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Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome
Open accessAbstract
Adults with Down syndrome (DS) develop Alzheimer neurofibrillary degeneration in the brain, but the underlying molecular mechanism is unknown. Here, we report that the presence of an extra copy of the dual‐specificity tyrosine‐phosphorylated and regulated kinase 1A ( Dyrk1A ) gene due to trisomy 21 resulted in overexpression of Dyrk1A and elevated kinase activity in DS brain. Dyrk1A phosphorylated tau at several sites, and these sites were hyperphosphory‐lated in adult DS brains. Phosphorylation of tau by Dyrk1A primed its further phosphorylation by glycogen synthase kinase‐3β (GSK‐3β). Dyrk1A‐induced tau phosphorylation inhibited tau's biological activity and promoted its self‐aggregation. In Ts65Dn mouse brain, an extra copy of the Dyrk1A gene caused increased expression and activity of Dyrk1A and resulted in increased tau phosphorylation. These findings strongly suggest a novel mechanism by which the overexpression of Dyrk1A in DS brain causes neurofibrillary degeneration via hyperphosphorylating tau. Liu, F., Liang, Z., Wegiel, J., Hwang, Y.‐W., Iqbal, K., Grundke‐Iqbal, I., Ramakrishna, N., Gong, C.‐X. Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome. FASEB J. 22, 3224–3233 (2008)
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“An approximate 1.5-fold increase in DYRK1A was found in homogenates from brains from human adults with DS and ~ 1.5-fold increase in DYRK1A from brain homogenates from 15-month-old Ts65Dn mice was observed (Liu et al., 2008).”
From Sex-specific developmental alterations in DYRK1A expression in the brain of a Down syndrome mouse model (2024) · cites this paper as Liu et al., 2008
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“An approximate 1.5-fold increase in DYRK1A was found in homogenates from brains from human adults with DS and ~ 1.5-fold increase in DYRK1A from brain homogenates from 15-month-old Ts65Dn mice was observed (Liu et al., 2008).”
From Sex-specific developmental alterations in DYRK1A expression in the brain of a Down syndrome mouse model (2024) · cites this paper as Liu et al., 2008
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Cites
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
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668
Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780
Self-citationThe specificities of protein kinase inhibitors: an update
BAIN, J., McLAUCHLAN, H., ELLIOTT, M., & COHEN, P. (2003) · Biochemical Journal · doi:10.1042/bj20021535 · Cited by 1,369 · cited 1×
“To verify the specificity of the assay, we added 10 M epigallocatechin-3-gallate (EGCG), a selective Dyrk1A inhibitor (22) into the assay mixture and found that EGCG inhibited 80% of the kinase activity in the brain extracts (Fig.”
MethodOccurrence of neuropathological changes and dementia of Alzheimer’s disease in Down’s syndrome
Wisniewski, K. E., Wisniewski, H. M., & Wen, G. Y. (1985) · Annals of Neurology · doi:10.1002/ana.410170310 · Cited by 1,159
Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903
Alonso, A. D. C., Zaidi, T., Novak, M., Grundke-Iqbal, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 827
Self-citationLiu, F., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04391.x · Cited by 759
Self-citationRole of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease.
Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5562 · Cited by 738
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Ballard, C., Gauthier, S., Corbett, A., Brayne, C., Aarsland, D., & Jones, E. (2011) · The Lancet · doi:10.1016/s0140-6736(10)61349-9 · Cited by 2,336
Antonarakis, S. E., Skotko, B. G., Rafii, M. S., Strydom, A., Pape, S. E., Bianchi, D. W., Sherman, S. L., & Reeves, R. H. (2020) · Nature Reviews Disease Primers · doi:10.1038/s41572-019-0143-7 · Cited by 964
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Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806
Self-citationMechanisms of tau-induced neurodegeneration
Iqbal, K., Liu, F., Gong, C.-X., Alonso, A. D. C., & Grundke-Iqbal, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0486-3 · Cited by 628
Self-citationA genetic cause of Alzheimer disease: mechanistic insights from Down syndrome
Wiseman, F. K., Al-Janabi, T., Hardy, J., Karmiloff-Smith, A., Nizetic, D., Tybulewicz, V. L. J., Fisher, E. M. C., & Strydom, A. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3983 · Cited by 562
Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction
Mietelska‐Porowska, A., Wasik, U., Goras, M., Filipek, A., & Niewiadomska, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034671 · Cited by 431
Dementia in Down syndrome: unique insights for Alzheimer disease research
Lott, I. T., & Head, E. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0132-6 · Cited by 383
Personality and risk of Alzheimer's disease: New data and meta‐analysis
Terracciano, A., Sutin, A. R., An, Y., O’Brien, R., Ferrucci, L., Zonderman, A. B., & Resnick, S. M. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.03.002 · Cited by 345
Down syndrome and Alzheimer's disease: common pathways, common goals
Hartley, D., Blumenthal, T., Carrillo, M., DiPaolo, G., Esralew, L., Gardiner, K., Granholm, A.-C., Iqbal, K., Krams, M., Lemere, C., et al. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.10.007 · Cited by 290
Self-citationThe role of DYRK1A in neurodegenerative diseases
Węgiel, J., Gong, C., & Hwang, Y. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07955.x · Cited by 307
Self-citationHarmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation
Göckler, N., Jofré, G., Papadopoulos, C., Soppa, U., Tejedor, F., & Becker, W. (2009) · The FEBS Journal · doi:10.1111/j.1742-4658.2009.07346.x · Cited by 266
Development of a novel selective inhibitor of the Down syndrome-related kinase Dyrk1A
Ogawa, Y., Nonaka, Y., Goto, T., Ohnishi, E., Hiramatsu, T., Kii, I., Yoshida, M., Ikura, T., Onogi, H., Shibuyà, H., et al. (2010) · Nature Communications · doi:10.1038/ncomms1090 · Cited by 276
Down syndrome--recent progress and future prospects
Wiseman, F. K., Alford, K. A., Tybulewicz, V. L. J., & Fisher, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp010 · Cited by 259
Deng, Y., Li, B., Liu, Y. M., Iqbal, K., Grundke, I., & Gong, C. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090157 · Cited by 233
Self-citationPhosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration
Alonso, A. D., Di Clerico, J., Li, B., Corbo, C. P., Alaniz, M. E., Grundke-Iqbal, I., & Iqbal, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110957 · Cited by 236
Self-citationMicroRNA: Implications for Alzheimer Disease and other Human CNS Disorders
Maes, O. C., Chertkow, H. M., Wang, E., & Schipper, H. M. (2009) · Current Genomics · doi:10.2174/138920209788185252 · Cited by 223
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
Duchon, A., & Herault, Y. (2016) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2016.00104 · Cited by 181
Shi, J., Zhang, T., Zhou, C., Chohan, M. O., Gu, X., Węgiel, J., Zhou, J., Hwang, Y., Iqbal, K., Grundke, I., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802645200 · Cited by 179
Self-citationDevelopmental regulation of tau phosphorylation, tau kinases, and tau phosphatases
Yu, Y., Run, X., Liang, Z., Li, Y., Liu, F., Liu, Y. M., Iqbal, K., Grundke, I., & Gong, C. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05882.x · Cited by 186
Self-citationDYRK1A and cognition: A lifelong relationship
Arbonés, M. L., Thomazeau, A., Nakano-Kobayashi, A., Hagiwara, M., & Delabar, J. M. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.09.010 · Cited by 174
Lee, G. S., & Leugers, C. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00004-7 · Cited by 173
Hamzé, R., Delangre, E., Tolu, S., Moreau, M., Janel, N., Bailbé, D., & Movassat, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315287 · Cited by 171
Soundararajan, M., Roos, A. K., Savitsky, P. A., Filippakopoulos, P., Kettenbach, A. N., Olsen, J. V., Gerber, S. A., Eswaran, J., Knapp, S., & Elkins, J. M. (2013) · Structure · doi:10.1016/j.str.2013.03.012 · Cited by 160
Neuropathological role of PI3K/Akt/mTOR axis in Down syndrome brain
Perluigi, M., Pupo, G., Tramutola, A., Cini, C., Coccia, R., Barone, E., Head, E., Butterfield, D. A., & Di Domenico, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.04.007 · Cited by 155
DYRK1A in neurodegeneration and cancer: Molecular basis and clinical implications
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Basheer, N., Smolek, T., Hassan, I., Liu, F., Iqbal, K., Zilka, N., & Novak, P. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02113-z · Cited by 159
Self-citationSmith, B. E., Medda, F., Gokhale, V. M., Dunckley, T. L., & Hulme, C. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300094k · Cited by 156
Down syndrome: searching for the genetic culprits
Lana‐Elola, E., Watson-Scales, S., Fisher, E., & Tybulewicz, V. L. J. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.008078 · Cited by 145
Communication breaks-Down: From neurodevelopment defects to cognitive disabilities in Down syndrome
Contestabile, A., Benfenati, F., & Gasparini, L. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.01.003 · Cited by 134
Dyrk1 inhibition improves Alzheimer's disease‐like pathology
Branca, C., Shaw, D. M., Belfiore, R., Gokhale, V. M., Shaw, A. Y., Foley, C., Smith, B. E., Hulme, C., Dunckley, T. L., Meechoovet, B., et al. (2017) · Aging Cell · doi:10.1111/acel.12648 · Cited by 132
Aneuploidy: From a Physiological Mechanism of Variance to Down Syndrome
Dierssen, M., Hérault, Y., & Estivill, X. (2009) · Physiological Reviews · doi:10.1152/physrev.00032.2007 · Cited by 143
Lü, J., Jun-Ye, M. I. A. O., Su, T., Liu, Y., & He, R. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.028 · Cited by 132
Tauopathy: A common mechanism for neurodegeneration and brain aging
Saha, P., & Sen, N. (2019) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2019.01.007 · Cited by 134
Węgiel, J., Dowjat, K., Kaczmarski, W., Kuchna, I., Nowicki, K., Frackowiak, J., Mazur‐Kolecka, B., Wegiel, J., Silverman, W. P., Reisberg, ., et al. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0419-6 · Cited by 113
Self-citationHyperphosphorylation-Induced Tau Oligomers
Iqbal, K., Gong, C., & Liu, F. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00112 · Cited by 120
Self-citationJin, N., Yin, X., Yu, D., Cao, M., Gong, C., Iqbal, K., Ding, F., Gu, X., & Liu, F. (2015) · Scientific Reports · doi:10.1038/srep08187 · Cited by 111
Self-citationNew Perspectives of Dyrk1A Role in Neurogenesis and Neuropathologic Features of Down Syndrome
Park, J., & Chung, K. C. (2013) · Experimental Neurobiology · doi:10.5607/en.2013.22.4.244 · Cited by 106
Intranasal rapamycin ameliorates Alzheimer-like cognitive decline in a mouse model of Down syndrome
Tramutola, A., Lanzillotta, C., Barone, E., Arena, A., Zuliani, I., Mosca, L., Blarzino, C., Butterfield, D. A., Marzia Perluigi, A., & Domenico, F. D. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0133-9 · Cited by 102
García-Cerro, S., Rueda, N., Vidal, V., Lantigua, S., & Martínez-Cué, C. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.06.010 · Cited by 100
Węgiel, J., Kaczmarski, W., Barua, M., Kuchna, I., Nowicki, K., Wang, K.-C., Wegiel, J., Mazur‐Kolecka, B., Frackowiak, J., Mazur‐Kolecka, B., et al. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318202bfa1 · Cited by 98
Self-citationYin, X., Jin, N., Shi, J., Zhang, Y., Wu, Y., Gong, C.-X., Iqbal, K., & Liu, F. (2017) · Scientific Reports · doi:10.1038/s41598-017-00682-y · Cited by 93
Self-citationThe genomically mosaic brain: Aneuploidy and more in neural diversity and disease
Bushman, D. M., & Chun, J. J. M. (2013) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.02.003 · Cited by 93
Yin, X., Jin, N., Gu, J., Shi, J., Zhou, J., Gong, C., Iqbal, K., Grundke, I., & Liu, F. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355412 · Cited by 93
Self-citationScales, T., Lin, S., Kraus, M., Goold, R., & Gordon-Weeks, P. (2009) · Journal of Cell Science · doi:10.1242/jcs.040162 · Cited by 4
Selective inhibition of the kinase DYRK1A by targeting its folding process
Kii, I., Sumida, Y., Goto, T., Sonamoto, R., Okuno, Y., Yoshida, S., Kato‐Sumida, T., Koike, Y., Abe, M., Nonaka, Y., et al. (2016) · Nature Communications · doi:10.1038/ncomms11391 · Cited by 94
Di Domenico, F., Tramutola, A., Foppoli, C., Head, E., Perluigi, M., & Butterfield, D. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.009 · Cited by 89
Neuroimaging and other modalities to assess Alzheimer's disease in Down syndrome
Neale, N., Padilla, C., Fonseca, L. M., Holland, T., & Zaman, S. H. (2017) · NeuroImage Clinical · doi:10.1016/j.nicl.2017.10.022 · Cited by 91
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Demuro, S., Martino, R. M. C. D., Ortega, J. A., & Cavalli, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169098 · Cited by 88
Park, J., Oh, Y., & Chung, K. C. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.1.006 · Cited by 86
Lott, I. T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.010 · Cited by 86
Protein Phosphorylation is a Key Mechanism in Alzheimer’s Disease
Oliveira, J. M., Costa, M. G. C., Cachide, M., Silva, O. A. B. D. C. E., & Henriques, A. G. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170176 · Cited by 84
Dyrk1A Inhibition as Potential Treatment for Alzheimer’S Disease
Stotani, S., Giordanetto, F., & Medda, F. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0013 · Cited by 78
Sitz, J. H., Baumgärtel, K., Hämmerle, B., Papadopoulos, C., Hekerman, P., Tejedor, F. J., Becker, W. B., & Lutz, B. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.09.034 · Cited by 79
Atas-Ozcan, H., Brault, V., Duchon, A., & Herault, Y. (2021) · Genes · doi:10.3390/genes12111833 · Cited by 78
The DREAM complex functions as conserved master regulator of somatic DNA-repair capacities
Bujarrabal-Dueso, A., Sendtner, G., Meyer, D. H., Chatzinikolaou, G., Stratigi, K., Garinis, G. A., & Schumacher, B. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00942-8 · Cited by 79
Dang, T., Duan, W. Y., Yu, B., Tong, D. L., Cheng, C., Zhang, Y. F., Wu, W., Ye, K., Zhang, W. X., Wu, M., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.253 · Cited by 80
Naert, G., Ferré, V. M., Meunier, J., Keller, E., Malmström, S., Givalois, L., Carreaux, F., Bazureau, J. P., & Maurice, T. (2015) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2015.03.018 · Cited by 77
Gourdain, S., Dairou, J., Denhez, C., Bui, L. C., Rodrigues‐Lima, F., Janel, N., Delabar, J. M., Cariou, K., & Dodd, R. H. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401049v · Cited by 79
Nakano-Kobayashi, A., Awaya, T., Kii, I., Sumida, Y., Okuno, Y., Yoshida, S., Sumida, T., Inoue, H., Hosoya, T., & Hagiwara, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704143114 · Cited by 76
Melchior, B., Mittapalli, G. K., Lai, C., Duong‐Polk, K., Stewart, J., Güner, B., Hofilena, B. J., Tjitro, A., Anderson, S., Herman, D. S., et al. (2019) · Aging Cell · doi:10.1111/acel.13000 · Cited by 73
Gerson, J. E., Castillo‐Carranza, D. L., & Kayed, R. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500143n · Cited by 75
Jin, N., Yin, X., Gu, J., Zhang, X., Shi, J., Qian, W., Ji, Y., Cao, M., Gu, X., Ding, F., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645507 · Cited by 74
Self-citationMaurice, T. (2015) · Behavioural Brain Research · doi:10.1016/j.bbr.2015.09.020 · Cited by 69
Martin, L., Page, G., & Terro, F. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.05.010 · Cited by 68
Schmitt, C., Kail, D., Mariano, M., Empting, M., Weber, N., Paul, T., Hartmann, R. W., & Engel, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087851 · Cited by 64
Role of Tau Protein in Neuronal Damage in Alzheimer's Disease and Down Syndrome
Cárdenas, A. M., Ardiles, Á. O., Barraza, N., Báez‐Matus, X., & Caviedes, P. A. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.012 · Cited by 68
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Hefti, M. M., Kim, S., Bell, A. J., Betters, R. K., Fiock, K. L., Iida, M. A., Smalley, M. E., Farrell, K. W., Fowkes, M. E., & Crary, J. F. (2019) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlz073 · Cited by 67
Bhardwaj, V. K., SINGH, R. K., Sharma, J., Das, P., & Purohit, R. (2020) · Computer Methods and Programs in Biomedicine · doi:10.1016/j.cmpb.2020.105494 · Cited by 61
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Dekker, A. D., Deyn, P. P. D., & Rots, M. G. (2014) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2014.05.004 · Cited by 64
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Ding, S., Shi, J., Qian, W., Iqbal, K., Grundke, I., Gong, C., & Liu, F. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.11.021 · Cited by 60
Self-citationAlzheimer's disease neurofibrillary degeneration: pivotal and multifactorial
Iqbal, K., Wang, X., Blanchard, J., Liu, F., Gong, C., & Grundke, I. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380962 · Cited by 61
Self-citationStringer, M., Abeysekera, I., Thomas, J. R., LaCombe, J., Stancombe, K., Stewart, R. B., Dria, K. J., Wallace, J. M., Goodlett, C. R., & Roper, R. J. (2017) · Physiology & Behavior · doi:10.1016/j.physbeh.2017.05.003 · Cited by 64
Tangles, Toxicity, and Tau Secretion in AD – New Approaches to a Vexing Problem
Gendreau, K. L., & Hall, G. F. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00160 · Cited by 67
Miyata, Y., & Nishida, E. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.023 · Cited by 60
Sachse, S., Lievens, S., Ribeiro, L. F., Dascenco, D., Masschaele, D., Horré, K., Misbaer, A., Vanderroost, N., de Smet, A.-S., Salta, E., et al. (2019) · The EMBO Journal · doi:10.15252/embj.201899669 · Cited by 62
Grygier, P., Pustelny, K., Nowak, J., Golik, P., Popowicz, G. M., Plettenburg, O., Dubin, G., Menezes, F., & Czarna, A. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01887 · Cited by 64
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Sheppard, O., Plattner, F., Rubin, A. N., Slender, A., Linehan, J. M., Brandner, S., Tybulewicz, V. L. J., Fisher, E., & Wiseman, F. K. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.025 · Cited by 55
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Toiber, D., Azkona, G., Ben‐Ari, S., Torán, N., Soreq, H., & Dierssen, M. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.06.011 · Cited by 55
Souchet, B., Audrain, M., Billard, J. M., Dairou, J., Fol, R. R., Orefice, N. S., Tada, S., Gu, Y., Dufayet‐Chaffaud, G., Limanton, E., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0678-6 · Cited by 60
Impact of increased APP gene dose in Down syndrome and the Dp16 mouse model
Sawa, M., Overk, C., Becker, A., Derse, D., Albay, R., Weldy, K., Salehi, A., Beach, T. G., Doran, E., Head, E., et al. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12463 · Cited by 54
Neurogenetic disorders across the lifespan: from aberrant development to degeneration
Hickman, R. A., O’Shea, S. A., Mehler, M. F., & Chung, W. K. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-021-00595-5 · Cited by 59
Kac, P. R., González‐Ortiz, F., Emeršič, A., Dulewicz, M., Koutarapu, S., Turton, M., An, Y., Smirnov, D. S., Kulczyńska‐Przybik, A., Varma, V. R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46876-7 · Cited by 56
Probable Participation of 14-3-3 in Tau Protein Oligomerization and Aggregation
Sluchanko, N. N., & Gusev, N. B. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110692 · Cited by 52
Nakano-Kobayashi, A., Fukumoto, A., Morizane, A., Nguyen, D. T., Le, T. M., Hashida, K., Hosoya, T., Takahashi, R., Takahashi, J. B., Hori, O., et al. (2020) · Science Advances · doi:10.1126/sciadv.abc1428 · Cited by 50
Perez, S. E., Miguel, J. C., He, B., Malek‐Ahmadi, M. H., Abrahamson, E. E., Ikonomović, M. D., Lott, I. T., Doran, E. W., Alldred, M. J., Ginsberg, S. D., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01965-6 · Cited by 48
Novel Scaffolds for Dual Specificity Tyrosine-Phosphorylation-Regulated Kinase (DYRK1A) Inhibitors
Czarna, A., Wang, J., Zelencova-Gopejenko, D., Liu, Y., Deng, X., Choi, H. G., Zhang, T., Zhou, W., Chang, J. W., Kildalsen, H., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01847 · Cited by 48
Miyata, Y., Shibata, T., Aoshima, M., Tsubata, T., & Nishida, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.586115 · Cited by 47
Targeting trisomic treatments: optimizing Dyrk1a inhibition to improve Down syndrome deficits
Stringer, M., Goodlett, C. R., & Roper, R. J. (2017) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.334 · Cited by 45
QSAR analysis of pyrazolidine-3,5-diones derivatives as Dyrk1A inhibitors
Koo, K. A., Kim, N. D., Chon, Y. S., Jung, M., Lee, B., Kim, J. H., & Song, W. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.02.062 · Cited by 46
Langerscheidt, F., Wied, T., Kabbani, M. A. A., van Eimeren, T., Wunderlich, G., & Zempel, H. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12314-3 · Cited by 52
Plasma DYRK1A as a novel risk factor for Alzheimer’s disease
Janel, N., Sarazin, M., Corlier, F. W., Corne, H., de Souza, L. C., Hamelin, L., Aka, A., Lagarde, J., Bléhaut, H., Hindie, V., et al. (2014) · Translational Psychiatry · doi:10.1038/tp.2014.61 · Cited by 45
Chronic Dyrk1 Inhibition Delays the Onset of AD-Like Pathology in 3xTg-AD Mice
Velázquez, R., Meechoovet, B., Ow, A., Foley, C., Shaw, A. Y., Smith, B. E., Oddo, S., Hulme, C., & Dunckley, T. L. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-01684-9 · Cited by 44
Goodlett, C. R., Stringer, M., LaCombe, J., Patel, R., Wallace, J. M., & Roper, R. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-67133-z · Cited by 43
Welden, J. R., Margvelani, G., Maquera, K. A. A., Gudlavalleti, B., Sardón, S. C. M., Campos, A. R., Robil, N., Lee, D. C., Hernandez, A. G., Wang, W., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1129 · Cited by 43
Dissecting Alzheimer disease in Down syndrome using mouse models
Choong, X. Y., Tosh, J., Pulford, L. J., & Fisher, E. (2015) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2015.00268 · Cited by 41
REST Regulates DYRK1A Transcription in a Negative Feedback Loop
Lü, M., Zheng, L., Han, B., Wang, L., Wang, P., Liu, H., & Sun, X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.174540 · Cited by 39
Alexeeva, M., Åberg, E., Engh, R. A., & Rothweiler, U. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004715005106 · Cited by 41
Modeling Down syndrome in animals from the early stage to the 4.0 models and next
Moreno, M. D. M. M., Brault, V., Birling, M., Pavlovic, G., & Hérault, Y. (2020) · Progress in brain research · doi:10.1016/bs.pbr.2019.08.001 · Cited by 35
Lee, H., Woo, H., Lee, H.-E., Jeon, H., Ryu, K., Nam, J. H., Jeon, S. G., Park, H., Lee, J.-S., Han, K., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.08.030 · Cited by 39
Metadata
- Authors
- Liu, F., Liang, Z., Wegiel, J., Hwang, Y., Iqbal, K., Grundke‐Iqbal, I., Ramakrishna, N., & Gong, C.
- Affiliations
- Department of Neurochemistry New York State Institute for Basic Research in Developmental Disabilities Staten Island New York USA
- Department of Developmental Neurobiology New York State Institute for Basic Research in Developmental Disabilities Staten Island New York USA
- Department of Molecular Biology New York State Institute for Basic Research in Developmental Disabilities Staten Island New York USA
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2008-05-28
- Volume
- 22
- Issue
- 9
- Pages
- 3224-3233
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- PMC
- PMC2518253
- OpenAlex
- W1986503994
- Cited by
- 272
- References
- 62
- Citations by year
- 2026: 19 · 2025: 16 · 2024: 18 · 2023: 17 · 2022: 20 · 2021: 18 · 2020: 13 · 2019: 13 · 2018: 11 · 2017: 23 · 2016: 8 · 2015: 11 · 2014: 15 · 2013: 16 · 2012: 9
- FWCI
- 10.19
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The FASEB Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (AG027429, HD043960, HD038295, AG019158)
- Alzheimer's Association (IIRG-05-13095)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Down syndrome and intellectual disability research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- DYRK1A, Down syndrome, neurofibrillary degeneration, tau hyperphosphorylation, glycogen synthase kinase-3β, kinase activity, Ts65Dn mouse model, Alzheimer's disease
- MeSH terms
- Glycogen Synthase Kinase 3 beta, Dyrk Kinases, Aged, Aged, 80 and over, Animals, Down Syndrome, Female, Humans, Male, Middle Aged, Nerve Degeneration, Phosphorylation, Protein-Tyrosine Kinases, Neurofibrillary Tangles, tau Proteins, Protein Serine-Threonine Kinases, Gene Expression Regulation, Developmental, Glycogen Synthase Kinase 3, Mice
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