Pathology of Neurodegenerative Diseases

Dugger, Brittany N.; Dickson, Dennis W.

doi:10.1101/cshperspect.a028035

Cited by 1,665Alzheimer's disease research and treatmentsAmyotrophic Lateral Sclerosis ResearchPrion Diseases and Protein Misfolding

Pathology of Neurodegenerative Diseases

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Dugger, Brittany N., Dickson, Dennis W.·2017·Cold Spring Harbor Perspectives in Biology

DOI 10.1101/cshperspect.a028035PMC PMC5495060

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Abstract

Neurodegenerative disorders are characterized by progressive loss of selectively vulnerable populations of neurons, which contrasts with select static neuronal loss because of metabolic or toxic disorders. Neurodegenerative diseases can be classified according to primary clinical features (e.g., dementia, parkinsonism, or motor neuron disease), anatomic distribution of neurodegeneration (e.g., frontotemporal degenerations, extrapyramidal disorders, or spinocerebellar degenerations), or principal molecular abnormality. The most common neurodegenerative disorders are amyloidoses, tauopathies, α-synucleinopathies, and TDP-43 proteinopathies. The protein abnormalities in these disorders have abnormal conformational properties. Growing experimental evidence suggests that abnormal protein conformers may spread from cell to cell along anatomically connected pathways, which may in part explain the specific anatomical patterns observed at autopsy. In this review, we detail the human pathology of select neurodegenerative disorders, focusing on their main protein aggregates.

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The presence of NFTs in the brain triggers a complex cascade of biochemical and cellular processes that result in neurodegeneration and neuronal loss.
“The presence of NFTs in the brain triggers a complex cascade of biochemical and cellular processes that result in neurodegeneration and neuronal loss [2].”
From Diffusion tensor imaging reveals whole-brain microstructural changes in the P301L mouse model of tauopathy. (2020) · cites this paper as [2]
The Alzheimer’s Disease section says that a neuron bearing a mature NFT dies. The paper also describes biochemical and cellular processes associated with neuronal death across neurodegenerative diseases, but it does not say that NFTs trigger that cascade. (LLM, conf=0.86)
Experimental — accuracy not yet measured
AD is the most prevalent of tauopathies and is considered a secondary tauopathy because tau aggregation is regarded as a response to other pathological proteins or events (Aβ), but it is not driven by tau mutations.
“AD is the most prevalent of tauopathies and is considered a secondary tauopathy because tau aggregation is regarded as a response to other pathological proteins or events (Aβ), but it is not driven by tau mutations (19, 65).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [65]
Both 3R- and 4R-tau isoforms were detected with no noticeable difference in the 3R to 4R ratio between LOAD and HC 3D-CNs.
“Both 3R- and 4R-tau isoforms were detected with no noticeable difference in the 3R to 4R ratio between LOAD and HC 3D-CNs, consistent with the concept that AD is a mixed 3R/4R tauopathy (65, 66) (Fig. 3D).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [65]

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Tau Positron Emission Tomography ImagingPreprint
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Neuropathological assessments of the pathology in frontotemporal lobar degeneration with TDP43-positive inclusions: an inter-laboratory study by the BrainNet Europe consortium
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Spongiform Change in Dementia With Lewy Bodies and Alzheimer Disease
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Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789 · see citing works
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
Prasad, A., Bharathi, V., Sivalingam, V., Girdhar, A., & Patel, B. K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00025 · Cited by 770 · see citing works
Phase separation and neurodegenerative diseases: a disturbance in the force
Zbinden, A., Pérez-Berlanga, M., De Rossi, P., & Polymenidou, M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.09.014 · Cited by 500 · see citing works
Genetics and Pathogenesis of Parkinson's Syndrome
Ye, H., Robak, L. A., Yu, M., Cykowski, M. D., & Shulman, J. M. (2022) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-031521-034145 · Cited by 474 · see citing works
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Cerneckis, J., Cai, H., & Shi, Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01809-0 · Cited by 452 · see citing works
Tauopathies: new perspectives and challenges
Zhang, Y., Wu, K.-M., Yang, L., Dong, Q., & Yu, J.-T. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00533-z · Cited by 323 · see citing works
A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation
Peskett, T. R., Rau, F., O’Driscoll, J., Patani, R., Lowe, A. R., & Saibil, H. R. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.007 · Cited by 321 · see citing works
Innate Immunity and Neurodegeneration
Labzin, L. I., Heneka, M. T., & Latz, E. (2018) · Annual Review of Medicine · doi:10.1146/annurev-med-050715-104343 · Cited by 319 · see citing works
The Role of NCOA4-Mediated Ferritinophagy in Ferroptosis
Santana-Codina, N., Gikandi, A., & Mancias, J. D. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_4 · Cited by 315 · see citing works
Amyloid β, Tau, and α-Synuclein aggregates in the pathogenesis, prognosis, and therapeutics for neurodegenerative diseases
Sengupta, U., & Kayed, R. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102270 · Cited by 303 · see citing works
Cellular functions of the protein kinase ATM and their relevance to human disease
Lee, J., & Paull, T. T. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00394-2 · Cited by 290 · see citing works
The gut microbiota–brain axis in neurological disorder
Ullah, H., Arbab, S., Tian, Y., Liu, C., Chen, Y., Li, Q., Khan, M. I. U., Hassan, I. U., & Li, K. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1225875 · Cited by 278 · see citing works
Roles of XBP1s in Transcriptional Regulation of Target Genes
Park, S.-M., Kang, T.-I., & So, J. (2021) · Biomedicines · doi:10.3390/biomedicines9070791 · Cited by 265 · see citing works
Impact of Natural Compounds on Neurodegenerative Disorders: From Preclinical to Pharmacotherapeutics
Sharifi‐Rad, M., Lankatillake, C., Dias, D. A., Docea, A. O., Mahomoodally, M. F., Lobine, D., Chazot, P. L., Kurt, B., Tumer, T. B., Moreira, A. C., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9041061 · Cited by 260 · see citing works
Antioxidant and Anti-Inflammatory Effects of Citrus Flavonoid Hesperetin: Special Focus on Neurological Disorders
Khan, A., Ikram, M. A., Hahm, J. R., & Kim, M. O. (2020) · Antioxidants · doi:10.3390/antiox9070609 · Cited by 258 · see citing works
Iron Metabolism, Ferroptosis, and the Links With Alzheimer’s Disease
Yan, N., & Zhang, J. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01443 · Cited by 254 · see citing works
A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology
Fu, H., Possenti, A., Freer, R., Nakano, Y., Villegas, N. C. H., Tang, M., Cauhy, P. M., Lassus, B., Chen, S., Fowler, S. L., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0298-7 · Cited by 252 · see citing works
Interpretable classification of Alzheimer’s disease pathologies with a convolutional neural network pipeline
Tang, Z., Chuang, K. V., DeCarli, C. S., Jin, L., Beckett, L. A., Keiser, M. J., & Dugger, B. N. (2019) · Nature Communications · doi:10.1038/s41467-019-10212-1 · Cited by 228 · see citing works
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Exploring the Etiological Links behind Neurodegenerative Diseases: Inflammatory Cytokines and Bioactive Kynurenines
Tanaka, M., Toldi, J., & Vécsei, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072431 · Cited by 225 · see citing works
Biological Effects of Indole-3-Propionic Acid, a Gut Microbiota-Derived Metabolite, and Its Precursor Tryptophan in Mammals’ Health and Disease
Konopelski, P., & Mogilnicka, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031222 · Cited by 218 · see citing works
Neuroprotective Potential of Limonene and Limonene Containing Natural Products
Eddin, L. B., Jha, N. K., Meeran, M. F. N., Kesari, K. K., Beiram, R., & Ojha, S. K. (2021) · Molecules · doi:10.3390/molecules26154535 · Cited by 212 · see citing works
Effects of curcumin on mitochondria in neurodegenerative diseases
Bagheri, H., Ghasemi, F., Barreto, G. E., Rafiee, R., Sathyapalan, T., & Sahebkar, A. (2019) · BioFactors · doi:10.1002/biof.1566 · Cited by 211 · see citing works
Small Molecule Targets TMED9 and Promotes Lysosomal Degradation to Reverse Proteinopathy
Dvela‐Levitt, M., Kost‐Alimova, M., Emani, M., Kohnert, E., Thompson, R. L., Sidhom, E.-H., Rivadeneira, A., Sahakian, N., Roignot, J., Papagregoriou, G., et al. (2019) · Cell · doi:10.1016/j.cell.2019.07.002 · Cited by 203 · see citing works
Neurodegenerative Disease and the NLRP3 Inflammasome
Holbrook, J. A., Jarosz-Griffiths, H., Caseley, E. A., Reyna, S. J. L., Poulter, J. A., Williams‐Gray, C. H., Peckham, D. G., & McDermott, M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.643254 · Cited by 197 · see citing works
Targeting microglial autophagic degradation in NLRP3 inflammasome-mediated neurodegenerative diseases
Wu, A., Zhou, X., Qiao, G., Yu, L., Tang, Y., Yan, L., Qiu, W., Pan, R., Yu, C., Law, B. Y. K., et al. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101202 · Cited by 193 · see citing works
Gut microbiome, cognitive function and brain structure: a multi-omics integration analysis
Liang, X., Fu, Y., Cao, W., Wang, Z., Zhang, K., Jiang, Z., Jia, X., Liu, C., Lin, H.-R., Zhong, H., et al. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00323-z · Cited by 188 · see citing works
Oxidative stress, the blood–brain barrier and neurodegenerative diseases: The critical beneficial role of dietary antioxidants
Feng, J., Zheng, Y., Guo, M., Arés, I., Martínez, M., López-Torres, B., Martínez‐Larrañaga, M., Wang, X., Anadón, A., & Martínez, M. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.07.010 · Cited by 181 · see citing works
Mechanisms tailoring the expression of heat shock proteins to proteostasis challenges
Boopathy, L. R. A., Jacob‐Tomas, S., Alecki, C., & Vera, M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101796 · Cited by 178 · see citing works
Targeting Akt/CREB/BDNF signaling pathway by ginsenosides in neurodegenerative diseases: A mechanistic approach
Zarneshan, S. N., Fakhri, S., & Khan, H. Z. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106099 · Cited by 175 · see citing works
Aging and Neurodegenerative Disease: Is the Adaptive Immune System a Friend or Foe?
Mayne, K., White, J. A., McMurran, C. E., Rivera, F. J., & de la Fuente, A. G. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.572090 · Cited by 167 · see citing works
Phytochemicals as Anti-Inflammatory Agents in Animal Models of Prevalent Inflammatory Diseases
Shin, S. A., Joo, B. J., Lee, J. S., Ryu, G., Han, M., Kim, W. Y., Park, H. H., Lee, J. H., & Lee, C. S. (2020) · Molecules · doi:10.3390/molecules25245932 · Cited by 166 · see citing works
Do Post-Translational Modifications Influence Protein Aggregation in Neurodegenerative Diseases: A Systematic Review
Schaffert, L.-N., & Carter, W. G. (2020) · Brain Sciences · doi:10.3390/brainsci10040232 · Cited by 165 · see citing works
Apoptosis and its therapeutic implications in neurodegenerative diseases
Erekat, N. S. (2021) · Clinical Anatomy · doi:10.1002/ca.23792 · Cited by 163 · see citing works
Mitochondrial Impairment: A Common Motif in Neuropsychiatric Presentation? The Link to the Tryptophan–Kynurenine Metabolic System
Tanaka, M., Szabó, Á., Spekker, E., Polyák, H., Tóth, F., & Vécsei, L. (2022) · Cells · doi:10.3390/cells11162607 · Cited by 160 · see citing works
Ferroptosis in Neurological Diseases
Ren, J., Sun, X., Yan, X., Guo, Z., & Yang, Y. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00218 · Cited by 158 · see citing works
Highly Multiplexed Immunohistochemical MALDI-MS Imaging of Biomarkers in Tissues
Yagnik, G. B., Liu, Z., Rothschild, K. J., & Lim, M. J. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00473 · Cited by 157 · see citing works
Resveratrol Derivatives as Potential Treatments for Alzheimer’s and Parkinson’s Disease
Arbo, B. D., André‐Miral, C., Nasre‐Nasser, R. G., Schimith, L. E., dos Santos, M. G., da Costa-Silva, D. G., Muccillo-Baisch, A. L., & Hort, M. A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00103 · Cited by 156 · see citing works
Misfolding and aggregation in neurodegenerative diseases: protein quality control machinery as potential therapeutic clearance pathways
Koszła, O., & Sołek, P. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01791-8 · Cited by 156 · see citing works
Searching for Peripheral Biomarkers in Neurodegenerative Diseases: The Tryptophan-Kynurenine Metabolic Pathway
Török, N., Tanaka, M., & Vécsei, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249338 · Cited by 152 · see citing works
Signaling pathways in macrophages: molecular mechanisms and therapeutic targets
Li, M., Wang, M., Wen, Y., Zhang, H., Zhao, G., & Gao, Q. (2023) · MedComm · doi:10.1002/mco2.349 · Cited by 153 · see citing works
The Contribution of Gut Microbiota–Brain Axis in the Development of Brain Disorders
Maiuolo, J., Gliozzi, M., Musolino, V., Carresi, C., Scarano, F., Nucera, S., Scicchitano, M., Oppedisano, F., Bosco, F., Ruga, S., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.616883 · Cited by 148 · see citing works
Polyphenols and Neurodegenerative Diseases: Potential Effects and Mechanisms of Neuroprotection
Arias-Sánchez, R. A., Torner, L., & Navarro, B. F. (2023) · Molecules · doi:10.3390/molecules28145415 · Cited by 146 · see citing works
Iron Homeostasis Disorder and Alzheimer’s Disease
Peng, Y., Chang, X., & Lang, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212442 · Cited by 143 · see citing works
Protein translation: biological processes and therapeutic strategies for human diseases
Jia, X., He, X., Huang, C., Li, J., Dong, Z., & Liu, K. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01749-9 · Cited by 143 · see citing works
Inflammation: A New Look at an Old Problem
Gusev, E., & Zhuravleva, Y. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094596 · Cited by 142 · see citing works
Mechanisms and roles of mitochondrial localisation and dynamics in neuronal function
Seager, R., Lee, L. J., Henley, J. M., & Wilkinson, K. A. (2020) · Neuronal Signaling · doi:10.1042/ns20200008 · Cited by 141 · see citing works
NEAT1 and paraspeckles in neurodegenerative diseases: A missing lnc found?
An, H., Williams, N. G., & Shelkovnikova, T. A. (2018) · Non-coding RNA Research · doi:10.1016/j.ncrna.2018.11.003 · Cited by 139 · see citing works
The Amygdala as a Locus of Pathologic Misfolding in Neurodegenerative Diseases
Nelson, P. T., Abner, E. L., Patel, E., Anderson, S., Wilcock, D. M., Kryscio, R. J., Eldik, L. J. V., Jicha, G. A., Gal, Z. T., Nelson, R. S., et al. (2017) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlx099 · Cited by 138 · see citing works
Kaempferol, a potential neuroprotective agent in neurodegenerative diseases: From chemistry to medicine
Jin, S., Zhang, L., & Wang, L. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115215 · Cited by 138 · see citing works
Cerebral consequences of environmental noise exposure
Hahad, O., Jiménez, M. T. B., Kuntić, M., Frenis, K., Steven, S., Daiber, A., & Münzel, T. F. (2022) · Environment International · doi:10.1016/j.envint.2022.107306 · Cited by 137 · see citing works
Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
Rinauro, D. J., Chiti, F., Vendruscolo, M., & Limbocker, R. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00651-2 · Cited by 132 · see citing works
Current understanding of the cGAS-STING signaling pathway: Structure, regulatory mechanisms, and related diseases
Pan, J., 宁波大学农产品质量安全危害因子与风险防控国家重点实验室, 浙. 宁. 3., Fei, C.-J., Hu, Y., Wu, X., Nie, L., Chen, J., 宁波大学梅山校区海洋学院生物化学与分子生物学实验室, 浙. 宁. 3., & 浙江省海洋生物工程重点实验室, 浙. 宁. 3. (2023) · 动物学研究 · doi:10.24272/j.issn.2095-8137.2022.464 · Cited by 129 · see citing works
Curcumin-Based Nanomedicines in the Treatment of Inflammatory and Immunomodulated Diseases: An Evidence-Based Comprehensive Review
Laurindo, L. F., de Carvalho, G. M., Zanuso, B. D. O., Figueira, M. E., Direito, R., Goulart, R. D. Á., Buglio, D. S., & Barbalho, S. M. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15010229 · Cited by 128 · see citing works
The bile acid TUDCA and neurodegenerative disorders: An overview
Zangerolamo, L., Vettorazzi, J. F., Rosa, L. R. D. O., Carneiro, E. M., & Barbosa, H. C. L. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119252 · Cited by 127 · see citing works
Ozone: a natural bioactive molecule with antioxidant property as potential new strategy in aging and in neurodegenerative disorders
Scassellati, C., Galoforo, A. C., Bonvicini, C., Esposito, C., & Ricevuti, G. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101138 · Cited by 121 · see citing works
Astrocyte-Neuron Metabolic Crosstalk in Neurodegeneration: A Mitochondrial Perspective
Mulica, P., Grünewald, A., & Pereira, S. L. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.668517 · Cited by 121 · see citing works
Review of immunohistochemistry techniques: Applications, current status, and future perspectives
Mebratie, D. Y., & Dagnaw, G. G. (2024) · Seminars in Diagnostic Pathology · doi:10.1053/j.semdp.2024.05.001 · Cited by 121 · see citing works
Health Benefits, Pharmacological Effects, Molecular Mechanisms, and Therapeutic Potential of α-Bisabolol
Eddin, L. B., Jha, N. K., Goyal, S. N., Agrawal, Y. O., Subramanya, S. B., Bastaki, S. M. A., & Ojha, S. K. (2022) · Nutrients · doi:10.3390/nu14071370 · Cited by 120 · see citing works
Therapeutic applications of mushrooms and their biomolecules along with a glimpse of in silico approach in neurodegenerative diseases
Nand, S., Mishra, D., Singh, P., Vamanu, E., & Singh, M. P. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111377 · Cited by 116 · see citing works
Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases
Gonçalves, P. B., Sodero, A. C. R., & Cordeiro, Y. (2021) · Biomolecules · doi:10.3390/biom11050767 · Cited by 115 · see citing works
The Credible Role of Curcumin in Oxidative Stress-Mediated Mitochondrial Dysfunction in Mammals
Sathyabhama, M., Dharshini, L. C. P., Karthikeyan, A., Senthil, K., & Min, T. (2022) · Biomolecules · doi:10.3390/biom12101405 · Cited by 115 · see citing works
Cannabidiol for neurodegenerative disorders: A comprehensive review
Bhunia, S., Kolishetti, N., Yndart, A., Vashist, A., & Nair, M. G. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.989717 · Cited by 115 · see citing works
New Insights into Oxidative Stress and Inflammatory Response in Neurodegenerative Diseases
Scarian, E., Viola, C., Dragoni, F., Gerlando, R. D., Rizzo, B., Diamanti, L., Gagliardi, S., Bordoni, M., & Pansarasa, O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052698 · Cited by 115 · see citing works
Nanomedicine for Neurodegenerative Disorders: Focus on Alzheimer’s and Parkinson’s Diseases
Jagaran, K., & Singh, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169082 · Cited by 114 · see citing works
Vitamin D and Neurodegenerative Diseases
Wang, W., Li, Y., & Meng, X. (2022) · Heliyon · doi:10.1016/j.heliyon.2023.e12877 · Cited by 112 · see citing works
Chaperone‐mediated autophagy: Molecular mechanisms, biological functions, and diseases
Yao, R., & Shen, J. (2023) · MedComm · doi:10.1002/mco2.347 · Cited by 111 · see citing works
Nanoparticles: A Hope for the Treatment of Inflammation in CNS
Zhu, F., Hu, Y.-J., Yu, L., Zhou, X., Wu, J., Tang, Y., Qin, D., Fan, Q., & Wu, A. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.683935 · Cited by 109 · see citing works
Effects of Ketogenic Diet on Neuroinflammation in Neurodegenerative Diseases
Jiang, Z., Yin, X., Wang, M., Chen, T., Wang, Y., Gao, Z., & Wang, Z. (2022) · Aging and Disease · doi:10.14336/ad.2021.1217 · Cited by 109 · see citing works
Histone Modifications in Alzheimer’s Disease
Santana, D. A., Smith, M. D. A. C., & Chen, E. (2023) · Genes · doi:10.3390/genes14020347 · Cited by 109 · see citing works
Role of NLRP3 inflammasome-mediated neuronal pyroptosis and neuroinflammation in neurodegenerative diseases
Han, Y., Liu, X., Jin, M., Sun, H., & Kwon, T. (2023) · Inflammation Research · doi:10.1007/s00011-023-01790-4 · Cited by 109 · see citing works
Ferroptosis regulation through Nrf2 and implications for neurodegenerative diseases
Xiang, Y., Song, X., & Long, D. (2024) · Archives of Toxicology · doi:10.1007/s00204-023-03660-8 · Cited by 109 · see citing works
Noncancerous disease-targeting AIEgens
Duo, Y., Luo, G., Zhang, W., Wang, R., Xiao, G. G., Li, Z., Li, X., Chen, M., Yoon, J., & Tang, B. Z. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00610c · Cited by 106 · see citing works
Vitamin D and Parkinson’s Disease
Pignolo, A., Mastrilli, S., Davì, C., Arnao, V., Aridon, P., Mendes, F. A. D. S., Gagliardo, C., & D’Amelio, M. (2022) · Nutrients · doi:10.3390/nu14061220 · Cited by 104 · see citing works
Neurodegenerative disorders and gut-brain interactions
Singh, A., Dawson, T. M., & Kulkarni, S. (2021) · Journal of Clinical Investigation · doi:10.1172/jci143775 · Cited by 102 · see citing works
Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD
Wood, A., Gurfinkel, Y., Polain, N., Lamont, W. G., & Rea, S. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094705 · Cited by 101 · see citing works
Fermented Soy Products: Beneficial Potential in Neurodegenerative Diseases
Jang, C. H., Oh, J., Lim, J. S., Kim, H. J., & Kim, J.-S. (2021) · Foods · doi:10.3390/foods10030636 · Cited by 100 · see citing works
Bioactive Compounds of the Mediterranean Diet as Nutritional Support to Fight Neurodegenerative Disease
Franco, G. A., Interdonato, L., Cordaro, M., Cuzzocrea, S., & Paola, R. D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087318 · Cited by 100 · see citing works
β‐Sitosterol Alleviates Inflammatory Response via Inhibiting the Activation of ERK/p38 and NF‐κB Pathways in LPS‐Exposed BV2 Cells
Sun, Y., Gao, L., Hou, W., & Wu, J. (2020) · BioMed Research International · doi:10.1155/2020/7532306 · Cited by 97 · see citing works
Identification of the molecular mechanism of insulin-like growth factor-1 (IGF-1): a promising therapeutic target for neurodegenerative diseases associated with metabolic syndrome
Arjunan, A., Sah, D. K., Woo, M., & Song, J. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00966-z · Cited by 97 · see citing works
Neurogranin: A Potential Biomarker of Neurological and Mental Diseases
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Authors: Dugger, B. N., & Dickson, D. W.
Affiliations: University of California, San Francisco (US)
Mayo Clinic in Florida (US)
ORCID: Dugger, Brittany N.
Dickson, Dennis W.
Venue: Cold Spring Harbor Perspectives in Biology
Publisher: Cold Spring Harbor Laboratory
Published: 2017-01-06
Volume: 9
Issue: 7
Pages: a028035
ISSN: 1943-0264 (ISSN-L)
DOI: 10.1101/cshperspect.a028035
PMC: PMC5495060
OpenAlex: W2570634615
Cited by: 1,665
References: 159
Citations by year: 2026: 161 · 2025: 265 · 2024: 319 · 2023: 334 · 2022: 233 · 2021: 210 · 2020: 98 · 2019: 21 · 2018: 14 · 2017: 7 · 2016: 1 · 2012: 1
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Cold Spring Harbor Perspectives in Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: Henry M. Jackson Foundation
CurePSP
Daiichi-Sankyo
National Institutes of Health (AG016574, NS084974, AG002132, NS072187, AG037491)
National Institute on Aging (P01AG002132, R01AG037491, P50AG016574)
National Institute of Neurological Disorders and Stroke (P01NS084974, P50NS072187)
Daiichi Sankyo Europe
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords: neurodegenerative diseases, proteinopathies, amyloidosis, tauopathy, synucleinopathies, TDP-43 proteinopathy, protein aggregation, protein conformation, prion-like spread, selective neuronal loss, dementia, parkinsonism, motor neuron disease, frontotemporal lobar degeneration, extrapyramidal disorders, spinocerebellar degeneration
MeSH terms: Humans, Protein Conformation, Neurodegenerative Diseases, Protein Aggregates

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