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

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

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

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359

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

Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,221

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

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

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

Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496

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

Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490

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

Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172

Identification of Low Allele Frequency Mosaic Mutations in Alzheimer Disease

Frigerio, C. S., Fiers, M. W. E. J., Voet, T., & Strooper, B. D. (2017) · Neuromethods · doi:10.1007/978-1-4939-7280-7_17 · Cited by 4

Synaptic and metabolic gene expression alterations in neurons that are recipients of proteopathic tau seeds

Pérez-Rando, M., Dujardin, S., Bennett, R. E., Commins, C., Nibhanupudy, T. J., & Hyman, B. T. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01049-7 · Cited by 4

Therapeutic Potential of Polyphenols in Alzheimer’s Therapy: Broad-Spectrum and Minimal Side Effects as Key Aspects

Shamsi, A., Anwar, S., Mohammad, T., Shahwan, M. J., Hassan, M. I., & Islam, A. (2021) · Springer eBooks · doi:10.1007/978-981-16-4558-7_7 · Cited by 4

Integrated multimodal imaging in neurodegenerative disease

Grossman, M. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)00182-9 · Cited by 4

Genetic risk factors of Alzheimer's disease and cell-to-cell transmission of Tau

Huttunen, H. J. (2016) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2016/2.1022 · Cited by 4

Poly (ADP-ribose) induces α-synuclein aggregation in neuronal-like cells and interacts with phosphorylated α-synuclein in post mortem PD samplesPreprint

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. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.08.032250 · Cited by 4

Synapse loss in the prefrontal cortex is associated with cognitive decline in amyotrophic lateral sclerosis

Henstridge, C. M., & Spires‐Jones, T. L. (2018) · doi:10.26226/morressier.5b31ec442afeeb001345a7e4 · Cited by 4

Human and Mouse Alzheimer's Seeds Differentially Affect Amyloid Deposition and Microglia‐Dependent Plaque Response in Aged Mice

Andreo‐Lopez, J., Nuñez‐Diaz, C., Huynh, K. D., Nguyen, M. M. T., Cunha, C. D., Cantero‐Molina, F., Campos‐Moreno, C., Zimbone, S., Bellia, F., Giuffrida, M. L., et al. (2025) · Aging Cell · doi:10.1111/acel.70094 · Cited by 3

Effects of low-dose radiation on neurological diseases

Dong, M.-X., Wang, H., & Liu, Q. (2025) · Journal of Aging and Rehabilitation · doi:10.1097/jagr.0000000000000029 · Cited by 3

Retrotransposons unplugged: Rewiring the nervous system and wreaking havoc

Whiteley, A. M., & Shepherd, J. D. (2025) · Neuron · doi:10.1016/j.neuron.2025.09.034 · Cited by 4

DDT exposure induces microglial activation and disease-associated microglial signatures: Relevance to mechanisms of Alzheimer’s disease

Mhatre‐Winters, I., Eid, A., Blum, N., Han, Y., Sammoura, F. M., Wu, L., & Richardson, J. (2025) · NeuroToxicology · doi:10.1016/j.neuro.2025.103343 · Cited by 4

Bioavailability as Proof to Authorize the Clinical Testing of Neurodegenerative Drugs—Protocols and Advice for the FDA to Meet the ALS Act Vision

Niazi, S. K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810211 · Cited by 3

NDDRF 2.0: An update and expansion of risk factor knowledge base for personalized prevention of neurodegenerative diseases

Bi, C., Zheng, X. H., Zhang, Y., Zhou, S., Song, J., Shang, H., & Shen, B. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70282 · Cited by 2

Predicting Parkinson’s disease and its progression based on radiomics in T1-weight images and α‑synuclein in cerebrospinal fluid

Zhang, X., Li, H., Xia, X., Wu, J., Shi, F., Zhao, C., Meng, X., & Ren, Q. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-01097-7 · Cited by 3

Schefflera arboricola Tablets Relieve Diabetic Neuropathic Pain: Involvement of Oxidative Stress and Inflammation

Lin, S., Shen, Y., Huang, X., Lin, S., & Shi, X. (2023) · Pharmacognosy Magazine · doi:10.1177/09731296231193801 · Cited by 3

Investigation of Potential Neuroprotective Role of Chitosan-Based Biomaterials and Their Derivatives by Targeting Glial Cells

Hamdan, Y. A., Rhazi, M., Kabdy, H., Benmaloui, A., Elouali, S., Laadraoui, J., Ahmad, Z. H., Eladlani, N., & Oudadesse, H. (2023) · Advances in bioinformatics and biomedical engineering book series · doi:10.4018/978-1-6684-9675-6.ch019 · Cited by 3

Combining data integration and molecular dynamics for target identification in α-Synuclein-aggregating neurodegenerative diseases: Structural insights on Synaptojanin-1 (Synj1)

Jenkins, K., Mateeva, T., Szabó, I., Melnik, A., Picotti, P., Csikász‐Nagy, A., & Rosta, E. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.04.010 · Cited by 3

Recent Developments in Treating Alzheimer’s Disease

Žerovnik, E., & Kopitar‐Jerala, N. (2016) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000220 · Cited by 3

Neuropathology correlates of cognitive assessments

Brett, F. M., & KEARNEY, H. F. (2018) · Irish Journal of Medical Science (1971 -) · doi:10.1007/s11845-017-1733-6 · Cited by 3

Smaller hippocampal volume in APOE ε4 carriers independent of amyloid-β (Aβ) burden

Suh, H., Lee, Y., Park, J., Lee, B. D., Moon, E., Jeong, H. J., Kim, S. Y., Lee, K. Y., Kim, H., Pak, K., et al. (2021) · Psychiatry Research Neuroimaging · doi:10.1016/j.pscychresns.2021.111381 · Cited by 3

3‐O‐Sulfation of Heparan Sulfate Enhances Tau Interaction and Cellular Uptake

Zhao, J., Zhu, Y., Song, X., Xiao, Y., Su, G., Liu, X., Wang, Z., Xu, Y., Liu, J., Eliezer, D., et al. (2019) · Angewandte Chemie · doi:10.1002/ange.201913029 · Cited by 3

How does “Protein Corona” Affect the In vivo Efficiency of Polymeric Nanoparticles? State of Art

(2017) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781681084930117020011 · Cited by 4

Exosome nanocarriers

Bhatti, J. S., Vijayvergiya, R., Singh, B., & Bhatti, G. K. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816200-2.00008-6 · Cited by 3

Recent Advances in Longitudinal Structural Neuroimaging of younger-onset Dementias

Landín-Romero, R., & Piguet, O. (2017) · Neurodegenerative Disease Management · doi:10.2217/nmt-2017-0057 · Cited by 3

Pathogenesis of Polyglutamine Diseases

Sahashi, K., & Katsuno, M. (2018) · Wiley eBooks · doi:10.1002/9780470015902.a0021486.pub2 · Cited by 3

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

Endogenous Retroviruses and TDP-43 Proteinopathy Form a Sustaining Feedback to Drive the Intercellular Spread of NeurodegenerationPreprint

Chang, Y., & Dubnau, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.20.500816 · Cited by 3

A Novel C. elegans Model for Tau Spreading Reveals Genes Critical for Endolysosomal Integrity and Seeded Tau AggregationPreprint

Sandhof, C. A., Martin, N., Tittelmeier, J., Schlüter, A., Pezzali, M., Schöndorf, D. C., Lange, T., Reinhardt, P., Ried, J. S., Liang, S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.13.619586 · Cited by 3

Novel subcellular regulatory mechanisms of protein homeostasis and its implications in amyotrophic lateral sclerosis

Zhan, A., Zhong, K., & Zhang, K. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151582 · Cited by 2

Comprehensive account of exosome isolation from rat substantia nigra for mass spectrometry-based proteomics study

Ghosh, S., Ghosh, S., Jana, A., Roy, R., & Ghosh, S. (2025) · Methods · doi:10.1016/j.ymeth.2025.06.002 · Cited by 2

Cerebellar contributions to tau-mediated cognitive and behavioral dysfunction

Angeles-Perez, L., Ren, C., Neniel, J., Widner, J., Yamashiro, K., Tak, Y., Batra, S., Tan, T., Nguyen, B., Diamond, M. I., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116036 · Cited by 2

Unraveling the Mystery of Hemoglobin in Hypoxia-Accelerated Neurodegenerative Diseases

Tian, Z., Jin, F., Geng, Z., Xu, Z., Shao, Q., Liu, G., Ji, X., & Liu, J. (2025) · Biomolecules · doi:10.3390/biom15091221 · Cited by 2

Structural basis for T-cell intracellular antigen-1 amyloid fibril formation revealed by cryo-electron microscopy

Inaoka, D., Miyata, T., Makino, F., Ohtani, Y., Ekari, M., Kobayashi, R., Imamura, K., Sakamoto, E., Kodama, T. S., Yoshida, N., et al. (2025) · PNAS Nexus · doi:10.1093/pnasnexus/pgaf388 · Cited by 2

Microengineering of the capillary interface of midbrain dopaminergic neurons to study Parkinson’s disease vascular alterations

Alim, A., Baek, Y., Lee, M., & Paek, J. (2026) · Communications Engineering · doi:10.1038/s44172-025-00581-5 · Cited by 4

Evaluation of CSF and plasma tau species as fluid surrogate candidates for tau PET in prodromal to moderate Alzheimer's disease

Lee, J., Olafson, E., Toth, B., Casavant, E., Schauer, S. P., Bittner, T., Meyer, M. R., Verghese, P. B., Venkatesh, V., West, T., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71604 · Cited by 3

An indicator cell assay for blood-based diagnostics

Danziger, S. A., Miller, L. R., Singh, K., Whitney, G. A., Peskind, E. R., Li, G., Lipshutz, R. J., Aitchison, J. D., & Smith, J. J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178608 · Cited by 2

The neural economics of brain aging

Kosyakovsky, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-91621-5 · Cited by 3

Parkinsons Disease-Like Neuropathology and Phenotype Following Induction of Oxidative Stress and Inflammation in the Brain

Ehsanifar, M., & Montazeri, Z. (2022) · Journal of Biomedical Research & Environmental Sciences · doi:10.37871/jbres1408 · Cited by 2

Doenças neurodegenerativas e canabinoides: revisão narrativa

Lopes, C. M., de Camargo, R. W., & de Bitencourt, R. M. (2023) · Revista Neurociências · doi:10.34024/rnc.2023.v31.14952 · Cited by 3

Structural and functional covariance architecture of major depressive disorder: A meta-analytic structural equation modeling approach to primary neuroimaging analysis

Gray, J. P., Price, L. R., Franklin, C. G., Leonardo, C. D., Chiang, F. L., Choi, K. S., Blangero, J., Glahn, D. C., Mayberg, H. S., & Fox, P. T. (2025) · Brain Organoid and Systems Neuroscience Journal · doi:10.1016/j.bosn.2025.04.008 · Cited by 2

Detergent-induced aggregation of an amyloidogenic intrinsically disordered protein

Arya, S., Dogra, P., Jain, N., & Mukhopadhyay, S. (2017) · Journal of Chemical Sciences · doi:10.1007/s12039-017-1386-z · Cited by 2

The molecular basis of interaction domains of full-length PrP with lipid membranes

Pan, Y., Wang, B., Reese, R. A., & Xu, B. (2019) · Nanoscale · doi:10.1039/c9nr02735a · Cited by 2

Prions et transconformation protéique: une perspective historique

Hauw, J., Haı̈k, S., & Brandel, J. (2015) · Bulletin de l Académie Nationale de Médecine · doi:10.1016/s0001-4079(19)30881-7 · Cited by 2

Basal Ganglia

ten Donkelaar, H. J., van de Warrenburg, B. P. C., Willemsen, M. A. A. P., Küsters, B., Hashizume, Y., & Hori, A. (2020) · Springer eBooks · doi:10.1007/978-3-030-41878-6_11 · Cited by 2

Hunting cellular mechanisms underlying the spreading of misfolded protein pathology in the brain

Pecho‐Vrieseling, E. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12264 · Cited by 2

Mammalian prion amyloid formation in bacteria

Macedo, B., Cordeiro, Y., & Ventura, S. (2016) · Prion · doi:10.1080/19336896.2016.1141859 · Cited by 2

Salience network atrophy links neuron type-specific pathobiology to loss of empathy in frontotemporal dementiaPreprint

Pasquini, L., Nana, A. L., Toller, G., Brown, J., Deng, J., Staffaroni, A., Kim, E.-J., Hwang, J.-H. L., Li, L., Park, Y., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/691212 · Cited by 2

GPCR-mediated clearance of tau in post-synaptic compartments attenuates tau pathology in vivoPreprint

Schaler, A. W., Runyan, A. M., Fowler, S. L., Figueroa, H. Y., Shioda, S., Santa‐María, I., Duff, K., & Myeku, N. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.21.914135 · Cited by 2

Calibration of Biophysical Models for tau-Protein Spreading in Alzheimer's Disease from PET-MRIPreprint

Scheufele, K., Subramanian, S., & Biros, G. (2020) · arXiv (Cornell University) · doi:10.48550/arxiv.2007.01236 · Cited by 5

VCP Protects Neurons from Proteopathic SeedingPreprint

Zhu, J., Pittman, S. K., Dhavale, D. D., French, R. L., Patterson, J. N., Kaleelurrrahuman, M. S., Sun, Y., Buscher, W. J., Bieschke, J., Kotzbauer, P. T., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.12.452081 · Cited by 2

LRP1 Regulates the Uptake and Propagation of α-SynucleinPreprint

Peng, C., Luo, H., Liu, J., Li, Q., Liu, C., & Chen, M. (2022) · Research Square · doi:10.21203/rs.3.rs-1411309/v1 · Cited by 2

The Potential of Low Molecular Weight (Poly)phenol Metabolites for Attenuating Neuroinflammation and Treatment of Neurodegenerative Diseases

Marques, D., Carecho, R., Carregosa, D., & dos Santos, C. N. (2023) · Wiley eBooks · doi:10.1002/9781119844792.ch4 · Cited by 2

Transcript errors generate a continuous stream of amyloid and prion-like proteins in human cellsPreprint

Chung, C. S., Kou, Y., Shemtov, S. J., Verheijen, B. M., Flores, I., Love, K., Dosso, A. D., Thorwald, M. A., Liu, Y., Toney, R. G., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.11.540433 · Cited by 2

Structures of AT8 and PHF1 Phospho-Mimetic Tau: Insights Into the Posttranslational Modification Code of Tau Amyloid FormationPreprint

Mammeri, N. E., Dregni, A. J., Duan, P., & Hong, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.04.556256 · Cited by 2

Why do we need new therapies for neurodegenerative disorders?

Azimi, M., & Atiq, M. A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15702-8.00033-6 · Cited by 1

Baicalein benefits amyotrophic lateral sclerosis via reduction of Intraneuronal misfolded protein

Ting, C.-H., Tai, S.-T., Chang, H., Huang, P.-Y., Cheng, L.-F., Lai, H., Kuo, Y.-C. J., Kao, C.-H., Wang, I., & Tsai, L. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130831 · Cited by 2

Neuroprotective Effects of Phosphodiesterase Inhibitors on Sestrin-2 (SESN2) Expression and Autophagy in Alzheimer’s Disease Model

Faikoğlu, G., Saygisever-Faikoglu, K., Özbaşak, H., Ugur, S. A., Uskur, T., Akkan, A. G., Kelicen‐Uğur, P., & Özyazgan, S. (2025) · Cureus · doi:10.7759/cureus.88449 · Cited by 1

Co‐localization of tau and TDP ‐43 after extracellular vesicle delivery to cells

Aliakbari, F., Volkening, K., Nayeri, Z., Polat, A. Y., Donison, N. S., Palik, J., & Strong, M. J. (2025) · FEBS Journal · doi:10.1111/febs.70336 · Cited by 2

Combined neocortical protein and morphological profiling of reactive microglia across Alzheimer’s and Creutzfeldt–Jakob disease

Tkach, V. V., Bager, N. S., Michaelsen, S. R., Litman, T., Josefsen, K. E., Kristensen, B. W., Lund, E. L., & Areškevičiūtė, A. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02163-0 · Cited by 1

Ubiquitin signatures on aggregating proteins in neurodegeneration

Sahoo, S., Padhy, A. A., Shivani, K., Misra, A., & Mishra, P. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253046 · Cited by 1

Cell-type-specific APOE4 cascade across the Alzheimer’s disease continuum

Shostak, D. M., Liang, Z., & Huang, Y. (2026) · Neuron · doi:10.1016/j.neuron.2026.04.024 · Cited by 1

Prion-like Protein TDP-43: Mechanisms, Diagnosis, and Therapeutic Prospects

Shimamura, M. I., & Satoh, K. (2026) · Pathogens · doi:10.3390/pathogens15090890 · Cited by 1

The preclinical stage of movement disorders

Eberhardt, O., & Topka, H. R. (2015) · Basal Ganglia · doi:10.1016/j.baga.2015.11.002 · Cited by 1

The Malignant Protein Puzzle.

Walker, L. C., & Jucker, M. (2016) · PubMed Central · Cited by 1

Clinical Stabilization in Parkinson´s Disease: The Multi-Target Treatment Description and Results

Nakanishi, T., & Tamai, I. (2019) · doi:10.17303/jnnd.2016.3.102 · Cited by 1

Progress toward the development of treatment of spinal and bulbar muscular atrophy

Sahashi, K., Hashizume, A., Sobue, G., & Katsuno, M. (2017) · Expert Opinion on Orphan Drugs · doi:10.1080/21678707.2017.1329088 · Cited by 1

Genetic Factors Influencing the Development and Treatment of Cognitive Impairment and Psychosis in Parkinson’s Disease

Perez‐Lloret, S., Bernath, V., & Barrantes, F. J. (2018) · Springer eBooks · doi:10.1007/978-3-319-95360-1_29 · Cited by 1

The Use of Co-immunoprecipitation to Study Conformation-Specific Protein Interactions of Oligomeric α-Synuclein Aggregates

Betzer, C., Kofoed, R. H., & Jensen, P. H. (2018) · Neuromethods · doi:10.1007/978-1-4939-8985-0_3 · Cited by 1

The experimental evidence for photobiomodulation-induced cellular and behavioral changes in animal models of Parkinson’s disease: a template for translation to patients

Massri, N. E., & Mitrofanis, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-815305-5.00017-8 · Cited by 1

Growth factors and their receptors

Lazaldin, M. A. M., Lambuk, L., Ahmad, S., & Mohamud, R. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-18677-6.00005-1 · Cited by 1

LEVERAGING SMALL MOLECULES TO MODULATE THE MICROBIOME TO TREAT HUMAN DISEASES

Gulati, A., & Guo, X. (2022) · Medicinal chemistry reviews · doi:10.1021/mc-2022-vol57.ch16 · Cited by 1

The impact of microbiological infections on neurodegenerative diseases

Dilawari, R., & Singh, E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-28822-7.00016-7 · Cited by 1

Molecular insight into cross-interaction between amyloid β isoforms and its effect on aggregation pathways

Wang, L., Park, S., Choi, J. H., Lee, C. Y., Eom, K., & Kwon, T. (2025) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2025.2475221 · Cited by 1

Quantitative Profiling of Nanoscopic Protein Aggregates Reveals Specific Fingerprint of TDP‐43‐Positive Assemblies in Motor Neuron Disease

Cox, D., Burke, M., Milani, S., White, M. A., Waldron, F. M., Böken, D., Lobanova, E., Sreedharan, J., Gregory, J. M., & Klenerman, D. (2025) · Advanced Science · doi:10.1002/advs.202505484 · Cited by 1

Quantifying the Effects of Systematic STN-DBS Programming on Rest and Postural Tremor in Idiopathic Parkinson Disease Patients

Ognjanovic, K. (2015) · Scholarship@Western (Western University) · Cited by 1

How Repair-or-Dispose Decisions Under Stress Can Initiate Disease Progression

Nold, A., Batulin, D., Birkner, K., Bittner, S., & Tchumatchenko, T. (2020) · iScience · doi:10.1016/j.isci.2020.101701 · Cited by 1

Neurodegenerative Erkrankungen

Biesalski, A., Becktepe, J. S., Bartsch, T., & Franke, C. (2018) · Springer eBooks · doi:10.1007/978-3-662-56784-5_4 · Cited by 1

Neuroprotective Effects of Thiazolidine-4-Carboxylic Acid Derivatives on Memory Impairment and Neurodegeneration

Ehsanifar, M., & Montazeri, Z. (2022) · Journal of Biomedical Research & Environmental Sciences · doi:10.37871/jbres1424 · Cited by 1

Sample preparation techniques for quantitative analysis in brain pharmacokinetics: Application to neurodegenerative diseases

Kumar, P., Lyngdoh, W., Lal, B., & Alexander, A. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85544-0.00011-3 · Cited by 1

Les maladies neurodégénératives et le vieillissement

Henry, J. (2022) · Biologie Aujourd hui · doi:10.1051/jbio/2022010 · Cited by 2

Focal ultrasound strikes a new tune for targeted drug delivery

Luk, K. C. (2018) · Movement Disorders · doi:10.1002/mds.27494 · Cited by 1

The role of tau and neuroinflammation in Progressive Supranuclear Palsy and Alzheimer's Disease

Rodríguez, P. V. (2019) · Apollo (University of Cambridge) · doi:10.17863/cam.45106 · Cited by 1

Modelling the Neuroanatomical Progression of Alzheimer's Disease and Posterior Cortical AtrophyPreprint

Marinescu, R. V. (2020) · arXiv (Cornell University) · doi:10.48550/arxiv.2003.04805 · Cited by 1

Transmission-selective muscle pathology induced by active propagation of mutant huntingtin across the human neuromuscular synapsePreprint

Margarita, D. C., Colombo, L., Urszulax, B., Grimm, A., Natalia, T., Fruh, I., Hossain, I., Daniela, G., Eckert, A., Matthias, M. M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.28.454044 · Cited by 1

Single cell transcriptomic profiling of tauopathy in a novel 3D neuron-astrocyte coculture modelPreprint

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Dietary Tyrosine Intake Is Associated with Locus Coeruleus Integrity, Attentive Cognitive Control and Grey Matter Maintenance: An MRI Structural Study on 398 Healthy Individuals of the Berlin Aging Study-IIPreprint

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