The DOI matches its Crossref record; 56 of the 57 references it cites were found in a registry or an index.
Tumor Necrosis Factor-α, Interleukin-1β, and Interferon-γ Stimulate γ-Secretase-mediated Cleavage of Amyloid Precursor Protein through a JNK-dependent MAPK Pathway
Open accessAbstract
The deposition of the amyloid beta (Abeta) peptide in neuritic plaques plays a critical role in the pathogenesis of Alzheimer's disease (AD). Abeta is generated through the proteolysis of amyloid precursor protein (APP) by the sequential actions of beta- and gamma-secretases. Although recent evidence has unveiled much about the biochemical identity and characteristics of gamma-secretase, the mechanism regulating endogenous gamma-secretase activity remains elusive. To identify possible extracellular signals and associated signaling cascades that could regulate APP proteolysis by gamma-secretase activity, we have developed a cell-based reporter gene assay by stably cotransfecting HEK293 cells with the Gal4-driven luciferase reporter gene and the Gal4/VP16-tagged C-terminal fragment of APP (C99-GV), the immediate substrate of gamma-secretase. The cleavage of C99-GV by gamma-secretase releases the transcription factor that activates luciferase expression, providing a quantitative measurement of gamma-secretase activity. Using this reporter assay, we have demonstrated that interferon-gamma, interleukin-1beta, and tumor necrosis factor-alpha can specifically stimulate gamma-secretase activity, concomitant with increased production of Abeta and the intracellular domain of APP (AICD). The gamma-secretase-dependent cleavage of Notch is also enhanced upon the stimulation of these cytokines. The cytokine-enhanced gamma-secretase activity can be suppressed by a potent inhibitor of c-Jun N-terminal kinase (JNK). Furthermore, cells transfected with dominant-positive MEKK1, one of the most potent activators of the JNK cascade, exhibit increased gamma-secretase activity, suggesting that the JNK-dependent mitogen-activated protein kinase pathway could mediate the cytokine-elicited regulation of gamma-secretase. Our studies provide direct evidence that cytokine-elicited signaling cascades control Abeta production by modulating gamma-secretase activity.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“B94 (GenBank M92357) is a TNF-α-inducible proinflammatory element (Colangelo et al., 2002; Liao et al., 2004).”
From Docosanoids and elovanoids from omega-3 fatty acids are pro-homeostatic modulators of inflammatory responses, cell damage and neuroprotection (2018) · cites this paper as Liao et al., 2004
In the citing paper
“IL-1β directly stimulates γ-secretase-mediated cleavage of βAPP into Aβ peptides through a JNK-dependent MAPK pathway (Liao et al., 2004).”
From Docosanoids and elovanoids from omega-3 fatty acids are pro-homeostatic modulators of inflammatory responses, cell damage and neuroprotection (2018) · cites this paper as Liao et al., 2004
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Nuclear Factor-κB — A Pivotal Transcription Factor in Chronic Inflammatory Diseases
Barnes, P. J., & Karin, M. (1997) · New England Journal of Medicine · doi:10.1056/nejm199704103361506 · Cited by 4,622
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase
Bennett, B. L., Sasaki, D. T., Murray, B. W., O'Leary, E. C., Sakata, S. T., Xu, W., Leisten, J. C., Motiwala, A., Pierce, S., Satoh, Y., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251194298 · Cited by 2,558
Signal transduction by tumor necrosis factor and its relatives.
Baud, V., & Karin, M. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02064-5 · Cited by 1,741
Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
Schroeter, E. H., Kisslinger, J. A., & Kopan, R. (1998) · Nature · doi:10.1038/30756 · Cited by 1,624
Amyloid, the presenilins and Alzheimer’s disease
Hardy, J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01030-2 · Cited by 1,370
The Molecular Cell Biology of Interferon-Gamma and Its Receptor
Farrar, M. A., & Schreiber, R. D. (1993) · Annual Review of Immunology · doi:10.1146/annurev.iy.11.040193.003035 · Cited by 1,353
Differential Activation of ERK and JNK Mitogen-Activated Protein Kinases by Raf-1 and MEKK
Minden, A., Lin, A., McMahon, M., Lange, C. A., Dérijard, B., Davis, R. J., Johnson, G. L., & Karin, M. (1994) · Science · doi:10.1126/science.7992057 · Cited by 1,069
Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
Yu, G., Nishimura, M., Arawaka, S., Levitan, D. J., Zhang, L., Tandon, A., Song, Y., Rogaeva, E. A., Chen, F., Kawarai, T., et al. (2000) · Nature · doi:10.1038/35024009 · Cited by 929
Flagged first, then by citations
1 of the 57 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 391
Liu, Y., Li, H., Wang, J., Xue, Q., Yang, X., Kang, Y., Li, M., Xu, J., Li, G., Li, C., et al. (2020) · JAMA Network Open · doi:10.1001/jamanetworkopen.2020.18777 · Cited by 90
Dunn, H. C., Ager, R. R., Baglietto‐Vargas, D., Cheng, D., Kitazawa, M., Cribbs, D. H., & Medeiros, R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-141335 · 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
Vingtdeux, V., Hamdane, M., Gompel, M., Bégard, S., Drobecq, H., Ghestem, A., Grosjean, M., Kostanjevečki, V., Grognet, P., Vanmechelen, E., et al. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.05.004 · Cited by 86
Increased frequency of α-synuclein in the substantia nigra in human immunodeficiency virus infection
Khanlou, N., Khanlou, N., Moore, D. J., Khanlou, N., Moore, D. J., Chana, G., Cherner, M., Lazzaretto, D., Dawes, S. E., Grant, I., et al. (2009) · Journal of NeuroVirology · doi:10.1080/13550280802578075 · Cited by 87
Sayed, A., Bahbah, E. I., Kamel, S., Barreto, G. E., Ashraf, G. M., & Elfil, M. (2020) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2020.577398 · Cited by 88
Clark, I. A., & Vissel, B. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13181 · Cited by 84
The Evolving Biology of Microglia in Alzheimer's Disease
Malm, T. M., Jay, T. R., & Landreth, G. E. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0316-8 · Cited by 85
Bot, N., Schweizer, C., Ben Halima, S., & Fraering, P. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.142521 · Cited by 81
Amyloid-β and Phosphorylated Tau are the Key Biomarkers and Predictors of Alzheimer’s Disease
Pradeepkiran, J. A., Baig, J., Islam, M. A., Kshirsagar, S., & Reddy, P. H. (2024) · Aging and Disease · doi:10.14336/ad.2024.0286 · Cited by 87
Wolfe, M. S., & Guénette, S. Y. (2007) · Journal of Cell Science · doi:10.1242/jcs.03481 · Cited by 77
Self-citationClark, I. A., Atwood, C., Bowen, R. L., Paz-Filho, G., & Vissel, B. (2012) · Pharmacological Reviews · doi:10.1124/pr.112.005850 · Cited by 76
RAGE is a key cellular target for A -induced perturbation in Alzheimer s disease
Yan, S. S. (2011) · Frontiers in Bioscience-Scholar · doi:10.2741/265 · Cited by 108
Hole, K. L., & Williams, R. J. (2020) · Brain Plasticity · doi:10.3233/bpl-200098 · Cited by 81
Plasma Aβ42 correlates positively with increased body fat in healthy individuals
Balakrishnan, K., Verdile, G., Mehta, P. D., Beilby, J. P., Nolan, D. A., Galvao, D. A., Newton, R. U., Gandy, S., & Martins, R. N. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-8305 · Cited by 76
Insulin resistance, neuroinflammation, and Alzheimer’s disease
Najem, D., Bamji‐Mirza, M., Chang, N., Liu, Q. Y., & Zhang, W. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2013-0050 · Cited by 76
Bulati, M., Buffa, S., Martorana, A., Gervasi, F., Camarda, C., Azzarello, D. M., Monastero, R., Caruso, C., & Colonna-Romano, G. (2015) · Journal of Alzheimer’s Disease · doi:10.3233/jad-142412 · Cited by 72
Wu, H., Qiu, W., Zhu, X., Li, X., Xie, Z., Carreras, I., Dedeoglu, A., Dyke, T. E. V., Han, Y. W., Karimbux, N. Y., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.912709 · Cited by 73
Association of Peripheral Blood Cell Profile With Alzheimer's Disease: A Meta-Analysis
Huang, L., Zhang, C., Wang, Y., & Wang, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.888946 · Cited by 76
Protease Regulation: The Yin and Yang of Neural Development and Disease
Bai, G., & Pfaff, S. L. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.012 · Cited by 70
Integrated communications between cyclooxygenase‐2 and Alzheimer's disease
Guan, P.-P., & Wang, P. (2018) · The FASEB Journal · doi:10.1096/fj.201800355rrrr · Cited by 70
Cellular and Molecular Mediators of Neuroinflammation in Alzheimer Disease
Yang, S. (2019) · International Neurourology Journal · doi:10.5213/inj.1938184.092 · Cited by 72
Molecular Mechanisms Underlying Neuroinflammation Elicited by Occupational Injuries and Toxicants
Pathak, D., & Sriram, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032272 · Cited by 72
Cao, L., Cao, X., Zhou, Y., Nagpure, B. V., Wu, Z., Hu, L. F., Yang, Y., Sethi, G., Moore, P. K., & Bian, J. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.07.005 · Cited by 64
Perispinal etanercept: a new therapeutic paradigm in neurology
Tobinick, E. L. (2010) · Expert Review of Neurotherapeutics · doi:10.1586/ern.10.52 · Cited by 64
Wang, P., Yu, X., Guan, P.-P., Guo, J., Wang, Y., Zhang, Y., Zhao, H., & Wang, Z. (2015) · Cellular and Molecular Immunology · doi:10.1038/cmi.2015.93 · Cited by 63
Lin, H., Hsieh, H.-M., Chen, Y.-H., & Hu, M. (2009) · NeuroToxicology · doi:10.1016/j.neuro.2009.03.011 · Cited by 62
Findeis, M. A., Schroeder, F. C., McKee, T. D., Yager, D., Fraering, P. C., Creaser, S. P., Austin, W., Clardy, J., Wang, R., Selkoe, D. J., et al. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn3000857 · Cited by 61
Couturier, J., Paccalin, M., Morel, M., Terro, F., Milin, S., Pontcharraud, R., Fauconneau, B., & Page, G. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-72 · Cited by 65
Actin dynamics shape microglia effector functions.
Uhlemann, R., Gertz, K., Boehmerle, W., Schwarz, T., Nolte, C., Freyer, D., Kettenmann, H., Endres, M., & Kronenberg, G. (2016) · Brain Structure and Function · doi:10.1007/s00429-015-1067-y · Cited by 61
Park, J., Lee, S., Shon, J., Kim, K., Lee, H. J., Kim, K., Lee, B.-Y., Oh, S., KIM, N. K., & Kim, O. J. (2019) · Cytotherapy · doi:10.1016/j.jcyt.2019.04.054 · Cited by 60
Paouri, E., Tzara, O., Zenelak, S., & Georgopoulos, S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170065 · Cited by 61
Inflammation as common link to progressive neurological diseases
Dias-Carvalho, A., Sá, S. I., Carvalho, F., Fernandes, E., & Costa, V. M. (2024) · Archives of Toxicology · doi:10.1007/s00204-023-03628-8 · Cited by 60
Review: The long‐term consequences of microglial activation following acute traumatic brain injury
Smith, C. (2012) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12006 · Cited by 61
Nutrients, Microglia Aging, and Brain Aging
Wu, Z., Yu, J., Zhu, A., & Nakanishi, H. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7498528 · Cited by 59
Kim, S., Nam, Y., Kim, C., Lee, H., Hong, S.-J., Kim, H. S., Shin, S. J., Park, Y. H., Mai, H. N., Oh, S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103678 · Cited by 55
Kuo, L.-H., Hu, M., Hsu, W., Tung, Y.-T., Wang, B., Tsai, W.-W., Yen, C., & Liao, Y.-F. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0987 · Cited by 55
Self-citationAlzheimer’s Disease and Helicobacter pylori Infection: Inflammation from Stomach to Brain?
Albaret, G., Sifré, E., Floch, P., Layé, S., Aubert, A., Dubus, P. R., Martin, L. A., Giese, A., Salles, N., Mégraud, F., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190496 · Cited by 56
Ruganzu, J. B., Peng, X., He, Y., Wu, X., Zheng, Q., Ding, B., Lin, C., Guo, H., Yang, Z., Zhang, X. L., et al. (2021) · Molecular Immunology · doi:10.1016/j.molimm.2021.12.018 · Cited by 56
Evidence for a role of the amyloid precursor protein in thyroid carcinogenesis
Krause, K., Karger, S., Sheu, S., Aigner, T. G., Kursawe, R., Gimm, O., Schmid, K.-W., Dralle, H., & Führer, D. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0005 · Cited by 55
Traumatic Brain Injury, Microglia, and Beta Amyloid
Mannix, R., & Whalen, M. J. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/608732 · Cited by 53
Zhang, W., Bai, M., Ye, X., Hao, J., Zhang, Z., Su, C., Lei, G., Miao, J., & Li, Z. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.12.023 · Cited by 53
RetractedTransforming Growth Factor β2 Is a Neuronal Death-Inducing Ligand for Amyloid-β Precursor Protein
Hashimoto, Y., Chiba, T., Yamada, M., Nawa, M., Kanekura, K., Suzuki, H., Terashita, K., Aiso, S., Nishimoto, I., & Matsuoka, M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9304-9317.2005 · Cited by 51
The Association between TNF-alpha, IL-1 alpha and IL-10 with Alzheimer's Disease
Čuljak, M., Perković, M. N., Uzun, S., Štrac, D. Š., Erjavec, G. N., Leko, M. B., Šimić, G., Tudor, L., Konjevod, M., Kozumplik, O., et al. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666201130092427 · Cited by 52
Anti-Neuroinflammatory Potential of Polyphenols by Inhibiting NF-Κb to Halt Alzheimer's Disease
Uddin, M. S., Hasana, S., Ahmad, J., Hossain, M. F., Rahman, M. M., Behl, T., Rauf, A., Ahmad, A., Hafeez, A., Perveen, A., et al. (2021) · Current Pharmaceutical Design · doi:10.2174/1381612826666201118092422 · Cited by 49
Anti-Amyloidogenic Effect of Thiacremonone through Anti-Inflamation In Vitro and In Vivo Models
Lin, G. H., Lee, Y., Choi, D., Han, S., Jung, J., Hwang, B. Y., Moon, D. C., Kim, Y. S., Lee, M. K., Oh, K., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111709 · Cited by 49
The Functions and Phenotypes of Microglia in Alzheimer’s Disease
Fujikawa, R., & Tsuda, M. (2023) · Cells · doi:10.3390/cells12081207 · Cited by 58
Lee, Y., Choi, D., Choi, I. S., Han, J., Jeong, H., Han, S., Oh, K., & Hong, J. T. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-132 · Cited by 48
Dong, Y., Dekens, D. W., Deyn, P. P. D., Naudé, P. J. W., & Eisel, U. L. M. (2015) · Antibodies · doi:10.3390/antib4040369 · Cited by 50
TNF alpha inhibitors in Alzheimer's disease: A systematic review
Ekert, J. O., Gould, R. L., Reynolds, G., & Howard, R. J. (2018) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.4871 · Cited by 51
Sleep Disturbances in MCI and AD: Neuroinflammation as a Possible Mediating Pathway
Pak, V. M., Onen, S. ‐., Bliwise, D. L., Kutner, N. G., Russell, K. L., & Onen, F. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00069 · Cited by 53
Ren, S., Breuillaud, L., Yao, W., Yin, T., Norris, K. A., Zehntner, S. P., & D’Adamio, L. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.016395 · Cited by 47
Barber, K., Mendonca, P., & Soliman, K. F. A. (2023) · Brain Sciences · doi:10.3390/brainsci13010145 · Cited by 51
Biomaterials-based anti-inflammatory treatment strategies for Alzheimer’s disease
Chu, J., Zhang, W., Liu, Y., Gong, B., Ji, W., Yin, T., Gao, C., Liangwen, D., Hao, M., Chen, C., et al. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.374137 · Cited by 48
Kalinowski, A., Plowes, N. J. R., Huang, Q., Berdejo‐Izquierdo, C., Russell, R. R., & Russell, K. S. (2010) · The FASEB Journal · doi:10.1096/fj.08-129072 · Cited by 47
Stress and Alzheimer’s disease: A senescence link?
Lyons, C. E., & Bartolomucci, A. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.05.010 · Cited by 49
Revisiting the Role of Vitamins and Minerals in Alzheimer’s Disease
Shah, H., Dehghani, F., Ramezan, M., Gannaban, R. B., Haque, Z. F., Rahimi, F. C., Abbasi, S., & Shin, A. C. (2023) · Antioxidants · doi:10.3390/antiox12020415 · Cited by 48
Mechanistic and therapeutic role of NLRP3 inflammasome in the pathogenesis of Alzheimer's disease
Jha, D., Bakker, E. N. T. P., & Kumar, R. K. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15788 · Cited by 48
Role of neurotoxicants in the pathogenesis of Alzheimer’s disease: a mechanistic insight
Nisa, F. Y., Rahman, M. A., Hossen, M. A., Khan, M. F., Khan, M. A. N., Majid, M., Sultana, F., & Haque, M. A. (2021) · Annals of Medicine · doi:10.1080/07853890.2021.1966088 · Cited by 44
Kok, F. K., van Leerdam, S., & de Lange, E. C. M. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-210607 · Cited by 46
Guarding the Blood–Brain Barrier: A Role for Estrogen in the Etiology of Neurodegenerative Disease
Sohrabji, F. (2006) · Gene Expression · doi:10.3727/000000006781510723 · Cited by 44
Amyloidosis in Retinal Neurodegenerative Diseases
Masuzzo, A., Dinet, V., Cavanagh, C., Mascarelli, F., & Krantic, S. M. (2016) · Frontiers in Neurology · doi:10.3389/fneur.2016.00127 · Cited by 45
Khezri, M. R., Yousefi, K., Mahboubi, N., Hodaei, D., & Ghasemnejad‐Berenji, M. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.114945 · Cited by 43
Cavanagh, C., Colby-Milley, J., Bouvier, D. S., Farso, M. C., Chabot, J., Quirion, R., & Krantic, S. M. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122131 · Cited by 44
Bakshi, P., Margenthaler, E., Reed, J. M., Crawford, F., & MULLAN, M. J. (2010) · Cytokine · doi:10.1016/j.cyto.2010.10.008 · Cited by 42
Novel Role of CXCR2 in Regulation of γ-Secretase Activity
Bakshi, P., Margenthaler, E., Laporte, V., Crawford, F., & MULLAN, M. J. (2008) · ACS Chemical Biology · doi:10.1021/cb800167a · Cited by 42
Xiong, W., Zhao, X., Xu, Q., Wei, G., Zhang, L., Fan, Y., Wen, L., Liu, Y., Zhang, T., Zhang, L., et al. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.114598 · Cited by 43
Sodium selenite inhibits γ-secretase activity through activation of ERK
Tung, Y.-T., Hsu, W., Wang, B., Wu, S.-Y., Yen, C., Hu, M., & Liao, Y.-F. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.05.048 · Cited by 41
Self-citationFang, Y., Yao, L., Li, C., Wang, J., Wang, J., Chen, S., Zhou, X., & Liao, H. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0522-x · Cited by 42
Cytokines and the Blood–Brain Barrier
Banks, W. A., Lynch, J. L., & Price, T. O. (2008) · Springer eBooks · doi:10.1007/978-0-387-84851-8_1 · Cited by 43
Mehta, N. H., Zhou, L., Li, Y., McIntire, L. B., Nordvig, A. S., Butler, T., de Leon, M. J., & Chiang, G. C.-Y. (2023) · Scientific Reports · doi:10.1038/s41598-023-34012-2 · Cited by 39
Soluble amyloid precursor proteins and secretases as Alzheimer's disease biomarkers
Perneczky, R., Alexopoulos, P., & Kurz, A. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.10.001 · Cited by 42
Zhao, Y., Cui, J.-G., & Lukiw, W. J. (2006) · Molecular Neurobiology · doi:10.1385/mn:34:3:181 · Cited by 38
Blaise, R., Mahjoub, M., Salvat, C., Barbe, U., Brou, C., Corvol, M. T., Savouret, J., Rannou, F., Berenbaum, F., & Bausero, P. (2009) · Arthritis & Rheumatism · doi:10.1002/art.24250 · Cited by 39
Oyeleke, M. B., & Owoyele, B. V. (2022) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2022.114997 · Cited by 38
CD40 deficiency mitigates Alzheimer's disease pathology in transgenic mouse models
Laporte, V., Ait‐Ghezala, G., Volmar, C., & MULLAN, M. J. (2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-3 · Cited by 36
Systemic inflammation as a central player in the initiation and development of Alzheimer’s disease
Bayraktaroğlu, I., Ortí-Casañ, N., Dam, D. V., Deyn, P. P. D., & Eisel, U. L. M. (2025) · Immunity & Ageing · doi:10.1186/s12979-025-00529-5 · Cited by 49
Jagged1 regulates the activation of astrocytes via modulation of NFκB and JAK/STAT/SOCS pathways
Morga, E., Mouad‐Amazzal, L., Felten, P., Heurtaux, T., Moro, M., Michelucci, A., Gabel, S., Grandbarbe, L., & Heuschling, P. (2009) · Glia · doi:10.1002/glia.20887 · Cited by 38
RetractedAtwood, C., & Bowen, R. L. (2015) · Hormones and Behavior · doi:10.1016/j.yhbeh.2015.06.021 · Cited by 38
γ-Secretase Is a Functional Component of Phagosomes
Jutras, I., Laplante, A., Boulais, J., Brunet, S., Thinakaran, G., & Desjardins, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504069200 · Cited by 39
Dendrimers and Derivatives as Multifunctional Nanotherapeutics for Alzheimer’s Disease
Moreira, D. A., Santos, S. D., Leiro, V., & Pêgo, A. P. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15041054 · Cited by 39
Kang, J. H., Lee, E. H., Park, S., & Chung, I. Y. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003606 · Cited by 37
Potential Immunotargets for Alzheimer's Disease Treatment Strategies
Fernández, P. L., Britton, G. B., & Rao, K. S. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121222 · Cited by 38
McCarty, M. F. (2006) · Medical Hypotheses · doi:10.1016/j.mehy.2006.04.067 · Cited by 37
Oprica, M., Hjorth, E., Spulber, S. D., Popescu, B. O., Ankarcrona, M., Winblad, B. G., & Schultzberg, M. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00074.x · Cited by 37
The Role of Insulin Signaling in Hippocampal-Related Diseases: A Focus on Alzheimer’s Disease
Liu, Q., Wang, Z., Cao, J., Dong, Y., & Chen, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214417 · Cited by 42
APOE epsilon-4 allele and cytokine production in Alzheimer's disease
Olgiati, P., Politis, A., Malitas, P., Albani, D., Dusi, S., Polito, L., De Mauro, S., Zisaki, A., Piperi, C., Stamouli, E., et al. (2010) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.2344 · Cited by 35
Kamal, M. A., Priyamvada, S., Anbazhagan, A. N., Jabir, N. R., Tabrez, S. S. M., & Greig, N. H. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/18715273113126660137 · Cited by 37
Rahman, S. O., Singh, R. K., Hussain, S., Akhtar, M., & Najmi, A. K. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.10.040 · Cited by 35
Zussy, C., Loustalot, F., Junyent, F., Gardoni, F., Bories, C., Valero, J., Desarménien, M. G., Bernex, F., Henaff, D., Bayó-Puxan, N., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0132-16.2016 · Cited by 37
Amoah, V., Atawuchugi, P., Yakubu, J., Tandoh, A., Ossei, P. P. S., ., G. H. S., & Ainooson, G. K. (2023) · Pharmaceutical Biology · doi:10.1080/13880209.2023.2209130 · Cited by 37
Hickey, J. P., Collins, A. E., Nelson, M. L., Chen, H., & Kalisch, B. E. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46050266 · Cited by 39
Alkaloids as Potential Multi-Target Drugs to Treat Alzheimer's Disease
Lima, J. A., & Hamerski, L. (2018) · Studies in natural products chemistry · doi:10.1016/b978-0-444-64183-0.00008-7 · Cited by 34
Martinez, B., & Peplow, P. V. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.251192 · Cited by 32
Arbo, B. D., Schimith, L. E., dos Santos, M. G., & Hort, M. A. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.174800 · Cited by 33
Zhang, H., Sachdev, P. S., Wen, W., Crawford, J. D., Brodaty, H., Baune, B. T., Kochan, N. A., Slavin, M. J., Reppermund, S., Kang, K., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.10.008 · Cited by 32
Lei, X., Yu, J. Q., Niu, Q., Liu, J., Fraering, P. C., & Wu, F. (2015) · Scientific Reports · doi:10.1038/srep16541 · Cited by 32
Yi, B., Jahangir, A. M., Evans, A. K., Briggs, D. I., Rāviņa, K., Ernest, J. P., Farimani, A. B., Sun, W., Rajadas, J., Green, M., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180319 · Cited by 33
Kapoor, A., Wang, B., Hsu, W., Chang, M., Liang, S., & Liao, Y.-F. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400039s · Cited by 32
Self-citationMosser, S., Alattia, J., Dimitrov, M. I., Matz, A., Pascual, J., Schneider, B. L., & Fraering, P. C. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu449 · Cited by 33
Metadata
- Authors
- Liao, Y.-F., Wang, B.-J., Cheng, H.-T., Kuo, L.-H., & Wolfe, M. S.
- Affiliations
- Academia Sinica (TW)
- Brigham and Women's Hospital (US)
- Corresponding author
- Liao, Yung-Feng
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-11
- Volume
- 279
- Issue
- 47
- Pages
- 49523-49532
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1992680479
- Cited by
- 389
- References
- 57
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 29 · 2023: 28 · 2022: 25 · 2021: 21 · 2020: 22 · 2019: 16 · 2018: 14 · 2017: 12 · 2016: 13 · 2015: 13 · 2014: 15 · 2013: 25 · 2012: 14
- FWCI
- 9.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- National Science Council
- Academia Sinica
- National Institutes of Health
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- gamma-secretase, amyloid precursor protein, amyloid-beta, Alzheimer's disease, TNF-α, IL-1β, interferon-gamma, JNK, MAPK signaling, MEKK1, Notch cleavage, APP intracellular domain, cytokine signaling
- MeSH terms
- Animals, Cell Line, DNA, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Genes, Dominant, Humans, Interferon-gamma, Interleukin-1, Luciferases, Membrane Proteins, Mutation, Endopeptidases, Transfection, Tumor Necrosis Factor-alpha, Blotting, Western, Signal Transduction, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Culture Media, Serum-Free, Protein Structure, Tertiary, Genes, Reporter, COS Cells, Mitogen-Activated Protein Kinase Kinases, MAP Kinase Signaling System, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase 4, Receptors, Notch, Amyloid Precursor Protein Secretases
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