Expanding insights of mitochondrial dysfunction in Parkinson's disease

Surfing the p53 network

Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · see citing works

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in <i>PINK1</i>

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

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

Chaperone Suppression of α-Synuclein Toxicity in a <i>Drosophila</i> Model for Parkinson's Disease

Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227 · see citing works

Mitochondrial pathology and apoptotic muscle degeneration in <i>Drosophila parkin</i> 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

Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons

Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913 · see citing works

Parkin-deficient mice are not a robust model of parkinsonism

Perez, F. A., & Palmiter, R. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409598102 · Cited by 477 · see citing works

Identification of the ubiquitin–protein ligase that recognizes oxidized IRP2

Yamanaka, K., Ishikawa, H., Megumi, Y., Tokunaga, F., Kanie, M., Rouault, T. A., Morishima, I., Minato, N., Ishimori, K., & Iwai, K. (2003) · Nature Cell Biology · doi:10.1038/ncb952 · Cited by 181 · see citing works

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 · see citing works

Mitochondrial membrane permeabilization in cell death

Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598 · see citing works

Enriched environments, experience-dependent plasticity and disorders of the nervous system

Nithianantharajah, J., & Hannan, A. J. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1970 · Cited by 1,771 · see citing works

Targeting Antioxidants to Mitochondria by Conjugation to Lipophilic Cations

Murphy, M. P., & Smith, R. A. J. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105110 · Cited by 1,173 · see citing works

Axonal transport deficits and neurodegenerative diseases

Millecamps, S., & Julien, J.-P. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3380 · Cited by 755 · see citing works

Calcium and neurodegeneration

Mattson, M. P. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00275.x · Cited by 751 · see citing works

Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment

Greene, A. W., Grenier, K., Aguileta, M. A., Muise, S., Farazifard, R., Haque, M. E., McBride, H. M., Park, D. S., & Fon, E. A. (2012) · The EMBO Reports · doi:10.1038/embor.2012.14 · Cited by 711 · see citing works

Mitochondrial dysfunction in Parkinson's disease

Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688 · see citing works

Mitochondrial Dysfunction in Parkinson’s Disease

Moon, H. E., & Paek, S. H. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.2.103 · Cited by 455 · see citing works

Bright Near-Infrared Aggregation-Induced Emission Luminogens with Strong Two-Photon Absorption, Excellent Organelle Specificity, and Efficient Photodynamic Therapy Potential

Zheng, Z., Zhang, T., Liu, H., Chen, Y., Kwok, R. T. K., Ma, C., Zhang, P., Sung, H. H. Y., Williams, I. D., Lam, J. W. Y., et al. (2018) · ACS Nano · doi:10.1021/acsnano.8b03138 · Cited by 340 · see citing works

Depletion of 26S Proteasomes in Mouse Brain Neurons Causes Neurodegeneration and Lewy-Like Inclusions Resembling Human Pale Bodies

Bedford, L., Hay, D., Devoy, A., Paine, S., Powe, D. G., Seth, R., Gray, T., Topham, I., Fone, K., Rezvani, N., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2218-08.2008 · Cited by 327 · see citing works

Rapamycin activation of 4E-BP prevents parkinsonian dopaminergic neuron loss

Tain, L. S., Mortiboys, H., Tao, R. N., Ziviani, E., Bandmann, O., & Whitworth, A. J. (2009) · Nature Neuroscience · doi:10.1038/nn.2372 · Cited by 323 · see citing works

PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons

Wood-Kaczmar, A., Gandhi, S., Yao, Z., Abramov, A. S. Y., Miljan, E. A., Keen, G., Stanyer, L., Hargreaves, I., Klupsch, K., Deas, E., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002455 · Cited by 316 · see citing works

PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

Lo, S.-C., & Hannink, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.02.014 · Cited by 300 · see citing works

Oxidative and nitrosative stress in Parkinson's disease

Tsang, A. H. K., & Chung, K. K. K. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.12.006 · Cited by 300 · see citing works

Ghrelin promotes and protects nigrostriatal dopamine function via a UCP2-dependent mitochondrial mechanism

Andrews, Z. B., Erion, D., Beiler, R., Liu, Z.-W., Abizaid, A., Zigman, J., Elsworth, J. D., Savitt, J. M., DiMarchi, R., Tschöp, M., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3890-09.2009 · Cited by 289 · see citing works

Studies of Mitochondrial and Nonmitochondrial Sources Implicate Nicotinamide Adenine Dinucleotide Phosphate Oxidase(s) in the Increased Skeletal Muscle Superoxide Generation That Occurs During Contractile Activity

Sakellariou, G. K., Vasilaki, A., Palomero, J., Kayani, A., Zibrik, L., McArdle, A., & Jackson, M. J. (2013) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2012.4623 · Cited by 276 · see citing works

The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinson's disease

Surmeier, D. J., Guzman, J. N., Sanchez-Padilla, J., & Schumacker, P. T. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.08.045 · Cited by 236 · see citing works

Depletion of PINK1 affects mitochondrial metabolism, calcium homeostasis and energy maintenance

Heeman, B., Van den Haute, C., Aelvoet, S.-A., Valsecchi, F., Rodenburg, R. J., Reumers, V., Debyser, Z., Callewaert, G., Koopman, W. J. H., Willems, P. H. G. M., et al. (2011) · Journal of Cell Science · doi:10.1242/jcs.078303 · Cited by 198 · see citing works

Silencing of PINK1 Expression Affects Mitochondrial DNA and Oxidative Phosphorylation in DOPAMINERGIC Cells

Gegg, M. E., Cooper, J. M., Schapira, A. H. V., & Taanman, J.-W. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004756 · Cited by 198 · see citing works

Metabolomics of Human Brain Aging and Age-Related Neurodegenerative Diseases

Jové, M., Portero-Otín, M., Naudí, A., Ferrer, I., & Pamplona, R. (2014) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0000000000000091 · Cited by 195 · see citing works

Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases

Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184 · see citing works

Loss of mitochondrial complex I activity potentiates dopamine neuron death induced by microtubule dysfunction in a Parkinson’s disease model

Choi, W.-S., Palmiter, R. D., & Xia, Z. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201009132 · Cited by 183 · see citing works

Resveratrol Brain Delivery for Neurological Disorders Prevention and Treatment

Andrade, S., Ramalho, M. J., Pereira, M. D. C., & Loureiro, J. A. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01261 · Cited by 173 · see citing works

Interaction of Mitochondrial Calcium and ROS in Neurodegeneration

Baev, A. Y., Vinokurov, A. Y., Novikova, I. N., Dremin, V. V., Potapova, E. V., & Abramov, A. Y. (2022) · Cells · doi:10.3390/cells11040706 · Cited by 162 · see citing works

Engrailed protects mouse midbrain dopaminergic neurons against mitochondrial complex I insults

Alvarez-Fischer, D., Fuchs, J., Castagner, F., Stettler, O., Massiani-Beaudoin, O., Moya, K. L., Bouillot, C., Oertel, W. H., Lombès, A., Faigle, W., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2916 · Cited by 150 · see citing works

The Eye, Oxidative Damage and Polyunsaturated Fatty Acids

Saccà, S. C., Cutolo, C. A., Ferrari, D., Corazza, P., & Traverso, C. E. (2018) · Nutrients · doi:10.3390/nu10060668 · Cited by 150 · see citing works

Disease model organism for Parkinson disease: <i>Drosophila melanogaster</i>

Aryal, B., & Lee, Y. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.4.204 · Cited by 111 · see citing works

Altered regulation of the PINK1 locus: a link between type 2 diabetes and neurodegeneration?

Scheele, C., Nielsen, A. R., Walden, T. B., Sewell, D. A., Fischer, C. P., Brogan, R. J., Petrovic, N., Larsson, O., Tesch, P. A., Wennmalm, K., et al. (2007) · The FASEB Journal · doi:10.1096/fj.07-8520com · Cited by 110 · see citing works

Endonuclease G mediates α‐synuclein cytotoxicity during Parkinson's disease

Büttner, S., Habernig, L., Broeskamp, F., Ruli, D., Vögtle, F. N., Vlachos, M., Macchi, F., Küttner, V., Carmona‐Gutierrez, D., Eisenberg, T., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.228 · Cited by 87 · see citing works

Treating neurodegeneration by modifying mitochondria: potential solutions to a “complex” problem

Swerdlow, R. H. (2007) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2007.1676 · Cited by 81 · see citing works

Oleuropein derivatives from olive fruit extracts reduce α-synuclein fibrillation and oligomer toxicity

Mohammad-Beigi, H., Aliakbari, F., Sahin, C., Lomax, C., Tawfike, A., Schafer, N. P., Amiri-Nowdijeh, A., Eskandari, H., Møller, I. M., Hosseini-Mazinani, M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005723 · Cited by 77 · see citing works

Extracellular Vesicles as Novel Diagnostic and Prognostic Biomarkers for Parkinson’s Disease

Leggio, L., Paternò, G., Vivarelli, S., Falzone, G. G., Giachino, C., Marchetti, B., & Iraci, N. (2021) · Aging and disease · doi:10.14336/ad.2021.0527 · Cited by 55 · see citing works

Mitochondrial DNA mutations and essential hypertension (Review)

DING, Y., XIA, B., YU, J., LENG, J., & HUANG, J. (2013) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2013.1459 · Cited by 27 · see citing works

Post-COVID-19 Parkinsonism and Parkinson’s Disease Pathogenesis: The Exosomal Cargo Hypothesis

Mysiris, D. S., Vavougios, G. D., Karamichali, E., Papoutsopoulou, S., Stavrou, V. T., Papayianni, E., Boutlas, S., Mavridis, T., Foka, P., Zarogiannis, S. G., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179739 · Cited by 25 · see citing works

A potential role for creatine in drug abuse?

D’Anci, K. E., Allen, P. J., & Kanarek, R. B. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8176-2 · Cited by 9 · see citing works