Decreased sirtuin deacetylase activity in LRRK2 G2019S iPSC-derived dopaminergic neurons

Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling

Chambers, S. M., Fasano, C. A., Papapetrou, E. P., Tomishima, M., Sadelain, M., & Studer, L. (2009) · Nature Biotechnology · doi:10.1038/nbt.1529 · Cited by 3,620 · see citing works

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works

Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works

Dopamine neurons derived from human ES cells efficiently engraft in animal models of Parkinson’s disease

Kriks, S., Shim, J., Piao, J., Ganat, Y. M., Wakeman, D. R., Xie, Z., Carrillo‐Reid, L., Auyeung, G., Antonacci, C. L., Buch, A., et al. (2011) · Nature · doi:10.1038/nature10648 · Cited by 1,912 · see citing works

The pathways of mitophagy for quality control and clearance of mitochondria

Ashrafi, G., & Schwarz, T. L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.81 · Cited by 1,900 · see citing works

The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase

North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542 · see citing works

Induced pluripotent stem cells from a spinal muscular atrophy patient

Ebert, A. D., Yu, J., Rose, F. F., Mattis, V. B., Lorson, C. L., Thomson, J. A., & Svendsen, C. N. (2009) · Nature · doi:10.1038/nature07677 · Cited by 1,441 · see citing works

Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation

Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310 · 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

Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation

Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works

Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction

Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works

Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease

Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., Volk, C. B., Maxwell, M. M., Rochet, J., McLean, P. J., et al. (2007) · Science · doi:10.1126/science.1143780 · Cited by 1,066 · see citing works

Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress

Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899 · see citing works

Human cerebral cortex development from pluripotent stem cells to functional excitatory synapses

Shi, Y., Kirwan, P., Smith, J., Robinson, H. P. C., & Livesey, F. J. (2012) · Nature Neuroscience · doi:10.1038/nn.3041 · Cited by 813 · see citing works

Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases

Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works

LRRK2 Mutant iPSC-Derived DA Neurons Demonstrate Increased Susceptibility to Oxidative Stress

Nguyen, H. N., Byers, B., Cord, B. J., Shcheglovitov, A., Byrne, J., Gujar, P., Kee, K., Schüle, B., Dolmetsch, R. E., Langston, J. W., et al. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.01.013 · Cited by 748 · see citing works

Kinase activity is required for the toxic effects of mutant LRRK2/dardarin

Greggio, E., Jain, S., Kingsbury, A. E., Bandopadhyay, R., Lewis, P. A., Kaganovich, A., van der Brug, M. P., Beilina, A. G., Blackinton, J. G., Craig, K. J. T., et al. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.04.001 · Cited by 731 · see citing works

SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes

Shi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works

Combined small-molecule inhibition accelerates developmental timing and converts human pluripotent stem cells into nociceptors

Chambers, S. M., Qi, Y., Mica, Y., Lee, G., Zhang, X., Niu, L., Bilsland, J., Cao, L., Stevens, E. B., Whiting, P. J., et al. (2012) · Nature Biotechnology · doi:10.1038/nbt.2249 · Cited by 605 · see citing works

Docking of Axonal Mitochondria by Syntaphilin Controls Their Mobility and Affects Short-Term Facilitation

Kang, J.-S., Tian, J.-H., Pan, P.-Y., Zald, P., Li, C., Deng, C., & Sheng, Z.-H. (2008) · Cell · doi:10.1016/j.cell.2007.11.024 · Cited by 598 · see citing works

Disease-specific phenotypes in dopamine neurons from human iPS-based models of genetic and sporadic Parkinson's disease

Sànchez-Dànes, A., Richaud-Patin, Y., Carballo-Carbajal, I., Jiménez-Delgado, S., Caig, C., Mora, S., Guglielmo, C. D., Ezquerra, M., Patel, B., Giralt, A., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200215 · Cited by 576 · see citing works

The Familial Parkinsonism Gene LRRK2 Regulates Neurite Process Morphology

MacLeod, D., Dowman, J., Hammond, R., Leete, T., Inoue, K., & Abeliovich, A. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.008 · Cited by 564 · see citing works

Modeling human cortical development in vitro using induced pluripotent stem cells

Mariani, J., Simonini, M. V., Palejev, D., Tomasini, L., Coppola, G., Szekely, A. M., Horvath, T. L., & Vaccarino, F. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202944109 · Cited by 526 · see citing works

Mitochondrial Trafficking in Neurons

Schwarz, T. L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011304 · Cited by 525 · see citing works

Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease

Ryan, B. J., Hoek, S., Fon, E. A., & Wade-Martins, R. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.02.003 · Cited by 524 · see citing works

Role of autophagy in G2019S‐LRRK2‐associated neurite shortening in differentiated SH‐SY5Y cells

Plowey, E., Cherra, S. J., Liu, Y.-J., & Chu, C. T. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05217.x · Cited by 523 · see citing works

LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity

Jaleel, M., Nichols, R. J., Deák, M., Campbell, D. G., Gillardon, F., Knebel, A., & Alessi, D. R. (2007) · Biochemical Journal · doi:10.1042/bj20070209 · Cited by 514 · see citing works

Pharmacological rescue of mitochondrial deficits in iPSC-derived neural cells from patients with familial Parkinson’s disease

Cooper, O., Seo, H., Andrabi, S., Guardia-Laguarta, C., Graziotto, J., Sundberg, M., McLean, J. R., Carrillo-Reid, L., Xie, Z., Osborn, T., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003985 · Cited by 508 · see citing works

Genetic Correction of a LRRK2 Mutation in Human iPSCs Links Parkinsonian Neurodegeneration to ERK-Dependent Changes in Gene Expression

Reinhardt, P., Schmid, B., Burbulla, L. F., Schöndorf, D. C., Wagner, L., Glatza, M., Höing, S., Hargus, G., Heck, S. A., Dhingra, A., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.01.008 · Cited by 500 · see citing works

Induced Pluripotent Stem Cells from Patients with Huntington’s Disease Show CAG Repeat Expansion Associated Phenotypes

Mattis, V. B., Svendsen, S. P., Ebert, A., Svendsen, C., King, A. R., Casale, M., Winokur, S., Batugedara, G., Vawter, M., Donovan, P., et al. (2012) · Cell Stem Cell · doi:10.1016/j.stem.2012.04.027 · Cited by 479 · see citing works

Calorie restriction and sirtuins revisited

Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464 · see citing works

Assessing bioenergetic function in response to oxidative stress by metabolic profiling

Dranka, B. P., Benavides, G. A., Diers, A. R., Giordano, S., Zelickson, B. R., Reily, C., Zou, L., Chatham, J. C., Hill, B. G., Zhang, J., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.005 · Cited by 436 · see citing works

Dopaminergic Neuronal Loss, Reduced Neurite Complexity and Autophagic Abnormalities in Transgenic Mice Expressing G2019S Mutant LRRK2

Ramonet, D., Daher, J. P. L., Lin, B. M., Stafa, K., Kim, J., Banerjee, R., Westerlund, M., Pletnikova, O., Glauser, L., Yang, L., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018568 · Cited by 405 · see citing works

Sirtuins mediate mammalian metabolic responses to nutrient availability

Chalkiadaki, A., & Guarente, L. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.225 · Cited by 342 · see citing works

Regulation of the autophagy protein LC3 by phosphorylation

Cherra, S. J., Kulich, S. M., Uechi, G. T., Balasubramani, M., Mountzouris, J. A., Day, B. W., & Chu, C. T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002108 · Cited by 341 · see citing works

Mitochondrial impairment in patients with Parkinson disease with the G2019S mutation in LRRK2

Mortiboys, H., Johansen, K. K., Aasly, J. O., & Bandmann, O. (2010) · Neurology · doi:10.1212/wnl.0b013e3181ff9685 · Cited by 309 · see citing works

Measuring energy metabolism in cultured cells, including human pluripotent stem cells and differentiated cells

Zhang, J., Nuebel, E., Wisidagama, D., Setoguchi, K., Hong, J. S., Horn, C. M. V., Imam, S. S., Vergnes, L., Malone, C., Koehler, C., et al. (2012) · Nature Protocols · doi:10.1038/nprot.2012.048 · Cited by 286 · see citing works

A Drosophila model for LRRK2 -linked parkinsonism

Liu, Z., Wang, X., Yu, Y., Li, X., Wang, T., Jiang, H., Ren, Q., Jiao, Y., Sawa, A., Moran, T. H., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708452105 · Cited by 279 · see citing works

Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations

Godena, V. K., Brookes-Hocking, N., Möller, A., Shaw, G., Oswald, M. C. W., Sancho, R. M., Miller, C. C. J., Whitworth, A. J., & Vos, K. J. D. (2014) · Nature Communications · doi:10.1038/ncomms6245 · Cited by 279 · see citing works

LRRK2 mutations cause mitochondrial DNA damage in iPSC-derived neural cells from Parkinson's disease patients: Reversal by gene correction

Sanders, L. H., Laganière, J., Cooper, O., Mak, S. K., Vu, B. J., Huang, Y. A., Paschon, D. E., Vangipuram, M., Sundararajan, R., Urnov, F. D., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.10.013 · Cited by 271 · see citing works

Progressive dopaminergic alterations and mitochondrial abnormalities in LRRK2 G2019S knock-in mice

Yue, M., Hinkle, K. M., Davies, P., Trushina, E. V., Fiesel, F. C., Christenson, T. A., Schroeder, A. S., Zhang, L., Bowles, E. E., Behrouz, B., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.031 · Cited by 270 · see citing works

HDAC6 Regulates Mitochondrial Transport in Hippocampal Neurons

Chen, S., Owens, G. C., Makarenkova, H. P., & Edelman, D. B. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010848 · Cited by 270 · see citing works

LRRK2 Modulates Vulnerability to Mitochondrial Dysfunction in Caenorhabditis elegans

Saha, S., Guillily, M. D., Ferree, A. W., Lanceta, J., Chan, D., Ghosh, J. G., Hsu, C. H., Segal, L., Raghavan, K., Matsumoto, K., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2281-09.2009 · Cited by 243 · see citing works

Sirtuin deacetylases in neurodegenerative diseases of aging

Herskovits, A. Z., & Guarente, L. (2013) · Cell Research · doi:10.1038/cr.2013.70 · Cited by 222 · see citing works

Generation of human induced pluripotent stem cells by simple transient transfection of plasmid DNA encoding reprogramming factors

Si‐Tayeb, K., Noto, F. K., Šepac, A., Sedlić, F., Bosnjak, Z. J., Lough, J., & Duncan, S. A. (2010) · BMC Developmental Biology · doi:10.1186/1471-213x-10-81 · Cited by 220 · see citing works

Parkin Protects against LRRK2 G2019S Mutant-Induced Dopaminergic Neurodegeneration in Drosophila

Ng, C.-H., Mok, S. Z. S., Koh, C., Ouyang, X., Fivaz, M. L., Tan, E.-K., Dawson, V. L., Dawson, T. M., Yu, F., & Lim, K. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2375-09.2009 · Cited by 211 · see citing works

An Acetylation Switch Modulates the Transcriptional Activity of Estrogen-Related Receptor α

Wilson, B. J., Tremblay, A. M., Deblois, G., Sylvain-Drolet, G., & Giguère, V. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0441 · Cited by 192 · see citing works

Mutant LRRK2 Elicits Calcium Imbalance and Depletion of Dendritic Mitochondria in Neurons

Cherra, S. J., Steer, E. K., Gusdon, A. M., Kiselyov, K. I., & Chu, C. T. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.10.027 · Cited by 189 · see citing works

G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization

Papkovskaia, T. D., Chau, K., Iñesta-Vaquera, F., Papkovsky, D. B., Healy, D. G., Nishio, K., Staddon, J. M., Duchen, M. R., Hardy, J., Schapira, A. H. V., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds244 · Cited by 164 · see citing works

The ways and means that fine tune Sirt1 activity

Revollo, J. R., & Li, X. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.12.004 · Cited by 161 · see citing works

GSK2578215A; A potent and highly selective 2-arylmethyloxy-5-substitutent-N-arylbenzamide LRRK2 kinase inhibitor

Reith, A. D., Bamborough, P., Jandu, K. S., Andreotti, D., Mensah, L. M., Acheson-Dossang, P., Choi, H. G., Deng, X., Zhang, J., Alessi, D. R., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.06.104 · Cited by 149 · see citing works

Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation

Luzón-Toro, B., de la Torre, E. R., Delgado, A., Pérez‐Tur, J., & Hilfiker, S. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm151 · Cited by 140 · see citing works

The Sirtuin-2 Inhibitor AK7 Is Neuroprotective in Models of Parkinson’s Disease but Not Amyotrophic Lateral Sclerosis and Cerebral Ischemia

Chen, X., Wales, P., Quinti, L., Zuo, F., Moniot, S., Hérisson, F., Rauf, N. A., Wang, H., Silverman, R. B., Ayata, C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116919 · Cited by 138 · see citing works

UDCA exerts beneficial effect on mitochondrial dysfunction in <i>LRRK2</i> ^{<i>G2019S</i>} carriers and in vivo

Mortiboys, H., Furmston, R., Bronstad, G., Aasly, J., Elliott, C., & Bandmann, O. (2015) · Neurology · doi:10.1212/wnl.0000000000001905 · Cited by 131 · see citing works

p53 Acetylation Is Crucial for Its Transcription-independent Proapoptotic Functions

Yamaguchi, H., Woods, N. T., Piluso, L. G., Lee, H., Chen, J., Bhalla, K. N., Monteiro, Á. N. A., Liu, X., Hung, M., & Wang, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809268200 · Cited by 130 · see citing works

PGC-1α/ERRα-Sirt3 Pathway Regulates DAergic Neuronal Death by Directly Deacetylating SOD2 and ATP Synthase β

Zhang, X., Ren, X., Zhang, Q., Li, Z., Ma, S., Bao, J., Li, Z., Bai, X., Zheng, L., Zhang, Z., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6403 · Cited by 129 · see citing works

Role of cellular bioenergetics in smooth muscle cell proliferation induced by platelet-derived growth factor

Perez, J. N., Hill, B. G., Benavides, G. A., Dranka, B. P., & Darley-Usmar, V. M. (2010) · Biochemical Journal · doi:10.1042/bj20100090 · Cited by 125 · see citing works

Dispensable role of Drosophila ortholog of LRRK2 kinase activity in survival of dopaminergic neurons

Wang, D., Tang, B., Zhao, G., Pan, Q., Xia, K., Bodmer, R., & Zhang, Z. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-3 · Cited by 119 · see citing works

EZ spheres: A stable and expandable culture system for the generation of pre-rosette multipotent stem cells from human ESCs and iPSCs

Ebert, A. D., Shelley, B., Hurley, A. M., Onorati, M., Castiglioni, V., Patitucci, T. N., Svendsen, S. P., Mattis, V. B., McGivern, J. V., Schwab, A. J., et al. (2013) · Stem Cell Research · doi:10.1016/j.scr.2013.01.009 · Cited by 110 · see citing works

The rescue of microtubule-dependent traffic recovers mitochondrial function in Parkinson's disease

Esteves, A. R., Gozes, I., & Cardoso, S. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.003 · Cited by 107 · see citing works

Who watches the watchmen? Regulation of the expression and activity of sirtuins

Buler, M., Andersson, U., & Hakkola, J. (2016) · The FASEB Journal · doi:10.1096/fj.201600410rr · Cited by 84 · see citing works

Neurite Aggregation and Calcium Dysfunction in iPSC-Derived Sensory Neurons with Parkinson’s Disease-Related LRRK2 G2019S Mutation

Schwab, A. J., & Ebert, A. D. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.11.004 · Cited by 83 · see citing works

The Discovery of a Highly Selective 5,6,7,8‐Tetrahydrobenzo[4,5]thieno[2,3‐d]pyrimidin‐4(3H)‐one SIRT2 Inhibitor that is Neuroprotective in an in vitro Parkinson’s Disease Model

Fruscia, P. D., Zacharioudakis, E., Liu, C., Moniot, S., Laohasinnarong, S., Khongkow, M., Harrison, I. F., Koltsida, K., Reynolds, C. R., Schmidtkunz, K., et al. (2014) · ChemMedChem · doi:10.1002/cmdc.201402431 · Cited by 73 · see citing works

SIRT3: A Central Regulator of Mitochondrial Adaptation in Health and Disease

Weir, H. J. M., Lane, J. D., & Balthasar, N. (2013) · Genes & Cancer · doi:10.1177/1947601913476949 · Cited by 72 · see citing works

Optimizing neuronal differentiation from induced pluripotent stem cells to model ASD

Kim, D.-S., Ross, P. J., Zaslavsky, K., & Ellis, J. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00109 · Cited by 70 · see citing works

SIRT3 Acts as a Neuroprotective Agent in Rotenone-Induced Parkinson Cell Model

Zhang, J., Deng, Y., Zhang, M., Su, H., & Qu, Q. (2016) · Neurochemical Research · doi:10.1007/s11064-016-1892-2 · Cited by 70 · see citing works

Mitochondrial Metabolism Regulates Microtubule Acetylome and Autophagy Trough Sirtuin-2: Impact for Parkinson’s Disease

Esteves, A. R., Arduíno, D. M., Silva, D. F., Viana, S., Pereira, F. C., & Cardoso, S. M. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0420-y · Cited by 67 · see citing works

SIRT2 enhances 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced nigrostriatal damage via apoptotic pathway

Liu, L., Arun, A., Ellis, L., Peritore, C., & Dönmez, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00184 · Cited by 63 · see citing works

Decreased SIRT2 activity leads to altered microtubule dynamics in oxidatively-stressed neuronal cells: Implications for Parkinson's disease

Patel, V. P., & Chu, C. T. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.04.024 · Cited by 51 · see citing works

Sirtuins as modifiers of Parkinson's disease pathology

Tang, B. L. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23806 · Cited by 40 · see citing works

The LRRK2 G2019S mutation in a series of Argentinean patients with Parkinson's disease: Clinical and demographic characteristics

Gatto, E. M., Parisi, V. L., Converso, D. P., Poderoso, J. J., Carreras, M. C., Martí-Massó, J. F., & Paisán‐Ruiz, C. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.01.011 · Cited by 38 · see citing works

SMN deficiency does not induce oxidative stress in SMA iPSC-derived astrocytes or motor neurons

Patitucci, T. N., & Ebert, A. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv489 · Cited by 37 · see citing works

Mitochondrial quality, dynamics and functional capacity in Parkinson’s disease cybrid cell lines selected for Lewy body expression

Cronin-Furman, E. N., Borland, M., Bergquist, K. E., Bennett, J. P., & Trimmer, P. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-6 · Cited by 30 · see citing works

Peroxisome proliferator‐activated receptor‐γ coactivator‐1α mediates neuroprotection against excitotoxic brain injury in transgenic mice: role of mitochondria and X‐linked inhibitor of apoptosis protein

Mäkelä, J., Mudò, G., Pham, D. D., Liberto, V. D., Eriksson, O., Louhivuori, L. M., Bruelle, C., Soliymani, R., Baumann, M., Korhonen, L., et al. (2016) · European Journal of Neuroscience · doi:10.1111/ejn.13157 · Cited by 13 · see citing works

NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential

Xie, N., Zhang, L., Gao, W. Q., Huang, C., Huber, P., Zhou, X., Li, C. L., Shen, G., & Zou, B. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00311-7 · Cited by 1,076 · see citing works

NAD+ in Brain Aging and Neurodegenerative Disorders

Lautrup, S., Sinclair, D. A., Mattson, M. P., & Fang, E. F. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.001 · Cited by 790 · see citing works

New insights into the complex role of mitochondria in Parkinson’s disease

Grünewald, A., Kumar, K. R., & Sue, C. M. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.09.003 · Cited by 362 · see citing works

Mitophagy in Parkinson’s Disease: From Pathogenesis to Treatment

Liu, J., Liu, W., Li, R., & Yang, H. (2019) · Cells · doi:10.3390/cells8070712 · Cited by 224 · see citing works

Mitophagy and Oxidative Stress: The Role of Aging

Gaetano, A. D., Gibellini, L., Zanini, G., Nasi, M., Cossarizza, A., & Pinti, M. (2021) · Antioxidants · doi:10.3390/antiox10050794 · Cited by 188 · see citing works

Genetic predispositions of Parkinson’s disease revealed in patient-derived brain cells

Tran, J., Anastacio, H. T. D., & Bardy, C. (2020) · npj Parkinson s Disease · doi:10.1038/s41531-020-0110-8 · Cited by 181 · see citing works

LRRK2 and mitochondria: Recent advances and current views

Singh, A., Zhi, L., & Zhang, H. (2018) · Brain Research · doi:10.1016/j.brainres.2018.06.010 · Cited by 131 · see citing works

Genome-wide histone acetylation analysis reveals altered transcriptional regulation in the Parkinson’s disease brain

Toker, L., Tran, G. T., Sundaresan, J., Tysnes, O., Alves, G. W., Haugarvoll, K., Nido, G. S., Dölle, C., & Tzoulis, C. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00450-7 · Cited by 129 · see citing works

Studying Human Neurological Disorders Using Induced Pluripotent Stem Cells: From 2D Monolayer to 3D Organoid and Blood Brain Barrier Models

Logan, S., Arzua, T., Canfield, S. G., Seminary, E. R., Sison, S. L., Ebert, A. D., & Bai, X. (2019) · Comprehensive physiology · doi:10.1002/cphy.c180025 · Cited by 139 · see citing works

Sirtuins in Neuroendocrine Regulation and Neurological Diseases

Fujita, Y., & Yamashita, T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00778 · Cited by 109 · see citing works

Mitophagy and reactive oxygen species interplay in Parkinson’s disease

Xiao, B., Kuruvilla, J., & Tan, E. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00402-y · Cited by 112 · see citing works

Axonal energy metabolism, and the effects in aging and neurodegenerative diseases

Yang, S., Park, J. H., & Lu, H.-C. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00634-3 · Cited by 94 · see citing works

Mitochondrial Behavior in Axon Degeneration and Regeneration

Wang, B., Huang, M., Shang, D., Yan, X., Zhao, B., & Zhang, X. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.650038 · Cited by 90 · see citing works

Oxidized nicotinamide adenine dinucleotide-dependent mitochondrial deacetylase sirtuin-3 as a potential therapeutic target of Parkinson’s disease

Zhou, Z., & Tan, E. K. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101107 · Cited by 76 · see citing works

Induced pluripotent stem cells: a tool for modeling Parkinson’s disease

Bose, A., Petsko, G. A., & Studer, L. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2022.05.001 · Cited by 70 · see citing works

Implications of NAD metabolism in pathophysiology and therapeutics for neurodegenerative diseases

Hikosaka, K., Yaku, K., Okabe, K., & Nakagawa, T. (2021) · Nutritional Neuroscience · doi:10.1080/1028415x.2019.1637504 · Cited by 62 · see citing works

The therapeutic perspective of NAD+ precursors in age-related diseases

Iqbal, T., & Nakagawa, T. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.149590 · Cited by 65 · see citing works

Unraveling Parkinson’s Disease Neurodegeneration: Does Aging Hold the Clues?

Coleman, C., & Martin, I. (2022) · Journal of Parkinson s Disease · doi:10.3233/jpd-223363 · Cited by 59 · see citing works

HDAC Inhibition by Valproic Acid Induces Neuroprotection and Improvement of PD-like Behaviors in LRRK2 R1441G Transgenic Mice

Kim, T., Song, S., Park, Y., Kang, S., & Seo, H. (2019) · Experimental Neurobiology · doi:10.5607/en.2019.28.4.504 · Cited by 58 · see citing works

Dysregulation of PGC-1α-Dependent Transcriptional Programs in Neurological and Developmental Disorders: Therapeutic Challenges and Opportunities

McMeekin, L. J., Fox, S. N., Boas, S. M., & Cowell, R. M. (2021) · Cells · doi:10.3390/cells10020352 · Cited by 51 · see citing works

Classic and evolving animal models in Parkinson's disease

Pingale, T. D., & Gupta, G. L. (2020) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2020.173060 · Cited by 54 · see citing works

Imbalance of Lysine Acetylation Contributes to the Pathogenesis of Parkinson’s Disease

Wang, R., Sun, H., Wang, G., & Ren, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197182 · Cited by 50 · see citing works

Cellular reprogramming as a tool to model human aging in a dish

Pitrez, P. R., Monteiro, L. M., Borgogno, O., Nissan, X., Mertens, J., & Ferreira, L. (2024) · Nature Communications · doi:10.1038/s41467-024-46004-5 · Cited by 49 · see citing works

Using Patient-Derived Induced Pluripotent Stem Cells to Identify Parkinson’s Disease-Relevant Phenotypes

Sison, S. L., Vermilyea, S., Emborg, M. E., & Ebert, A. D. (2018) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-018-0893-8 · Cited by 46 · see citing works

Mitochondrial dysfunction and oxidative stress in induced pluripotent stem cell models of Parkinson's disease

Bose, A., & Beal, M. F. (2018) · European Journal of Neuroscience · doi:10.1111/ejn.14264 · Cited by 41 · see citing works

Mitochondrial dysfunction in neurodegenerative diseases: A focus on iPSC-derived neuronal models

Trombetta-Lima, M., Sabogal-Guáqueta, A. M., & Dolga, A. M. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102362 · Cited by 41 · see citing works

Modelling Parkinson’s Disease: iPSCs towards Better Understanding of Human Pathology

Avazzadeh, S., Baena-Montes, J. M., Keighron, C. N., Sánchez, Y. F., & Quinlan, L. R. (2021) · Brain Sciences · doi:10.3390/brainsci11030373 · Cited by 36 · see citing works

The Protective Effects of Mogroside V Against Neuronal Damages by Attenuating Mitochondrial Dysfunction via Upregulating Sirtuin3

Luo, H., Peng, C., Xu, X., Peng, Y., Shi, F., Li, Q., Dong, J., & Chen, M. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02689-z · Cited by 36 · see citing works

3D human brain cell models: New frontiers in disease understanding and drug discovery for neurodegenerative diseases

Korhonen, P., Malm, T., & White, A. R. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.08.012 · Cited by 34 · see citing works

Modeling Parkinson’s Disease Using Induced Pluripotent Stem Cells

Hu, X., Mao, C., Fan, L., Luo, H., Hu, Z., Zhang, S., Yang, Z., Zheng, H., Sun, H., Fan, Y., et al. (2020) · Stem Cells International · doi:10.1155/2020/1061470 · Cited by 34 · see citing works

SIRT3-Mediated Deacetylation of SDHA Rescues Mitochondrial Bioenergetics Contributing to Neuroprotection in Rotenone-Induced PD Models

Shen, Y., Wang, X., Nan, N., Fu, X., Zeng, R., Yang, Y., Xian, S., Shi, J., Wu, Q., & Zhou, S. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03830-w · Cited by 32 · see citing works

Recent advances of induced pluripotent stem cells application in neurodegenerative diseases

Amin, N., Tan, X., Ren, Q., Zhu, N., Botchway, B. O. A., Hu, Z., & Fang, M. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.109674 · Cited by 33 · see citing works

Boosting mitochondrial health to counteract neurodegeneration

Burtscher, J., Romani, M., Bernardo, G., Popa, T., Ziviani, E., Hummel, F. C., Sorrentino, V., & Millet, G. P. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102289 · Cited by 34 · see citing works

Role of Sirtuins in Physiology and Diseases of the Central Nervous System

Chojdak-Łukasiewicz, J., Bizoń, A., Waliszewska‐Prosół, M., Piwowar, A., Budrewicz, S. P., & Pokryszko‐Dragan, A. (2022) · Biomedicines · doi:10.3390/biomedicines10102434 · Cited by 33 · see citing works

Induced pluripotent stem cell‐based modeling of mutant LRRK 2‐associated Parkinson's disease

Weykopf, B., Haupt, S., Jungverdorben, J., Flitsch, L. J., Hebisch, M., Liu, G., Suzuki, K., Belmonte, J. C. I., Peitz, M., Blaess, S., et al. (2019) · European Journal of Neuroscience · doi:10.1111/ejn.14345 · Cited by 29 · see citing works

Patient-Derived Induced Pluripotent Stem Cell-Based Models in Parkinson’s Disease for Drug Identification

Kouroupi, G., Antoniou, N., Prodromidou, K., Taoufik, E., & Matsas, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197113 · Cited by 29 · see citing works

NAD+ Metabolism and Diseases with Motor Dysfunction

Lundt, S., & Ding, S. (2021) · Genes · doi:10.3390/genes12111776 · Cited by 27 · see citing works

Progresses in both basic research and clinical trials of NAD+ in Parkinson’s disease

Maria Jose Perez, J., Baden, P., & Deleidi, M. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111499 · Cited by 25 · see citing works

Studying Human Neurological Disorders Using Induced Pluripotent Stem Cells: From 2D Monolayer to 3D Organoid and Blood Brain Barrier Models

Logan, S., Arzua, T., Canfield, S. G., Seminary, E. R., Sison, S. L., Ebert, A. D., & Bai, X. (2019) · Comprehensive physiology · doi:10.1002/j.2040-4603.2019.tb00076.x · Cited by 24 · see citing works

Modeling Neuropsychiatric and Neurodegenerative Diseases With Induced Pluripotent Stem Cells

LaMarca, E. A., Powell, S. K., Akbarian, S., & Brennand, K. (2018) · Frontiers in Pediatrics · doi:10.3389/fped.2018.00082 · Cited by 24 · see citing works

The Role of LRRK2 in Intracellular Organelle Dynamics

Boecker, C. A. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.167998 · Cited by 23 · see citing works

SIRT3‐Mediated Deacetylation of DRP1 K711 Prevents Mitochondrial Dysfunction in Parkinson's Disease

Ye, X., Tao, K., Wen, X., Feng, D., Mai, Z., Ding, H., Mao, H., Wang, M., Yang, Q., Xiang, J., et al. (2025) · Advanced Science · doi:10.1002/advs.202411235 · Cited by 22 · see citing works

Molecular Pathways Involved in LRRK2-Linked Parkinson’s Disease: A Systematic Review

Ravinther, A. I., Dewadas, H. D., Tong, S. R., Foo, C. N., Lin, Y., Chien, C., & Lim, Y. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911744 · Cited by 24 · see citing works

A naturally occurring variant of SHLP2 is a protective factor in Parkinson’s disease

Kim, S., Miller, B., Hartel, N. G., Ramírez, R., Braniff, R. G., Leelaprachakul, N., Huang, A., Wang, Y., Arpawong, T. E., Crimmins, E. M., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-023-02344-0 · Cited by 21 · see citing works

Unraveling mitochondrial dysfunction: comprehensive perspectives on its impact on neurodegenerative diseases

Yusoff, A. A. M., & Khair, S. Z. N. M. (2024) · Reviews in the Neurosciences · doi:10.1515/revneuro-2024-0080 · Cited by 22 · see citing works

The multifaceted role of LRRK2 in Parkinson's disease: From human iPSC to organoids

Oun, A., Sabogal-Guáqueta, A. M., Galuh, S., Alexander, A., Kortholt, A., & Dolga, A. M. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105837 · Cited by 22 · see citing works

High-content phenotyping of Parkinson's disease patient stem cell-derived midbrain dopaminergic neurons using machine learning classification

Vuidel, A., Cousin, L., Weykopf, B., Haupt, S., Hanifehlou, Z., Wiest-Daesslé, N., Segschneider, M., Lee, J., Kwon, Y., Peitz, M., et al. (2022) · Stem Cell Reports · doi:10.1016/j.stemcr.2022.09.001 · Cited by 21 · see citing works

Mitochondrial Phenotypes in Parkinson’s Diseases—A Focus on Human iPSC-Derived Dopaminergic Neurons

Heger, L. M., Wise, R. M., Hees, J. T., Harbauer, A. B., & Burbulla, L. F. (2021) · Cells · doi:10.3390/cells10123436 · Cited by 19 · see citing works

The Enzymatic Core of the Parkinson’s Disease-Associated Protein LRRK2 Impairs Mitochondrial Biogenesis in Aging Yeast

Aufschnaiter, A., Kohler, V., Walter, C., Tosal-Castano, S., Habernig, L., Wolinski, H., Keller, W., Vögtle, F. ‐., & Büttner, S. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00205 · Cited by 18 · see citing works

Acetylome in Human Fibroblasts From Parkinson's Disease Patients

Yakhine-Diop, S. M. S., Rodríguez‐Arribas, M., Martínez-Chacón, G., Uribe-Carretero, E., Gómez‐Sánchez, R., Aiastui, A., de Munaín, A. L., Pedro, J. M. B., Niso‐Santano, M., González‐Polo, R. A., et al. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00097 · Cited by 17 · see citing works

SRCP1 Conveys Resistance to Polyglutamine Aggregation

Santarriaga, S., Haver, H. N., Kanack, A. J., Fikejs, A. S., Sison, S. L., Egner, J. M., Bostrom, J. R., Seminary, E. R., Hill, R. B., Link, B. A., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.008 · Cited by 16 · see citing works

Patient-Specific iPSCs-Based Models of Neurodegenerative Diseases: Focus on Aberrant Calcium Signaling

Grekhnev, D. A., Kaznacheyeva, E. V., & Vigont, V. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020624 · Cited by 16 · see citing works

Age-related Mitochondrial Dysfunction in Parkinson's Disease: New Insights Into the Disease Pathology

Rani, L., Sahu, M. R., & Mondal, A. C. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.07.007 · Cited by 16 · see citing works

Human Induced Pluripotent Stem Cell Phenotyping and Preclinical Modeling of Familial Parkinson’s Disease

Kim, J. J., Daadi, E. W., Oh, T. T., Daadi, E. S., & Daadi, M. M. (2022) · Genes · doi:10.3390/genes13111937 · Cited by 14 · see citing works

The Double-Faceted Role of Leucine-Rich Repeat Kinase 2 in the Immunopathogenesis of Parkinson’s Disease

Zhang, M., Li, C., Ren, J., Wang, H., Fang, Y., Wu, J., & Tang, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.909303 · Cited by 16 · see citing works

The paradigm of protein acetylation in Parkinson’s disease

Yakhine-Diop, S. M. S., Martínez-Chacón, G., Uribe-Carretero, E., Niso‐Santano, M., González‐Polo, R. A., & Fuentes, J. M. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.250575 · Cited by 14 · see citing works

The parkinsonian LRRK2 R1441G mutation shows macroautophagy-mitophagy dysregulation concomitant with endoplasmic reticulum stress

Yakhine-Diop, S. M. S., Rodríguez‐Arribas, M., Canales-Cortés, S., Martínez-Chacón, G., Uribe-Carretero, E., Blanco-Benítez, M., Duque-González, G., Paredes-Barquero, M., Alegre-Cortés, E., Climent, V. E., et al. (2021) · Cell Biology and Toxicology · doi:10.1007/s10565-021-09617-w · Cited by 14 · see citing works

Pluripotent stem cells for neurodegenerative disease modeling: an expert view on their value to drug discovery

Chen, S.-D., Li, H., Cui, M., Dong, Q., & Yu, J. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1767579 · Cited by 14 · see citing works

An Efficient 2D Protocol for Differentiation of iPSCs into Mature Postmitotic Dopaminergic Neurons: Application for Modeling Parkinson’s Disease

Lebedeva, O. S., Sharova, E. I., Grekhnev, D. A., Skorodumova, L., Kopylova, I. V., Vassina, E. M., Oshkolova, A., Novikova, I. V., Krisanova, A. V., Olekhnovich, E. I., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087297 · Cited by 13 · see citing works

Mind the Gap: LRRK2 Phenotypes in the Clinic vs. in Patient Cells

Goveas, L. M., Mutez, E., Chartier‐Harlin, M., & Taymans, J. (2021) · Cells · doi:10.3390/cells10050981 · Cited by 12 · see citing works

Epigenetic Analysis in Human Neurons: Considerations for Disease Modeling in PD

de Boni, L., & Wüllner, U. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00276 · Cited by 10 · see citing works

Protective Activity of Aspirin Eugenol Ester on Paraquat‐Induced Cell Damage in SH‐SY5Y Cells

Zhang, Z., Yang, Y., Qin, Z., Liu, X., Li, S., Bai, L., & Li, J. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6697872 · Cited by 9 · see citing works

Exploring the focal role of LRRK2 kinase in Parkinson’s disease

Kumar, S., Behl, T., Sehgal, A., Chigurupati, S., Singh, S., Mani, V., Aldubayan, M. A., Alhowail, A., Kaur, S., Bhatia, S., et al. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-022-19082-5 · Cited by 8 · see citing works

Micro-and mesoscale aspects of neurodegeneration in engineered human neural networks carrying the LRRK2 G2019S mutation

Valderhaug, V. D., Ramstad, O. H., van de Wijdeven, R., Heiney, K., Nichele, S., Sandvig, A., & Sandvig, I. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1366098 · Cited by 8 · see citing works

Stem Cell-Based Approaches in Parkinson's Disease Research

Kim, M. S., Yoon, S., Choi, J., Kim, Y. J., & Lee, G. (2024) · International Journal of Stem Cells · doi:10.15283/ijsc23169 · Cited by 7 · see citing works

Progressive Motor and Non-Motor Symptoms in Park7 Knockout Zebrafish

Chavali, L., Yddal, I., Bifulco, E., Mannsåker, S., Røise, D., Law, J. O., Frøyset, A. K., Grellscheid, S. N., & Fladmark, K. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076456 · Cited by 7 · see citing works

Decreased NAD+ in dopaminergic neurons

Sison, S. L., & Ebert, A. D. (2018) · Aging · doi:10.18632/aging.101433 · Cited by 7 · see citing works

Clinical Trial Highlights: Modulators of Mitochondrial Function

Capriglia, F., Burgess, T., Bandmann, O., & Mortiboys, H. (2023) · Journal of Parkinson s Disease · doi:10.3233/jpd-239003 · Cited by 5 · see citing works

Stem cells technology: a powerful tool behind new brain treatments

Duru, L. N., Quan, Z., Qazi, T. J., & Qing, H. (2018) · Drug Delivery and Translational Research · doi:10.1007/s13346-018-0548-y · Cited by 5 · see citing works

Structural and functional alterations associated with the LRRK2 G2019S mutation revealed in structured human neural networksPreprint

Valderhaug, V. D., Ramstad, O. H., van de Wijdeven, R., Heiney, K., Nichele, S., Sandvig, A., & Sandvig, I. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.02.073726 · Cited by 5 · see citing works

A review article on the development of dopaminergic neurons and establishment of dopaminergic neuron–based in vitro models by using immortal cell lines or stem cells to study and treat Parkinson's disease

Erol, A. Y. G. (2024) · International Journal of Developmental Neuroscience · doi:10.1002/jdn.10383 · Cited by 3 · see citing works

Nicotinamide mononucleotide treatment increases NAD+ levels in an iPSC Model of Parkinson’s DiseasePreprint

Fulleylove-Krause, B., Sison, S. L., & Ebert, A. D. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.06.080911 · Cited by 2 · see citing works

Modulations of SIRTUINs and Management of Brain Disorders

Shekhar, S. K., Siddiqui, S. A., & Rai, G. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815040197123010006 · Cited by 1 · see citing works

Machine learning-aided multidimensional phenotyping of Parkinson’s disease patient stem cell-derived midbrain dopaminergic neuronsPreprint

Vuidel, A., Cousin, L., Weykopf, B., Haupt, S., Hanifehlou, Z., Wiest-Daesslé, N., Segschneider, M., Peitz, M., Ogier, A., Brino, L., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.01.482490 · Cited by 1 · see citing works

The mitochondrial network in Parkinson's disease

Aufschnaiter, A., Kohler, V., & Büttner, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815950-7.00008-4

Activation of SIRT3 alleviates neurodegeneration via rescuing mitochondrial succinate dehydrogenase activity and bioenergy supply in rotenone-induced PD modelsPreprint

Shen, Y., Wang, X., Nan, N., Fu, X., Zeng, R., Yang, Y., Xuan, S., Shi, J., Wu, Q., & Zhou, S. (2022) · doi:10.22541/au.164873429.98144663/v1

Faculty Opinions recommendation of SRCP1 conveys resistance to polyglutamine aggregation.

Gomer, R. H. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733671907.793549116

Immune function of LRRK2

Oun, A. (2022) · doi:10.33612/diss.253651629

Nicotinamide Adenine Dinucleotide and Parkinson’s Disease

Cheng, Y., Yang, D.-C., & Lin, F. (2025) · Springer eBooks · doi:10.1007/978-981-97-9877-3_35

A combined artificial intelligence–wet lab approach identifies a pivotal role of the NAD + –mitophagy axis on aging and neurodegeneration

Lautrup, S., Cao, S., Long, X., Liu, B. H. M., Escobar-Doncel, B., Ferrante, A., Frank, J., Schmauck‐Medina, T., Leung, G. H. D., Liang, K. X., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71680

Mitochondrial impairment in patients with Parkinson disease with the G2019S mutation in LRRK2

Mortiboys, H., Johansen, K. K., Aasly, J. O., & Bandmann, O. (2010) · Neurology · doi:10.1212/wnl.0b013e3181ff9685 · Cited by 309 · see citing works

G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization

Papkovskaia, T. D., Chau, K., Iñesta-Vaquera, F., Papkovsky, D. B., Healy, D. G., Nishio, K., Staddon, J. M., Duchen, M. R., Hardy, J., Schapira, A. H. V., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds244 · Cited by 164 · see citing works

Dopamine D2 receptor-mediated neuroprotection in a G2019S Lrrk2 genetic model of Parkinson’s disease

Tozzi, A., Tantucci, M., Marchi, S., Mazzocchetti, P., Morari, M., Pinton, P., Mancini, A., & Calabresi, P. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0221-2 · Cited by 54 · see citing works

Leucine rich repeat kinase 2 in the pathogenesis of Parkinson's disease

Papkovskaia, T. (2013) · UCL Discovery (University College London)

Mitochondrial dysfunction and mitophagy defects in LRRK2-R1441C Parkinson’s disease models

Williamson, M. G., Madureira, M., McGuinness, W., Heon‐Roberts, R., Mock, E. D., Naidoo, K., Cramb, K. M. L., Caiazza, M. C., Malpartida, A. B., Lavelle, M., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad102 · Cited by 55 · see citing works