Spread of α-synuclein pathology through the brain connectome is modulated by selective vulnerability and predicted by network analysis

Generalized Additive Models: An Introduction with R

Wood, S. N. (2017) · doi:10.1201/9781315370279 · Cited by 13,852 · see citing works

Staging of brain pathology related to sporadic Parkinson’s disease

Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777 · see citing works

Fast Stable Restricted Maximum Likelihood and Marginal Likelihood Estimation of Semiparametric Generalized Linear Models

Wood, S. N. (2010) · Journal of the Royal Statistical Society Series B (Statistical Methodology) · doi:10.1111/j.1467-9868.2010.00749.x · Cited by 7,538 · see citing works

Genome-wide atlas of gene expression in the adult mouse brain

Lein, E. S., Hawrylycz, M. J., Ao, N., Ayres, M., Bensinger, A., Bernard, A., Boe, A. F., Boguski, M. S., Brockway, K. S., Byrnes, E. J., et al. (2007) · Nature · doi:10.1038/nature05453 · Cited by 5,572 · see citing works

Generalized Additive Models

Wood, S. N. (2006) · doi:10.1201/9781420010404 · Cited by 4,953 · see citing works

α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 3,151 · see citing works

A mesoscale connectome of the mouse brain

Oh, S. W., Harris, J. A., Ng, L., Winslow, B., Cain, N., Mihalas, S., Wang, Q., Lau, C., Kuan, L., Henry, A. M., et al. (2014) · Nature · doi:10.1038/nature13186 · Cited by 2,612 · see citing works

Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works

Stable and Efficient Multiple Smoothing Parameter Estimation for Generalized Additive Models

Wood, S. (2004) · Journal of the American Statistical Association · doi:10.1198/016214504000000980 · Cited by 2,046 · see citing works

Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.

(1998) · Europe PMC (PubMed Central) · Cited by 1,594 · see citing works

Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death

Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569 · see citing works

Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study

Healy, D. G., Falchi, M., O’Sullivan, S. S., Bonifati, V., Dürr, A., Bressman, S., Brice, A., Aasly, J. O., Zabetian, C. P., Goldwurm, S., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70117-0 · Cited by 1,523 · 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

Selective neuronal vulnerability in Parkinson disease

Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,120 · see citing works

Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Cairns, N. J., Lantos, P. L., & Goedert, M. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00504-7 · Cited by 1,026 · see citing works

Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells

Luk, K. C., Song, C., O’Brien, P., Stieber, A., Branch, J. R., Brunden, K. R., Trojanowski, J. Q., & Lee, V. M. ‐. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908005106 · Cited by 958 · see citing works

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3

Mao, X., Ou, M. T., Karuppagounder, S. S., Kam, T., Yin, X., Xiong, Y., Ge, P., Umanah, G. K. E., Brahmachari, S., Shin, J., et al. (2016) · Science · doi:10.1126/science.aah3374 · Cited by 739 · see citing works

Addition of exogenous α-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous α-synuclein to Lewy body and Lewy neurite–like aggregates

Volpicelli-Daley, L. A., Luk, K. C., & Lee, V. M.-Y. (2014) · Nature Protocols · doi:10.1038/nprot.2014.143 · Cited by 731 · 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

A network diffusion model of disease progression in dementia

Raj, A., Kuceyeski, A., & Weiner, M. (2012) · Neuron · doi:10.1016/j.neuron.2011.12.040 · Cited by 723 · see citing works

Staging of the intracerebral inclusion body pathology associated with idiopathic Parkinson's disease (preclinical and clinical stages)

Braak, H., Tredici, K. D., Bratzke, H., Hamm-Clement, J., Sandmann-Keil, D., & Rüb, U. (2002) · Journal of Neurology · doi:10.1007/s00415-002-1301-4 · Cited by 710 · see citing works

Unified staging system for Lewy body disorders: correlation with nigrostriatal degeneration, cognitive impairment and motor dysfunction

the Arizona Parkinson’s Disease Consortium, Beach, T. G., Adler, C. H., Lue, L., Sue, L. I., Bachalakuri, J., Henry-Watson, J., Sasse, J., Boyer, S., Shirohi, S., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0538-8 · Cited by 698 · see citing works

LRRK2 activation in idiopathic Parkinson’s disease

Maio, R. D., Hoffman, E. K., Rocha, E. M., Keeney, M. T., Sanders, L. H., Miranda, B. R. D., Zharikov, A., Laar, A. D. V., Stepan, A. F., Lanz, T. A., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aar5429 · Cited by 571 · see citing works

Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of α-synuclein, and apoptotic cell death in aged mice

Tong, Y., Yamaguchi, H., Giaime, E., Boyle, S., Kopan, R., Kelleher, R. J., & Shen, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004676107 · Cited by 502 · see citing works

The physics of brain network structure, function and control

Lynn, C. W., & Bassett, D. S. (2019) · Nature Reviews Physics · doi:10.1038/s42254-019-0040-8 · Cited by 438 · 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

Widespread transneuronal propagation of α-synucleinopathy triggered in olfactory bulb mimics prodromal Parkinson’s disease

Rey, N. L., Steiner, J. A., Maroof, N., Luk, K. C., Madaj, Z., Trojanowski, J. Q., Lee, V. M. ‐., & Brundin, P. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20160368 · Cited by 389 · see citing works

Ser 1292 Autophosphorylation Is an Indicator of LRRK2 Kinase Activity and Contributes to the Cellular Effects of PD Mutations

Sheng, Z., Zhang, S., Bustos, D. J., Kleinheinz, T., Pichon, C. E. L., Domínguez, S. L., Solanoy, H. O., Drummond, J., Zhang, X., Ding, X., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004485 · Cited by 348 · see citing works

Enhanced Striatal Dopamine Transmission and Motor Performance with LRRK2 Overexpression in Mice Is Eliminated by Familial Parkinson's Disease Mutation G2019S

Li, X., Patel, J. C., Wang, J., Avshalumov, M. V., Nicholson, C., Buxbaum, J. D., Elder, G. A., Rice, M. E., & Yue, Z. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5604-09.2010 · Cited by 342 · see citing works

Novel antibodies to synuclein show abundant striatal pathology in Lewy body diseases

Duda, J. E., Giasson, B. I., Mabon, M. E., Lee, V. M. ‐., & Trojanowski, J. Q. (2002) · Annals of Neurology · doi:10.1002/ana.10279 · Cited by 329 · see citing works

α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration

Tran, H., Chung, C. H.-Y., Iba, M., Zhang, B., Trojanowski, J. Q., Luk, K. C., & Lee, V. M. ‐. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.033 · Cited by 324 · see citing works

Progressive Aggregation of Alpha-Synuclein and Selective Degeneration of Lewy Inclusion-Bearing Neurons in a Mouse Model of Parkinsonism

Osterberg, V. R., Spinelli, K. J., Weston, L. J., Luk, K. C., Woltjer, R. L., & Unni, V. K. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.060 · Cited by 240 · see citing works

Spread of aggregates after olfactory bulb injection of α-synuclein fibrils is associated with early neuronal loss and is reduced long term

Rey, N. L., George, S., Steiner, J. A., Madaj, Z., Luk, K. C., Trojanowski, J. Q., Lee, V. M.-Y., & Brundin, P. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1792-9 · Cited by 215 · see citing works

(G2019S) LRRK2 activates MKK4-JNK pathway and causes degeneration of SN dopaminergic neurons in a transgenic mouse model of PD

Chen, C.-Y., Weng, Y.-H., Chien, K.-Y., Lin, K.-J., Yeh, T.-H., Cheng, Y.-P., Lu, C.-S., & Wang, H.-L. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.42 · Cited by 189 · see citing works

G2019S-LRRK2 Expression Augments -Synuclein Sequestration into Inclusions in Neurons

Volpicelli‐Daley, L. A., Abdelmotilib, H., Liu, Z., Stoyka, L. E., Daher, J. P. L., Milnerwood, A. J., Unni, V. K., Hirst, W. D., Yue, Z., Zhao, H., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3642-15.2016 · Cited by 185 · see citing works

LRRK2 modifies α-syn pathology and spread in mouse models and human neurons

Bieri, G., Brahic, M., Bousset, L., Couthouis, J., Kramer, N. J., Ma, R. K., Nakayama, L., Monbureau, M., Defensor, E. B., Schüle, B., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01995-0 · Cited by 182 · see citing works

Colloquium : Control of dynamics in brain networks

Tang, E., & Bassett, D. S. (2018) · Reviews of Modern Physics · doi:10.1103/revmodphys.90.031003 · Cited by 165 · see citing works

Penetrance estimate of LRRK2 p.G2019S mutation in individuals of non‐Ashkenazi Jewish ancestry

Lee, A., Wang, Y., Alcalay, R. N., Mejia‐Santana, H., Saunders-Pullman, R. J., Bressman, S., Corvol, J., Brice, A., Lesage, S., Mangone, G., et al. (2017) · Movement Disorders · doi:10.1002/mds.27059 · Cited by 164 · see citing works

Progression in the LRRK2-Associated Parkinson Disease Population

Saunders-Pullman, R. J., Mirelman, A., Alcalay, R. N., Wang, C., Ortega, R. A., Raymond, D., Mejia‐Santana, H., Orbe‐Reilly, M., Johannes, B. A., Thaler, A., et al. (2018) · JAMA Neurology · doi:10.1001/jamaneurol.2017.4019 · Cited by 148 · see citing works

Age-Dependent Dopaminergic Neurodegeneration and Impairment of the Autophagy-Lysosomal Pathway in LRRK-Deficient Mice

Giaime, E., Tong, Y., Wagner, L. K., Yang, Y. H., Huang, G., & Shen, J. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.036 · Cited by 131 · see citing works

Robust kinase- and age-dependent dopaminergic and norepinephrine neurodegeneration in LRRK2 G2019S transgenic mice

Xiong, Y., Neifert, S., Karuppagounder, S. S., Liu, Q., Stankowski, J. N., Lee, B. D., Ko, H. S., Lee, Y., Grima, J. C., Mao, X., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1712648115 · Cited by 95 · see citing works

G2019S LRRK2 mutation facilitates α-synuclein neuropathology in aged mice

Novello, S., Arcuri, L., Doveró, S., Dutheil, N., Shimshek, D. R., Bézard, E., & Morari, M. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.08.018 · Cited by 68 · see citing works

Bent out of shape: α‐Synuclein misfolding and the convergence of pathogenic pathways in Parkinson's disease

Luna, E., & Luk, K. C. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.023 · Cited by 65 · see citing works

LRRK2 mouse models: dissecting the behavior, striatal neurochemistry and neurophysiology of PD pathogenesis

Volta, M., & Melrose, H. L. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160238 · Cited by 63 · see citing works

Who was the man who discovered the “Lewy bodies”?

Silva, A. M. R. E., Geldsetzer, F. O., Holdorff, B., KIELHORN, F., Balzer‐Geldsetzer, M., Oertel, W. H., Hurtig, H. H., & Dodel, R. C. (2010) · Movement Disorders · doi:10.1002/mds.22956 · Cited by 58 · see citing works

Neuromelanin, neurotransmitter status and brainstem location determine the differential vulnerability of catecholaminergic neurons to mitochondrial DNA deletions

Elstner, M., Müller, S. K., Leidolt, L., Laub, C., Krieg, L., Schlaudraff, F., Liss, B., Morris, C. M., Turnbull, D. M., Masliah, E., et al. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-43 · Cited by 49 · see citing works

LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic mice

Henderson, M. X., Sengupta, M., McGeary, I., Zhang, B., Olufemi, M. F., Brown, H. J., Trojanowski, J. Q., & Lee, V. M. ‐. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0679-5 · Cited by 48 · see citing works

Regional levels of physiological α-synuclein are directly associated with Lewy body pathology

Erskine, D., Patterson, L., Alexandris, A. S., Hanson, P. S., McKeith, I. G., Attems, J., & Morris, C. M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1787-6 · Cited by 42 · see citing works

Unbiased Proteomics of Early Lewy Body Formation Model Implicates Active Microtubule Affinity-Regulating Kinases (MARKs) in Synucleinopathies

Henderson, M. X., Chung, C. H.-Y., Riddle, D. M., Zhang, B., Gathagan, R. J., Seeholzer, S. H., Trojanowski, J. Q., & Lee, V. M. ‐. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2705-16.2017 · Cited by 38 · see citing works

Predictive Model of Spread of Progressive Supranuclear Palsy Using Directional Network Diffusion

Pandya, S., Mezias, C., & Raj, A. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00692 · Cited by 37 · see citing works

Universal framework for edge controllability of complex networks

Pang, S., Wang, W.-X., Hao, F., & Lai, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-04463-5 · Cited by 35 · see citing works

Testing the Protein Propagation Hypothesis of Parkinson Disease

Dagher, A., & Zeighami, Y. (2018) · Journal of Experimental Neuroscience · doi:10.1177/1179069518786715 · Cited by 28 · see citing works

Functional and behavioral consequences of Parkinson's disease-associated LRRK2-G2019S mutation

Benson, D. L., Matikainen‐Ankney, B. A., Hussein, A., & Huntley, G. W. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180468 · Cited by 20 · see citing works

Diffusion control in multi-agent networks

Chan, W. H. R., Wildemeersch, M., & Quek, T. Q. S. (2015) · IEEE Conference on Decision and Control (CDC) · doi:10.1109/cdc.2015.7402872 · Cited by 6 · see citing works

Characterization and Control of Diffusion Processes in Multi-Agent NetworksPreprint

Chan, W. H. R., Wildemeersch, M., & Quek, T. Q. S. (2015) · arXiv (Cornell University) · doi:10.48550/arxiv.1508.06738 · Cited by 4 · see citing works

Glymphatic failure as a final common pathway to dementia

Nedergaard, M., & Goldman, S. A. (2020) · Science · doi:10.1126/science.abb8739 · Cited by 1,145 · see citing works

Alpha-synuclein in Parkinson’s disease and other synucleinopathies: from overt neurodegeneration back to early synaptic dysfunction

Calabresi, P., Mechelli, A., Natale, G., Volpicelli‐Daley, L. A., Lazzaro, G. D., & Ghiglieri, V. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05672-9 · Cited by 836 · see citing works

Standardizing workflows in imaging transcriptomics with the abagen toolbox

Markello, R. D., Arnatkevičiūtė, A., Poline, J., Fulcher, B. D., Fornito, A., & Mišić, B. (2021) · eLife · doi:10.7554/elife.72129 · Cited by 541 · see citing works

Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases

Nixon, R. A., & Rubinsztein, D. C. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00757-5 · Cited by 435 · see citing works

Mechanisms of secretion and spreading of pathological tau protein

Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304 · see citing works

The α-Synuclein Origin and Connectome Model (SOC Model) of Parkinson’s Disease: Explaining Motor Asymmetry, Non-Motor Phenotypes, and Cognitive Decline

Borghammer, P. (2021) · Journal of Parkinson's Disease · doi:10.3233/jpd-202481 · Cited by 259 · see citing works

Neuronal NLRP3 is a parkin substrate that drives neurodegeneration in Parkinson’s disease

Panicker, N., Kam, T., Wang, H., Neifert, S., Chou, S.-C., Kumar, M., Brahmachari, S., Jhaldiyal, A., Hinkle, J. T., Akkentli, F., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.05.009 · Cited by 220 · see citing works

Advances in understanding the function of alpha-synuclein: implications for Parkinson’s disease

Calabresi, P., Lazzaro, G. D., Marino, G., Campanelli, F., & Ghiglieri, V. (2023) · Brain · doi:10.1093/brain/awad150 · Cited by 168 · see citing works

Connectome-based modelling of neurodegenerative diseases: towards precision medicine and mechanistic insight

Vogel, J. W., Corriveau‐Lecavalier, N., Franzmeier, N., Pereira, J. B., Brown, J. A., Maaß, A., Botha, H., Seeley, W. W., Bassett, D. S., Jones, D. T., et al. (2023) · Nature reviews. Neuroscience · doi:10.1038/s41583-023-00731-8 · Cited by 160 · see citing works

Glucocerebrosidase Activity Modulates Neuronal Susceptibility to Pathological α-Synuclein Insult

Henderson, M. X., Sedor, S. F., McGeary, I., Cornblath, E. J., Peng, C., Riddle, D. M., Li, H. L., Zhang, B., Brown, H. J., Olufemi, M. F., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.12.004 · Cited by 147 · see citing works

Cell-to-Cell Transmission of Tau and α-Synuclein

Uemura, N., Uemura, M. T., Luk, K. C., Lee, V. M. ‐., & Trojanowski, J. Q. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.03.012 · Cited by 141 · see citing works

Prion-like spreading of Alzheimer’s disease within the brain’s connectome

Fornari, S., Schäfer, A., Jucker, M., Goriely, A., & Ellen Kuhl, A. (2019) · Journal of The Royal Society Interface · doi:10.1098/rsif.2019.0356 · Cited by 137 · see citing works

The enigma and implications of brain hemispheric asymmetry in neurodegenerative diseases

Lubben, N., Ensink, E., Coetzee, G. A., & Labrie, V. (2021) · Brain Communications · doi:10.1093/braincomms/fcab211 · Cited by 132 · see citing works

Local molecular and global connectomic contributions to cross-disorder cortical abnormalities

Hansen, J. Y., Shafiei, G., Vogel, J. W., Smart, K. A., Bearden, C. E., Hoogman, M., Franke, B., van Rooij, D., Buitelaar, J. K., McDonald, C. R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32420-y · Cited by 125 · see citing works

Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis

Mukherjee, S., Sakunthala, A., Gadhe, L. G., Poudyal, M., Sawner, A. S., Kadu, P., & Maji, S. K. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167713 · Cited by 129 · see citing works

Dopamine-dependent early synaptic and motor dysfunctions induced by α-synuclein in the nigrostriatal circuit

Tozzi, A., Sciaccaluga, M., Loffredo, V., Megaro, A., Ledonne, A., Cardinale, A., Federici, M., Bellingacci, L., Paciotti, S., Ferrari, E. S., et al. (2021) · Brain · doi:10.1093/brain/awab242 · Cited by 127 · see citing works

Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies

Cascella, R., Bigi, A., Cremades, N., & Cecchi, C. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04166-9 · Cited by 125 · see citing works

Initiation and progression of α-synuclein pathology in Parkinson’s disease

Tofaris, G. K. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04240-2 · Cited by 121 · see citing works

Towards a biologically annotated brain connectome

Bazinet, V., Hansen, J. Y., & Mišić, B. (2023) · Nature reviews. Neuroscience · doi:10.1038/s41583-023-00752-3 · Cited by 108 · see citing works

<scp>α‐Synuclein</scp> in Plasma‐Derived Extracellular Vesicles Is a Potential Biomarker of Parkinson's Disease

Stuendl, A., Kraus, T., Chatterjee, M., Zapke, B., Sadowski, B., Moebius, W., Hobert, M. A., Deuschle, C., Brockmann, K., Maetzler, W., et al. (2021) · Movement Disorders · doi:10.1002/mds.28639 · Cited by 108 · see citing works

Neural connectivity predicts spreading of alpha-synuclein pathology in fibril-injected mouse models: Involvement of retrograde and anterograde axonal propagation

Mezias, C., Rey, N. L., Brundin, P., & Raj, A. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104623 · Cited by 106 · see citing works

Genetic, cellular, and connectomic characterization of the brain regions commonly plagued by glioma

Mandal, A. S., Romero-García, R., Hart, M. G., & John Suckling, A. (2020) · Brain · doi:10.1093/brain/awaa277 · Cited by 105 · see citing works

Determinants of seeding and spreading of α-synuclein pathology in the brain

Henrich, M. T., Geibl, F. F., Harini, L., Stegmann, A., Giasson, B. I., Mao, X., Dawson, V. L., Dawson, T. M., Oertel, W. H., & Surmeier, D. J. (2020) · Science Advances · doi:10.1126/sciadv.abc2487 · Cited by 101 · see citing works

α-Synuclein pathology as a target in neurodegenerative diseases

Park, H.-J., Kam, T., Dawson, V. L., & Dawson, T. M. (2024) · Nature Reviews Neurology · doi:10.1038/s41582-024-01043-w · Cited by 113 · see citing works

Loss of Presynaptic Terminal Integrity in the Substantia Nigra in Early Parkinson's Disease

Delva, A., Weehaeghe, D. V., Koole, M. J. B., Laere, K. V., & Vandenberghe, W. (2020) · Movement Disorders · doi:10.1002/mds.28216 · Cited by 97 · see citing works

Phenotypic manifestation of α-synuclein strains derived from Parkinson’s disease and multiple system atrophy in human dopaminergic neurons

Tanudjojo, B., Shaikh, S. S., Fenyi, A., Bousset, L., Agarwal, D., Marsh, J., Zois, C. E., Heman-Ackah, S. M., Fischer, R., Sims, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23682-z · Cited by 92 · see citing works

Protein-protein interactions in neurodegenerative diseases: A conspiracy theory

Thompson, T., Chaggar, P., Ellen Kuhl, A., Goriely, A., & Initiative, A. D. N. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008267 · Cited by 90 · see citing works

LRRK2 and α-Synuclein: Distinct or Synergistic Players in Parkinson’s Disease?

O’Hara, D. M., Pawar, G. N., Kalia, S. K., & Kalia, L. V. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00577 · Cited by 84 · see citing works

Multiple system atrophy-associated oligodendroglial protein p25α stimulates formation of novel α-synuclein strain with enhanced neurodegenerative potential

Ferreira, N., Gram, H., Sorrentino, Z. A., Gregersen, E., Schmidt, S. I., Reimer, L., Betzer, C., Pérez-Gozalbo, C., Beltoja, M., Nagaraj, M., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02316-0 · Cited by 86 · see citing works

The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding

Courte, J., Bousset, L., von Boxberg, Y., Villard, C., Melki, R., & Peyrin, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-61757-x · Cited by 80 · see citing works

Neuronal FAM171A2 mediates α-synuclein fibril uptake and drives Parkinson’s disease

Wu, K., Xu, Q., Liu, Y., Feng, Y., Han, S., Zhang, Y.-R., Chen, S.-D., Guo, Y. X., Wu, B., Ma, L., et al. (2025) · Science · doi:10.1126/science.adp3645 · Cited by 84 · see citing works

Selective neuronal vulnerability in Parkinson's disease

González‐Rodríguez, P., Zampese, E., & Surmeier, D. J. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2020.02.005 · Cited by 75 · see citing works

Discovering a reaction–diffusion model for Alzheimer’s disease by combining PINNs with symbolic regression

Zhang, Z., Zou, Z., Ellen Kuhl, A., & Karniadakis, G. E. (2023) · Computer Methods in Applied Mechanics and Engineering · doi:10.1016/j.cma.2023.116647 · Cited by 80 · see citing works

Spatial transcriptomics reveals molecular dysfunction associated with cortical Lewy pathology

Goralski, T. M., Meyerdirk, L. K., Breton, L., Brasseur, L., Kurgat, K., DeWeerd, D., Turner, L., Becker, K., Adams, M., Newhouse, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47027-8 · Cited by 77 · see citing works

Targeting α-Synuclein for PD Therapeutics: A Pursuit on All Fronts

Teil, M., Arotçarena, M.-L., Faggiani, E., Laferrière, F., Bézard, E., & Dehay, B. (2020) · Biomolecules · doi:10.3390/biom10030391 · Cited by 78 · see citing works

Animal models of brain-first and body-first Parkinson's disease

Berge, N. V. D., & Ulusoy, A. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105599 · Cited by 78 · see citing works

Neuronal activity modulates alpha-synuclein aggregation and spreading in organotypic brain slice cultures and in vivo

Wu, Q., Shaikh, M., Meymand, E. S., Zhang, B., Luk, K. C., Trojanowski, J. Q., & Lee, V. M. ‐. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02227-6 · Cited by 71 · see citing works

Brain atrophy progression in Parkinson’s disease is shaped by connectivity and local vulnerability

Tremblay, C., Rahayel, S., Vo, A., Morys, F., Shafiei, G., Abbasi, N., Markello, R. D., Gan‐Or, Z., Mišić, B., & Dagher, A. (2021) · Brain Communications · doi:10.1093/braincomms/fcab269 · Cited by 66 · see citing works

Propagation of tau and α-synuclein in the brain: therapeutic potential of the glymphatic system

Lopes, D. M., Llewellyn, S. K., & Harrison, I. F. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00293-2 · Cited by 74 · see citing works

The multi‐faceted role of mitochondria in the pathology of Parkinson’s disease

Trinh, D., Israwi, A. R., Arathoon, L. R., Gleave, J. A., & Nash, J. E. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15154 · Cited by 72 · see citing works

Advanced human iPSC-based preclinical model for Parkinson’s disease with optogenetic alpha-synuclein aggregation

Kim, M. S., Ra, E. A., Kweon, S. H., Seo, B. A., Ko, H. S., Oh, Y., & Lee, G. (2023) · Cell stem cell · doi:10.1016/j.stem.2023.05.015 · Cited by 71 · see citing works

Organotypic slice culture model demonstrates inter-neuronal spreading of alpha-synuclein aggregates

Elfarrash, S., Jensen, N. M., Ferreira, N., Betzer, C., Thevathasan, J. V., Diekmann, R., Adel, M., Omar, N. M., Boraie, M. Z., Gad, S., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0865-5 · Cited by 70 · see citing works

Differentially targeted seeding reveals unique pathological alpha-synuclein propagation patterns

Rahayel, S., Mišić, B., Zheng, Y., Liu, Z.-Q., Abdelgawad, A. A., Abbasi, N., Caputo, A., Zhang, B., Lo, A., Kehm, V. M., et al. (2021) · Brain · doi:10.1093/brain/awab440 · Cited by 64 · see citing works

Trans-synaptic and retrograde axonal spread of Lewy pathology following pre-formed fibril injection in an in vivo A53T alpha-synuclein mouse model of synucleinopathy

Schaser, A. J., Stackhouse, T. L., Weston, L. J., Kerstein, P. C., Osterberg, V. R., López, C. S., Dickson, D. W., Luk, K. C., Meshul, C. K., Woltjer, R. L., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01026-0 · Cited by 62 · see citing works

Hemispheric asymmetry in the human brain and in Parkinson’s disease is linked to divergent epigenetic patterns in neurons

Li, P., Ensink, E., Lang, S., Marshall, L. L., Schilthuis, M., Lamp, J. A., Vega, I. E., & Labrie, V. (2020) · Genome biology · doi:10.1186/s13059-020-01960-1 · Cited by 65 · see citing works

Nanomedicine-based immunotherapy for central nervous system disorders

Hanif, S., Muhammad, P., Chesworth, R., Rehman, F. U., Qian, R., Zheng, M., & Shi, B. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0429-z · Cited by 68 · see citing works

Computational modeling of tau pathology spread reveals patterns of regional vulnerability and the impact of a genetic risk factor

Cornblath, E. J., Li, H. L., Changolkar, L., Zhang, B., Brown, H. J., Gathagan, R. J., Olufemi, M. F., Trojanowski, J. Q., Bassett, D. S., Lee, V. M. Y., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg6677 · Cited by 66 · see citing works

Integrating multimodal and multiscale connectivity blueprints of the human cerebral cortex in health and disease

Hansen, J. Y., Shafiei, G., Voigt, K., Liang, E. X., Cox, S. M. L., Leyton, M., Jamadar, S. D., & Mišić, B. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002314 · Cited by 68 · see citing works

Exploring the role of nanomedicines for the therapeutic approach of central nervous system dysfunction: At a glance

Rhaman, M. M., Islam, M. R., Akash, S., Mim, M., Noor alam, M., Nepovimova, E., Valis, M., Kuca, K., & Sharma, R. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.989471 · Cited by 63 · see citing works

α ‐Synuclein Spread from Olfactory Bulb Causes Hyposmia, Anxiety, and Memory Loss in BAC‐ SNCA Mice

Uemura, N., Ueda, J., Yoshihara, T., Ikuno, M., Uemura, M. T., Yamakado, H., Asano, M., Trojanowski, J. Q., & Takahashi, R. (2021) · Movement Disorders · doi:10.1002/mds.28512 · Cited by 61 · see citing works

Spatially-extended nucleation-aggregation-fragmentation models for the dynamics of prion-like neurodegenerative protein-spreading in the brain and its connectome

Fornari, S., Schäfer, A., Ellen Kuhl, A., & Goriely, A. (2019) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2019.110102 · Cited by 57 · see citing works

Neuronal identity defines α-synuclein and tau toxicity

Praschberger, R., Kuenen, S., Schoovaerts, N., Kaempf, N., Singh, J., Janssens, J., Swerts, J., Nachman, E., Calatayud, C., Aerts, S., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.02.033 · Cited by 63 · see citing works

Cognitive heterogeneity in Parkinson’s disease: A mechanistic view

Carceles‐Cordon, M., Weintraub, D., & Chen‐Plotkin, A. S. (2023) · Neuron · doi:10.1016/j.neuron.2023.03.021 · Cited by 58 · see citing works

Pathogenic Mutations Differentially Regulate Cell-to-Cell Transmission of α-Synuclein

Guan, Y., Zhao, X., Liu, F., Yan, S., Wang, Y., Du, C., Cui, X., Li, R., & Zhang, C. X. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00159 · Cited by 54 · see citing works

Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in Disease

Gracia, P., Camino, J. D., Volpicelli‐Daley, L. A., & Cremades, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218043 · Cited by 55 · see citing works

A framework For brain atlases: Lessons from seizure dynamics

Revell, A. Y., Silva, A. B., Arnold, T. C., Stein, J. M., Das, S. R., Shinohara, R. T., Bassett, D. S., Litt, B., & Davis, K. A. (2022) · NeuroImage · doi:10.1016/j.neuroimage.2022.118986 · Cited by 56 · see citing works

Solving brain circuit function and dysfunction with computational modeling and optogenetic fMRI

Lee, J. H., Liu, Q., & Dadgar‐Kiani, E. (2022) · Science · doi:10.1126/science.abq3868 · Cited by 57 · see citing works

Pharmacological inhibition and knockdown of O‐GlcNAcase reduces cellular internalization of α‐synuclein preformed fibrils

Tavassoly, O., Yue, J., & Vocadlo, D. J. (2020) · FEBS Journal · doi:10.1111/febs.15349 · Cited by 52 · see citing works

Functional Connectomics and Disease Progression in Drug‐Naïve Parkinson's Disease Patients

Micco, R. D., Agosta, F., Basaia, S., Siciliano, M., Cividini, C., Tedeschi, G., Filippi, M., & Tessitore, A. (2021) · Movement Disorders · doi:10.1002/mds.28541 · Cited by 53 · see citing works

Linking α-synuclein-induced synaptopathy and neural network dysfunction in early Parkinson’s disease

Kulkarni, A. S., Burns, M. R., Brundin, P., & Wesson, D. W. (2022) · Brain Communications · doi:10.1093/braincomms/fcac165 · Cited by 48 · see citing works

Cerebro-cerebellar motor networks in clinical subtypes of Parkinson’s disease

Basaia, S., Agosta, F., Francia, A., Cividini, C., Balestrino, R., Stojković, T., Stanković, I., Marković, V., Sarasso, E., Gardoni, A., et al. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00377-w · Cited by 50 · see citing works

Hijacking Endocytosis and Autophagy in Extracellular Vesicle Communication: Where the Inside Meets the Outside

Pedrioli, G., & Paganetti, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.595515 · Cited by 48 · see citing works

Disrupting the α-synuclein-ESCRT interaction with a peptide inhibitor mitigates neurodegeneration in preclinical models of Parkinson’s disease

Nim, S., O’Hara, D. M., Corbi‐Verge, C., Perez‐Riba, A., Fujisawa, K., Kapadia, M., Chau, H., Albanese, F., Pawar, G. N., de Snoo, M. L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37464-2 · Cited by 46 · see citing works

Investigation of somatic CNVs in brains of synucleinopathy cases using targeted SNCA analysis and single cell sequencing

Pérez‐Rodríguez, D., Kalyva, M., Leija‐Salazar, M., Lashley, T., Tarabichi, M., Chelban, V., Gentleman, S., Schottlaender, L., Franklin, H., Vasmatzis, G., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0873-5 · Cited by 50 · see citing works

A Summary of Phenotypes Observed in the In Vivo Rodent Alpha-Synuclein Preformed Fibril Model

Polinski, N. K. (2021) · Journal of Parkinson s Disease · doi:10.3233/jpd-212847 · Cited by 46 · see citing works

Characterization of novel conformation-selective α-synuclein antibodies as potential immunotherapeutic agents for Parkinson's disease

Henderson, M. X., Covell, D. J., Chung, C. H.-Y., Pitkin, R. M., Frasier, R. M., Decker, S. C., Riddle, D. M., Zhang, B., Gathagan, R. J., James, M. J., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104712 · Cited by 46 · see citing works

Environmental triggers of Parkinson's disease – Implications of the Braak and dual-hit hypotheses

Chen, H., Wang, K., Scheperjans, F., & Killinger, B. A. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105601 · Cited by 44 · see citing works

Neuronal Oscillations on Evolving Networks: Dynamics, Damage, Degradation, Decline, Dementia, and Death

Goriely, A., Ellen Kuhl, A., & Bick, C. (2020) · Physical Review Letters · doi:10.1103/physrevlett.125.128102 · Cited by 39 · see citing works

Network Diffusion Modeling Explains Longitudinal Tau PET Data

Schäfer, A., Mormino, E. C., & Ellen Kuhl, A. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.566876 · Cited by 41 · see citing works

Efficient coding in the economics of human brain connectomics

Zhou, D., Lynn, C. W., Cui, Z., Ćirić, R., Baum, G. L., Moore, T. M., Roalf, D. R., Detre, J. A., Gur, R. C., Gur, R. E., et al. (2021) · Network Neuroscience · doi:10.1162/netn_a_00223 · Cited by 38 · see citing works

The Evolution-Driven Signature of Parkinson’s Disease

Diederich, N. J., Uchihara, T., Grillner, S. E., & Goetz, C. G. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.05.001 · Cited by 39 · see citing works

Phosphorylation of endogenous α-synuclein induced by extracellular seeds initiates at the pre-synaptic region and spreads to the cell body

Awa, S., Suzuki, G., Masuda‐Suzukake, M., Nonaka, T., Saito, M., & Hasegawa, M. (2022) · Scientific Reports · doi:10.1038/s41598-022-04780-4 · Cited by 39 · see citing works

Alpha-Synuclein Pathophysiology in Neurodegenerative Disorders: A Review Focusing on Molecular Mechanisms and Treatment Advances in Parkinson’s Disease

Yaribash, S., Mohammadi, K., & Sani, M. A. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01544-2 · Cited by 41 · see citing works

α-Synuclein aggregation and transmission in Parkinson’s disease: a link to mitochondria and lysosome

Wang, R., Sun, H., Ren, H., & Wang, G. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1756-9 · Cited by 38 · see citing works

Extracellular alpha-synuclein: Sensors, receptors, and responses

Domingues, R., Sant’Anna, R., da Fonseca, A. C. C., Robbs, B. K., Foguel, D., & Outeiro, T. F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105696 · Cited by 37 · see citing works

Oligonucleotides as therapeutic tools for brain disorders: Focus on major depressive disorder and Parkinson’s disease.

Bortolozzi, A., Manashirov, S., Chen, A., & Artigas, F. (2021) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2021.107873 · Cited by 37 · see citing works

The Neurodegenerative Elderly Syndrome (NES) hypothesis: Alzheimer and Parkinson are two faces of the same disease

Caligiore, D., Giocondo, F., & Silvetti, M. (2022) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2022.09.007 · Cited by 36 · see citing works

Inhibiting the Hexosamine Biosynthetic Pathway Lowers O-GlcNAcylation Levels and Sensitizes Cancer to Environmental Stress

Walter, L. A., Lin, Y., Halbrook, C. J., Chuh, K. N., He, L., Pedowitz, N. J., Batt, A. R., Brennan, C. K., Stiles, B. L., Lyssiotis, C. A., et al. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00560 · Cited by 37 · see citing works

Vesicular Dysfunction and the Pathogenesis of Parkinson’s Disease: Clues From Genetic Studies

Ebanks, K., Lewis, P. A., & Bandopadhyay, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01381 · Cited by 36 · see citing works

The roles of connectivity and neuronal phenotype in determining the pattern of α-synuclein pathology in Parkinson's disease

Henderson, M. X., Henrich, M. T., Geibl, F. F., Oertel, W. H., Brundin, P., & Surmeier, D. J. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105687 · Cited by 35 · see citing works

Polo-like kinase 2 inhibition reduces serine-129 phosphorylation of physiological nuclear alpha-synuclein but not of the aggregated alpha-synuclein

Elfarrash, S., Jensen, N. M., Ferreira, N., Schmidt, S. I., Gregersen, E., Vestergaard, M. V., Nabavi, S., Meyer, M., & Jensen, P. H. (2021) · PLoS ONE · doi:10.1371/journal.pone.0252635 · Cited by 35 · see citing works

Parkinson Disease: Translating Insights from Molecular Mechanisms to Neuroprotection

Pirooznia, S. K., Rosenthal, L. S., Dawson, V. L., & Dawson, T. M. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000189 · Cited by 36 · see citing works

Spatial transcriptomic patterns underlying amyloid-β and tau pathology are associated with cognitive dysfunction in Alzheimer’s disease

Yu, M., Risacher, S. L., Nho, K. T., Wen, Q., Oblak, A. L., Unverzagt, F. W., Apostolova, L. G., Farlow, M. R., Brosch, J. R., Clark, D. G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113691 · Cited by 34 · see citing works

Current insights and assumptions on α-synuclein in Lewy body disease

Leak, R. K., Clark, R. N., Abbas, M., Xu, F., Brodsky, J. L., Chen, J., Hu, X., & Luk, K. C. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02781-3 · Cited by 38 · see citing works

Risk of Transmissibility From Neurodegenerative Disease-Associated Proteins: Experimental Knowns and Unknowns

Asher, D. M., Belay, E. D., Bigio, E. H., Brandner, S., Brubaker, S. A., Caughey, B. W., Clark, B., Damon, I. K., Diamond, M. I., Freund, M. P., et al. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlaa109 · Cited by 34 · see citing works

Synaptic location is a determinant of the detrimental effects of α-synuclein pathology to glutamatergic transmission in the basolateral amygdala

Chen, L., Nagaraja, C., Daniels, S. R., Fisk, Z. A., Dvorak, R., Meyerdirk, L. K., Steiner, J. A., Galvis, M. L. E., Henderson, M. X., Rousseaux, M. W. C., et al. (2022) · eLife · doi:10.7554/elife.78055 · Cited by 34 · see citing works

Mechanisms of Glucocerebrosidase Dysfunction in Parkinson’s Disease

Chatterjee, D., & Krainc, D. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168023 · Cited by 34 · see citing works

Learning interpretable dynamics of stochastic complex systems from experimental data

Gao, T.-T., Barzel, B., & Yan, G. F. (2024) · Nature Communications · doi:10.1038/s41467-024-50378-x · Cited by 32 · see citing works

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases

Sokratian, A., Zhou, Y., Tatli, M., Burbidge, K. J., Xu, E., Viverette, E., Donzelli, S., Duda, A. M., Yuan, Y., Li, H., et al. (2024) · Science Advances · doi:10.1126/sciadv.adq3539 · Cited by 32 · see citing works

Network models to enhance the translational impact of cross-species studies

Brynildsen, J. K., Rajan, K., Henderson, M. X., & Bassett, D. S. (2023) · Nature reviews. Neuroscience · doi:10.1038/s41583-023-00720-x · Cited by 29 · see citing works

Epigenetic inactivation of the autophagy–lysosomal system in appendix in Parkinson’s disease

Gordevičius, J., Li, P., Marshall, L. L., Killinger, B. A., Lang, S., Ensink, E., Kuhn, N. C., Cui, W., Maroof, N., Lauria, R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25474-x · Cited by 32 · see citing works

Role of NLRP3 in Parkinson's disease: Specific activation especially in dopaminergic neurons

Yu, J., Zhao, Z., Li, Y., Chen, J., Huang, N., & Luo, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e28838 · Cited by 30 · see citing works

Inflammation in Experimental Models of α ‐Synucleinopathies

Harms, A. S., Kordower, J. H., Sette, A., Arlehamn, C. S. L., Sulzer, D. L., & Mach, R. H. (2020) · Movement Disorders · doi:10.1002/mds.28264 · Cited by 30 · see citing works

Lewy pathology formation in patient-derived GBA1 Parkinson’s disease midbrain organoids

Frattini, E., Faustini, G., Lopez, G., Carsana, E. V., Tosi, M., Trezzi, I., Magni, M., Soldà, G., Straniero, L., Facchi, D., et al. (2024) · Brain · doi:10.1093/brain/awae365 · Cited by 30 · see citing works

Leveraging the preformed fibril model to distinguish between alpha-synuclein inclusion- and nigrostriatal degeneration-associated immunogenicity

Stoll, A. C., & Sortwell, C. E. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105804 · Cited by 29 · see citing works

Stress-inducible phosphoprotein 1 (HOP/STI1/STIP1) regulates the accumulation and toxicity of α-synuclein in vivo

Lackie, R. E., de Miranda, A. S., Lim, M. P., Novikov, V., Madrer, N., Karunatilleke, N. C., Rutledge, B. S., Tullo, S., Brickenden, A. M., Maitland, M. E. R., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02491-8 · Cited by 29 · see citing works

Physiological and pathological insights into exosomes in the brain

Li, X., 合肥230001，中国, 中., Zhang, J., Li, D., Wu, W., Xie, Z., Liu, Q., 合肥230036，中国, 安., 合肥230026，中国, 中., 合肥230001，中国, 中., et al. (2020) · 动物学研究 · doi:10.24272/j.issn.2095-8137.2020.043 · Cited by 28 · see citing works

Age-related demethylation of the TDP-43 autoregulatory region in the human motor cortex

Koike, Y. M., Sugai, A., Hara, N., Itô, J., Yokoseki, A., Ishihara, T., Yamagishi, T., Tsuboguchi, S., Tada, M., Ikeuchi, T., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02621-0 · Cited by 28 · see citing works

The role of LRRK2 in the periphery: link with Parkinson's disease and inflammatory diseases

Tsafaras, G., & Baekelandt, V. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105806 · Cited by 28 · see citing works

Beyond the usual suspects: multi-factorial computational models in the search for neurodegenerative disease mechanisms

Khan, A. F., & Iturria‐Medina, Y. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03073-w · Cited by 28 · see citing works

Connectivity and vulnerability determine α-synuclein spread

Lemprière, S. A. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0251-8

[Re] Spread of alpha-synuclein pathology through the brain connectome is modulated by selective vulnerability and predicted by network analysis

Paul, T. E., & Bourdenx, M. (2021) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.5379630

The connectome is necessary but not sufficient for the spread of alpha -synuclein pathology in ratsPreprint

Oliveira, M. A. P., Arreckx, S., Monte, D. A. D., Preciat, G., Ulusoy, A., & Fleming, R. M. T. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/567222 · Cited by 3 · see citing works

Key Connectomes and Synaptic‐Compartment‐Specific Risk Genes Drive Pathological α‐Synuclein Spreading

Li, Y., Torok, J., Zhang, S., Ding, J. L., Wang, N., Lau, C., Kulkarni, S., Anand, C., Tran, J., Cheng, M., et al. (2025) · Advanced Science · doi:10.1002/advs.202413052 · Cited by 5 · see citing works

Local vulnerability and global connectivity jointly shape neurodegenerative disease propagation

Zheng, Y., Zhang, Y., Yau, Y. H. C., Zeighami, Y., Larcher, K. M.-H., Mišić, B., & Dagher, A. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000495 · Cited by 116 · see citing works