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

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

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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

Connectome-based biophysics models of Alzheimer’s disease diagnosis and prognosis

Torok, J., Anand, C., Verma, P., & Raj, A. (2022) · Translational research · doi:10.1016/j.trsl.2022.08.008 · Cited by 11

Reorganization of the outer layer of a model of the plasma membrane induced by a neuroprotective aminosterol

Barletti, B., Lucchesi, G., Muscat, S., Errico, S., Barbut, D., Danani, A., ZASLOFF, M. A., Grasso, G., Chiti, F., & Caminati, G. (2022) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2022.113115 · Cited by 11

Mitochondrial Signaling and Neurodegeneration

Picard, M. A., & McManus, M. J. (2016) · Springer eBooks · doi:10.1007/978-3-319-28637-2_5 · Cited by 11

Potential role of exosome in post-stroke reorganization and/or neurodegeneration

Azizi, F., Askari, S., Javadpour, P., Hadjighassem, M., & Ghasemi, R. (2020) · EXCLI journal · doi:10.17179/excli2020-3025 · Cited by 12

Aetiology and pathophysiology of neurodegenerative disorders

Sahoo, R. K., Gupta, T., Smily, Kumar, V., Rani, S., & Gupta, U. D. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85544-0.00006-x · Cited by 13

Limitations and potential strategies of immune checkpoint blockade in age-related neurodegenerative disorders

Lasheen, N. N., Allam, S., Elgarawany, A., Aswa, D. W., Mansour, R., & Farouk, Z. E. (2024) · The Journal of Physiological Sciences · doi:10.1186/s12576-024-00933-4 · Cited by 12

Quinic acid protects against the development of Huntington’s disease in Caenorhabditis elegans model

Din, R. H. E., & Thabit, S. (2024) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-024-04670-4 · Cited by 10

Design Chemical Exchange Saturation Transfer Contrast Agents and Nanocarriers for Imaging Proton Exchange in Vivo

Su, H., & Chan, K. W. Y. (2024) · ACS Nano · doi:10.1021/acsnano.4c05923 · Cited by 10

Evaluation of Nanomaterials as Effective Carriers Targeted to Traverse Blood–Brain Barrier for Theragnostics of Neurodegenerative Diseases: An Overview

Vengadesan, D., Arumugam, N., Manikandan, E., & Mandal, A. (2024) · BioNanoScience · doi:10.1007/s12668-024-01773-7 · Cited by 10

Effects of Heparan Sulfate Trisaccharide Containing Oleanolic Acid in Attenuating Hyperphosphorylated Tau-Induced Cell Dysfunction Associated with Alzheimer’s Disease

Zhu, S., Song, Z., Tapayan, A. S., Singh, K., Wang, K., Hagar, H. C., Zhang, J., Kim, H., Thepsuwan, P., Kuo, M., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02563 · Cited by 10

The Limbic System

ten Donkelaar, H. J., Insausti, R., van Domburg, P., Küsters, B., Hashizume, Y., & Hori, A. (2020) · Springer eBooks · doi:10.1007/978-3-030-41878-6_14 · Cited by 12

Default Mode Network quantitative diffusion and resting‐state functional magnetic resonance imaging correlates in sporadic Creutzfeldt‐Jakob disease

Paoletti, M., Caverzasi, E., Mandelli, M. L., Brown, J. A., Henry, R. G., Miller, B. L., Rosen, H. J., DeArmond, S. J., Bastianello, S., Seeley, W. W., et al. (2022) · Human Brain Mapping · doi:10.1002/hbm.25945 · Cited by 10

Novel naturally occurring autoantibodies attenuate α‐synuclein pathology in a mouse model of Parkinson's disease

Li, Y., Wang, T., Meng, L., Lei, J., Liu, C., Liang, Y., Ren, L., Liu, Y., Liu, Y., Liu, S., et al. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12860 · Cited by 10

Development and Implementation of an Internal Quality Control Sample to Standardize Oligomer-Based Diagnostics of Alzheimer’s Disease

Pils, M., Dybala, A., Rehn, F., Blömeke, L., Bujnicki, T., Kraemer‐Schulien, V., Hoyer, W., Riesner, D., Willbold, D., & Bannach, O. (2023) · Diagnostics · doi:10.3390/diagnostics13101702 · Cited by 10

Structural Basis for Recognition of a Unique Epitope by a Human Anti-tau Antibody

Zhang, H., Zhu, X., Pascual, G., Wadia, J. S., Keogh, E. A., Hoozemans, J. J. M., Siregar, B., Inganäs, H., Stoop, E. J. M., Goudsmit, J., et al. (2018) · Structure · doi:10.1016/j.str.2018.08.012 · Cited by 10

Meta-analysis on big data of bioactive compounds from mangrove ecosystem to treat neurodegenerative disease

George, B., Varathan, P., & Vasu, S. T. (2020) · Scientometrics · doi:10.1007/s11192-020-03355-2 · Cited by 10

Supramolecular organizing centers at the interface of inflammation and neurodegeneration

Sušjan, P., Ramuta, T. Ž., Boršić, E., Orehek, S., & Hafner‐Bratkovič, I. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.940969 · Cited by 11

Proteome-Scale Mapping of Perturbed Proteostasis in Living CellsPreprint

Lam, I., Hallacli, E., & Khurana, V. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034124 · Cited by 9

The Brain Network Hub Degeneration in Alzheimer’s Disease

Jin, S., Wang, J., & Yong He, A. (2024) · Biophysics Reports · doi:10.52601/bpr.2024.230025 · Cited by 11

Extracellular PHF-tau modulates astrocyte mitochondrial dynamics and mediates neuronal connectivity

Zufferey, V., Barve, A., Parietti, E., Belinga, L. N., Bringaud, A., Varisco, Y., Fabbri, K., Capotosti, F., Bezzi, P., Déglon, N., et al. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00474-9 · Cited by 11

Normative structural connectome constrains spreading transient brain activity in generalized epilepsy

Xia, J., Yang, S., Li, J., Meng, Y., Niu, J., Chen, H., Zhang, Z., & Liao, W. (2025) · BMC Medicine · doi:10.1186/s12916-025-04099-7 · Cited by 9

Interneuron transcriptomics reveals pathologic markers of Alzheimer's disease progression

Chen, K. S., Noureldein, M. H., Rigan, D. M., Hayes, J. M., Loi, K. J., Hur, J., Savelieff, M. G., & Feldman, E. L. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107012 · Cited by 9

Physiological and Pathological Roles of the Cytohesin Family in Neurons

Ito, A., Fukaya, M., Okamoto, H., & Sakagami, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095087 · Cited by 9

Could the Urease of the Gut Bacterium Proteus mirabilis Play a Role in the Altered Gut–Brain Talk Associated with Parkinson’s Disease?

Grahl, M. V. C., Andrade, B. D. S., Perin, A. P. A., Neves, G. A., Duarte, L. D. S., Uberti, A. F., Hohl, K. S., Follmer, C., & Carlini, C. R. (2023) · Microorganisms · doi:10.3390/microorganisms11082042 · Cited by 12

Investigating the discrimination ability of 3D convolutional neural networks applied to altered brain MRI parametric maps

Mattia, G. M., Villain, E., Nemmi, F., Lann, M. V. L., Franceries, X., & Péran, P. (2024) · Artificial Intelligence in Medicine · doi:10.1016/j.artmed.2024.102897 · Cited by 9

Proteopathic seed amplification assays in easily accessible specimens for human synucleinopathies, tauopathies, and prionopathies: A scoping review

Salciccia, C., Costanzo, M., Ruocco, G., Porreca, F., Vivacqua, G., Fabbrini, G., Belvisi, D., Ladogana, A., & Poleggi, A. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105997 · Cited by 11

PET tracer development for imaging α-synucleinopathies

Alam, M. M., Lee, S. H., Wasim, S., & Lee, S. (2025) · Archives of Pharmacal Research · doi:10.1007/s12272-025-01538-0 · Cited by 9

Understanding the Relevance of Aging-Related Tau Astrogliopathy (ARTAG)

Kovács, G. G. (2018) · Neuroglia · doi:10.3390/neuroglia1020023 · Cited by 9

A Novel Tau Antibody Detecting the First Amino-Terminal Insert Reveals Conformational Differences Among Tau Isoforms

Verelst, J., Geukens, N., Eddarkaoui, S., Vliegen, D., Smidt, E. D., Rosseels, J., Franssens, V., Molenberghs, S., François, C., Stoops, E., et al. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00048 · Cited by 11

Bacopa monnieri (Brahmi)

Joshi, T., Gupta, A., Kumar, P., Singh, A., & Kumar, A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819212-2.00020-7 · Cited by 9

Alzheimer diseases

Savonenko, A. V., Wong, P. C., & Li, T. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00022-8 · Cited by 8

Alzheimer’s disease susceptibility genes modify the risk of Parkinson disease and Parkinson’s disease-associated cognitive impairment

Fang, L., Tang, B.-S., Fan, K., Wan, C.-M., Yan, X., & Guo, J. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.042 · Cited by 9

Network spreading and local biological vulnerability in amyotrophic lateral sclerosis

Farahani, A., Hansen, J. Y., Bazinet, V., Shafiei, G., Collins, D. L., Dadar, M., Kalra, S., Dagher, A., & Mišić, B. (2025) · Communications Biology · doi:10.1038/s42003-025-08561-3 · Cited by 7

Heterogeneous Dynamics of the Fuzzy Coat of Full-Length Phospho-Mimetic Tau Fibrils

Zhang, J. Y., Dregni, A. J., & Hong, M. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c18540 · Cited by 8

How fiber bundle alterations differ in presumed LATE and amnestic Alzheimer's disease

Lebrun, A., Leprince, Y., Lagarde, J., Olivieri, P., Moussion, M., Noiray, C., Bottlaender, M., & Sarazin, M. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14156 · Cited by 8

Calibration‐free whole‐brain CEST imaging at 7T with parallel transmit pulse design for saturation homogeneity utilizing universal pulses (PUSHUP)

Völzke, Y., Akbey, S., Löwen, D., Pracht, E., Stirnberg, R., Gras, V., Boulant, N., Zaiß, M., & Stöcker, T. (2024) · Magnetic Resonance in Medicine · doi:10.1002/mrm.30305 · Cited by 8

Perspectives on How Human Simultaneous Multi-Modal Imaging Adds Directionality to Spread Models of Alzheimer’s Disease

Neitzel, J., Nuttall, R., & Sorg, C. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00026 · Cited by 7

Connectomics of neurodegeneration

Ellen Kuhl, A. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0459-3 · Cited by 8

Protein aggregation detection with fluorescent macromolecular and nanostructured probes: challenges and opportunities

Cingolani, M., Mummolo, L., Lugli, F., Zaffagnini, M., & Genovese, D. (2021) · New Journal of Chemistry · doi:10.1039/d1nj01606g · Cited by 8

Effect of Renal Ischemia Reperfusion on Brain Neuroinflammation

Lee, B.-N., Ines, I., Je, J., Park, E., Seong, H., Min, G.-J., Kim, H., Kim, S.-H., Kim, S., Kim, H., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10112993 · Cited by 8

Distinct responses of human peripheral blood cells to different misfolded protein oligomers

Leal‐Lasarte, M., Mannini, B., Chiti, F., Vendruscolo, M., Dobson, C. M., Roodveldt, C., & Pozo, D. (2021) · Immunology · doi:10.1111/imm.13377 · Cited by 8

Can Creutzfeldt-Jakob disease unravel the mysteries of Alzheimer?

Kovács, G. G. (2016) · Prion · doi:10.1080/19336896.2016.1228507 · Cited by 8

An Overview of the Latest Developments in the Electrochemical Aptasensing of Neurodegenerative Diseases

Mikuła, E., & Malecka, K. (2023) · Coatings · doi:10.3390/coatings13020235 · Cited by 7

(Dys)functional insights into nucleic acids and RNA-binding proteins modulation of the prion protein and α-synuclein phase separation

Cordeiro, Y., Freire, M. H. O., Wiecikowski, A. F., & do Amaral, M. J. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01067-4 · Cited by 7

Mapping amyloid beta predictors of entorhinal tau in preclinical Alzheimer's disease

Zamani, J., Vahid, A., Avelar‐Pereira, B., Gozdas, E., Hosseini, S. M. H., & Initiative, A. D. N. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.14499 · Cited by 9

Proline-Rich Region II (PRR2) Plays an Important Role in Tau–Glycan Interaction: An NMR Study

Murray, A., Yan, L., Gibson, J. M., Liu, J., Eliezer, D., Lippens, G. M., Zhang, F., Linhardt, R. J., Zhao, J., & Wang, C. (2022) · Biomolecules · doi:10.3390/biom12111573 · Cited by 6

Pathological α-synuclein accumulation, CSF metabolites changes and brain microstructures in cynomolgus monkeys treated with 6-hydroxydopamine

Gan, X., Ren, J., Huang, T., Wu, K., Li, S., Duan, Y., Wang, Z., Si, W., & Wei, J. (2022) · NeuroToxicology · doi:10.1016/j.neuro.2022.12.001 · Cited by 7

Synthesis, characterization and biological evaluation of aurones as potential neuroprotective agents

Ayaz, M., Shah, S. W. A., Shoaib, M., Shah, F. A., & Ahmed, F. (2024) · Future Medicinal Chemistry · doi:10.1080/17568919.2024.2363713 · Cited by 7

Frontotemporal lobar degeneration targets brain regions linked to expression of recently evolved genes

Pasquini, L., Pereira, F. L., Seddighi, S., Zeng, Y., Wei, Y., Illán‐Gala, I., Vatsavayai, S. C., Friedberg, A., Lee, A. J., Brown, J. A., et al. (2024) · Brain · doi:10.1093/brain/awae205 · Cited by 8

Imaging Clinical Subtypes and Associated Brain Networks in Alzheimer’s Disease

Herholz, K. (2022) · Brain Sciences · doi:10.3390/brainsci12020146 · Cited by 8

Protein Homeostasis Dysregulation in Pathogenesis of Neurodegenerative Diseases

Kukharsky, M. S., Everett, M. W., Lytkina, O. A., Raspopova, M. A., Kovrazhkina, E. A., Овчинников, Р. К., Antohin, A., & Московцев, А. А. (2022) · Molecular Biology · doi:10.1134/s0026893322060115 · Cited by 6

Salt-regulated reversible fibrillation of Mycobacterium tuberculosis isocitrate lyase: Concurrent restoration of structure and activity

Shukla, H., Kumar, R., Sonkar, A. K., Mitra, K., Akhtar, M. S., & Tripathi, T. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.06.008 · Cited by 7

Functional Effects of a Neuromelanin Analogue on Dopaminergic Neurons in 3D Cell Culture

Collins, W., Rouleau, N., Bonzanni, M., Kapner, K. S., Jeremiah, A., Du, C., Pothos, E. N., & Kaplan, D. L. (2018) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.8b00976 · Cited by 7

Symmetric Bihemispheric Postmortem Brain Cutting to Study Healthy and Pathological Brain Conditions in Humans

Iacono, D., Geraci-Erck, M., Peng, H., & Bouffard, J. (2016) · Journal of Visualized Experiments · doi:10.3791/54602 · Cited by 8

New Insight in The Molecular Mechanisms of Neurodegenerative Disease

Meiliana, A., Dewi, N. M., & Wijaya, A. (2018) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v10i1.448 · Cited by 6

Characterization of Salt-Induced Oligomerization of Human β2-Microglobulin at Low pH

Narang, D., Singh, A., Swasthi, H. M., & Mukhopadhyay, S. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b05619 · Cited by 7

3D Mapping of Neurofibrillary Tangle Burden in the Human Medial Temporal LobePreprint

Yushkevich, P. A., Muñoz, M., Martin, M. M. I. D. O., Ittyerah, R., Lim, S., Ravikumar, S., Bedard, M. L., Pickup, S., Liu, W., Wang, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.15.421909 · Cited by 7

The integrity of dopaminergic and noradrenergic brain regions is associated with different aspects of late-life memory performancePreprint

Dahl, M. J., Bachman, S. L., Dutt, S., Düzel, S., Bodammer, N., Lindenberger, U., Kühn, S., Werkle‐Bergner, M., & Mather, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.12.511748 · Cited by 6

Iron-Mediated Overexpression of Amyloid Precursor Protein via Iron Responsive mRNA in Alzheimer’s Disease

Khan, M. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115283 · Cited by 8

A novel C. elegans model for MAPT/Tau spreading reveals genes critical for endolysosomal integrity and seeded MAPT/Tau aggregation

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. (2025) · Autophagy · doi:10.1080/15548627.2025.2551676 · Cited by 12

Engineered core–shell magnetic nanoparticle for MR dual-modal tracking and safe magnetic manipulation of ependymal cells in live rodents

Peng, Y., Lui, C. N. P., Chen, Y.-W., Chou, S., Chou, P., Yung, K. K. L., & Tsang, S. C. E. (2017) · Nanotechnology · doi:10.1088/1361-6528/aa96eb · Cited by 6

An anthraquinone compound and its protective effects against homocysteine-induced cytotoxicity and oxidative stress

Lin, L., & Du, H. (2018) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2018.05.058 · Cited by 6

Inflammation-Mediated Responses in the Development of Neurodegenerative Diseases

Nainu, F., Mamada, S. S., Harapan, H., & Emran, T. B. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-981-19-7376-5_3 · Cited by 6

Evaluation of N- and O-Linked Indole Triazines for a Dual Effect on α-Synuclein and Tau Aggregation

Ramirez, E., Ganegamage, S. K., Min, S., Patel, H., Ogunware, A. E., Plascencia‐Villa, G., Alnakhala, H., Shimanaka, K., Tripathi, A., Wang, K., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00464 · Cited by 8

Interaction of polymers with amyloidogenic peptides

Abraham, J. N., & Nardin, C. (2017) · Polymer International · doi:10.1002/pi.5483 · Cited by 6

RTD-Fluxgate magnetometers for detecting iron accumulation in the brain

Trigona, C., Sinatra, V., Andò, B., Baglio, S., & Bulsara, A. R. (2020) · IEEE Instrumentation & Measurement Magazine · doi:10.1109/mim.2020.8979517 · Cited by 6

Identification of an Orally Bioavailable, Brain-Penetrant Compound with Selectivity for the Cannabinoid Type 2 Receptor

Ospanov, M., Sulochana, S. P., Paris, J. J., Rimoldi, J. M., Ashpole, N. M., Walker, L., Ross, S. A., Shilabin, A. G., & Ibrahim, M. A. (2022) · Molecules · doi:10.3390/molecules27020509 · Cited by 6

La transconformation protéique, nouveau paradigme en neurologie

Hauw, J., Haı̈k, S., & Duyckaerts, C. J. (2015) · Revue Neurologique · doi:10.1016/j.neurol.2015.09.010 · Cited by 6

Brain network dynamics determine tau presence while regional vulnerability governs tau load in Alzheimer’s diseasePreprint

Xiao, Y., Spotorno, N., An, L., Bazinet, V., Hansen, J. Y., Strandberg, O. T., Shafiei, G., Behjat, H., Funck, T., Salvadó, G., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.17.648358 · Cited by 6

Mapping multipathology via spatial omic integration

Palaganas, R. G., Sidiropoulos, D. N., Morris, M., & Stein-O’Brien, G. (2025) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2025.103398 · Cited by 6

Network Models of Neurodegeneration: Bridging Neuronal Dynamics and Disease Progression

Alexandersen, C. G., Brennan, G. S., Brynildsen, J. K., Henderson, M. X., Iturria‐Medina, Y., & Bassett, D. S. (2026) · IEEE Reviews in Biomedical Engineering · doi:10.1109/rbme.2025.3643310 · Cited by 9

Amyloid Oligomers: Expediting Crystal Growth and Revisiting the Corkscrew Structures

Hirschbeck, S. S., Sawaya, M. R., Lindberg, E. T., Limbach, M. N., Jang, J. H., Cantrell, K. L., Eisenberg, D. S., & Do, T. D. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c00656 · Cited by 5

RNA-seq analyses reveal the relevance of RNAs involved in ribosomal complex to induce mammalian prion protein aggregation and phase separation in vitro

Tahira, A. C., Gomes, M. P. B., Freire, M. H. O., Muxfeldt, M., Prosdocimi, F., Passos, Y. M., Amaral, M. S., Valadão, L. P. F., Rangel, L. P., Silva, J. L., et al. (2025) · RNA Biology · doi:10.1080/15476286.2025.2508107 · Cited by 5

RTD-fluxgate sensor for measurements of metal compounds in neurodegenerative diseases

Trigona, C., Sinatra, V., Andò, B., Baglio, S., Mostile, G., Nicoletti, A. S. Q., Zappia, M., & Bulsara, A. R. (2017) · IEEE International Instrumentation and Measurement Technology Conference · doi:10.1109/i2mtc.2017.7969672 · Cited by 5

Progressive supranuclear palsy: Neuropathology of patients with a short disease duration due to unexpected death

Zhang, L., Toyoshima, Y., Takeshima, A., Shimizu, H., Tomita, I., Onodera, O., Takahashi, H., & Kakita, A. (2020) · Neuropathology · doi:10.1111/neup.12707 · Cited by 5

Antemortem network analysis of spreading pathology in autopsy-confirmed frontotemporal degeneration

Chen, M., Burke, S., Olm, C. A., Irwin, D. J., Massimo, L. M., Lee, E. B., Trojanowski, J. Q., Gee, J. C., & Grossman, M. (2023) · Brain Communications · doi:10.1093/braincomms/fcad147 · Cited by 4

Dietary Tyrosine Intake (FFQ) Is Associated with Locus Coeruleus, Attention and Grey Matter Maintenance: An MRI Structural Study on 398 Healthy Individuals of the Berlin Aging Study-II

Plini, E. R. G., Melnychuk, M. C., Harkin, A., Dahl, M. J., McAuslan, M. J., Kühn, S., Boyle, R. T., Whelan, R., Andrews, R., Düzel, S., et al. (2023) · The journal of nutrition health & aging · doi:10.1007/s12603-023-2005-y · Cited by 5

Building an Understanding of Proteostasis in Reproductive Cells: The Impact of Reactive Carbonyl Species on Protein Fate

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Role of Thrombosis in Neurodegenerative Diseases: An Intricate Mechanism of Neurovascular Complications

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