The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Up-regulation of mitogen-activated protein kinases ERK1/2 and MEK1/2 is associated with the progression of neurofibrillary degeneration in Alzheimer’s disease
Abstract
The abnormal hyperphosphorylation of tau in Alzheimer's disease (AD) has been proposed to involve the extracellular-signal-regulated protein kinase (ERK) of the mitogen-activated protein (MAP) kinase family. ERK is phosphorylated and thereby activated by MAP kinase kinase (MEK). In the present study, we determined the intracellular and regional distribution of the active forms of both MEK1/2 and ERK1/2, i.e. p-MEK1/2 and p-ERK1/2 in the entorhinal, hippocampal, and temporal cortices of 49 brains staged for neurofibrillary changes according to Braak and Braak's protocol. We found that p-MEK1/2 and p-ERK1/2 were present in the initial stages of neurofibrillary degeneration in the projecting neurons in the transentorhinal region, and extended into other brain regions co-incident with the progressive sequence of neurofibrillary changes up to and including Braak stage VI. It appeared that the accumulation of p-MEK1/2 and p-ERK1/2 was initiated in the cytoplasm of pretangle neurons in varying size granules, which grew into large aggregates co-existing with the progressive development of neurofibrillary tangles. Accumulation of p-MEK1/2 and p-ERK1/2 was found in cases with stages I-III neurofibrillary degeneration, which were devoid of amyloid deposition. These data provide direct in situ evidence consistent with the possible involvement of MAP kinase pathway in the hyperphosphorylation of tau and the presence of this lesion before deposition of beta-amyloid in AD.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“ERK can phosphorylate tau (29), and elevated activity of MAPK/ERK has been reported in several tauopathies and may play a role in early stages of neurofibriliary tangle (NFT) formation (82,130,131).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [130]
Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Self-citationGrundke-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
Self-citationNeurofibrillary 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
Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876
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-citationAnderson, N. G., Maller, J. L., Tonks, N. K., & Sturgill, T. W. (1990) · Nature · doi:10.1038/343651a0 · Cited by 1,064
Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 769
Self-citationDEFECTIVE BRAIN MICROTUBULE ASSEMBLY IN ALZHEIMER'S DISEASE
Iqbal, K., Zaidi, T., Wen, G. Y., Grundke, I., MERZ, P. A., Shaikh, S., Wisniewski, H., Alafuzoff, I. I., & Winblad, B. G. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92134-3 · Cited by 737
Self-citationHanger, D. P., Hughes, K., Woodgett, J. R., Brion, J.-P., & Anderton, B. H. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90774-2 · Cited by 737
Identification of normal and pathological aging in prospectively studied nondemented elderly humans
Dickson, D. W., Crystal, H. A., Mattiace, L. A., Masur, D. M., Blau, A. D., Davies, P., Yen, S.-H., & Aronson, M. K. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90027-u · Cited by 643
Research works printed but not linked: 2
- Campbell, 1987, Alzheimer’s plaques and tangles: a controlled and enhanced silver-staining method, Soc. Neurosci. Abstr., 13, H678
- Pei, 1999, The distribution of active form of mitogen activated protein (MAP) kinase in Alzheimer’s neurofibrillary pathology, Soc. Neurosci. Abstr., 25, 1181
Cited by
Sorted by citations
Moloney, A. M., Griffin, R. J., Timmons, S., O’Connor, R., Ravid, R., & O’Neill, C. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.04.002 · Cited by 764
Tau protein kinases: Involvement in Alzheimer's disease
Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631
Alzheimer's disease: the two-hit hypothesis
Zhu, X., Raina, A. K., Perry, G. L., & Smith, M. A. (2004) · The Lancet Neurology · doi:10.1016/s1474-4422(04)00707-0 · Cited by 431
Oxidative stress signalling in Alzheimer's disease
Zhu, X., Raina, A. K., Lee, H., Casadesús, G., Smith, M. A., & Perry, G. L. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.012 · Cited by 396
Therapeutic approaches to Alzheimer's disease
Klafki, H., Staufenbiel, M., Kornhuber, J., & Wiltfang, J. (2006) · Brain · doi:10.1093/brain/awl280 · Cited by 362
Li, X., Alafuzoff, I., Soininen, H., Winblad, B., & Pei, J. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04833.x · Cited by 324
Self-citationPerluigi, M., Di Domenico, F., & Butterfield, D. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.014 · Cited by 339
An, W.-L., Cowburn, R. F., Li, L., Braak, H., Alafuzoff, I., Iqbal, K., Iqbal, I.-G., Winblad, B., & Pei, J.-J. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63687-5 · Cited by 312
Self-citationChu, C. T., Levinthal, D. J., Kulich, S. M., Chalovich, E. M., & DeFranco, D. B. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04132.x · Cited by 273
Mitochondrially localized ERK2 regulates mitophagy and autophagic cell stress
Dagda, R. K., Zhu, J., Kulich, S. M., & Chu, C. T. (2008) · Autophagy · doi:10.4161/auto.6458 · Cited by 275
ERK and cell death: ERK1/2 in neuronal death
Subramaniam, S., & Unsicker, K. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07367.x · Cited by 263
Phosphorylation meets nuclear import: a review
Nardozzi, J. D., Lott, K., & Cingolani, G. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-32 · Cited by 251
Tau protein phosphatases in Alzheimer's disease: The leading role of PP2A
Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., & Terro, F. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.008 · Cited by 265
Sun, J., & Nan, G. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.2962 · Cited by 245
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-citationAn inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice
Corre, S. L., Klafki, H., Plesnila, N., Hübinger, G., Obermeier, A., Sahagún, H., Monse, B., Seneci, P., Lewis, J. M., Eriksen, J. L., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602913103 · Cited by 232
Tau Phosphorylation and Sevoflurane Anesthesia: An Association to Postoperative Cognitive Impairment
Le Freche, H., Brouillette, J., Fernandez-Gomez, F.-J., Patin, P., Caillierez, R., Zommer, N., Sergeant, N., Buée-Scherrer, V., Lebuffe, G., Blum, D., et al. (2012) · Anesthesiology · doi:10.1097/aln.0b013e31824be8c7 · Cited by 212
Kirouac, L., Rajic, A. J., Cribbs, D. H., & Padmanabhan, J. (2017) · eneuro · doi:10.1523/eneuro.0149-16.2017 · Cited by 207
Lüth, H. J. (2004) · Cerebral Cortex · doi:10.1093/cercor/bhh123 · Cited by 192
Impaired insulin signalling and allostatic load in Alzheimer disease
Felice, F. G. D., Gonçalves, R. A., & Ferreira, S. T. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00558-9 · Cited by 183
Developmental 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-citationMcKeever, P. M., Schneider, R., Taghdiri, F., Weichert, A., Multani, N., Brown, R. A., Boxer, A. L., Karydas, A., Miller, B., Robertson, J., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1032-x · Cited by 166
Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications
Butterfield, D. A., Marzia Perluigi, A., Reed, T. T., Muharib, T., Hughes, C. P., Robinson, R. A. S., & Rukhsana Sultana, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4109 · Cited by 171
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
Role of protein kinase B in Alzheimer's neurofibrillary pathology
Pei, J.-J., Khatoon, S., An, W., Nordlinder, M., Tanaka, T., Braak, H., Tsujio, I., Takeda, M., Alafuzoff, I. I., Winblad, B. G., et al. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0657-y · Cited by 169
Self-citationLimorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168
Emerging Role for ERK as a Key Regulator of Neuronal Apoptosis
Cheung, E. C., & Slack, R. S. (2004) · Science s STKE · doi:10.1126/stke.2512004pe45 · Cited by 162
Wang, X., Zheng, W. H., Xie, J., Wang, T., Wang, S., Teng, W., & Wang, Z. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-46 · Cited by 161
Increased MAP kinase activity in Alzheimer's and Down syndrome but not in schizophrenia human brain
SWATTON, J. E., Sellers, L. A., Faull, R. L. M., Holland, A. J., Iritani, S., & Bahn, S. (2004) · European Journal of Neuroscience · doi:10.1111/j.0953-816x.2004.03365.x · Cited by 158
Harris, F. M., Brecht, W. J., Xu, Q., Mahley, R. W., & Huang, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408127200 · Cited by 151
ABCA7 Deficiency Accelerates Amyloid-β Generation and Alzheimer's Neuronal Pathology
Sakae, N., Liu, C., Shinohara, M., Frisch‐Daiello, J. L., Ma, L., Yamazaki, Y., Tachibana, M., Younkin, L. H., Kurti, A., Carrasquillo, M. M., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3757-15.2016 · Cited by 151
Tau-Based Treatment Strategies in Neurodegenerative Diseases
Schneider, A., & Mandelkow�, E. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.006 · Cited by 145
Pei, J.-J., Gong, C., An, W., Winblad, B. G., Cowburn, R. F., Grundke, I., & Iqbal, K. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63445-1 · Cited by 142
Self-citationReversible oxidation of ERK-directed protein phosphatases drives oxidative toxicity in neurons
Levinthal, D. J., & DeFranco, D. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410771200 · Cited by 126
Mammalian Target of Rapamycin (mTor) Mediates Tau Protein Dyshomeostasis
Tang, Z., Bereczki, E., Zhang, H., Wang, S., Li, C., Ji, X., Branca, R. M., Lehtiö, J., Guan, Z., Filipčík, P., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.435123 · Cited by 124
Self-citationVeeranna, Kaji, T., Boland, B., Odrljin, T. M., Mohan, P. S., Basavarajappa, B. S., Peterhoff, C. M., Cataldo, A. M., Rudnicki, A., Amin, N. D., et al. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63342-1 · Cited by 123
Grape Derived Polyphenols Attenuate Tau Neuropathology in a Mouse Model of Alzheimer's Disease
Wang, J., Santa‐María, I., Ho, L., Ksiȩżak-Reding, H., Ono, K., Teplow, D. B., & Pasinetti, G. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101074 · Cited by 123
Padmanabhan, J., Levy, M. M., Dickson, D. W., & Potter, H. (2006) · Brain · doi:10.1093/brain/awl255 · Cited by 124
Ooigawa, H., Nawashiro, H., Fukui, S., Otani, N., 大角, 篤., Toyooka, T., & Shima, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0108-2 · Cited by 121
P70 S6 kinase mediates tau phosphorylation and synthesis
Pei, J.-J., An, W., Zhou, X., Nishimura, T., Norberg, J., Benedikz, E., Götz, J., & Winblad, B. G. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.059 · Cited by 121
Self-citationMKP-1 reduces Aβ generation and alleviates cognitive impairments in Alzheimer’s disease models
Du, Y., Du, Y., Zhang, Y., Huang, Z., Fu, M., Li, J., Pang, Y., Lei, P., Wang, Y. T., Song, W., et al. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0091-4 · Cited by 117
Anesthesia Induces Phosphorylation of Tau
Run, X., Liang, Z., Zhang, L., Iqbal, K., Grundke, I., & Gong, C. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1003 · Cited by 112
Self-citationAmbegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113
“ERK can phosphorylate tau (29), and elevated activity of MAPK/ ERK has been reported in several tauopathies and may play a role in early stages of neurofibriliary tangle (NFT) formation (82,130,131).”
BackgroundmTor mediates tau localization and secretion: implication for Alzheimer’s disease
Tang, Z., Ioja, E., Bereczki, E., Hultenby, K., Li, C., Guan, Z., Winblad, B., & Pei, J.-J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.003 · Cited by 112
Self-citationKamat, P. K., Rai, S., Swarnkar, S., Shukla, R., & Nath, C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8699-4 · Cited by 112
Multiple pathways of apolipoprotein E signaling in primary neurons
Hoe, H., Harris, D. C., & Rebeck, G. W. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.03007.x · Cited by 111
Liu, Q., Zhang, J., Zhu, H., Qin, C., Chen, Q., & Zhao, B. (2006) · The FASEB Journal · doi:10.1096/fj.06-5841com · Cited by 112
An, W., Björkdahl, C., Liu, R., Cowburn, R. F., Winblad, B. G., & Pei, J.-J. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02948.x · Cited by 107
Self-citationArrazola Sastre, A., Luque Montoro, M., Gálvez-Martín, P., Lacerda, H. M., Lucia, A., Llavero, F., & Zugaza, J. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176312 · Cited by 103
Echeverrı́a, V., Ducatenzeiler, A., Dowd, E., Jänne, J., Grant, S. M., Szyf, M., Wandosell, F. G., Ávila, J., Grimm, H. S., Dunnett, S. B., et al. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.07.036 · Cited by 104
Heat Shock Protein 90 in Alzheimer’s Disease
Ou, J.-R., Tan, M., Xie, A., Yu, J., & Tan, L. (2014) · BioMed Research International · doi:10.1155/2014/796869 · Cited by 102
Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Tanaka, F., Doyu, M., & Sobue, G. (2006) · Journal of Molecular Medicine · doi:10.1007/s00109-006-0066-0 · Cited by 100
Signal Transduction Cascades Associated with Oxidative Stress in Alzheimer's Disease
Petersen, R. B., Nunomura, A., Lee, H., Casadesús, G., Perry, G. L., Smith, M. A., & Zhu, X. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11202 · Cited by 101
ERK1/2 is an endogenous negative regulator of the γsecretase activity
Kim, S., Park, H., Hong, H. S., Baik, E. J., Jung, M. W., & Mook‐Jung, I. (2006) · The FASEB Journal · doi:10.1096/fj.05-4055fje · Cited by 92
Phosphorylated Tau: Toxic, Protective, or None of the Above
Castellani, R. J., Nunomura, A., Lee, H., Perry, G. L., & Smith, M. A. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14404 · Cited by 94
Domenico, F. D., Rukhsana Sultana, A., Barone, E., Marzia Perluigi, A., Cini, C., Mancuso, C., Cai, J., Pierce, W. M. J., & Butterfield, D. A. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.03.033 · Cited by 91
Recent developments of protein kinase inhibitors as potential AD therapeutics
Tell, V., & Hilgeroth, A. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00189 · Cited by 92
Khezri, M. R., Yousefi, K., Esmaeili, A., & Ghasemnejad‐Berenji, M. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01191-x · Cited by 93
Aberrant phosphorylation in the pathogenesis of Alzheimer's disease
Chung, S. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.8.467 · Cited by 92
Phosphorylated eukaryotic translation factor 4E is elevated in Alzheimer brain
Li, X., An, W.-L., Alafuzoff, I., Soininen, H., Winblad, B., & Pei, J.-J. (2004) · NeuroReport · doi:10.1097/00001756-200410050-00019 · Cited by 84
Self-citationExtracellular signal-regulated kinase as an inducer of non-apoptotic neuronal death
Subramaniam, S., & Unsicker, K. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2005.12.013 · Cited by 86
Marzia Perluigi, A., Barone, E., Domenico, F. D., & Butterfield, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.005 · Cited by 86
JNK and ERK1/2 pathways have a dual opposite effect on the expression of BACE1
Tamagno, E., Guglielmotto, M., Giliberto, L., Vitali, A., Borghi, R., Autelli, R., Danni, O., & Tabaton, M. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.12.015 · Cited by 84
Shahani, N., Subramaniam, S., Wolf, T., Tackenberg, C., & Brandt, R. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4245-05.2006 · Cited by 81
Secreted β-amyloid precursor protein activates microglia via JNK and p38-MAPK
Bodles, A. M., & Barger, S. W. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.022 · Cited by 82
Du, L., Xie, J., Cheng, X., Li, X.-H., Kong, F., Jiang, X., Ma, Z., Wang, J., Chen, C., & Zhou, X. (2013) · AGE · doi:10.1007/s11357-013-9592-1 · Cited by 86
Zeitlin, R., Patel, S., Burgess, S., Arendash, G. W., & Echeverrı́a, V. (2011) · Brain Research · doi:10.1016/j.brainres.2011.08.036 · Cited by 84
Early Life Stress and Epigenetics in Late-onset Alzheimer’s Dementia: A Systematic Review
Lemche, E. (2018) · Current Genomics · doi:10.2174/1389202919666171229145156 · Cited by 84
Shin, M., Liu, Q. F., Choi, B., Shin, C., Lee, B., Yuan, C., Song, Y. J., Yun, H. S., Lee, I.-S., Koo, B.-S., et al. (2020) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b19-00495 · Cited by 80
Location, Location, Location: Altered Transcription Factor Trafficking in Neurodegeneration
Chu, C. T., Plowey, E., Wang, Y., Patel, V., & Jordan-Sciutto, K. (2007) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/nen.0b013e318156a3d7 · Cited by 77
Intracellular and Extracellular Aβ, a Tale of Two Neuropathologies
Cuello, A. C. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00101.x · Cited by 80
Pal, R., Oien, D. B., Ersen, F. Y., & Moskovitz, J. (2007) · Experimental Brain Research · doi:10.1007/s00221-007-0903-6 · Cited by 78
Hole, K. L., & Williams, R. J. (2020) · Brain Plasticity · doi:10.3233/bpl-200098 · Cited by 81
p70 S6 Kinase and Tau in Alzheimer's Disease
Pei, J.-J., Björkdahl, C., Zhang, H., Zhou, X., & Winblad, B. G. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14405 · Cited by 75
Self-citationMajd, S., Power, J. H. T., & Grantham, H. J. M. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0211-1 · Cited by 79
Accumulation of tumor-suppressor PTEN in Alzheimer neurofibrillary tangles
Sonoda, Y., Mukai, H., Matsuo, K., Takahashi, M., Ono, Y., Maeda, K., Akiyama, H., & Kawamata, T. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.12.078 · Cited by 74
Vreones, M. P., Mustapić, M., Moaddel, R., Pucha, K. A., Lovett, J., Seals, D. R., Kapogiannis, D., & Martens, C. R. (2022) · Aging Cell · doi:10.1111/acel.13754 · Cited by 80
Al‐kuraishy, H. M., Jabir, M. S., Albuhadily, A. K., Al-Gareeb, A. I., & Rafeeq, M. F. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102084 · Cited by 75
Sanderson, T. M., Hogg, E. L., Collingridge, G. L., & Corrêa, S. A. L. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13592 · Cited by 72
Manganese Induces Tau Hyperphosphorylation through the Activation of ERK MAPK Pathway in PC12 Cells
Cai, T., Che, H., Yao, T. S., Chen, Y., Huang, C., Zhang, W., Du, K., Zhang, J., Cao, Y., Chen, J., et al. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq308 · Cited by 67
Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase
Qi, H., Prabakaran, S., Cantrelle, F., Chambraud, B., Gunawardena, J., Lippens, G. M., & Landrieu, I. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700914 · Cited by 73
Zhou, X., Li, X., Björkdahl, C., Sjögren, M. J. C., Alafuzoff, I. I., Soininen, H. S., Grundke, I., Iqbal, K., Winblad, B. G., & Pei, J.-J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.01.006 · Cited by 65
Self-citationGao, T., Jernigan, J. E., Raza, S. A., Dammer, E. B., Xiao, H., Seyfried, N. T., Levey, A. I., & Rangaraju, S. (2019) · Glia · doi:10.1002/glia.23678 · Cited by 68
Piccialli, I., Tedeschi, V., Caputo, L., Amato, G., De Martino, L., De Feo, V., Secondo, A., & Pannaccione, A. (2021) · Antioxidants · doi:10.3390/antiox10060937 · Cited by 64
Pearson, A. G., Curtis, M. A., Waldvogel, H. J., Faull, R. L. M., & Dragunow, M. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.02.029 · Cited by 63
Gui, Y.-X., Wang, X., Kang, W., Zhang, Y., Zhang, Y., Zhou, Y. F., Quinn, T. J., Liu, J., & Chen, S. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.001 · Cited by 67
Distribution, levels, and activation of MEK1 in Alzheimer's disease
Zhu, X.-W., Sun, Z., Lee, H.-G., Siedlak, S., Perry, G., & Smith, M. A. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01820.x · Cited by 60
Zinc in Cognitive Impairment and Aging
Sun, R., Wang, J., Feng, J., & Cao, B. (2022) · Biomolecules · doi:10.3390/biom12071000 · Cited by 70
Kerr, F., Rickle, A., Nayeem, N., Brandner, S., Cowburn, R. F., & Lovestone, S. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.064 · Cited by 60
Self-citationCai, X., Zhang, K., Xie, X., Zhu, X., Feng, J., Jin, Z., Zhang, H., Tian, M., & Chen, H. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119678 · Cited by 59
Chen, D., Mei, Y., Kim, N., Lan, G., Gan, C., Fan, F., Zhang, T., Xia, Y., Wang, L., Lin, C., et al. (2020) · Journal of Pineal Research · doi:10.1111/jpi.12665 · Cited by 59
Activation of ERK1/2 MAP kinases in Familial Amyloidotic Polyneuropathy
Monteiro, F. A., Sousa, M. M., Cardoso, I., do Amaral, B., Guimarães, A., & Saraiva, M. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03716.x · Cited by 57
Ruegsegger, G. N., Manjunatha, S., Summer, P., Gopala, S., Zabeilski, P., Dasari, S., Vanderboom, P. M., Lanza, I. R., Klaus, K. A., & Nair, K. S. (2019) · The FASEB Journal · doi:10.1096/fj.201802043r · Cited by 57
Li, L., Wu, X., Zhao, X.-J., Xu, L., Pan, C., & Zhang, Z. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01744-1 · Cited by 56
Leugers, C. J., & Lee, G. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105387 · Cited by 60
Activated c-Jun is present in neurofibrillary tangles in Alzheimer's disease brains
Pearson, A. G., Byrne, U. T. E., MacGibbon, G. A., Faull, R. L. M., & Dragunow, M. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.01.031 · Cited by 51
Alleviating Neurodegeneration by an Anticancer Agent
Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Tanaka, F., & Sobue, G. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.012 · Cited by 50
Heat Shock Protein 90 Indirectly Regulates ERK Activity by Affecting Raf Protein Metabolism
Dou, F., Yuan, L.-D., & Zhu, J. (2005) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2005.00069.x · Cited by 49
Niño, S. A., Martel‐Gallegos, G., Castro‐Zavala, A., Ortega-Berlanga, B., Delgado, J. M., Hernández‐Mendoza, H., Romero-Guzmán, E. T., Ríos-Lugo, M. J., Rosales‐Mendoza, S., Jiménez-Capdeville, M. E., et al. (2017) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.7b00215 · Cited by 50
Gao, B., Zhou, S.-T., Sun, C., Cheng, D., Zhang, Y., Li, X., Zhang, L., Zhao, J., Xu, D., & Bai, Y. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00089 · Cited by 50
Metadata
- Authors
- Pei, J.-J., Braak, H., An, W.-L., Winblad, B., Cowburn, R. F., Iqbal, K., & Grundke-Iqbal, I.
- Affiliations
- Karolinska Institutet (SE)
- Goethe University Frankfurt (DE)
- Corresponding author
- Pei, Jin-Jing
- Venue
- Molecular Brain Research
- Publisher
- Elsevier BV
- Published
- 2002-12
- Volume
- 109
- Issue
- 1-2
- Pages
- 45-55
- ISSN
- 0169-328X (ISSN-L)
- OpenAlex
- W2046431926
- Cited by
- 247
- References
- 62
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 6 · 2023: 8 · 2022: 19 · 2021: 12 · 2020: 12 · 2019: 12 · 2018: 12 · 2017: 11 · 2016: 8 · 2015: 5 · 2014: 8 · 2013: 7 · 2012: 11
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular Brain Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag008076-09, 5r01ns018105-17)
- National Institute on Aging (AG19158, AG 08076, R01AG019158)
- National Institute of Neurological Disorders and Stroke (NS 18105)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, neurofibrillary degeneration, tau hyperphosphorylation, ERK1/2, MEK1/2, MAPK signaling, neurofibrillary tangles, Braak staging, entorhinal cortex, hippocampus, temporal cortex, amyloid deposition
- MeSH terms
- Adult, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Brain, Female, Fluorescent Dyes, Humans, Immunohistochemistry, Male, Middle Aged, Neurofibrils, Neurons, Phosphorylation, Protein-Tyrosine Kinases, Up-Regulation, tau Proteins, Protein Serine-Threonine Kinases, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinase 3, MAP Kinase Kinase 1, MAP Kinase Kinase 2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review