Cited by 291Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 60 of the 61 references it cites were found in a registry or an index.

Activation of c-Jun N-Terminal Kinase and p38 in an Alzheimer's Disease Model Is Associated with Amyloid Deposition

Open access

Savage, Mary J., Lin, Yin-Guo, Ciallella, John R., Flood, Dorothy G., Scott, Richard W.·2002·The Journal of Neuroscience

DOI 10.1523/jneurosci.22-09-03376.2002PMC PMC6758401

Open this paper in CoChat — free account Open PDF

Abstract

The mechanisms by which neurons and synapses are lost in Alzheimer's disease (AD) are not completely understood. To characterize potential signaling events linked to AD pathogenesis, activation-specific antibodies were used to examine mitogen-activated protein kinase (MAPK) kinase pathways at various ages in mice transgenic for human amyloid precursor protein-695 with the Swedish familial AD mutations (Tg2576) and homozygous for a P264L familial AD mutation introduced by targeting of the presenilin-1 gene (PS1(P264L)). Although the c-Jun N-terminal kinase (JNK) and p38 pathways were significantly activated in the cortex at both 7 and 12 months of age, there was no significant activation of the extracellular signal-regulated kinase pathway. MAPK kinase-4, an upstream activator of JNK, was also significantly activated at 7 and 12 months, whereas c-Jun, a downstream effector of JNK-associated apoptotic signaling, was not induced. The lack of c-Jun activation is consistent with the absence of neuronal loss in both cortex and hippocampal CA1 at 12 months. The JNK activation was localized to amyloid deposits, within neurites containing phosphorylated tau. Synaptophysin was quantified biochemically as a measure of synaptic integrity and was significantly reduced in an age-dependent manner in the Tg2576/PS1(P264L) cortex but not in either PS1(P264L) or Tg2576 cortex. Stress-responsive MAP kinase pathways were activated in the brain of the Tg2576/PS1(P264L) AD model, and this activation was coincident with the age-dependent increase in amyloid deposition, tau phosphorylation, and loss of synaptophysin.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1523/jneurosci.22-09-03376.2002

Cites

60 of 60 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Mammalian MAP kinase signalling cascades
Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,118
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation
Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,400
Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
High-Level Neuronal Expression of Aβ1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
Gómez‐Isla, T., Hollister, R., West, H., Mui, S., Growdon, J. H., Petersen, R. C., Parisi, J. E., & Hyman, B. T. (1997) · Annals of Neurology · doi:10.1002/ana.410410106 · Cited by 1,489
Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease
West, M. J., Coleman, P. D., Flood, D. G., & Troncoso, J. C. (1994) · The Lancet · doi:10.1016/s0140-6736(94)92338-8 · Cited by 1,267 · cited 2×
“The memory impairments in Alzheimer’s disease (AD) are attributable to the loss of both neurons and synapses (West et al., 1994; DeKosky et al., 1996; Gomez-Isla et al., 1997).”
BackgroundSelf-citation

Show all 61 references

Sorted by citations

Items 201–291 of 291

Carbamate JNK3 Inhibitors Show Promise as Effective Treatments for Alzheimer’s Disease: In Vivo Studies on Mouse Models
Jun, J., Moon, H., Yang, S., Lee, J.-H., Baek, J., Kim, H., Cho, H., Hwang, K., Ahn, S., Kim, Y., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00393 · Cited by 21
Crosstalk Between Insulin and Toll-like Receptor Signaling Pathways in the Central Nervous system
Hemmati, F., Ghasemi, R., Ibrahim, N. M., Dargahi, L., Mohamed, Z., Raymond, A. A., & Ahmadiani, A. (2014) · Molecular Neurobiology · doi:10.1007/s12035-013-8631-3 · Cited by 21
Fibrillar Amyloid-β Accumulation Triggers an Inflammatory Mechanism Leading to Hyperphosphorylation of the Carboxyl-Terminal End of Tau Polypeptide in the Hippocampal Formation of the 3×Tg-AD Transgenic Mouse
Ontiveros‐Torres, M. Á., Labra‐Barrios, M. L., Díaz-Cintra, S. Y., Aguilar-Vázquez, A. R., Moreno-Campuzano, S., Flores-Rodríguez, P., Luna-Herrera, C., Mena, R., Perry, G. L., Florán, B., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150837 · Cited by 21
Aged dominant negative p38α MAPK mice are resistant to age-dependent decline in adult-neurogenesis and context discrimination fear conditioning
Cortez, I., Bulavin, D. V., Wu, P., McGrath, E. L., Cunningham, K. A., Wakamiya, M., Papaconstantinou, J., & Dineley, K. T. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.10.023 · Cited by 21
Role of WWOX WOX1 in Alzheimer s disease pathology and in cell death signaling
Teng, C.-C. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s358 · Cited by 22
β-Amyloid overload does not directly correlate with SAPK/JNK activation and tau protein phosphorylation in the cerebellar cortex of Ts65Dn mice
Lomoio, S., Scherini, E., & Necchi, D. (2009) · Brain Research · doi:10.1016/j.brainres.2009.08.052 · Cited by 20
3,5,4′-trihydroxy-6,7,3′-trimethoxyflavone protects against beta amyloid-induced neurotoxicity through antioxidative activity and interference with cell signaling
Telerman, A., Ofir, R., Kashman, Y., & Elmann, A. (2017) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-017-1840-y · Cited by 19
Interaction of ASK1 and the β-amyloid precursor protein in a stress-signaling complex
Galván, V., Banwait, S., Spilman, P. R., Gorostiza, O. F., Peel, A. L., Ataie, M., Crippen, D., Huang, W., Sidhu, G., Ichijo, H., et al. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.06.017 · Cited by 20
Recent advances in experimental modeling of the assembly of tau filaments
Ko, L., Deture, M. A., Sahara, N., Chihab, R., Vega, I. E., & Yen, S.-H. C. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.004 · Cited by 19
Involvement of P38MAPK activation by NMDA receptors and non-NMDA receptors in amyloid-β peptide-induced neuronal loss in rat hippocampal CA1 and CA3 subfields
Xu, Y., Cao, D.-H., Wu, G., & Hou, X. (2014) · Neuroscience Research · doi:10.1016/j.neures.2014.05.011 · Cited by 17
Enhancement of β-amyloid oligomer accumulation after intracerebroventricular injection of streptozotocin, which involves central insulin signaling in a transgenic mouse model
Lin, F., Jia, J., & Qin, W. (2014) · Neuroreport · doi:10.1097/wnr.0000000000000261 · Cited by 17
Folicitin abrogates scopolamine induced hyperlipidemia and oxidative stress mediated neuronal synapse and memory dysfunction in mice
Gul, S., Attaullah, S., Alsugoor, M. H., Bawazeer, S., Shah, S. A., Khan, S., Salahuddin, H. S., & Ullah, M. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e16930 · Cited by 17
Region-specific neuron and synapse loss in the hippocampus of APPSL/PS1 knock-in mice
Brasnjevic, I., Lardenoije, R., Schmitz, C., van der Kolk, N. M., Dickstein, D. L., Takahashi, H., Hof, P. R., Steinbusch, H. W. M., & Rutten, B. P. F. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0111-8 · Cited by 16
Induction of GADD34 Regulates the Neurotoxicity of Amyloid β
Xu, N., Xiao, Z.-J., Zou, T., & Huang, Z. (2014) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317514545616 · Cited by 16
Dissociation of ERK and Akt signaling in endothelial cell angiogenic responses to β-amyloid
Magrané, J., Christensen, R. A., Rosen, K. M., Veereshwarayya, V., & Querfurth, H. W. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.12.009 · Cited by 16
Bag1-L Is a Phosphorylation-Dependent Coactivator of c-Jun during Neuronal Apoptosis
Costa, C. D., Villadiego, J., Sancho, R., Fontana, X., Packham, G., Nateri, A. S., & Behrens, A. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01610-09 · Cited by 16
Neuroprotective effects of N-acetyl cysteine on primary hippocampus neurons against hydrogen peroxide-induced injury are mediated via inhibition of mitogen-activated protein kinases signal transduction and antioxidative action
Wu, W., Liu, B., Xie, C., Xia, X., & Zhang, Y. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.8699 · Cited by 15
Gene Knockout of tau Expression Does Not Contribute to the Pathogenesis of Prion Disease
Lawson, V., Klemm, H. M. J., Welton, J. M., Masters, C. L., Crouch, P. J., Cappai, R., & Ciccotosto, G. D. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318235b471 · Cited by 15
Phosphorylated p38MAPK specific antibodies cross‐react with sarkosyl‐insoluble hyperphosphorylated tau proteins
Sahara, N., Vega, I. E., Ishizawa, T., Lewis, J., McGowan, E., Hutton, M., Dickson, D., & Yen, S. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02558.x · Cited by 15
β-amyloid cytotoxicity is prevented by natural achillolide A
Elmann, A., Telerman, A., Ofir, R., Kashman, Y., & Lazarov, O. (2018) · Journal of Natural Medicines · doi:10.1007/s11418-018-1191-0 · Cited by 14
Cognitive and Alzheimer's disease biomarker effects of oral nicotinamide riboside (NR) supplementation in older adults with subjective cognitive decline and mild cognitive impairment
Wu, C., Kupferschmid, A. C., Liu, C., McManus, A. J., Kivisäkk, P., Galler, J. A., Schwab, N. A., DesRuisseaux, L. A., Williams, V. J., Gerber, J. A., et al. (2025) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.70023 · Cited by 18
c-Jun N-Terminal Kinases in Alzheimer’s Disease: A Possible Target for the Modulation of the Earliest Alterations
Busquets, O., Parcerisas, A., Verdaguer, E., Ettcheto, M., Camins, A., Beas‐Zárate, C., Castro-Torres, R. D., & Auladell, C. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201053 · Cited by 14
Alzheimer’s disease pathology and the unfolded protein response: prospective pathways and therapeutic targets
Koss, D. J., & Platt, B. (2017) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000299 · Cited by 12
Systemic Metabolism and Mitochondria in the Mechanism of Alzheimer’s Disease: Finding Potential Therapeutic Targets
Song, M., & Fan, X. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098398 · Cited by 11
Triiodothyronine Treatment reverses Depression-Like Behavior in a triple-transgenic animal model of Alzheimer’s Disease
Maglione, A., do Nascimento, B. P. P., Ribeiro, M. O., de Souza, T. J. L., da Silva, R. E. C., Sato, M. A., Penatti, C. A. A., Britto, L. R., de Souza, J. S., Maciel, R. M. B., et al. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-022-01055-9 · Cited by 11
Nonfibrillar Abeta1–42 Inhibits Glutamate Uptake and Phosphorylates p38 in Human Fibroblasts
Zoia, C., Riva, C., Isella, V., Proserpio, P., Terruzzi, A., Arban, S., Salerno, D., Cassina, V., Mantegazza, F., Tremolizzo, L., et al. (2010) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0b013e3181f9860f · Cited by 11
Brimapitide Reduced Neuronal Stress Markers and Cognitive Deficits in 5XFAD Transgenic Mice
Gourmaud, S., Lopes, P. T., Thomasseau, S., Tible, M., Abadie, C., Paquet, C., & Hugon, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171099 · Cited by 11
The increased density of p38 mitogen-activated protein kinase-immunoreactive microglia in the sensorimotor cortex of aged TgCRND8 mice is associated predominantly with smaller dense-core amyloid plaques
Chlan‐Fourney, J., Zhao, T., Walz, W., & Mousseau, D. D. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07597.x · Cited by 11
Cytotoxic Intermediates in the Fibrillation Pathway: Aβ Oligomers in Alzheimer’s Disease as a Case Study
Klein, W. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_4 · Cited by 11
Hexa (ethylene glycol) derivative of benzothiazole aniline promotes dendritic spine formation through the RasGRF1–Ras dependent pathway
Lee, N. J., Song, J. M., Cho, H.-J., Sung, Y. M., Lee, T., Chung, A., Hong, S., Cifelli, J. L., Rubinshtein, M., Habib, L. K., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.007 · Cited by 11
Targeting JNK3 for Alzheimer's disease: Design and synthesis of novel inhibitors with aryl group diversity utilizing wide pocket
Kim, H., Park, H., Jun, J., Moon, J., Oh, J., Bhujbal, S. P., & Hah, J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117209 · Cited by 10
Microcurrent therapy as the nonpharmacological new protocol against Alzheimer’s disease
Kim, E. H., Lee, W. S., Lee, J. H., & Kwon, D. R. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1344072 · Cited by 10
A Brief Ischemic Postconditioning Protects Against Amyloid-β Peptide Neurotoxicity by Downregulating MLK3-MKK3/6-P38MAPK Signal in Rat Hippocampus
Li, H., Luo, X.-B., Xu, Y., & Hou, X. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190207 · Cited by 10
Evolving significance of kinase inhibitors in the management of Alzheimer's disease
Ansari, M. M., Sahu, S. K., Singh, T. G., Singh, S. R. J., & Kaur, P. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176816 · Cited by 9
Molecular and Biochemical Pathways Encompassing Diabetes Mellitus and Dementia
Behl, T., Arora, A., Sehgal, A., Singh, S., Sharma, N., Bhatia, S., Al‐Harrasi, A., BUNGAU, S. G., & Mostafavi, E. (2021) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527320666211110115257 · Cited by 9
Amyloid Aβ1−40preconditions non‐apoptotic signalsin vivoand protects fetal rat brain from intrauterine ischemic stress
Kuperstein, F., Brand, A., & Yavin, E. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02778.x · Cited by 9
Cerebellar Insulin/IGF-1 signaling in diabetic rats: Effects of exercise training
Borges, M. E., Ribeiro, A. M., Pauli, J. R., Arantes, L. M., Luciano, E., de Moura, L. P., Leme, J. A. C. D. A., Medeiros, A., Bertolini, N. O., Sibuya, C. Y., et al. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.12.059 · Cited by 8
Peroxisome proliferator‐activated receptor alpha accelerates neuronal differentiation and this might involve the mitogen‐activated protein kinase pathway
Lin, C., Chen, P., Chan, H., Huang, Y., & Chang, N.-W. (2018) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2018.08.006 · Cited by 10
Dose-dependent neuroprotective effect of the JNK inhibitor Brimapitide in 5xFAD transgenic mice
Porte, B., Marguerit, G., Thomasseau, S., Paquet, C., & Hugon, J. (2019) · Brain Research · doi:10.1016/j.brainres.2019.146587 · Cited by 8
Cytoplasmic Tail Adaptors of Alzheimer's Amyloid-β Protein Precursor
Kawasumi, M., Matsuda, S., Matsuoka, M., & Nishimoto, I. (2004) · Molecular Neurobiology · doi:10.1385/mn:30:2:185 · Cited by 9
Vanadyl acetylacetonate attenuates Aβ pathogenesis in APP/PS1 transgenic mice depending on the intervention stage
Tan, C., Dong, Y., Wang, J., & Yang, X. (2019) · New Journal of Chemistry · doi:10.1039/c9nj00820a · Cited by 8
Date palm: a potential nutraceutical and phytomedicine in most frequent aging associated diseases
Albishi, T. S. (2024) · Journal of Umm Al-Qura University for Applied Sciences · doi:10.1007/s43994-024-00190-6 · Cited by 8
DNA-PK and P38 MAPK: A Kinase Collusion in Alzheimer’s Disease?
Kanungo, J. (2017) · Brain Disorders & Therapy · doi:10.4172/2168-975x.1000232 · Cited by 7
Aging Increases Hippocampal DUSP2 by a Membrane Cholesterol Loss-Mediated RTK/p38MAPK Activation Mechanism
Martín‐Segura, A., Casadomé‐Perales, Á., Fazzari, P., Mas, J. M., Artigas, L., Valls, R., Nebreda, Á. R., & Dotti, C. G. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00675 · Cited by 7
Saikosaponin C ameliorates tau-related pathology by modulating oxidative stress and MAPK axis in Alzheimer's disease
Chen, D., Li, R., She, F., Chen, J., Cho, S. M., Yang, B., Tian, Y., Guan, L., Zheng, X., Wang, Q., et al. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120221 · Cited by 6
QSAR modelling, molecular docking studies and ADMET predictions of polysubstituted pyridinylimidazoles as dual inhibitors of JNK3 and p38α MAPK
Živadinović, B., Stamenović, J., Živadinović, J., Živadinović, L., Sokolović, M., Filipović, S. S., Sokolovic, D. T., & Veselinović, A. M. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.133504 · Cited by 6
Inhibiting p38 mitogen-activated protein kinase attenuates cerebral ischemic injury in Swedish mutant amyloid precursor protein transgenic mice.
Zou, L., Qin, H., He, Y., Huang, H., Lu, Y., & Chu, X. (2012) · PubMed Central · doi:10.3969/j.issn.1673-5374.2012.14.007 · Cited by 6
Effects of propofol on hippocampal neuron viability
Xu, X., Wu, G., Liu, Y., & Zhang, L. (2020) · Child s Nervous System · doi:10.1007/s00381-020-04548-z · Cited by 6
Early Changes in Behavior Deficits, Amyloid β-42 Deposits and MAPK Activation in Doubly Transgenic Mice Co-expressing NSE-Controlled Human Mutant PS2 and APPsw
Hwang, D. Y., Cho, J. S., Oh, J. H., Shim, S. B., Jee, S. W., Lee, S. H., Seo, S. J., Song, C. W., Lee, S. H., & Kim, Y. K. (2005) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-005-4950-x · Cited by 6
The Protective Role of Vitamin E in Vascular Amyloid β-Mediated Damage
Muñoz, F. J., Solé, M., & Coma, M. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_7 · Cited by 7
Identification of Novel Cdc37 Interacting Proteins and Pathways in Human Alzheimer’ s Disease Brain Tissue Using Mass Spectrometry
Narayan, M., & Kirouac, L. (2016) · Journal of Data Mining in Genomics & Proteomics · doi:10.4172/2153-0602.1000193 · Cited by 4
JNK3 Overexpression in the Entorhinal Cortex Impacts on the Hippocampus and Induces Cognitive Deficiencies and Tau Misfolding
Ardanaz, C. G., Ezkurdia, A., Bejarano, A., Echarte, B., Smerdou, C., Martišová, E., Martínez-Valbuena, I., Luquín, M. R., Ramírez, M. J., & Solas, M. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00092 · Cited by 5
The Role of Presenilin-1 in the Excitotoxicity of Ethanol Withdrawal
Jung, M. E., Metzger, D. B., & Das, H. K. (2016) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.116.233361 · Cited by 5
JNK Signaling Pathway Activity Alterations in the Rat Hippocampus: Effect of Age, Alzheimer’s Disease-Like Pathology Development, and the JNK Inhibitor IQ-1S
Muraleva, N. A., Александровна, Ж. А., Khlebnikov, А. I., & Kolosova, N. G. (2025) · Biochemistry (Moscow) · doi:10.1134/s0006297924603903 · Cited by 4
Ethanol extract of Moschus attenuates glutamate-induced cytotoxicity in HT22 cells by regulating the Nrf2 and MAPK pathways
Chu, Z., Chen, Y., Xie, D., Song, C., Lin, Y., Qin, T., Zhai, Z., Cao, Z., Xu, Y., & Sun, T. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.119879 · Cited by 5
Self-citation
Gene Expression Profile in Different Age Groups and Its Association with Cognitive Function in Healthy Malay Adults in Malaysia
Sani, N. F. A., Hamzah, A. I. Z. A., Bakar, Z. H. A., Yusof, Y. A. M., Makpol, S., Ngah, W. Z. W., & Damanhuri, H. A. (2021) · Cells · doi:10.3390/cells10071611 · Cited by 4
Research on the Chemical Constituents against Alzheimer's Disease of the Fruits of Physalis alkekengi L. var. franchetii (Mast.) Makino
Teng, Y., Yuan, Q., Wu, Y., Wu, S., Su, J., Zhang, P., & Zhang, Y. (2023) · Chemistry & Biodiversity · doi:10.1002/cbdv.202301075 · Cited by 4
Molecular Aspects of Memory Dysfunction in Alzheimer’s Disease
Chin, J., Roberson, E. D., & Mucke, L. (2008) · Elsevier eBooks · doi:10.1016/b978-012370509-9.00015-2 · Cited by 5
Beneficial effects of phenolic compounds from fruit and vegetables in neurodegenerative diseases
Singh, M., & Ramassamy, C. (2008) · Elsevier eBooks · doi:10.1533/9781845694289.2.145 · Cited by 5
Identification and analysis of the jnk1 gene in polyploid hybrids of red crucian carp (Carassius auratus red var.) and common carp (Cyprinus carpio L.)
Xiao, Y., Jiang, M. G., Luo, Z., Zhou, Y., Wen, S., Wang, M., Zhang, C., & Liu, S. J. (2014) · Genetics and Molecular Research · doi:10.4238/2014.february.19.1 · Cited by 3
Cell-permeable p38 MAP kinase protects adult hippocampal neurons from cell death
Shigiyama, F., Hamanoue, M., Kobayashi, M., & Takamatsu, K. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.02.002 · Cited by 3
Immediate Early Genes, Inducible Transcription Factors and Stress Kinases in Alzheimer’s Disease
Ferrer, I., Santpere, G., & Puig, B. (2006) · Springer eBooks · doi:10.1007/978-0-387-33604-6_13 · Cited by 2
Investigating the ameliorative effect of Kalanchoe pinnata on neuroinflammation-associated Alzheimer’s disease using network pharmacology, molecular docking, and in vitro studies
Khandayataray, P., & Murthy, M. K. (2025) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-025-00688-z · Cited by 2
The effects of short-term JNK inhibition on the survival and growth of aged sympathetic neurons
Guha, I., Slámová, I., Chun, S., Clegg, A., Golos, M. R., Thrasivoulou, C., Simons, J. P., & Al‐Shawi, R. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.06.016 · Cited by 2
Natural antioxidants in prevention and management of Alzheimer's disease
Zhao, Y. M. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/516 · Cited by 2
Diet, Abeta Oligomers and Defective Insulin and Neurotrophic Factor Signaling in Alzheimer’s Disease
Cole, G. M., Ma, Q., Yang, F., Deshpande, A. M., Ubeda, O. J., & Frautschy, S. A. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0_11 · Cited by 1
Neuroprotective strategies in Alzheimer’s disease
Longo, F. M., & Massa, S. M. (2004) · Neurotherapeutics · doi:10.1007/bf03206572 · Cited by 1
Resistance of E2F4DN to p38 MAPK phosphorylation attenuates DNA damage-induced neuronal death via Cited2Preprint
Llabrés-Mas, A. M., López-Sánchez, N., Garrido‐García, A., Cano‐Daganzo, V., & Frade, J. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.29.620791 · Cited by 1
Vascular aspects of Alzheimer's disease: role of oxidative stress on vascular miocytes B-amyloid production and B-amyloid-induced toxicity in endothelial cells
Coma, M. (2007) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Thinking Outside the Box in Alzheimer Disease Treatment
Castellani, R. J., Marlatt, M. W., Nunomura, A., Moreira, P. I., Lee, H., Casadesús, G., Zhu, X., Perry, G. L., & Smith, M. A. (2011) · Wiley eBooks · doi:10.1002/9780470571224.pse457
Effect of nitric oxide and inflammatory mediators on axonal transport
Stagi, M. (2005) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-604
Animal Models of Tauopathy
Duff, K., Krishnamurthy, P., Planel, E., & Hutton, M. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_13
Endosomes élargis et cholestérol : De la trisomie 21 à la maladie d'Alzheimer
Cossec, J. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique)
Alterações neurogliais em ratos expostos ao ácido ocadáico como modelo de demência
Costa, A. P. (2011) · Americanae (AECID Library)
Therapeutic Opportunities in Alzheimer Disease: Current Concepts
Marlatt, M. W., Moreira, P. I., Lee, H., Casadesús, G., Castellani, R. J., Takeda, A., Nunomura, A., Zhu, X., Perry, G. L., & Smith, M. A. (2010) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/978160805207310904010767
Non‐amyloid Approaches To Alzheimer's Disease
Veng, L., Savage, M. J., Barrow, J. C., & Zerbinatti, C. (2010) · Wiley eBooks · doi:10.1002/0471266949.bmc253
Self-citation
The distribution of p38(MAPK) in the sensorimotor cortex of a mouse model of Alzheimer’s disease
Zhao, T. (2011)
El 17-?-estradiol frente a la muerte apoptótica en neuronas granulares de cerebelo: efectos sobre la supervivencia y modulación de la plasticidad neuronal
Molina, M. A., & Jesús, A. (2007) · TDX (Tesis Doctorals en Xarxa)
Pathways of p38, GSK3b, and Their Extensions to Mental Health
Carr, A. G. (2017) · ScholarWorks -A service of University of Vermont Libraries (University of Vermont)
METAPLASTICITY IN A MOUSE MODEL OF ALZHEIMER’S DISEASE AND POSSIBLE THERAPEUTIC INTERVENTIONS
Megill, A. (2014)
Investigation into the molecular complexity of Alzheimer's disease : an amyloid-β centered approach
Cioffi, F. (2019) · doi:10.3990/1.9789036548410
Thrombopoietin Receptor Agonist Eltrombopag Prevents Insulin Resistance and Synaptic Pathology via HIF1α/COX2/Sirt1 Signaling PathwayPreprint
Yu, H., Wang, X., liu, L., Chen, B., Feng, S., Lu, X., You, R., & Ding, S. (2021) · Research Square · doi:10.21203/rs.3.rs-308317/v1
JNK3 overexpression in the entorhinal cortex disseminates to the hippocampus and induces cognitive deficiencies and Tau misfoldingPreprint
Ardanaz, C. G., Bejarano, A., Echarte, B., Smerdou, C., Martišová, E., Martínez-Valbuena, I., Luquín, M. R., Ramírez, M. J., & Solas, M. (2022) · Research Square · doi:10.21203/rs.3.rs-1381483/v1
JNK3 overexpression in the entorhinal cortex disseminates to the hippocampus and induces cognitive deficiencies and Tau misfoldingPreprint
Ardanaz, C. G., Bejarano, A., Echarte, B., Smerdou, C., Martišová, E., Martínez-Valbuena, I., Luquín, M. R., Ramírez, M. J., & Solas, M. (2022) · Research Square · doi:10.21203/rs.3.rs-1381483/v2
Molecular Basis of Role of Insulin Resistance in Pathophysiology of Alzheimer’s Disease
Gupta, A. (2022) · International Journal of Health Sciences and Pharmacy · doi:10.47992/ijhsp.2581.6411.0094
Oxidative Stress Associated Signal Transduction Cascades in Alzheimer Disease
Petersen, R. B., Nunomura, A., Lee, H., Casadesús, G., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Contemporary clinical neuroscience · doi:10.1007/978-1-60327-342-8_8
The Emphatic Role of Mitogen-Activated Protein Kinases (MAPKs) in the Cellular Mechanisms Mediating Alzheimer's Disease
Haddad, J. J. (2007) · Technische Universität Dortmund Eldorado (Technische Universität Dortmund) · doi:10.17877/de290r-7331
Targeting autophagy-related serine/threonine kinases to combat neurodegenerative disorders
Liu, W., & Liu, B. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44173-8.00016-4
BindingDB Entry 50023403: Targeting JNK3 for Alzheimer's disease: Design and synthesis of novel inhibitors with aryl group diversity utilizing wide pocket.
BindingDB (2026) · UC San Diego · doi:10.7270/q2mw2p23
BindingDB Entry 50021501: Targeting protein kinases for the treatment of Alzheimer's disease: Recent progress and future perspectives.
BindingDB (2025) · UC San Diego · doi:10.7270/q2z89j1j
BindingDB Entry 50019685: Carbamate JNK3 Inhibitors Show Promise as Effective Treatments for Alzheimer's Disease: In Vivo Studies on Mouse Models.
BindingDB (2024) · UC San Diego · doi:10.7270/q2v98df9

Authors: Savage, M. J., Lin, Y.-G., Ciallella, J. R., Flood, D. G., & Scott, R. W.
ORCID: Scott, Richard W.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2002-05-01
Volume: 22
Issue: 9
Pages: 3376-3385
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.22-09-03376.2002
PMC: PMC6758401
OpenAlex: W1558509021
Cited by: 291
References: 61
Citations by year: 2026: 2 · 2025: 9 · 2024: 6 · 2023: 11 · 2022: 10 · 2021: 8 · 2020: 8 · 2019: 15 · 2018: 8 · 2017: 8 · 2016: 16 · 2015: 9 · 2014: 14 · 2013: 9 · 2012: 6
FWCI: 12.81
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Neuroscience (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: Alzheimer's disease, c-Jun N-terminal kinase, p38 MAPK, amyloid deposition, MAPK signaling, Tg2576 mice, amyloid precursor protein, MAPKAPK4, c-Jun, tau phosphorylation, synaptophysin, synaptic integrity, neuronal loss, hippocampal CA1
MeSH terms: Aging, Alzheimer Disease, Amyloid, Animals, Cell Count, Cerebral Cortex, Disease Models, Animal, Enzyme Activation, Hippocampus, Humans, Immunohistochemistry, Membrane Proteins, Mice, Transgenic, Neurons, Phosphorylation, Signal Transduction, Neurites, Amyloid beta-Protein Precursor, Synaptophysin, tau Proteins, Gene Targeting, Amino Acid Substitution, Mitogen-Activated Protein Kinases, JNK Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases, Mice, Presenilin-1

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

Activation of c-Jun N-Terminal Kinase and p38 in an Alzheimer's Disease Model Is Associated with Amyloid Deposition

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks