are intimately involved in various key cellular processes, such as the regulation of calcium homeostasis, stress response and cell death pathways. Thus, it is not surprising that an impairment of mitochondrial function results in cellular damage and is linked to aging and neurodegeneration. Many lines of evidence suggest that mitochondrial dysfunction plays a central role in the pathogenesis of Parkinson's disease (PD), starting in the early 1980s with the observation that an inhibitor of complex I of the electron transport chain can induce parkinsonism. Remarkably, recent research indicated that several PD-associated genes interface with pathways regulating mitochondrial function, morphology, and dynamics. In fact, sporadic and familial PD seem to converge at the level of mitochondrial integrity.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.bbadis.2009.08.013

Cites

325 of 325 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269
α-Synuclein in Lewy bodies
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
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
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Parkinson's Disease
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
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
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
α-Synuclein Locus Triplication Causes Parkinson's Disease
Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026

Show all 326 references

Sorted by citations

Items 401–500 of 690

Gateways for Glutamate Neuroprotection in Parkinson’s Disease (PD): Essential Role of EAAT3 and NCX1 Revealed in an In Vitro Model of PD
Piccirillo, S., Magi, S., Preziuso, A., Castaldo, P., Amoroso, S., & Lariccia, V. (2020) · Cells · doi:10.3390/cells9092037 · Cited by 19
“Numerous studies showed that mitochondrial dysfunction and oxidative damage, whether triggered by environmental and/or genetic factors, contribute to the cascade of events leading to the PD neurodegeneration [21,58].”
Background
The Pharmacological Activity of Garlic (Allium sativum) in Parkinson’s Disease: From Molecular Mechanisms to the Therapeutic Potential
Rakshit, D., Nayak, S., Kundu, S., Angelopoulou, E., Pyrgelis, E.-S., Piperi, C., & Mishra, A. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00789 · Cited by 20
The role of α-synuclein in neurodegeneration — An update
Jellinger, K. A. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0013-1 · Cited by 19
Effects of TAT-conjugated platinum nanoparticles on lifespan of mitochondrial electron transport complex I-deficient Caenorhabditis elegans, nuo-1
Miyamoto (2010) · International Journal of Nanomedicine · doi:10.2147/ijn.s12439 · Cited by 19
Psychotropic and neurological medication effects on mitochondrial complex I and IV in rodent models
Holper, L., Ben‐Shachar, D., & Mann, J. J. (2019) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2019.06.010 · Cited by 18
Four novel mutations in the mitochondrial ND4 gene of complex�I in patients with multiple sclerosis
Alharbi, M. A., Al‐Kafaji, G., Khalaf, N. B., Messaoudi, S. A., Taha, S., Daif, A., & Bakhiet, M. (2019) · Biomedical Reports · doi:10.3892/br.2019.1250 · Cited by 19
The ubiquitous role of mitochondria in Parkinson and other neurodegenerative diseases
Theocharopoulou, G. (2020) · AIMS neuroscience · doi:10.3934/neuroscience.2020004 · Cited by 19
Mitochondrial proteomics as a selective tool for unraveling Parkinson’s disease pathogenesis
Pienaar, I. S., Dexter, D. T., & Burkhard, P. R. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.8 · Cited by 19
Adverse Outcome Pathway on Inhibition of the mitochondrial complex I of nigro-striatal neurons leading to parkinsonian motor deficits
Bal‐Price, A., Leist, M., Schildknecht, S., Monnet‐Tschudi, F., Paini, A., & Terron, A. (2018) · OECD series on adverse outcome pathways · doi:10.1787/b46c3c00-en · Cited by 22
Cocoa Extract Provides Protection against 6-OHDA Toxicity in SH-SY5Y Dopaminergic Neurons by Targeting PERK
Vestuto, V., Amodio, G., Pepe, G., Basilicata, M. G., Belvedere, R., Napolitano, E., Guarnieri, D., Pagliara, V., Paladino, S., Rodriquez, M., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10082009 · Cited by 18
The marine toxin okadaic acid induces alterations in the expression level of cancer-related genes in human neuronal cells
Valdiglesias, V., Fernandez-Tajes, J. J., Méndez, J., Pásaro, E., & Laffón, B. (2013) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2013.03.009 · Cited by 18
“Indeed, mitochondrial dysfunction has been previously associated with several neurodegenerative disorders such as Parkinson's disease (Winklhofer and Haass, 2010), epilepsy (Folbergrová and Kunz, 2012) and Alzheimer's disease (Maruszak and Żekanowski, 2011), among others.”
Background
Evaluation of phytomedicinal potential of perillyl alcohol in an in vitro Parkinson's Disease model
Anis, E., Zafeer, M. F., Firdaus, F., Islam, S. N., Fatima, M., & Hossain, M. S. (2018) · Drug Development Research · doi:10.1002/ddr.21436 · Cited by 18
Protective effects of vitamin K2 on 6-OHDA-induced apoptosis in PC12 cells through modulation bax and caspase-3 activation
Ramazani, E., Fereidoni, M., & Tayarani‐Najaran, Z. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-05011-2 · Cited by 18
Excessive Cu2+ deteriorates arsenite-induced apoptosis in chicken brain and resulting in immunosuppression, not in homeostasis
Wang, Y., Zhao, H., Yang, X., Mu, M., Zong, H., Luo, L., & Xing, M. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.124758 · Cited by 17
Induced Pluripotent Stem Cell-Derived Dopaminergic Neurons from Familial Parkinson’s Disease Patients Display α-Synuclein Pathology and Abnormal Mitochondrial Morphology
Diao, X., Wang, F., Becerra-Calixto, A., Soto, C. A., & Mukherjee, A. (2021) · Cells · doi:10.3390/cells10092402 · Cited by 19
“Several fPD-causing mutations in genes such as Parkin, PINK1, and DJ-1 are directly implicated in the abnormality of mitochondrial function and maintenance [7].”
BackgroundInfluential
Tat-Frataxin protects dopaminergic neuronal cells against MPTP-induced toxicity in a mouse model of Parkinson's disease
Kim, M. J., Kim, D. W., Jeong, H. J., Sohn, E. J., Shin, M. J., Ahn, E. H., Kwon, S. W., Kim, Y. N., Kim, D., Park, J., et al. (2012) · Biochimie · doi:10.1016/j.biochi.2012.07.005 · Cited by 18
REMOVED: Co-administration of TiO2-nanowired dl-3-n-butylphthalide (dl-NBP) and mesenchymal stem cells enhanced neuroprotection in Parkinson's disease exacerbated by concussive head injury
Niu, F., Sharma, A., Wang, Z., Feng, L., Muresanu, D. F., Sahib, S., Tian, Z. R., Lafuente, J. V., Buzoianu, A. D., Nozari, A., et al. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.09.011 · Cited by 17
Treatment-Specific Network Modulation of MRI-Guided Focused Ultrasound Thalamotomy in Essential Tremor
Xiong, Y., Lin, J., Bian, X., Lu, H., Zhou, J., Zhang, D., Pan, L., & Lou, X. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01294-9 · Cited by 18
“In addition, previous findings have revealed that mitochondrial dysfunction plays a critical role in the pathogenesis of Parkinson’s disease [40, 41].”
Background
Celecoxib, indomethacin, and ibuprofen prevent 6-hydroxydopamine-induced PC12 cell death through the inhibition of NFκB and SAPK/JNK pathways.
Ramazani, E., Tayarani‐Najaran, Z., & Fereidoni, M. (2019) · PubMed Central · doi:10.22038/ijbms.2019.34011.8091 · Cited by 17
Cyclophilin D binds to the acidic C-terminus region of α-Synuclein and affects its aggregation characteristics
Torpey, J. H., Madine, J., Wood, A. C., & Lian, L. (2020) · Scientific Reports · doi:10.1038/s41598-020-66200-9 · Cited by 17
Mfn2 Overexpression Attenuates MPTP Neurotoxicity In Vivo
Zhao, F., Austria, Q. M., Wang, W., & Zhu, X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020601 · Cited by 19
Neuroprotective Properties of Bis-Sulfonamide Derivatives Against 6-OHDA-Induced Parkinson's Model via Sirtuin 1 Activity and in silico Pharmacokinetic Properties
Apiraksattayakul, S., Pingaew, R., Prachayasittikul, V., Ruankham, W., Jongwachirachai, P., Songtawee, N., Suwanjang, W., Tantimongcolwat, T., Prachayasittikul, S., Prachayasittikul, V., et al. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.890838 · Cited by 17
Neurochemical Evidence that the Metabolites Accumulating in 3-Methylcrotonyl-CoA Carboxylase Deficiency Induce Oxidative Damage in Cerebral Cortex of Young Rats
Zanatta, Â., Moura, A. P., Tonin, A. M., Knebel, L. A., Grings, M., Lobato, V. G. A., Ribeiro, C. A. J., Dutra‐Filho, C. S., Leipnitz, G., & Wajner, M. (2012) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-012-9879-2 · Cited by 17
Negative Conditioning of Mitochondrial Dysfunction in Age-related Neurodegenerative Diseases.
Selvaraji, S., Poh, L., Natarajan, V., Mallilankaraman, K. B., & Arumugam, T. V. (2019) · PubMed · Cited by 17
R492X mutation in PTEN-induced putative kinase 1 induced cellular mitochondrial dysfunction and oxidative stress
Yuan, X.-L., Guo, J., Shi, Z., Zhi-qian, X., Yan, X., Zhao, B., & Tang, B. (2010) · Brain Research · doi:10.1016/j.brainres.2010.06.005 · Cited by 17
Prothrombin Kringle-2: a potential inflammatory pathogen in the parkinsonian dopaminergic system
Leem, E., Jeong, K. H., Won, S.-Y., Shin, W.-H., & Kim, S. R. (2016) · Experimental Neurobiology · doi:10.5607/en.2016.25.4.147 · Cited by 16
An Eu 3+ -functionalized metal–organic framework (Eu@Zn-MOF) for the highly sensitive detection of rotenone in serum
Jin, Y., Xu, X., Ma, W., & Yan, B. (2022) · New Journal of Chemistry · doi:10.1039/d2nj03640a · Cited by 16
The neuroprotective effect of vitamin D in Parkinson's disease: association or causation
Hafiz, A. A. (2023) · Nutritional Neuroscience · doi:10.1080/1028415x.2023.2259680 · Cited by 16
“…(MPTP) or rotenone in mice aggravates the development of mitochondrial dysfunction via the inhibition of mitochondrial complex I, suggesting that the inhibition of mitochondrial complex I and promulgation of mitochondrial dysfunction could be the primary event in PD neuropathology [119].”
Background
Standardized Centella Asiatica Increased Brain- Derived Neurotrophic Factor and Decreased Apoptosis of Dopaminergic Neuron in Rotenone-Induced Zebrafish
Khotimah, H., Sumitro, S. B., Ali, M., & Widodo, M. A. (2015) · GSTF Journal of Psychology · doi:10.7603/s40790-015-0004-0 · Cited by 16
Biomarkers of Oxidative Stress in Neurodegenerative Diseases
Rukhsana Sultana, A., Cenini, G., & Butterfield, D. A. (2013) · Wiley eBooks · doi:10.1002/9781118355886.ch14 · Cited by 16
Neuroprotective effects of ATPase inhibitory factor 1 preventing mitochondrial dysfunction in Parkinson's disease
Chung, I., Park, H., Kang, J. M., Kim, H., Hah, S. M., Lee, J., Kim, H. S., Choi, W., Chung, J. H., & Shin, M. (2022) · Scientific Reports · doi:10.1038/s41598-022-07851-8 · Cited by 17
BrainPhys Neuronal Media Support Physiological Function of Mitochondria in Mouse Primary Neuronal Cultures
Faria‐Pereira, A., Temido‐Ferreira, M., & Morais, V. A. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.837448 · Cited by 18
Protective effects of veskamide, enferamide, becatamide, and oretamide on H2O2-induced apoptosis of PC-12 cells
Park, J. B. (2011) · Phytomedicine · doi:10.1016/j.phymed.2011.01.025 · Cited by 15
“In actual fact, neurodegenrative processes are very much responsible for several neuronal iseases such as Alzheimer’s, Parkinson’s, and Huntington’s disases (Duyckaerts et al. 2009; Winklhofer and Haass 2010; Bates 003).”
Background
A study on the interaction of the amyloid fibrils of α-synuclein and hen egg white lysozyme with biological membranes
Zadali, R., Hassani, V., Rafiei, Y., Meratan, A. A., Mamashli, F., & Nemat‐Gorgani, M. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183776 · Cited by 14
A genome-wide association study in the genetic analysis of idiopathic thrombophilia project suggests sex-specific regulation of mitochondrial DNA levels
López, S., Buil, A., Souto, J. C., Casademont, J., Martínez-Pérez, Á., Almasy, L. A., & Soria, J. M. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.09.004 · Cited by 16
“This is compatible with thewidely accepted role of mitochondrial dysfunction in PD (Winklhofer and Haass, 2010).”
Background
Mitochondria in the context of Parkinson's disease
Kortázar, D., Villacé, P., & Mella, R. M. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.200802 · Cited by 15
Association analysis of SNP rs11868035 in SREBF1 with sporadic Parkinson’s disease, sporadic amyotrophic lateral sclerosis and multiple system atrophy in a Chinese population
Yuan, X., Cao, B., Wu, Y., Chen, Y., Wei, Q., Ou, R., Yang, J., Chen, X.-P., Zhao, B., Song, W., et al. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.11.015 · Cited by 16
A Propagated Skeleton Approach to High Throughput Screening of Neurite Outgrowth for In Vitro Parkinson’s Disease Modelling
Schikora, J., Kiwatrowski, N., Förster, N., Selbach, L., Ostendorf, F., Pallapies, F., Hasse, B., Metzdorf, J., Gold, R., Axel Mosig, A., et al. (2021) · Cells · doi:10.3390/cells10040931 · Cited by 15
“Pathological aSYN accumulation, impaired mitochondrial dynamics and high levels of reactive oxygen species cause dysfunction of mitochondria resulting in higher oxidative stress, which also contributes to neuronal death [2,5,6].”
Background
The Effects of Piroxicam in the Attenuation of MPP+/MPTP Toxicity In Vitro and In Vivo
Soliman, Y. I., Jackson, T., MAZZIO, E. A., & Soliman, K. F. A. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9779-5 · Cited by 15
An angiogenic inhibitor, cyclic RGDfV, attenuates MPTP-induced dopamine neuron toxicity
Patel, A., Toia, G. V., Colletta, K., Bradaric, B. D., Carvey, P. M., & Hendey, B. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.06.004 · Cited by 15
Decoding natural products for neuroprotection: Pathway networks and structural insights for drug development
Ghosh, S., Debnath, I., Bhunia, S., Nandi, S., Ashique, S., Nayak, A., Mallick, S., & Basak, S. (2025) · Chinese Herbal Medicines · doi:10.1016/j.chmed.2025.09.005 · Cited by 16
“In diseases like PD, the suppression of mitochondrial complex I results in oxidative stress and the production of apoptogenic substances, which promote neuronal damage through both caspase-dependent and caspase-independent routes (Perier et al., 2012; Winklhofer & Haass, 2010).”
STAT3 protects dopaminergic neurons against degeneration in animal model of Parkinson's disease
Smit, R. D., Ghosh, B., Campion, T. J., III, Stingel, R. L., Lavell, E., Hooper, R., Fan, X., Soboloff, J., & Smith, G. M. (2023) · Brain Research · doi:10.1016/j.brainres.2023.148691 · Cited by 14
“…evidence suggests a range of factors including oxidative stress, mitochondrial dysfunction, and activation of an apoptotic cascade (Bove and Perier, 2012; Fahn and Cohen, 1992; Hastings et al., 1996; Luo et al., 2015; Mann et al., 1994; Martinez and Greenamyre, 2012; Winklhofer and Haass, 2010).”
Redox modulatory role of DJ-1 in Parkinson’s disease
Alshammari, Q. A. (2025) · Biogerontology · doi:10.1007/s10522-025-10227-w · Cited by 15
“In PD, mitochondria are important for pathogenesis due to their role as key sites for the production and energy generation of ROS in neurons (Winklhofer and Haass 2010).”
Genetic analysis of lysosomal alpha-galactosidase A gene in sporadic Parkinson's disease
Wu, G., Pang, S., Feng, X., Zhang, A., Li, J., Gu, K., Huang, J. A., Dong, H., & Yan, B. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.05.238 · Cited by 14
Mitochondrial complex I gene variations; as a potential genetic risk factor in pathogenesis of multiple sclerosis
Zonouzi, A. P., Ghorbian, ‪., Abkar, M., Zonouzi, A. A. P., & Azadi, A. (2014) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2014.07.051 · Cited by 14
“Increasing evidences suggest that the mitochondria may play a fundamental role in the pathogenesis of neurodegenerative diseases such as MS, and Alzheimer's and Parkinson's diseases [13–17].”
Background
Whole genome expression profile in neuroblastoma cells exposed to 1-methyl-4-phenylpyridine
MAZZIO, E. A., & Soliman, K. F. A. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.06.009 · Cited by 13
Pretreatment of glial cell‐derived neurotrophic factor and geranylgeranylacetone ameliorates brain injury in Parkinson's disease by its anti‐apoptotic and anti‐oxidative property
Yue, P., Gao, L., Wang, X., Ding, X., & Teng, J. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26712 · Cited by 14
Transdermal delivery of mitochondrial-targeted hydrogen sulphide donor, AP39 protects against 6-hydroxydopamine-induced mitochondrial dysfunction
Marwah, M. K., Manhoosh, B., Shokr, H., Tahan, M. A. A., Stewart, R., Iqbal, M., Sanchez, L. D., Abdullah, S., Ahmad, S., Wang, K., et al. (2023) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2023.09.004 · Cited by 15
Targeting mitochondrial biogenesis for promoting health
Stefano, G. B., Kim, C., Mantione, K. J., Casares, F. M., & Kream, R. M. (2012) · Medical Science Monitor · doi:10.12659/msm.882526 · Cited by 13
International Journal for Pharmaceutical Research Scholars (IJPRS)
Thanikachalam, S., Chandrasekharan, A., Vijayakumar, H., Chidambaram, S., & Bhaskar, L. V. (2014) · Cited by 13
Global mapping of transcription factor motifs in human aging
Alfego, D., Rodeck, U., & Kriete, A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0190457 · Cited by 13
The efficacy of a “cocktail therapy” on Parkinson’s disease with dementia
Zhang, C., Zang, Y., Song, Q., Li, H., Hu, L., Zhao, W., Feng, S., Gu, F., Zhao, F., & Zhang, C. (2019) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s179453 · Cited by 13
Loss-of-Function NUBPL Mutation May Link Parkinson's Disease to Recessive Complex I Deficiency
Eis, P. S., Huang, N., Langston, J. W., Hatchwell, E., & Schüle, B. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.555961 · Cited by 13
“Given the extensive evidence for mitochondrial dysfunction — particularly reduced CI activity in late-onset neurological disorders (2), we believe this novel finding provides a basis for the nomination of NUBPL as a gene that may cause or contribute to PD pathology.”
Background
Defining (and blocking) neuronal death in Parkinson’s disease: Does it matter what we call it?
Memou, A., Dimitrakopoulos, L., Kedariti, M., Kentros, M., Lamprou, A., Petropoulou-Vathi, L., Valkimadi, P., & Rideout, H. J. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147639 · Cited by 14
Microarray Expression Analysis for the Paradoxical Roles ofAcanthopanax senticosusHarms in Treating α-Synucleinopathies
Li, X., Zhang, S., Lu, F., & Liu, S. (2015) · Phytotherapy Research · doi:10.1002/ptr.5522 · Cited by 13
Monte Carlo cross-validation analysis screens pathway cross-talk associated with Parkinson’s disease
Li, T., Tang, W., & Zhang, L. (2016) · Neurological Sciences · doi:10.1007/s10072-016-2595-9 · Cited by 13
New Targets for Parkinson's Disease: Adhesion G Protein-Coupled Receptor B1 is Downregulated by AMP-Activated Protein Kinase Activation
Choi, J., Bae, W., Nam, S., & Jeong, J. (2018) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2018.0047 · Cited by 13
“Many PD-associated genes, such as PINK1, PARK2, and PARK7 , interface with pathways that regulate the function and dynamics of mitochondria (Winklhofer and Haass, 2010).”
Accelerated telomere shortening independent of LRRK2 variants in Chinese patients with Parkinson's disease
Wu, Y., Pei, Y., Yang, Z., Li, K., Lou, X., & Cui, W. (2020) · Aging · doi:10.18632/aging.103878 · Cited by 12
The Common Denominators of Parkinson’s Disease Pathogenesis and Methamphetamine Abuse
Vincent, B., & Shukla, M. (2023) · Current Neuropharmacology · doi:10.2174/1570159x21666230907151226 · Cited by 13
Capturing ER calcium dynamics
Jaepel, J., & Blum, R. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.02.010 · Cited by 12
The function of bacterial HtrA is evolutionally conserved in mammalian HtrA2/Omi
Chung, H., Jamal, M. A. H. M., & Hong, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-62309-z · Cited by 12
Effects of the neurotoxin MPTP and pargyline protection on extracellular energy metabolites and dopamine levels in the striatum of freely moving rats
Bazzu, G., Rocchitta, G., Migheli, R., Alvau, M. D., Zinellu, M., Puggioni, G., Calia, G., Mercanti, G., Giusti, P., Desole, M. S., et al. (2013) · Brain Research · doi:10.1016/j.brainres.2013.09.037 · Cited by 12
The metabolomics of alpha-synuclein (SNCA) gene deletion and mutation in mouse brain
Musgrove, R. E., Horne, J., Wilson, R., King, A. E., Edwards, L. M., & Dickson, T. C. (2013) · Metabolomics · doi:10.1007/s11306-013-0561-6 · Cited by 12
The Mitochondrial Permeability Transition Pore
Morganti, C., Bonora, M., Sbano, L., Morciano, G., Aquila, G., Campo, G. C., Wieckowski, M. R., Giorgi, C., & Pinton, P. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_5 · Cited by 13
Our Tau Tales from Normal to Pathological Behavior
Alonso, A. D. C., & Cohen, L. S. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179906 · Cited by 12
An investigation into closed-loop treatment of neurological disorders based on sensing mitochondrial dysfunction
Adams, S. D., Kouzani, A. Z., Tye, S. J., Bennet, K. E., & Berk, M. (2018) · Journal of NeuroEngineering and Rehabilitation · doi:10.1186/s12984-018-0349-z · Cited by 12
Gene therapy for the mitochondrial genome: Purging mutations, pacifying ailments
Siva, A., Mahalakshmi, R., Bhakta-Guha, D., & Guha, G. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.06.002 · Cited by 12
Punicalagin Exerts Beneficial Functions in 6-Hydroxydopamine-Treated SH-SY5Y Cells by Attenuating Mitochondrial Dysfunction and Inflammatory Responses
Chu, J., & Han, W. (2018) · Medical Science Monitor · doi:10.12659/msm.909969 · Cited by 12
Ulmosides A: Flavonoid 6-C-glycosides from Ulmus wallichiana attenuates lipopolysacchride induced oxidative stress, apoptosis and neuronal death
Gupta, P., Singh, A., Tiwari, S., Mishra, A., Maurya, R., & Singh, S. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.02.017 · Cited by 12
Alteration of Mitochondrial Function in Oxidative Stress in Parkinsonian Neurodegeneration
Qadri, R., Goyal, V., Behari, M., Subramanian, A., Datta, S. K., & Mukhopadhyay, A. K. (2021) · Annals of Indian Academy of Neurology · doi:10.4103/aian.aian_392_20 · Cited by 12
A Genetic View of the Mitochondrial Role in Ageing: Killing Us Softly
Levin, L., & Mishmar, D. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-2404-2_4 · Cited by 11
3-O-Demethylswertipunicoside Protects against Oxidative Toxicity in PC12 Cells
Zhang, S., Du, X., & Pu, X. (2010) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.33.1529 · Cited by 12
Replicated association between genetic variation in the PARK2 gene and blood pressure
Jin, H., Hong, K., Kim, B. Y., Kim, J., Yoo, Y. H., Oh, B., & Jeong, S. (2011) · Clinica Chimica Acta · doi:10.1016/j.cca.2011.05.026 · Cited by 12
1,5-Benzodiazepin-2(3H)-ones: In Vitro Evaluation as Antiparkinsonian Agents
Ortíz de Zárate, A., Pérez-Torralba, M., Bonet Isidro, I., López, C., Claramunt, R. M., Martínez-Casanova, D., Sánchez-Vera, I., Jiménez-González, J., & Lavandera, J. L. (2021) · Antioxidants · doi:10.3390/antiox10101584 · Cited by 11
“Substantial evidence links pathophysiological alterations observed in sporadic PD to some associated genes that may be involved in the disruption of mitochondrial integrity, triggering mitochondrial dysfunction, oxidative stress, and an increase in protein misfolding and aggregation [25,26].”
The Determination of Trimethylamine N-Oxide and Organic Acids Connected with Gut Microbiota in the Urine of Parkinson’s Disease Patients: A Pilot Study
Gątarek, P., Pawelczyk, M., Bobrowska‐Korczak, B., Giebułtowicz, J., Glabinski, A. R., & Kałużna‐Czaplińska, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104575 · Cited by 11
DRP1 Inhibition Rescues Mitochondrial Integrity and Excessive Apoptosis in CS-A Disease Cell Models
Pascucci, B., Spadaro, F., Pietraforte, D., Nuccio, C. D., Visentin, S., Giglio, P., Eugenia Dogliotti, Y., & D’Errico, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137123 · Cited by 11
V63 and N65 of overexpressed α-synuclein are involved in mitochondrial dysfunction
Zhang, H., Liu, J., Wang, X., Duan, C., Wang, X., & Yang, H. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.002 · Cited by 11
Animal Models for the Study of Human Neurodegenerative Diseases
Colpo, G. D., Ribeiro, F. M., Rocha, N. P., & Teixeira, A. L. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809468-6.00042-5 · Cited by 12
Mitochondrial Diseases as Model of Neurodegeneration
Selim, L., & Hassaan, H. M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-60733-7_8 · Cited by 11
Differential Effects of Yeast NADH Dehydrogenase (Ndi1) Expression on Mitochondrial Function and Inclusion Formation in a Cell Culture Model of Sporadic Parkinson’s Disease
Cronin-Furman, E. N., Barber‐Singh, J., Bergquist, K. E., Yagi, T., & Trimmer, P. A. (2019) · Biomolecules · doi:10.3390/biom9040119 · Cited by 13
The histopathological, cytopathological and ultrastructural effects of carbaryl on gills of Oreochromis niloticus (Linnaeus, 1758)
Uğurlu, P., Satar, E. İ., & Çiçek, T. (2019) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2019.103217 · Cited by 11
Mitochondrial transplant to replenish damaged mitochondria: A novel therapeutic strategy for neurodegenerative diseases?
Mukherjee, A., Calixto, A., Chavez, M., Delgado, J. P., & Soto, C. A. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.10.001 · Cited by 11
Synthesis and characterization of brain penetrant prodrug of neuroprotective D-264: Potential therapeutic application in the treatment of Parkinson’s disease
Dholkawala, F. S., Voshavar, C., & Dutta, A. K. (2016) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2016.03.017 · Cited by 11
Small Molecules Targeting the Mitochondrial Permeability Transition
Šileikytė, J., Roy, S., Porubsky, P. R., Neuenswander, B., Wang, J., Hedrick, M., Pinkerton, A. B., Salaniwal, S., Kung, P., Mangravita-Novo, A., et al. (2015) · Cited by 10
Editorial: The Protein Alpha-Synuclein: Its Normal Role (in Neurons) and Its Role in Disease
Perez, R. G. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00116 · Cited by 11
“Mitochondrial impairment, which is common in PD, influences energy metabolism, homeostasis, the stress response, and apoptosis (Winklhofer and Haass, 2010).”
Background
Brain Effects of SC-Nanophytosomes on a Rotenone-Induced Rat Model of Parkinson’s Disease—A Proof of Concept for a Mitochondria-Targeted Therapy
Mendes, D., Peixoto, F., Oliveira, M. M., Andrade, P. B., & Videira, R. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012699 · Cited by 10
Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo
Gong, G., & Wang, W. (2013) · Journal of Visualized Experiments · doi:10.3791/50818 · Cited by 10
Engineered Disulfide Bonds Restore Chaperone-like Function of DJ-1 Mutants Linked to Familial Parkinson’s Disease
Logan, T., Clark, L. D., & Ray, S. S. (2010) · Biochemistry · doi:10.1021/bi902164h · Cited by 10
Natural variation in Caenorhabditis briggsae mitochondrial form and function suggests a novel model of organelle dynamics
Hicks, K. A., Denver, D. R., & Estes, S. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.12.006 · Cited by 10
Protein Aggregation in a Nutshell: The Splendid Molecular Architecture of the Dreaded Amyloid Fibrils
Horváth, D., Menyhárd, D. K., & Perczel, A. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190925102832 · Cited by 9
Nrf2 Deficiency Attenuates Testosterone Efficiency in Ameliorating Mitochondrial Function of the Substantia Nigra in Aged Male Mice
Ren, B., Zhang, T., Guo, Q., Che, J., Kang, Y., Cui, R., Wang, Y., Ji, X., Zhang, G., & Shi, G. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/3644318 · Cited by 11
“Mitochondrial dysfunction, such as the decreased oxidative phosphorylation, the increased reactive oxygen species (ROS), and oxidative damage, is found in aged subjects and subjects with aging-related neurodegeneration [1].”
Activation of Mitochondrial Complex II-Dependent Respiration Is Beneficial for α-Synucleinopathies
Fröhlich, C., Zschiebsch, K., Gröger, V., Paarmann, K., Steffen, J., Thurm, C., Schropp, E.-M., Brüning, T., Gellerich, F. N., Radloff, M., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9399-4 · Cited by 10
Molecular Imaging of Cell Death in an Experimental Model of Parkinson’s Disease with a Novel Apoptosis-Targeting Peptide
Lee, M. J., Wang, K., Kim, I.-S., Lee, B.-H., & Han, H. S. (2011) · Molecular Imaging and Biology · doi:10.1007/s11307-011-0497-z · Cited by 10
“(SNpc) [1–4].”
Identification of Multiple QTLs Linked to Neuropathology in the Engrailed-1 Heterozygous Mouse Model of Parkinson’s Disease
Kurowska, Z., Jewett, M. A. S., Brattås, P. L., Jiménez-Ferrer, I., Kenéz, X., Björklund, T., Nordström, U., Brundin, P., & Swanberg, M. (2016) · Scientific Reports · doi:10.1038/srep31701 · Cited by 10
From Obesity to Mitochondrial Dysfunction in Peripheral Tissues and in the Central Nervous System
Marino, F., Petrella, L., Cimmino, F., Pizzella, A., Monda, A., Allocca, S., Rotondo, R., D’Angelo, M., Musco, N., Iommelli, P., et al. (2025) · Biomolecules · doi:10.3390/biom15050638 · Cited by 11
“Furthermore, partial inhibition of complex I in rat synapses has been shown to increase mitochondrial ROS production [107].”
The Roles of Calcium Ions in Parkinson’s Disease: Calcium Channel Inhibitors as a Novel Agents?
Alam, M. R., Raj, K., & Singh, S. (2022) · Journal of Molecular Pathology · doi:10.3390/jmp3040021 · Cited by 9
“However, the experimental designs of the investigations differed, making it difﬁcult to draw a broad conclusion [157].”
A Case of Emergent Restless Legs Syndrome With Lurasidone Therapy
Ghori, A. K., Sajatovic, M., & Tampi, R. R. (2016) · Journal of Clinical Psychopharmacology · doi:10.1097/jcp.0000000000000496 · Cited by 9
Preliminary investigation of the neuroprotective potentials of Crossyne guttata in MPP+-induced toxicity in SH-SY5Y
Omoruyi, S. I., Enogieru, A. B., Hussein, A. A., & Ekpo, O. E. (2019) · Journal of African Association of Physiological Sciences · Cited by 9
A versatile color and fluorescence pH sensor based on AIE and open-loop synergy effect: Crystal structure and its application in cell imaging
Liu, Z., Wang, L., Zhu, W., Ding, Y.-J., Liu, S., Wang, Q., & Chen, Y. (2021) · Dyes and Pigments · doi:10.1016/j.dyepig.2021.109310 · Cited by 9
Parkinson’s disease biomarker: a patent evaluation of WO2013153386
Geldenhuys, W. J., Abdelmagid, S. M., Gallegos, P. J., & Safadi, F. F. (2014) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2014.931375 · Cited by 9

Authors: Winklhofer, K. F., & Haass, C.
Affiliations: German Center for Neurodegenerative Diseases (DE)
Corresponding author: Winklhofer, Konstanze F.
ORCID: Winklhofer, Konstanze F.
Haass, Christian
Venue: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Publisher: Elsevier BV
Published: 2010-01
Volume: 1802
Issue: 1
Pages: 29-44
ISSN: 0925-4439 (ISSN-L)
DOI: 10.1016/j.bbadis.2009.08.013
OpenAlex: W2130497877
Cited by: 688
References: 326
Citations by year: 2026: 10 · 2025: 16 · 2024: 13 · 2023: 27 · 2022: 30 · 2021: 37 · 2020: 55 · 2019: 38 · 2018: 72 · 2017: 51 · 2016: 61 · 2015: 39 · 2014: 29 · 2013: 37 · 2012: 49
FWCI: 5.83
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1784 d)
Locations: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft (SFB 596)
German Ministry for Education and Research
the Helmholtz Alliance “Mental Health in an Ageing Society,”
the Center for Integrated Protein Science Munich
the Hans and Ilse Breuer Foundation
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: mitochondrial dysfunction, Parkinson's disease, mitochondrial dynamics, mitochondrial morphology, mitochondrial complex I inhibition, parkinsonism, electron transport chain, calcium homeostasis, stress response, cell death pathways, neurodegeneration, aging, familial Parkinson's disease, sporadic Parkinson's disease
MeSH terms: Animals, DNA, Mitochondrial, Humans, Mitochondria, Models, Biological, Parkinson Disease, Oxidative Stress, Mitochondrial Proteins

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

Mitochondrial dysfunction in Parkinson's disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks