Spreading of pathology in neurodegenerative diseases: a focus on human studies

Neuropathological stageing of Alzheimer-related changes.

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Staging of brain pathology related to sporadic Parkinson’s disease

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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

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Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

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Novel Proteinaceous Infectious Particles Cause Scrapie

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Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

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Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B

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Phases of Aβ-deposition in the human brain and its relevance for the development of AD

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Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry

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Amyloid aggregates of the deubiquitinase OTUB1 are neurotoxic, suggesting that they contribute to the development of Parkinson's disease

Kumari, R., Kumar, R., Kumar, S., Singh, A. K., Hanpude, P., Jangir, D. K., & Maiti, T. K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009546 · Cited by 36

Transcriptional mutagenesis by 8-oxodG in α-synuclein aggregation and the pathogenesis of Parkinson’s disease

Basu, S., Je, G., & Kim, Y. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2015.54 · Cited by 39

Regulation of protein homeostasis by unconventional protein secretion in mammalian cells

Ye, Y. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.03.006 · Cited by 33

Tissue Clearing and Expansion Methods for Imaging Brain Pathology in Neurodegeneration: From Circuits to Synapses and Beyond

Parra‐Damas, A., & Saura, C. A. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00914 · Cited by 35

Sulfated glycosaminoglycans mediate prion-like behavior of p53 aggregates

Iwahashi, N., Ikezaki, M., Nishikawa, T., Namba, N., Ohgita, T., Saito, H., Ihara, Y., Shimanouchi, T., Ino, K., Uchimura, K., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009931117 · Cited by 37

Synthesis of a Bis-thio-acetone (BTA) Analogue of the Lysine Isopeptide Bond and its Application to Investigate the Effects of Ubiquitination and SUMOylation on α-Synuclein Aggregation and Toxicity

Lewis, Y. E., Abeywardana, T., Lin, Y., Galesic, A., & Pratt, M. R. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b01042 · Cited by 36

The Role of Extracellular Matrix Components in the Spreading of Pathological Protein Aggregates

Moretto, E., Stuart, S., Surana, S., Vargas, J. N. S., & Schiavo, G. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.844211 · Cited by 32

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 36

Phosphorylation at Ser8 as an Intrinsic Regulatory Switch to Regulate the Morphologies and Structures of Alzheimer's 40-residue β-Amyloid (Aβ40) Fibrils

Hu, Z., Ma, M.-R., Chen, Y., Zhao, Y., Qiang, W., & Li, Y. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.757179 · Cited by 34

Delivery systems for theranostics in neurodegenerative diseases

Li, Y., Liu, R., Ji, W., Li, Y., Liu, L., & Zhang, X. (2018) · Nano Research · doi:10.1007/s12274-018-2067-z · Cited by 35

PM 2.5 Associated With Gray Matter Atrophy Reflecting Increased Alzheimer Risk in Older Women

Younan, D., Wang, X., Casanova, R., Barnard, R., Gaussoin, S. A., Saldana, S. J., Petkus, A. J., Beavers, D. P., Resnick, S. M., Manson, J. E., et al. (2020) · Neurology · doi:10.1212/wnl.0000000000011149 · Cited by 37

Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains

Alijanvand, S. H., Peduzzo, A., & Buell, A. K. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.669994 · Cited by 35

Role of microRNAs As Biomarkers in Sepsis-Associated Encephalopathy

Osca-Verdegal, R., Beltrán-García, J., Pallardó, F. V., & García‐Giménez, J. L. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02445-3 · Cited by 34

Corticoefferent pathology distribution in amyotrophic lateral sclerosis: in vivo evidence from a meta-analysis of diffusion tensor imaging data

Gorges, M., Tredici, K. D., Dreyhaupt, J., Braak, H., Ludolph, A. C., Müller, H., & Kassubek, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-33830-z · Cited by 35

Effects of microbiome-based interventions on neurodegenerative diseases: a systematic review and meta-analysis

Chui, Z. S. W., Chan, L. M. L., Zhang, E. W. H., Liang, S., Choi, E. P. H., Lok, K. Y. W., Tun, H. M., & Kwok, J. Y. Y. (2024) · Scientific Reports · doi:10.1038/s41598-024-59250-w · Cited by 45

Spinal cord injury and Alzheimer’s disease risk: a population-based, retrospective cohort study

Yeh, T., Ho, Y., Hsu, C., & Pan, S. (2017) · Spinal Cord · doi:10.1038/s41393-017-0009-3 · Cited by 33

Disentangling the Amyloid Pathways: A Mechanistic Approach to Etiology

Malmberg, M., Malm, T., Gustafsson, O., Sturchio, A., Graff, C., Espay, A. J., Wright, A. P. H., Andaloussi, S. E., Lindén, A., & Ezzat, K. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00256 · Cited by 30

Antagonistic roles for Ataxin-2 structured and disordered domains in RNP condensation

Singh, A., Huelsmeier, J., Kandi, A. R., Pothapragada, S. S., Hillebrand, J., Petrauskas, A., Agrawal, K., Krishnan, R., Thiagarajan, D., Jayaprakashappa, D., et al. (2021) · eLife · doi:10.7554/elife.60326 · Cited by 32

Pharmacological inhibition of nSMase2 reduces brain exosome release and α-synuclein pathology in a Parkinson’s disease model

Zhu, C., Bilousova, T. V., Focht, S., Jun, M., Elias, C. J., Melnik, M., Chandra, S., Campagna, J. J., Cohn, W., Hatami, A., et al. (2021) · Molecular Brain · doi:10.1186/s13041-021-00776-9 · Cited by 39

Extracellular Vesicles as Innovative Treatment Strategy for Amyotrophic Lateral Sclerosis

Wang, K., Yu, L., Ren, C., Wang, Y., He, W., & Jiang, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.754630 · Cited by 34

Extra-motor abnormalities in amyotrophic lateral sclerosis: another layer of heterogeneity

McCombe, P., Wray, N. R., & Henderson, R. D. (2016) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2017.1273772 · Cited by 35

Visual hallucinations in Parkinson’s disease: spotlight on central cholinergic dysfunction

Ignatavicius, A., Matar, E., & Lewis, S. J. G. (2025) · Brain · doi:10.1093/brain/awae289 · Cited by 32

Longitudinal Diffusion Tensor Imaging-Based Assessment of Tract Alterations: An Application to Amyotrophic Lateral Sclerosis

Baldaranov, D., Khomenko, A., Kobor, I., Bogdahn, U., Gorges, M., Kassubek, J., & Müller, H. (2017) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2017.00567 · Cited by 33

Secretion of misfolded cytosolic proteins from mammalian cells is independent of chaperone-mediated autophagy

Lee, J., Xu, Y., Zhang, T., Cui, L., Saidi, L. F., & Ye, Y. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003660 · Cited by 35

Role of Polyphenols on Gut Microbiota and the Ubiquitin-Proteasome System in Neurodegenerative Diseases

Nargeh, H., Aliabadi, F., Ajami, M., & Pazoki–Toroudi, H. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c00923 · Cited by 32

Atomic force microscopy as an advanced tool in neuroscience

Jembrek, M. J., Šimić, G., Hof, P. R., & Šegota, S. (2015) · Translational Neuroscience · doi:10.1515/tnsci-2015-0011 · Cited by 33

GABA and glutamate moderate beta-amyloid related functional connectivity in cognitively unimpaired old-aged adults

Quevenco, F. C., Schreiner, S. J., Preti, M. G., Bergen, J. M. G. V., Kirchner, T., Wyss, M. T., Steininger, S. C., Gietl, A. F., Leh, S. E., Buck, A., et al. (2019) · NeuroImage Clinical · doi:10.1016/j.nicl.2019.101776 · Cited by 31

Progress and challenges in the diagnosis of dementia: a critical review

Paraskevaidi, M., Martin-Hirsch, P. L., & Martin, F. L. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00007 · Cited by 31

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 32

Amyotrophic lateral sclerosis — a multisystem neurodegenerative disorder

Grossman, M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0103-y · Cited by 31

Advanced neuroimaging approaches in amyotrophic lateral sclerosis: refining the clinical diagnosis

Kassubek, J., & Müller, H. (2020) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2020.1715798 · Cited by 31

Serine phosphorylation and arginine methylation at the crossroads to neurodegeneration

Basso, M., & Pennuto, M. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.003 · Cited by 31

Brain network mapping and glioma pathophysiology

Mandal, A. S., Brem, S. S., & Suckling, J. (2023) · Brain Communications · doi:10.1093/braincomms/fcad040 · Cited by 33

The underlying mechanism of prodromal PD: insights from the parasympathetic nervous system and the olfactory system

Liu, S., Chan, P., & Stoessl, A. J. (2017) · Translational Neurodegeneration · doi:10.1186/s40035-017-0074-8 · Cited by 32

Rhodamine-Based Metal Chelator: A Potent Inhibitor of Metal-Catalyzed Amyloid Toxicity

Pradhan, K., Das, G., Kar, C., Mukherjee, N., Khan, J., Mahata, T., Barman, S., & Ghosh, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c02235 · Cited by 30

Making biological membrane resistant to the toxicity of misfolded protein oligomers: a lesson from trodusquemine.

Errico, S., Lucchesi, G., Odino, D., Muscat, S., Capitini, C., Bugelli, C., Canale, C., Ferrando, R., Grasso, G., Barbut, D., et al. (2020) · Nanoscale · doi:10.1039/d0nr05285j · Cited by 24

Neuroprotective effects of glucomoringin-isothiocyanate against H2O2-Induced cytotoxicity in neuroblastoma (SH-SY5Y) cells

Mohammed, J. S., Nordin, N., Rosli, R., Shaari, K., Bako, H. Y., Saad, N., Noor, N. M., & Razis, A. F. A. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.09.008 · Cited by 33

Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo

Riemenschneider, H., Simonetti, F., Sheth, U., Katona, E., Roth, S., Hutten, S., Farny, D., Michaelsen, M., Nuscher, B., Schmidt, M. K., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01592-z · Cited by 31

Conformational Analysis of Misfolded Protein Aggregation by FRET and Live-Cell Imaging Techniques

Kitamura, A., Nagata, K., & Kinjo, M. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16036076 · Cited by 28

Microbial dysbiosis and microbiota–gut–retina axis: The lesson from brain neurodegenerative diseases to primary open-angle glaucoma pathogenesis of autoimmunity

Chaiwiang, N., & Poyomtip, T. (2019) · Acta Microbiologica et Immunologica Hungarica · doi:10.1556/030.66.2019.038 · Cited by 29

The interplay between aging‐associated loss of protein homeostasis and extracellular vesicles in neurodegeneration

Guix, F. X. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24526 · Cited by 30

Engineering NIR-II luminescent lanthanide nanoprobes for imaging brain diseases in vivo

Du, Y., Ni, S., Ma, Q., Song, X., & Yang, H. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215401 · Cited by 29

Comparison of Amyloid β and Tau Spread Models in Alzheimer’s Disease

Kim, H., Lee, P., Seo, S. W., Roh, J. H., Oh, M., Oh, J. S., Oh, S. J., Kim, J. S., & Jeong, Y. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhy311 · Cited by 32

Identifying the Pathological Domain of Alpha- Synuclein as a Therapeutic for Parkinson’s Disease

Shen, N., Song, G., Yang, H., Lin, X., Brown, B., Hong, Y., Cai, J., & Cao, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092338 · Cited by 28

Formation of toxic oligomers of polyQ-expanded Huntingtin by prion-mediated cross-seeding

Gropp, M., Klaips, C. L., & Hartl, F. U. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.031 · Cited by 28

The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis

Hanspal, M. A., Dobson, C. M., Yerbury, J. J., & Kumita, J. R. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.07.007 · Cited by 30

HERBAL MEDICINES AS NEUROPROTECTIVE AGENT: A MECHANISTIC APPROACH

Roy, S., & Awasthi, H. (2017) · International Journal of Pharmacy and Pharmaceutical Sciences · doi:10.22159/ijpps.2017v9i11.19444 · Cited by 28

α-Methyl-α-phenylsuccinimide ameliorates neurodegeneration in a C. elegans model of TDP-43 proteinopathy

Wong, S. Q., Pontifex, M. G., Phelan, M. M., Pidathala, C., Kraemer, B. C., Barclay, J. W., Berry, N. G., O’Neill, P. M., Burgoyne, R. D., & Morgan, A. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.06.013 · Cited by 28

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 31

FTIR imaging of the molecular burden around Aβ deposits in an early-stage 3-Tg-APP-PSP1-TAU mouse model of Alzheimer's disease

Surówka, A. D., Pilling, M. J., Henderson, A., Boutin, H., Christie, L., Szczerbowska‐Boruchowska, M., & Gardner, P. (2016) · The Analyst · doi:10.1039/c6an01797e · Cited by 26

In vivo localization of human acetylcholinesterase-derived species in a β-sheet conformation at the core of senile plaques in Alzheimer's disease

Jean, L., Brimijoin, S., & Vaux, D. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006230 · Cited by 27

Effect of atorvastatin on Aβ1–42-induced alteration of SESN2, SIRT1, LC3II and TPP1 protein expressions in neuronal cell cultures

Çelik, H., Karahan, H., & Kelicen‐Uğur, P. (2019) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13208 · Cited by 28

The pROS of Autophagy in Neuronal Health

Sedlackova, L., Kelly, G., & Korolchuk, V. I. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.020 · Cited by 28

Manipulated Mesenchymal Stem Cells Applications in Neurodegenerative Diseases

Sadatpoor, S. O., Salehi, Z., Rahban, D., & Salimi, A. (2020) · International Journal of Stem Cells · doi:10.15283/ijsc19031 · Cited by 29

Altered limbic functional connectivity in individuals with subjective cognitive decline: Converging and diverging findings across Chinese and German cohorts

Jiang, X., Hu, X., Daamen, M., Wang, X., Fan, C., Meiberth, D. U., Spottke, A. E., Roeske, S., Fließbach, K., Spruth, E. J., et al. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.13068 · Cited by 27

Molecular Mechanisms of Transdifferentiation of Adipose-Derived Stem Cells into Neural Cells: Current Status and Perspectives

Luo, L., Hu, D., Yin, J. Q., & Xu, R.-X. (2018) · Stem Cells International · doi:10.1155/2018/5630802 · Cited by 27

A short perspective on the long road to effective treatments for Alzheimer's disease

Reynolds, D. S. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14581 · Cited by 28

In vitro and in vivo evaluation of the neuroprotective activity of Uncaria hirsuta Haviland

Lin, C., Lin, Y.-T., Lee, T.-L., Imtiyaz, Z., Hou, W., & Lee, M. (2019) · Journal of Food and Drug Analysis · doi:10.1016/j.jfda.2019.10.004 · Cited by 27

Oligomeric amyloid-β induces early and widespread changes to the proteome in human iPSC-derived neurons

Sackmann, C., & Hallbeck, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-63398-6 · Cited by 27

Exercise, Neuroprotective Exerkines, and Parkinson’s Disease: A Narrative Review

Mitchell, A. K., Bliss, R. R., & Church, F. (2024) · Biomolecules · doi:10.3390/biom14101241 · Cited by 33

Long-Term Effects of Sports Concussions: Bridging the Neurocognitive Repercussions of the Injury with the Newest Neuroimaging Data

Henry, L. C., Tremblay, S., & Beaumont, L. D. (2016) · The Neuroscientist · doi:10.1177/1073858416651034 · Cited by 26

Studying tau protein propagation and pathology in the mouse brain using adeno-associated viruses

Wegmann, S., Bennett, R. E., Amaral, A. C. S., & Hyman, B. T. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.014 · Cited by 29

Poly (ADP-ribose) Interacts With Phosphorylated α-Synuclein in Post Mortem PD Samples

Puentes, L. N., Lengyel‐Zhand, Z., Lee, J. Y., Hsieh, C., Schneider, M. E., Edwards, K. J., Luk, K. C., Lee, V. M. ‐., Trojanowski, J. Q., & Mach, R. H. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.704041 · Cited by 30

Rat Models of Vocal Deficits in Parkinson’s Disease

Krasko, M. N., Hoffmeister, J. D., Schaen‐Heacock, N. E., Welsch, J. M., Kelm‐Nelson, C. A., & Ciucci, M. R. (2021) · Brain Sciences · doi:10.3390/brainsci11070925 · Cited by 26

P62 accumulates through neuroanatomical circuits in response to tauopathy propagation

de Thé, F.-X. B., Lassus, B., Schaler, A. W., Fowler, S. L., Goulbourne, C. N., Jeggo, R., la Cour, C. M., Millan, M. J., & Duff, K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01280-w · Cited by 28

Modulation of Amyloid Aggregates into Nontoxic Coaggregates by Hydroxyquinoline Appended Polyfluorene

Chowdhury, S. R., Agarwal, M., Meher, N., Balakrishnan, M., & Iyer, P. K. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b03668 · Cited by 26

Amyloid single-cell cytotoxicity assays by nanomotion detection

Ruggeri, F. S., Mahul‐Mellier, A., Kasas, S., Lashuel, H. A., Longo, G., & Dietler, G. (2017) · Cell Death Discovery · doi:10.1038/cddiscovery.2017.53 · Cited by 26

Evidence for sortilin modulating regional accumulation of human tau prions in transgenic mice

Johnson, N. R., Condello, C., Guan, S., Oehler, A., Becker, J., Gavidia, M., Carlson, G. A., Giles, K., & Prusiner, S. B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717193114 · Cited by 25

Lack of pathogenic potential of peripheral α-synuclein aggregates from Parkinson’s disease patients

Recasens, A., Carballo‐Carbajal, I., Parent, A., Bové, J., Gelpí, E., TOLOSA, E. S., & Vila, M. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0509-1 · Cited by 27

PIKfyve inhibition blocks endolysosomal escape of α-synuclein fibrils and spread of α-synuclein aggregationPreprint

See, S. K., Chen, M., Bax, S., Tian, R., Woerman, A. L., Tse, E., Johnson, I. E., Nowotny, C., Muñoz, E. N., Sengstack, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.21.427704 · Cited by 24

Microbial amyloids in neurodegenerative amyloid diseases

Sampson, T. R. (2023) · FEBS Journal · doi:10.1111/febs.17023 · Cited by 25

Exploring Protein Misfolding and Aggregate Pathology in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Interventions

Johnson, J. T., Fila, W. A., & Anumudu, C. K. (2025) · Applied Sciences · doi:10.3390/app151810285 · Cited by 29

Systemic AAV6-synapsin-GFP administration results in lower liver biodistribution, compared to AAV1&2 and AAV9, with neuronal expression following ultrasound-mediated brain delivery

Weber‐Adrian, D., Kofoed, R. H., Silburt, J., Noroozian, Z., Shah, K., Burgess, A., Rideout, S., Kügler, S., Hynynen, K., & Aubert, I. (2021) · Scientific Reports · doi:10.1038/s41598-021-81046-5 · Cited by 27

Early loss of cerebellar Purkinje cells in human and a transgenic mouse model of Alzheimer’s disease

Chaudhari, K., Wang, L., Kruse, J. J., Winters, A., Sumien, N., Shetty, R. A., Prah, J., Liu, R., Shi, J., Forster, M. J., et al. (2021) · Neurological Research · doi:10.1080/01616412.2021.1893566 · Cited by 24

Neuroprotective Effects and Mechanisms of Procyanidins In Vitro and In Vivo

Chen, J., Chen, Y., Zheng, Y., Zhao, J., Yu, H., Zhu, J., & Li, D. (2021) · Molecules · doi:10.3390/molecules26102963 · Cited by 25

Effects of Alpha-Synuclein Targeted Antisense Oligonucleotides on Lewy Body-Like Pathology and Behavioral Disturbances Induced by Injections of Pre-Formed Fibrils in the Mouse Motor Cortex

Boutros, S. W., Raber, J., & Unni, V. K. (2021) · Journal of Parkinson s Disease · doi:10.3233/jpd-212566 · Cited by 28

Intermittent Fasting on Neurologic Diseases: Potential Role of Gut Microbiota

Guo, M., Wang, X., Li, Y., Luo, A., Zhao, Y., Luo, X., & Li, S. (2023) · Nutrients · doi:10.3390/nu15234915 · Cited by 25

Structural connectivity centrality changes mark the path toward Alzheimer's disease

Peraza, L. R., Díaz‐Parra, A., Kennion, O., Moratal, D., Taylor, J., Kaiser, M., Bauer, R., & Initiative, A. D. N. (2019) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2018.12.004 · Cited by 24

A manifesto for Alzheimer’s disease drug discovery in the era of disease-modifying therapies

Hering, H., Bussière, T., Liu, C., Glajch, K. E., Weihofen, A., Grogan, J. L., & Walsh, D. M. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00872-7 · Cited by 28

Distinct white matter injury associated with medial temporal lobe atrophy in Alzheimer's versus semantic dementia

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Design, Synthesis, and Neuroprotective Effects of a Series of Pyrazolines against 6-Hydroxydopamine-Induced Oxidative Stress

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