SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

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Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

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Neurodegenerative Tauopathies

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SUMO

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Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study

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SUMO-1 Modification of IκBα Inhibits NF-κB Activation

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Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules

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Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

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Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

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Dysregulated proteostasis network in neuronal diseases

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Alzheimer’s Disease: From Molecular Mechanisms to Promising Therapeutic Strategies

Ivanova, A. V., Kutuzova, A. D., Kuzmichev, I., & Abakumov, M. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26199444 · Cited by 33

Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?

Cheng, X., Yang, W., Lin, W., & Mei, F. C. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000784 · Cited by 25

Modulation of Tau Pathology in Alzheimer’s Disease by Dietary Bioactive Compounds

Shi, H., & Zhao, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020831 · Cited by 26

Age-related p53 SUMOylation accelerates senescence and tau pathology in Alzheimer’s disease

Wan, L., Yang, F., Yin, A., Luo, Y., Yi, L. I. U., Liu, F., Wang, J., Liu, R., & Wang, X. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01448-0 · Cited by 26

Dangerous Liaisons: Tau Interaction with Muscarinic Receptors

Wysocka, A., Pałasz, E., Steczkowska, M., & Niewiadomska, G. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200424134311 · Cited by 24

Can We Treat Neurodegenerative Proteinopathies by Enhancing Protein Degradation?

Engelender, S., Stefanis, L., Oddo, S., & Bellucci, A. (2022) · Movement Disorders · doi:10.1002/mds.29058 · Cited by 23

SUMO1 Modification of Tau in Progressive Supranuclear Palsy

Takamura, H., Nakayama, Y., Ito, H., Katayama, T., Fraser, P. E., & Matsuzaki, S. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02734-5 · Cited by 24

Heparan Sulfate Proteoglycans in Tauopathy

Zhu, Y., Gandy, L. A., Zhang, F., Liu, J., Wang, C., Blair, L. J., Linhardt, R. J., & Wang, L. (2022) · Biomolecules · doi:10.3390/biom12121792 · Cited by 27

Illuminating Neural Circuits in Alzheimer’s Disease

Yang, Y., & Wang, J. (2021) · Neuroscience Bulletin · doi:10.1007/s12264-021-00716-6 · Cited by 24

A tau dephosphorylation-targeting chimera selectively recruits protein phosphatase-1 to ameliorate Alzheimer’s disease and tauopathies

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Clinical relevance of biomarkers, new therapeutic approaches, and role of post-translational modifications in the pathogenesis of Alzheimer’s disease

Mumtaz, I., Ayaz, M. O., Khan, M. S., Manzoor, U., Ganayee, M. A., Bhat, A. Q., Dar, G. H., Alghamdi, B. S. A., Hashem, A. M., Dar, M. J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.977411 · Cited by 23

Chemical Synthesis of Microtubule-Associated Protein Tau

Powell, W. C., Jing, R., & Walczak, M. A. A. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c07338 · Cited by 24

Post-translational and transcriptional dynamics – regulating extracellular vesicle biology

Claridge, B., Kastaniegaard, K., Stensballe, A., & Greening, D. W. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1551135 · Cited by 21

Ubiquitin-like modification dependent proteasomal degradation and disease therapy

Wang, T., Jiang, J., Zhang, X., Ke, X., & Qu, Y. (2024) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2024.05.005 · Cited by 20

Protein modification in neurodegenerative diseases

Ramazi, S., Dadzadi, M., Darvazi, M., Seddigh, N., & Allahverdi, A. (2024) · MedComm · doi:10.1002/mco2.674 · Cited by 25

An overview of the possible therapeutic role of SUMOylation in the treatment of Alzheimer’s disease

Marcelli, S., Ficulle, E., Piccolo, L., Corbo, M., & Feligioni, M. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.12.023 · Cited by 21

Senescence may mediate conversion of tau phosphorylation-induced apoptotic escape to neurodegeneration

Wang, J., & Wang, Z.-H. (2015) · Experimental Gerontology · doi:10.1016/j.exger.2015.03.007 · Cited by 20

Sumoylation in Cellular Senescence and Aging

Gong, L., Sun, Q., & Li, D. (2017) · Current Molecular Medicine · doi:10.2174/1566524016666161223104915 · Cited by 19

SUMO 1‐conjugation is altered during normal aging but not by increased amyloid burden

Stankova, T., Piepkorn, L., Bayer, T. A., Jahn, O., & Tirard, M. (2018) · Aging Cell · doi:10.1111/acel.12760 · Cited by 20

Differential effects of SUMO1 and SUMO2 on circadian protein PER2 stability and function

Chen, L.-C., Hsieh, Y.-L., Tan, G. Y. T., Kuo, T.-Y., Chou, Y., Hsu, P., & Hwang‐Verslues, W. W. (2021) · Scientific Reports · doi:10.1038/s41598-021-93933-y · Cited by 22

SUMO modulation of protein aggregation and degradation

Feligioni, M., Marcelli, S., Knock, E., Nadeem, U., Arancio, O., & Fraser, P. E. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.4.382 · Cited by 19

SET SUMOylation promotes its cytoplasmic retention and induces tau pathology and cognitive impairments

Qin, M., Li, H., Bao, J., Xia, Y., Ke, D., Wang, Q., Liu, R., Wang, J., Zhang, B., Shu, X., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0663-0 · Cited by 19

Ubiquitin and Ubiquitin-Like Proteins in the Critical Equilibrium between Synapse Physiology and Intellectual Disability

Folci, A., Mirabella, F., & Fossati, M. (2020) · eNeuro · doi:10.1523/eneuro.0137-20.2020 · Cited by 22

Functions of nuclear receptors SUMOylation

Liu, W., Min De, Z. E. N. G., & Fu, N. (2021) · Clinica Chimica Acta · doi:10.1016/j.cca.2021.01.007 · Cited by 19

Contributive Role of Hyperglycemia and Hypoglycemia Towards the Development of Alzheimer’s Disease

Chakrabarty, R., Yousuf, S., & Singh, M. P. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02846-y · Cited by 20

Inhibition of CDK1 activity by sumoylation

Xiao, Y., Lucas, B., Molcho, E., Schiff, T., & Vigodner, M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.051 · Cited by 18

Divergent signaling via SUMO modification: potential for CFTR modulation

Ahner, A., Gong, X., & Frizzell, R. A. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00124.2015 · Cited by 17

Myristoylation-dependent palmitoylation of cyclin Y modulates long-term potentiation and spatial learning

Seo, J., Hwang, H., Choi, Y., Jung, S., Hong, J., Yoon, B.-J., Rhim, H., & Park, M. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102349 · Cited by 16

Estrogen Modulates ubc9 Expression and Synaptic Redistribution in the Brain of APP/PS1 Mice and Cortical Neurons

Lai, Y., Liu, L., Hu, X., He, L., & Chen, G. (2017) · Journal of Molecular Neuroscience · doi:10.1007/s12031-017-0884-2 · Cited by 18

T217-Phosphorylation Exacerbates Tau Pathologies and Tau-Induced Cognitive Impairment

Wang, X., Liu, Q. R., Li, X., Zhou, Q., Wu, D., Li, S., Liu, Y., & Wang, J. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210297 · Cited by 17

Utilizing Optimized Tools to Investigate PTM Crosstalk: Identifying Potential PTM Crosstalk of Acetylated Mitochondrial Proteins

Horita, H. N., Law, A., & Middleton, K. M. (2018) · Proteomes · doi:10.3390/proteomes6020024 · Cited by 17

Current Understanding of Protein Aggregation in Neurodegenerative Diseases

Hu, C., Lin, M., Wang, C., & Zhang, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110568 · Cited by 21

Posttranslational modifications & lithium’s therapeutic effect—Potential biomarkers for clinical responses in psychiatric & neurodegenerative disorders

Khayachi, A., Schorova, L., Alda, M., Rouleau, G. A., & Milnerwood, A. J. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.05.002 · Cited by 15

Molecular signature for senile and complicated cataracts derived from analysis of sumoylation enzymes and their substrates in human cataract lenses

Liu, F., Fu, J., Wang, L., Nie, Q., Luo, Z., Hou, M., Yang, Y., Gong, X., Wang, Y., Xiao, Y., et al. (2020) · Aging Cell · doi:10.1111/acel.13222 · Cited by 16

High Fat Diet Mediates Amyloid-β Cleaving Enzyme 1 Phosphorylation and SUMOylation, Enhancing Cognitive Impairment in APP/PS1 Mice

Bao, J., Liang, Z., Gong, X., Yu, J. H., Xiao, Y., Liu, W. D., Wang, X., Wang, J., & Shu, X. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215299 · Cited by 16

TPPU protects tau from H2O2-induced hyperphosphorylation in HEK293/tau cells by regulating PI3K/AKT/GSK-3β pathway

Yao, E., Tang, Y., Liu, X.-H., & Wang, M.-H. (2016) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-016-1662-z · Cited by 16

The Involvement of Post-Translational Modifications in Regulating the Development and Progression of Alzheimer’s Disease

Guan, P.-P., & Wang, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03277-z · Cited by 15

Pharmacological Activities of Ginkgolic Acids in Relation to Autophagy

Ding, Y. F., Ding, Z., Xu, J., Li, Y., & Chen, M. (2022) · Pharmaceuticals · doi:10.3390/ph15121469 · Cited by 15

Therapeutic strategies for tauopathies and drug repurposing as a potential approach

Islam, M., Shen, F., Regmi, D., & Du, D. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.114979 · Cited by 14

The interplay between SUMOylation and phosphorylation of PKCδ facilitates oxidative stress‐induced apoptosis

Gao, S., Zhao, X., Hou, L., Ma, R., Zhou, J., Zhu, M. X., Pan, S., & Li, Y. (2021) · FEBS Journal · doi:10.1111/febs.16050 · Cited by 13

BACE1 SUMOylation deregulates phosphorylation and ubiquitination in Alzheimer's disease pathology

Zhao, Y., Zhou, H., Zhao, Y., Liang, Z., Gong, X., Yu, J., Huang, T., Yang, C., Wu, M., Xiao, Y., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15870 · Cited by 13

The hidden players: Shedding light on the significance of post-translational modifications and miRNAs in Alzheimer's disease development

Singh, R. J., Hussain, J., Kaur, A., Jamdare, B. G., Pathak, D., Garg, K., Kaur, R., Shankar, S., & Sunkaria, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102002 · Cited by 14

Developing Practical Therapeutic Strategies that Target Protein SUMOylation

Cox, O. F., & Huber, P. W. (2018) · Current Drug Targets · doi:10.2174/1389450119666181026151802 · Cited by 15

Oligodendrocyte Dysfunction in Tauopathy: A Less Explored Area in Tau-Mediated Neurodegeneration

Majumder, M., & Dutta, D. (2024) · Cells · doi:10.3390/cells13131112 · Cited by 14

SUMOylation of microtubule-cleaving enzyme KATNA1 promotes microtubule severing and neurite outgrowth

Li, S., Liang, Y., Zou, J., Cai, Z., Yang, H., Yang, J., Zhang, Y., Lin, H., Zhang, G., & Tan, M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102292 · Cited by 13

A novel cell-permeable peptide prevents protein SUMOylation and supports the mislocalization and aggregation of TDP-43

Marino, R., Buccarello, L., Hassanzadeh, K., Akhtari, K., Palaniappan, S., Corbo, M., & Feligioni, M. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106342 · Cited by 11

SUMOylation of Warts kinase promotes neural stem cell reactivation

Gao, Y., Tan, Y. S., Lin, J., Chew, L. Y., Aung, H. Y., Palliyana, B., Gujar, M. R., Lin, K., Kondo, S., & Wang, H. (2024) · Nature Communications · doi:10.1038/s41467-024-52569-y · Cited by 11

Effects of aerobic exercise on hippocampal SUMOylation in APP/PS1 transgenic mice

Zhang, C., Yu, H., Xia, J., Zhao, N., & Xu, B. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136303 · Cited by 10

Ubiquitination and SUMOylation of Amyloid and Amyloid-like Proteins in Health and Disease

Ford, L. K., Fioriti, L., & Kandel, E. R. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.195 · Cited by 10

Big versus small: The impact of aggregate size in disease

Hnath, B., Chen, J., Reynolds, J., Choi, E. S., Wang, J., Zhang, D., Sha, C. M., & Dokholyan, N. V. (2023) · Protein Science · doi:10.1002/pro.4686 · Cited by 8

Deciphering the endogenous SUMO-1 landscape: a novel combinatorial peptide enrichment strategy for global profiling and disease association

Zhang, X., Zhong, B., Sun, Y., Liu, D., Zhang, X., Wang, D., Wang, C., Gao, H., Zhong, M., Qin, H., et al. (2024) · Chemical Science · doi:10.1039/d4sc07379g · Cited by 8

Genetic and pharmacologic enhancement of SUMO2 conjugation prevents and reverses cognitive impairment and synaptotoxicity in a preclinical model of Alzheimer's disease

Fioriti, L., Wijesekara, N., Argyrousi, E. K., Matsuzaki, S., Takamura, H., Satoh, K., Han, K., Yamauchi, H., Staniszewski, A., Acquarone, E., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70030 · Cited by 8

Aging-associated REGγ proteasome decline predisposes to tauopathy

Tu, J., Zhang, H., Yang, T., Liu, Y., Kibreab, S., Zhang, Y., Gao, L., Moses, R. E., O’Malley, B. W., Xiao, J., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102571 · Cited by 9

Deep Phosphoproteomic Measurements Pinpointing Drug Induced Protective Mechanisms in Neuronal Cells

Yu, C., Gao, J., Zhou, Y., Chen, X., Xiao, R., Zheng, J., Liu, Y., & Zhou, H. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00635 · Cited by 8

Comprehensive review on Alzheimer's disease: From the posttranslational modifications of Tau to corresponding treatments

Li, X., Ba, Z., Huang, J., Chen, J., Jiang, J., Huang, N., & Luo, Y. (2024) · Ibrain · doi:10.1002/ibra.12176 · Cited by 7

Tau post-translational modifications in Alzheimer's disease: Insights into pathogenesis, therapeutic strategies, and diagnostic advances

Lei, H., Chen, X., Ruan, L., Liu, X., Ye, F., Li, K., Cheng, W., Yu, B., Di, C., & Di, C. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102927 · Cited by 7

Tau protein: Physiological functions and multifaceted roles in neurodegenerative and psychiatric disorders

Tang, F., Wei, J., Wong, M.-L., & Lei, P. (2025) · Genomic psychiatry : · doi:10.61373/gp025i.0122 · Cited by 7

Tau-aggregation inhibition: promising role of nanoencapsulated dietary molecules in the management of Alzheimer’s disease

Nagaraju, P. G., Ashwini, S., & G., P. P. C. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2092446 · Cited by 7

SARS-CoV-2 Nucleocapsid Protein Induces Tau Pathological Changes That Can Be Counteracted by SUMO2

Orsini, F., Bosica, M., Martucci, A., Paola, M. D., Comolli, D., Pascente, R., Forloni, G., Fraser, P. E., Arancio, O., & Fioriti, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137169 · Cited by 7

SUMO1 modification of 0N4R-tau is regulated by PIASx, SENP1, SENP2, and TRIM11

Wada, H., Maruyama, T., & Niikura, T. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101800 · Cited by 7

Molecular signatures of regional vulnerability to tauopathy in excitatory cortical neurons

Broekaart, D. W. M., Sharma, A., Ramakrishnan, A., Chongtham, A., Günther, D. M., Subramaniyan, S., Wang, M., Patel, V., Zhang, B., Grinberg, L. T., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02879-2 · Cited by 7

Untangling the Complexity and Impact of Tau Protein Ubiquitination

Trivellato, D., Munari, F., Assfalg, M., Capaldi, S., & D’Onofrio, M. (2024) · ChemBioChem · doi:10.1002/cbic.202400566 · Cited by 6

Ang II Promotes SUMO2/3 Modification of RhoGDI1 Through Aos1 and Uba2 Subunits, and then Regulates RhoGDI1 Stability and Cell Proliferation

Qi, Y., Guan, H., Liang, X., Sun, J., & Yao, W. (2021) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-021-07173-3 · Cited by 6

5-Heptadecylresorcinol alleviated high-fat diet induced obesity and insulin resistance by activating brown adipose tissue

Yang, Z., Yang, S., Wang, Z., Hao, Y., Wang, Z., Wei, Y., Ye, G., Liu, J., & Wang, J. (2023) · Food & Function · doi:10.1039/d3fo00071k · Cited by 6

TRIMming the tangles

Lei, P., & Ayton, S. (2023) · 中国科学通报：英文版 · doi:10.1016/j.scib.2023.09.019 · Cited by 6

Ginkgolic acid inhibited Tau phosphorylation and improved cognitive ability through the SUMO-1/GSK3β pathway in Aβ-Induced Alzheimer’s disease model rats

Chen, K., Shi, R., Huang, P., Guo, S., Hu, J., Han, B., Wang, P., Zou, Y., Tan, X., Li, L., et al. (2024) · Journal of Functional Foods · doi:10.1016/j.jff.2024.106183 · Cited by 6

Influence of Sox protein SUMOylation on neural development and regeneration

Chang, K. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.320968 · Cited by 6

The Cajal body marker protein coilin is SUMOylated and possesses SUMO E3 ligase-like activity

Lett, K. E., McLaurin, D. M., Tucker, S. K., & Hebert, M. D. (2023) · Frontiers in RNA Research · doi:10.3389/frnar.2023.1197990 · Cited by 6

Advances in Alzheimer’s disease: mechanistic insights and therapeutic targets

Jia, Y.-J., Ge, Y., Li, B., Yang, Y., Chen, H., Liu, J., Guo, J., Yu, J., Ye, K., Wang, J., et al. (2026) · Science China Life Sciences · doi:10.1007/s11427-025-2991-7 · Cited by 6

Landscape of Protein Post-Translational Modifications in Age-Related Neurodegenerative Disorders: Implications in Protein Aggregation, Altered Cellular Processes, and Therapeutics

Singh, A. K., & Kundu, T. K. (2026) · ACS Omega · doi:10.1021/acsomega.5c00905 · Cited by 5

Identification of a reciprocal negative feedback loop between tau-modifying proteins MARK2 kinase and CBP acetyltransferase

Tabassum, Z., Tseng, J., Isemann, C., Tian, X., Chen, Y., Herring, L. E., & Cohen, T. J. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101977 · Cited by 5

Polyubiquitination and SUMOylation Sites Regulate the Stability of ZO-2 Protein and the Sealing of Tight Junctions

Cano-Cortina, M., Alarcón, L., Miranda, J., Huber, O., & González‐Mariscal, L. (2022) · Cells · doi:10.3390/cells11203296 · Cited by 5

Molecular Mechanism of Tau Misfolding and Aggregation: Insights from Molecular Dynamics Simulation

Zhong, H., Liu, H., & Liu, H. (2023) · Current Medicinal Chemistry · doi:10.2174/0929867330666230409145247 · Cited by 5

SUMO2 rescues neuronal and glial cells from the toxicity of P301L Tau mutant

Orsini, F., Pascente, R., Martucci, A., Palacino, S., Fraser, P. E., Arancio, O., & Fioriti, L. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1437995 · Cited by 5

SUMO2 Protects Against Tau-induced Synaptic and Cognitive DysfunctionPreprint

Orsini, F., Argyrousi, E. K., Restelli, E., Ford, L. K., Takamura, H., Matsuzaki, S., Zentilin, L., Pascente, R., Kanaan, N. M., Soni, R. K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.11.516192 · Cited by 5

Targeted tau protein degradation: a promising therapeutic approach for tauopathies

Baazaoui, N., Alfaifi, M. Y., Shati, A. A., Saad, R. B., & Garzoli, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.11.041 · Cited by 5

Classification of helical polymers with deep-learning language models

Li, D., & Jiang, W. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.108041 · Cited by 4

The Dynamic SUMOylation Changes and Their Potential Role in the Senescence of APOE4 Mice

Xu, Y., Cai, W., Sang, S., Cheng, X., Jin, B., Zhao, X., & Zhong, C. (2023) · Biomedicines · doi:10.3390/biomedicines12010016 · Cited by 4

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Horita, H. N., Law, A., & Middleton, K. M. (2018) · Journal of Visualized Experiments · doi:10.3791/56912 · Cited by 4

Minimotifs dysfunction is pervasive in neurodegenerative disorders

Sharma, S., Young, R. J., Chen, J., Chen, X., Oh, E. C. T., & Schiller, M. R. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.005 · Cited by 4

SUMO inhibits Tau aggregation in Alzheimer’s disease

Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.02.001 · Cited by 4

A mass-producible macaque model displays a durable Alzheimer-like cognitive deficit and hallmark amyloid-β/tau/neurofilament light chain pathologies

He, F., Shi, W.-J., Liu, W., Fan, J.-X., He, Z., Zhang, Y., Xiao, J., Ruan, W., Gai, Y., Zhang, H., et al. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251334316 · Cited by 4

Biomolecular phase separation of microtubule-associated protein tau and its role in the genesis of brain disorders

Bhandari, A. K., Dhami, A. S., Hemanthlumar, R. T., Mishra, N., Joslyn, B., Roy, S., Srinivasan, J., Prajapati, K. P., Kar, K., & Anand, B. G. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102879 · Cited by 4

Death-associated protein kinase 1-dependent SENP1 degradation increases tau SUMOylation and leads to cognitive dysfunction in a mouse model for tauopathy

Shui, X., Zheng, X., Wu, J., Zhang, M., Kim, G., Chen, R., Peng, L., Wang, Z., Zheng, Y., Zhang, L., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00911-3 · Cited by 4

Tau protein aggregation: A therapeutic target for neurodegenerative diseases

Duggal, A., Mahindru, D., Baghel, K., Mehrotra, S., & Prajapati, V. K. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.11.012 · Cited by 2

Cycloheximide Treatment Causes a ZVAD-Sensitive Protease-Dependent Cleavage of Human Tau in Drosophila Cells

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