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

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

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,296

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

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480

SUMO

Hay, R. T. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.012 · Cited by 1,656

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

Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588

SUMO-1 Modification of IκBα Inhibits NF-κB Activation

Desterro, J. M. P., Rodríguez, M. S., & Hay, R. T. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80133-1 · Cited by 1,050

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

Alonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859

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

Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843

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

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779

Tau in physiology and pathology

Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251

Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies.

Zhang, J., Zhang, Y., Wang, J., Xia, Y., Zhang, J., & Chen, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01911-3 · Cited by 1,138

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994

Control of protein stability by post-translational modifications

Lee, J. M., Hammarén, H. M., Savitski, M. M., & Baek, S. H. (2023) · Nature Communications · doi:10.1038/s41467-023-35795-8 · Cited by 896

Phosphorylated Tau in Alzheimer’s Disease and Other Tauopathies

Rawat, P., Sehar, U., Bisht, J., Selman, A., Culberson, J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112841 · Cited by 509

Current understanding of metal ions in the pathogenesis of Alzheimer’s disease

Wang, L., Yin, Y.-L., Liu, X.-Z., Shen, P., Zheng, Y.-G., Lan, X.-R., Lu, C.-B., & Wang, J.-Z. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00189-z · Cited by 454

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442

Alzheimer’s disease: insights into pathology, molecular mechanisms, and therapy

Zheng, Q., & Wang, X. (2024) · Protein & Cell · doi:10.1093/procel/pwae026 · Cited by 483

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains

Arakhamia, T., Lee, C. E., Carlomagno, Y., Kumar, M., Duong, D. M., Wesseling, H., Kundinger, S. R., Wang, K., Williams, D., Deture, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.01.027 · Cited by 411

Phosphorylation of different tau sites during progression of Alzheimer’s disease

Neddens, J., Temmel, M., Flunkert, S., Kerschbaumer, B., Hoeller, C., Loeffler, T., Niederkofler, V., Daum, G., Attems, J., & Hutter-Paier, B. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0557-6 · Cited by 384

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367

A walk through tau therapeutic strategies

Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 299

Tau Proteins and Tauopathies in Alzheimer’s Disease

Chong, F. P., Ng, K. Y., Koh, R. Y., & Chye, S. M. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0574-1 · Cited by 260

Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts

Celen, A. B., & Şahin, U. (2020) · FEBS Journal · doi:10.1111/febs.15319 · Cited by 252

Protein SUMOylation modification and its associations with disease

Yang, Y., He, Y., Wang, X., liang, Z., He, G., Zhang, P., Zhu, H., Xu, N., & Liang, S. (2017) · Open Biology · doi:10.1098/rsob.170167 · Cited by 216

MAPT/Tau accumulation represses autophagy flux by disrupting IST1-regulated ESCRT-III complex formation: a vicious cycle in Alzheimer neurodegeneration

Feng, Q., Luo, Y., Zhang, X., Yang, X., Hong, X.-Y., Sun, D., Li, X., Hu, Y., Li, X., Zhang, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1633862 · Cited by 213

Updates in Alzheimer's disease: from basic research to diagnosis and therapies

Liu, E., Zhang, Y., & Wang, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00432-x · Cited by 241

It’s all about tau

Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207

SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation

Rott, R., Szargel, R., Shani, V., Hamza, H., Savyon, M., Elghani, F. A., Bandopadhyay, R., & Engelender, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704351114 · Cited by 196

Tau accumulation induces synaptic impairment and memory deficit by calcineurin-mediated inactivation of nuclear CaMKIV/CREB signaling

Yin, Y., Gao, D., Wang, Y., Wang, Z.-H., Wang, X., Ye, J., Wu, D., Fang, L., Pi, G., Yang, Y., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604519113 · Cited by 179

Modifications and Trafficking of APP in the Pathogenesis of Alzheimer’s Disease

Wang, X., Zhou, X., Li, G., Zhang, Y., Wu, Y., & Song, W. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00294 · Cited by 183

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 169

Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168

Amyloidogenesis of Tau protein

Niżyński, B., Dzwolak, W., & Nieznański, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 166

Discovering the landscape of protein modifications

Keenan, E. K., Zachman, D. K., & Hirschey, M. D. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.015 · Cited by 160

Palmitoylation in Alzheimers disease and other neurodegenerative diseases

Cho, E., & Park, M. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.06.008 · Cited by 151

Lysine-Directed Post-translational Modifications of Tau Protein in Alzheimer's Disease and Related Tauopathies

Kontaxi, C., Piccardo, P., & Gill, A. C. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00056 · Cited by 138

Relevance of Phosphorylation and Truncation of Tau to the Etiopathogenesis of Alzheimer’s Disease

Zhou, Y., Shi, J., Chu, D., Hu, W. H., Guan, Z., Gong, C., Iqbal, K., & Liu, F. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00027 · Cited by 130

Tau interactome mapping based identification of Otub1 as Tau deubiquitinase involved in accumulation of pathological Tau forms in vitro and in vivo

Wang, P., Joberty, G., Buist, A., Vanoosthuyse, A., Stancu, I., Vasconcelos, B., Pierrot, N., Faelth-Savitski, M., Kienlen‐Campard, P., Octave, J., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1663-9 · Cited by 120

Methylation as a key regulator of Tau aggregation and neuronal health in Alzheimer’s disease

Balmik, A. A., & Chinnathambi, S. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00732-z · Cited by 110

Amyloid, tau, pathogen infection and antimicrobial protection in Alzheimer’s disease –conformist, nonconformist, and realistic prospects for AD pathogenesis

Li, H., Liu, C.-C., Zheng, H., & Huang, T. Y. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0139-3 · Cited by 103

Pathological Changes of Tau Related to Alzheimer’s Disease

Chu, D., & Liu, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00457 · Cited by 106

Ubiquitin-dependent and independent roles of SUMO in proteostasis

Liebelt, F., & Vertegaal, A. C. O. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00091.2016 · Cited by 101

Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies

Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 119

Asperterpenes A and B, two unprecedented meroterpenoids from Aspergillus terreus with BACE1 inhibitory activities

Qi, C., Bao, J., Wang, J., Zhu, H., Xue, Y., Wang, X., Li, H., Sun, W., Gao, W., Lai, Y., et al. (2016) · Chemical Science · doi:10.1039/c6sc02464e · Cited by 96

A farnesyltransferase inhibitor activates lysosomes and reduces tau pathology in mice with tauopathy

Hernández, I., Luna, G., Rauch, J. N., Reis, S. A., Giroux, M., Karch, C. M. M., Boctor, D., Sibih, Y., Storm, N. J., Díaz, A., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aat3005 · Cited by 95

Sumoylation in Physiology, Pathology and Therapy

Şahin, U., de Thé, H., & Lallemand-Breitenbach, V. (2022) · Cells · doi:10.3390/cells11050814 · Cited by 98

Small molecule therapeutics for tauopathy in Alzheimer’s disease: Walking on the path of most resistance

Wang, L., Bharti, Kumar, R., Pavlov, P. F., & Winblad, B. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112915 · Cited by 92

Liquid–liquid phase separation of Tau by self and complex coacervation

Najafi, S., Lin, Y., Longhini, A. P., Zhang, X., Delaney, K. T., Kosik, K. S., Fredrickson, G. H., Shea, J., & Han, S. (2021) · Protein Science · doi:10.1002/pro.4101 · Cited by 90

Alpha-Synuclein Post-translational Modifications: Implications for Pathogenesis of Lewy Body Disorders

Manzanza, N. D. O., Sedlackova, L., & Kalaria, R. N. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.690293 · Cited by 98

A novel dephosphorylation targeting chimera selectively promoting tau removal in tauopathies

Zheng, J., Tian, N., Liu, F., Zhang, Y., Su, J., Gao, Y., Deng, M., Wei, L., Ye, J., Li, H., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00669-2 · Cited by 78

Extranuclear SUMOylation in Neurons

Henley, J. M., Carmichael, R. E., & Wilkinson, K. A. (2018) · Trends in Neurosciences · doi:10.1016/j.tins.2018.02.004 · Cited by 81

Composition of the Intranuclear Inclusions of Fragile X-associated Tremor/Ataxia Syndrome

Ma, L., Herren, A. W., Espinal, G. M., Randol, J. L., McLaughlin, B. E., Martínez‐Cerdeño, V., Pessah, I. N., Hagerman, R. J., & Hagerman, P. J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0796-1 · Cited by 78

Autophagic Pathways to Clear the Tau Aggregates in Alzheimer’s Disease

Gorantla, N. V., & Chinnathambi, S. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00897-0 · Cited by 74

Human Tau Isoforms and Proteolysis for Production of Toxic Tau Fragments in Neurodegeneration

Boyarko, B., & HOOK, V. Y. H. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.702788 · Cited by 81

The Role of Post-Translational Modifications on the Structure and Function of Tau Protein

Ye, H., Han, Y., Li, P., Su, Z., & Huang, Y. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02002-0 · Cited by 76

The Crosstalk Between Pathological Tau Phosphorylation and Mitochondrial Dysfunction as a Key to Understanding and Treating Alzheimer’s Disease

Guha, S. K., Johnson, G. V. W., & Nehrke, K. W. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02084-0 · Cited by 77

Role of Post‐translational Modifications in Alzheimer's Disease

Ramesh, M., Gopinath, P., & Govindaraju, T. (2019) · ChemBioChem · doi:10.1002/cbic.201900573 · Cited by 68

Sumoylation in Synaptic Function and Dysfunction

Schorova, L., & Martin, S. (2016) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2016.00009 · Cited by 72

Role of microtubule-associated protein tau phosphorylation in Alzheimer’s disease

Ma, R.-H., Zhang, Y., Hong, X.-Y., Zhang, J., Wang, J., & Liu, G. (2017) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-017-1732-x · Cited by 66

Targeting tau in Alzheimer's disease: from mechanisms to clinical therapy

Ye, J., Wan, H., Chen, S., & Liu, G. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385847 · Cited by 74

SUMOylation in Neurodegenerative Diseases

Princz, A., & Tavernarakis, N. (2019) · Gerontology · doi:10.1159/000502142 · Cited by 62

Ubiquitin and Ubiquitin-like Proteins in Cancer, Neurodegenerative Disorders, and Heart Diseases

Hwang, J., Lee, A., & Kho, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095053 · Cited by 63

Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease

Cario, A., & Berger, C. L. (2023) · BioEssays · doi:10.1002/bies.202200138 · Cited by 70

Sumoylation: Implications for Neurodegenerative Diseases

Anderson, D. B., Zanella, C. A., Henley, J. M., & Cimarosti, H. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50044-7_16 · Cited by 63

Role of SUMOylation in Neurodegenerative Diseases

Mandel, N., & Agarwal, N. (2022) · Cells · doi:10.3390/cells11213395 · Cited by 62

Protein aggregation and its affecting mechanisms in neurodegenerative diseases

Wu, J., Wu, J., Chen, T., Cai, J., & Ren, R. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105880 · Cited by 62

Acetylated tau exacerbates learning and memory impairment by disturbing with mitochondrial homeostasis

Liu, Q., Wang, X., Hu, Y., Zhao, J.-N., Huang, C.-H., Li, T., Zhang, B.-G., He, Y., Wu, Y.-Q., Zhang, Z.-J., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102697 · Cited by 58

Posttranslational Modifications of α-Synuclein, Their Therapeutic Potential, and Crosstalk in Health and Neurodegenerative Diseases

Hassanzadeh, K., Liu, J., Maddila, S. C., & Mouradian, M. M. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.123.001111 · Cited by 56

BACE1 SUMOylation increases its stability and escalates the protease activity in Alzheimer’s disease

Bao, J., Qin, M., Mahaman, Y. A. R., Zhang, B., Huang, F., Zeng, K., Xia, Y., Ke, D., Wang, Q., Liu, R., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800498115 · Cited by 50

Epigallocatechin-3-gallate modulates Tau Post-translational modifications and cytoskeletal network

Sonawane, S. K., & Chinnathambi, S. (2021) · Oncotarget · doi:10.18632/oncotarget.27963 · Cited by 51

SUMOylation-Mediated Response to Mitochondrial Stress

He, J., Cheng, J., & Wang, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165657 · Cited by 56

Tau Spreading Mechanisms; Implications for Dysfunctional Tauopathies

Fuster-Matanzo, A., Hernández, F., & Ávila, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030645 · Cited by 50

SUMO paralogue–specific functions revealed through systematic analysis of human knockout cell lines and gene expression data

Bouchard, D., Wang, W., Yang, W.-C., He, S., Garcia, A., & Matunis, M. J. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-01-0031 · Cited by 47

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms

Yang, Y., & Wang, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170788 · Cited by 46

Paralogue-Specific Roles of SUMO1 and SUMO2/3 in Protein Quality Control and Associated Diseases

Wang, W., & Matunis, M. J. (2023) · Cells · doi:10.3390/cells13010008 · Cited by 45

Cytoskeletal Proteins and Alzheimer’s Disease Pathogenesis: Focusing on the Interplay with Tau Pathology

Jiang, G., Xie, G., Li, X., & Xiong, J. (2025) · Biomolecules · doi:10.3390/biom15060831 · Cited by 48

Sex Differences in the Cognitive and Hippocampal Effects of Streptozotocin in an Animal Model of Sporadic AD

Bao, J., Mahaman, Y. A. R., Liu, R., Wang, J., Zhang, Z., Zhang, B., & Wang, X. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00347 · Cited by 47

A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function

Dustrude, E. T., Perez‐Miller, S., François‐Moutal, L., Moutal, A., Khanna, M., & Khanna, R. (2017) · Channels · doi:10.1080/19336950.2017.1299838 · Cited by 44

Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders

Loh, D., & Reiter, R. J. (2021) · Antioxidants · doi:10.3390/antiox10091483 · Cited by 45

Experimental Evidence of the Benefits of Acupuncture for Alzheimer's Disease: An Updated Review

Yu, C.-C., Du, Y., Wang, S., Liu, L.-B., Shen, F., Wang, L., Lin, Y.-F., & Kong, L.-H. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.549772 · Cited by 43

To target Tau pathologies, we must embrace and reconstruct their complexities

Limorenko, G., & Lashuel, H. A. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105536 · Cited by 41

USP10 deubiquitinates Tau, mediating its aggregation

Wei, Z. C., Zeng, K., Hu, J., Li, X., Huang, F., Zhang, B., Wang, J., Liu, R., Li, H., & Wang, X. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05170-4 · Cited by 44

ASC-J9 ® suppresses prostate cancer cell invasion via altering the sumoylation-phosphorylation of STAT3

Lin, W.-Y., Luo, J., Sun, Y., Lin, C.-Y., Li, G., Niu, Y., & Chang, C. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.02.007 · Cited by 40

Signaling pathways and posttranslational modifications of tau in Alzheimer's disease: the humanization of yeast cells

Heinisch, J. J., & Brandt, R. (2016) · Microbial Cell · doi:10.15698/mic2016.04.489 · Cited by 41

SUMOylation Prevents Huntingtin Fibrillization and Localization onto Lipid Membranes

Sedighi, F., Adegbuyiro, A., & Legleiter, J. A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00509 · Cited by 40

SUMOylation in α-Synuclein Homeostasis and Pathology

Savyon, M., & Engelender, S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00167 · Cited by 39

The function of SUMOylation and its crucial roles in the development of neurological diseases

Chen, X., Zhang, Y., Wang, Q., Qin, Y., Yang, X., Xing, Z., Shen, Y., Wu, H., & Qi, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202002702r · Cited by 39

The propagation mechanisms of extracellular tau in Alzheimer’s disease

Wei, Y., Liu, M., & Wang, D. (2021) · Journal of Neurology · doi:10.1007/s00415-021-10573-y · Cited by 40

SUMO1 impact on Alzheimer disease pathology in an amyloid-depositing mouse model

Knock, E., Matsuzaki, S., Takamura, H., Satoh, K., Rooke, G., Han, K., Zhang, H., Staniszewski, A., Katayama, T., Arancio, O., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.11.015 · Cited by 37

Drp1 SUMO/deSUMOylation by Senp5 isoforms influences ER tubulation and mitochondrial dynamics to regulate brain development

Yamada, S., Sato, A., Ishihara, N., Akiyama, H., & Sakakibara, S. (2021) · iScience · doi:10.1016/j.isci.2021.103484 · Cited by 37

Sequential posttranslational modifications regulate PKC degradation

Wang, Y., Wang, Y., Zhang, H., Gao, Y., Huang, C., Zhou, A., Zhou, Y., & Li, Y. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-09-0624 · Cited by 36

SUMOylation of the transcription factor ZFHX3 at Lys-2806 requires SAE1, UBC9, and PIAS2 and enhances its stability and function in cell proliferation

Wu, R., Fang, J., Liu, M., Jun, A., Liu, J., Chen, W., Li, J., Ma, G., Zhang, Z., Zhang, B., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012338 · Cited by 36

Tau in Alzheimer’s Disease: Pathological Alterations and an Attractive Therapeutic Target

Gu, J., & Liu, F. (2020) · Current Medical Science · doi:10.1007/s11596-020-2282-1 · Cited by 41

RhoGDI stability is regulated by SUMOylation and ubiquitination via the AT1 receptor and participates in Ang II-induced smooth muscle proliferation and vascular remodeling

Dai, F., Qi, Y., Guan, W., Meng, G., Liu, Z., Zhang, T., & Yao, W. (2019) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2019.07.010 · Cited by 35

Activating transcription factor 3 SUMOylation is involved in angiotensin II-induced endothelial cell inflammation and dysfunction

Zhang, Z.-B., Ruan, C., Chen, D.-R., Zhang, K., Chen, Y., & Gao, P. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.02.001 · Cited by 34

Tau Post-Translational Modifications: Potentiators of Selective Vulnerability in Sporadic Alzheimer’s Disease

Carroll, T., Guha, S. K., Nehrke, K. W., & Johnson, G. V. W. (2021) · Biology · doi:10.3390/biology10101047 · Cited by 39

Intracellular and extracellular microtubule associated protein tau as a therapeutic target in Alzheimer disease and other tauopathies

Ávila, J., Pallas‐Bazarra, N., Bolós, M., Sayas, C. L., & Hernández, F. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1131269 · Cited by 36

Genetic Analyses of Alzheimer’s Disease in China: Achievements and Perspectives

Zhang, D., Xu, M., Bi, R., & Yao, Y. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00435 · Cited by 32

PDPK1 regulates autophagosome biogenesis by binding to PIK3C3

Hu, B., Zhang, Y., Deng, T., Gu, J., Liu, J., Yang, H. M., Xu, Y., Yan, Y., Yang, F., Zhang, H., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1817279 · Cited by 32

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

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

SUMOylation as a Therapeutic Target for Myocardial Infarction

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Free d-aspartate triggers NMDA receptor-dependent cell death in primary cortical neurons and perturbs JNK activation, Tau phosphorylation, and protein SUMOylation in the cerebral cortex of mice lacking d-aspartate oxidase activity

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