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Regulation of Amyloid Precursor Protein Catabolism Involves the Mitogen-Activated Protein Kinase Signal Transduction Pathway
Open accessAbstract
Catabolic processing of the amyloid precursor protein (APP) is subject to regulatory control by protein kinases. We hypothesized that this regulation involves sequential activation of the enzymes mitogen-activated protein kinase kinase (MEK) and extracellular signal-regulated protein kinase (ERK). In the present investigation, we provide evidence that MEK is critically involved in regulating APP processing by both nerve growth factor and phorbol esters. Western blot analysis of the soluble N-terminal APP derivative APP s demonstrated that the synthetic MEK inhibitor PD 98059 antagonized nerve growth factor stimulation of both APP s production and ERK activation in PC12 cells. Moreover, PD 98059 inhibited phorbol ester stimulation of APP s production and activation of ERK in both human embryonic kidney cells and cortical neurons. Furthermore, overexpression of a kinase-inactive MEK mutant inhibited phorbol ester stimulation of APP secretion and activation of ERK in human embryonic kidney cell lines. Most important, PD 98059 antagonized phorbol ester-mediated inhibition of Aβ secretion from cells overexpressing human APP 695 carrying the “Swedish mutation.” Taken together, these data indicate that MEK and ERK may be critically involved in protein kinase C and nerve growth factor regulation of APP processing. The mitogen-activated protein kinase cascade may provide a novel target for altering catabolic processing of APP.
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“ERK activation has been shown to modulate APP processing and Aβ generation (24, 25, 36).”
From Serotonin signaling is associated with lower amyloid-β levels and plaques in transgenic mice and humans (2011) · cites this paper as [36]
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Citations
Cites
High-Efficiency Transformation of Mammalian Cells by Plasmid DNA
Chen, C., & Okayama, H. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.8.2745 · Cited by 5,327
Alessi, D. R., Cuenda, A., Cohen, P., Dudley, D. T., & Saltiel, A. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27489 · Cited by 3,374
A synthetic inhibitor of the mitogen-activated protein kinase cascade.
Dudley, D. T., Pang, L., Decker, S. J., Bridges, A. J., & Saltiel, A. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7686 · Cited by 2,679
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Cobb, M. H., & Goldsmith, E. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14843 · Cited by 1,718
Borchelt, D. R., Thinakaran, G., Eckman, C. B., Lee, M. K., Davenport, F., Ratovitsky, T., Prada, C.-M., Kim, G., Seekins, S., Yager, D., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80230-5 · Cited by 1,478
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
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
Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997) · Nature Medicine · doi:10.1038/nm0197-67 · Cited by 1,271
Gel electrophoresis of proteins: a practical approach
HAMES, B. D., & RICKWOOD, D. (1981) · Cited by 1,088
Anderson, N. G., Maller, J. L., Tonks, N. K., & Sturgill, T. W. (1990) · Nature · doi:10.1038/343651a0 · Cited by 1,064
Payne, D. M., Rossomando, A. J., Martino, P. A., Erickson, A. K., Her, J. H., Shabanowitz, J., Hunt, D. F., Weber, M. J., & Sturgill, T. W. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb08021.x · Cited by 1,041
Meisenhelder, J., Suh, P., Rhee, S. G., & Hunter, T. R. (1989) · Cell · doi:10.1016/0092-8674(89)90048-2 · Cited by 955
Nitsch, R. M., Slack, B. E., Wurtman, R. J., & Growdon, J. H. (1992) · Science · doi:10.1126/science.1411529 · Cited by 898
Pang, L., Sawada, T., Decker, S. J., & Saltiel, A. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.13585 · Cited by 896
Evidence that β-Amyloid Protein in Alzheimer's Disease Is Not Derived by Normal Processing
Sisodia, S. S., Koo, E. H., Beyreuther, K. T., Unterbeck, A., & Price, D. L. (1990) · Science · doi:10.1126/science.1691865 · Cited by 894
Self-citationAlzheimer's Disease--Genotypes, Phenotype, and Treatments
Selkoe, D. J. (1997) · Science · doi:10.1126/science.275.5300.630 · Cited by 879
(1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(97)88594-9 · Cited by 709
Selkoe, D. J., Podlisny, M. B., Joachim, C. L., Vickers, E., Lee, G. S., Fritz, L. C., & Oltersdorf, T. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.19.7341 · Cited by 579
Buxbaum, J. D., Oishi, M., Chen, H. I., Pinkas‐Kramarski, R., JAFFE, E. A., Gandy, S., & Greengard, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10075 · Cited by 563
Lemere, C. A., Lopera, F., Kosik, K. S., Lendon, C. L., Ossa, J., Saido, T. C., Yamaguchi, H., Ruiz, A., Martinez, A., Madrigal, L., et al. (1996) · Nature Medicine · doi:10.1038/nm1096-1146 · Cited by 487
Ida, N., Hartmann, T., Pantel, J., Schrüder, J., Zerfaß, R., Fürstl, H., Sandbrink, R., Masters, C. L., & Beyreuther, K. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22908 · Cited by 478
Self-citationBuxbaum, J. D., Gandy, S., Cicchetti, P., Ehrlich, M. E., Czernik, A. J., Fracasso, R. P., Ramabhadran, T. V., Unterbeck, A., & Greengard, P. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.6003 · Cited by 450
Furukawa, K., Sopher, B. L., Rydel, R. E., Begley, J. G., Pham, D. G., Martin, G. M., Fox, M., & Mattson, M. P. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67051882.x · Cited by 414
Activation of protein kinase C inhibits cellular production of the amyloid beta-protein.
Hung, A. Y., Haass, C., Nitsch, R. M., Qiu, W. Q., Citron, M., Wurtman, R. J., Growdon, J. H., & Selkoe, D. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49409-x · Cited by 400
Lazar, D. F., Wiese, R. J., Brady, M. J., Mastick, C. C., Waters, S. B., Yamauchi, K., Pessin, J. E., Cuatrecasas, P., & Saltiel, A. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.35.20801 · Cited by 396
MAP Kinases: Charting the Regulatory Pathways
Pelech, S., & Sanghera, J. S. (1992) · Science · doi:10.1126/science.1382311 · Cited by 364
Self-citationEstrogen regulates metabolism of Alzheimer amyloid beta precursor protein.
Jaffe, A. B., Toran‐Allerand, C. D., Greengard, P., & Gandy, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36796-0 · Cited by 363
The regulation of amyloid β protein precursor secretion and its modulatory role in cell adhesion
Schubert, D. A., Jin, L.-W., Saitoh, T., & Cole, G. M. (1989) · Neuron · doi:10.1016/0896-6273(89)90237-7 · Cited by 353
Slunt, H. H., Thinakaran, G., von Koch, C., Lo, A., Tanzi, R. E., & Sisodia, S. S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41992-2 · Cited by 346
Protein phosphorylation regulates secretion of Alzheimer beta/A4 amyloid precursor protein.
Caporaso, G. L., Gandy, S., Buxbaum, J. D., Ramabhadran, T. V., & Greengard, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.3055 · Cited by 338
Requirements for Phosphorylation of Map Kinase During Meiosis in Xenopus Oocytes
Posada, J. A., & Cooper, J. A. (1992) · Science · doi:10.1126/science.1313186 · Cited by 316
Citron, M., Diehl, T. S., Gordon, G., Biere, A. L., Seubert, P. A., & Selkoe, D. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.13170 · Cited by 287
Ehlers, M. R., & Riordan, J. F. (1991) · Biochemistry · doi:10.1021/bi00106a001 · Cited by 280
Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide.
Buxbaum, J. D., Koo, E. H., & Greengard, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.9195 · Cited by 276
Malarkey, K., BELHAM, C. M., Paul, A., Graham, A. M., McLees, A., Scott, P., & Plevin, R. J. (1995) · Biochemical Journal · doi:10.1042/bj3090361 · Cited by 267
Calcium Ionophore Increases Amyloid .beta. Peptide Production by Cultured Cells
Querfurth, H. W., & Selkoe, D. J. (1994) · Biochemistry · doi:10.1021/bi00181a016 · Cited by 247
Cellular signaling roles of TGFβ, TNFα and βAPP in brain injury responses and Alzheimer's disease
Mattson, M. P., Barger, S. W., Furukawa, K., Bruce‐Keller, A. J., Wyss‐Coray, T., Mark, R. J., & Mucke, L. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(96)00014-8 · Cited by 243
Rönnstrand, L., Mori, S., Arridsson, A. K., Eriksson, A. B., Wernstedt, C., Hellman, U., Claesson, L., & Heldin, C. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05484.x · Cited by 229
Downing, J. R., Roussel, M. F., & Sherr, C. J. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.7.2890 · Cited by 227
Frödin, M., Sekine, N., Roche, E., Filloux, C., Prentki, M., Wollheim, C. B., & OBBERGHEN, E. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.14.7882 · Cited by 220
Serotonin 5-HT2a and 5-HT2c Receptors Stimulate Amyloid Precursor Protein Ectodomain Secretion
Nitsch, R. M., Deng, M., Growdon, J. H., & Wurtman, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4188 · Cited by 219
Seger, R., Seger, D., Reszka, A. A., Munar, E., Eldar-Finkelman, H., Dobrowolska, G., Jensen, A., Campbell, J. S., Fischer, E. H., & Krebs, E. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47305-x · Cited by 216
Weidemann, A., Paliga, K., Dürrwang, U., Czech, C., Evin, G. M., Masters, C. L., & Beyreuther, K. T. (1997) · Nature Medicine · doi:10.1038/nm0397-328 · Cited by 214
Self-citationExact cleavage site of Alzheimer amyloid precursor in neuronal PC-12 cells
Anderson, J. P., Esch, F. S., Keim, P. S., Sambamurti, K., Lieberburg, I. M., & Robakis, N. K. R. K. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90775-o · Cited by 212
Aplin, A. E., Gibb, G. M., Jacobsen, J. S., Gallo, J., & Anderton, B. H. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67020699.x · Cited by 201
Wolf, B. A., Wertkin, A. M., Jolly, Y. C., Yasuda, R. P., Wolfe, B. B., Konrad, R. J., Manning, D. R., Ravi, S., WILLIAMSON, J. R., & Lee, V. M. ‐. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4916 · Cited by 190
Buxbaum, J. D., Ruefli, A. A., Parker, C. A., Cypess, A. M., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4489 · Cited by 184
Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors.
Lee, R. K., Wurtman, R. J., Cox, A. J., & Nitsch, R. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.8083 · Cited by 181
Wang, R., Meschia, J. F., Cotter, R. J., & Sisodia, S. S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55397-7 · Cited by 178
Greenberg, S. M., Koo, E. H., Selkoe, D. J., Qiu, W. Q., & Kosik, K. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7104 · Cited by 163
Regulated secretion of beta-amyloid precursor protein in rat brain
Farber, S., Nitsch, R. M., Schulz, J., & Wurtman, R. J. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-11-07442.1995 · Cited by 155
Transforming growth factor-alpha and beta-amyloid precursor protein share a secretory mechanism.
Arribas, J., & Massagué, J. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.128.3.433 · Cited by 150
Evidence for phosphorylation and oligomeric assembly of presenilin 1
Seeger, M., Nordstedt, C., Petanceska, S. S., Kovacs, D. M., Gouras, G. K., Hahne, S., Fraser, P., Lévesque, L., Czernik, A. J., George‐Hyslop, P. S., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5090 · Cited by 146
Selective ectodomain phosphorylation and regulated cleavage of beta‐amyloid precursor protein.
Hung, A. Y., & Selkoe, D. J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06291.x · Cited by 141
Bardwell, L., & Thorner, J. W. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)30032-7 · Cited by 141
Fiore, R. S., Murphy, T. H., Sanghera, J. S., Pelech, S., & Baraban, J. M. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09796.x · Cited by 140
Self-citationActivation of mitogen-activating protein kinase by glucose is not required for insulin secretion
Khoo, S., & Cobb, M. H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5599 · Cited by 139
Inhibition of β‐Amyloid Production by Activation of Protein Kinase C
Gabuzda, D. H., Busciglio, J. A., & Yankner, B. A. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07479.x · Cited by 138
Multiple signals activate cleavage of the membrane transforming growth factor-alpha precursor.
Pandiella, A., & Massagué, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67662-3 · Cited by 130
Refolo, L. M., Salton, S. R., Anderson, J. P., Mehta, P. D., & Robakis, N. K. R. K. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91511-8 · Cited by 129
Middlemas, D. S., Meisenhelder, J., & Hunter, T. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37708-6 · Cited by 123
Protein kinase C activity is rate limiting for shedding of the interleukin-6 receptor
Müllberg, J., Schooltink, H., Stoyan, T., Heinrich, P. C., & Rose‐John, S. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)92272-y · Cited by 116
Walter, J., Grünberg, J., Capell, A., Pesold, B., Schindzielorz, A., Citron, M., Mendla, K. D., George‐Hyslop, P. S., Multhaup, G., Selkoe, D. J., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5349 · Cited by 107
Electrophoretic Separation of βA4 Peptides (1–40) and (1–42)
Klafki, H.-W., Wiltfang, J., & Staufenbiel, M. (1996) · Analytical Biochemistry · doi:10.1006/abio.1996.0195 · Cited by 99
Role of neurotransmission in the regulation of amyloid β-protein precursor processing
Nitsch, R. M., & Growdon, J. H. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90325-5 · Cited by 99
Bardwell, L. (1996) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(96)30032-7 · Cited by 95
The release of Alzheimer's disease beta amyloid peptide is reduced by phorbol treatment.
Jacobsen, J. S., Spruyt, M. A., Brown, A. M., Sahasrabudhe, S. R., Blume, A. J., Vitek, M. P., Muenkel, H. A., & Sonnenberg‐Reines, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37204-6 · Cited by 91
Protein Serine/Threonine Kinases of the MAPK Cascade
Graves, J. D., Campbell, J. S., & Krebs, E. G. (1995) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1995.tb26684.x · Cited by 86
Ectodomain Phosphorylation of β-Amyloid Precursor Protein at Two Distinct Cellular Locations
Walter, J., Capell, A., Hung, A. Y., Langen, H., Schnölzer, M., Thinakaran, G., Sisodia, S. S., Selkoe, D. J., & Haass, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.1896 · Cited by 84
Xu, H., Sweeney, D. A., Greengard, P., & Gandy, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4081 · Cited by 84
Slack, B. E., Breu, J., Petryniak, M. A., Srivastava, K., & Wurtman, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.14.8337 · Cited by 78
Networking with mitogen-activated protein kinases
Pelech, S., Charest, D. L., Mordret, G. P., Siow, Y. L., Palaty, C., Campbell, D., Charlton, L., Samiei, M., & Sanghera, J. S. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076767 · Cited by 71
Self-citationRegulated cleavage of alzheimer β-amyloid precursor protein in the absence of the cytoplasmic tail
Silva, O. A. B. D. C. E., Iverfeldt, K., Oltersdorf, T., Sinha, S., Lieberburg, I. M., Ramabhadran, T. V., Suzuki, T., Sisodia, S. S., Gandy, S., & Greengard, P. (1993) · Neuroscience · doi:10.1016/0306-4522(93)90031-a · Cited by 70
Stratton, K. R., Worley, P. F., Litz, J. S., Parsons, S. J., Huganir, R. L., & Baraban, J. M. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb02574.x · Cited by 58
MAP kinase-dependent pathways in cell cycle control
Pelech, S., & Charest, D. L. (1995) · Springer eBooks · doi:10.1007/978-1-4615-1809-9_4 · Cited by 55
Self-citationFukuyama, R., Chandrasekaran, K., & Rapoport, S. I. (1993) · Molecular Brain Research · doi:10.1016/0169-328x(93)90067-y · Cited by 55
Nånberg, E., Rupp, E., Carpenter, G. F., Eriksson, A. B., Rönnstrand, L., Engström, U., Hellman, U., Heldin, C., & Claesson, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7773 · Cited by 54
Raymond, L. A., Moshaver, A., Tingley, W. G., Shalaby, I., & Huganir, R. L. (1996) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1996.0008 · Cited by 48
Cox, M., Ely, C. M., Catling, A. D., Weber, M. J., & Parsons, S. J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66031103.x · Cited by 46
Amino-terminal region of the β-amyloid precursor protein activates mitogen-activated protein kinase
Greenberg, S. M., Qiu, W. Q., Selkoe, D. J., Ben-Itzhak, A., & Kosik, K. S. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11944-r · Cited by 42
Stein, J. A., & Rettenmier, C. W. (1991) · PubMed · Cited by 38
Regulation of APP Expression, Biogenesis and Metabolism by Extracellular Matrix and Cytokinesa
Beyreuther, K. T., Multhaup, G., Mönning, U., Sandbrink, R., Beher, D., Hesse, L., Small, D. H., & Masters, C. L. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34403.x · Cited by 33
Self-citationRegulation of APP Processing Potential for the Therapeutical Reduction of Brain Amyloid Burdena
Nitsch, R. M., Wurtman, R. J., & Growdon, J. H. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34416.x · Cited by 29
Regulation of APP Processing by Intra‐ and Intercellular Signalsa
Buxbaum, J. D., & Greengard, P. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34441.x · Cited by 20
Phosphoinositide Turnover Associated with Synaptic Transmission
Murphy, T. H., Wright, D. D., & Baraban, J. M. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10130.x · Cited by 13
Mills, J., & Reiner, P. B. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67041511.x · Cited by 9
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Metadata
- Authors
- Mills, J., Laurent Charest, D., Lam, F., Beyreuther, K., Ida, N., Pelech, S. L., & Reiner, P. B.
- Affiliations
- Heidelberg University (DE)
- University of British Columbia (CA)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 1997-12-15
- Volume
- 17
- Issue
- 24
- Pages
- 9415-9422
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6573401
- OpenAlex
- W1794943105
- Cited by
- 134
- References
- 87
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2018: 1 · 2017: 3 · 2016: 1 · 2015: 3 · 2014: 2 · 2013: 2 · 2012: 4
- FWCI
- 5.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer Society
- Medical Research Council
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid precursor protein, mitogen-activated protein kinase, MEK, ERK, PD98059, nerve growth factor, phorbol ester, protein kinase C, amyloid-beta secretion, Swedish mutation, APP695, PC12 cells, cortical neurons
- MeSH terms
- Alzheimer Disease, Animals, Carcinogens, Cells, Cultured, Cerebral Cortex, Enzyme Inhibitors, Female, Flavonoids, Humans, Kidney, Neurons, Phorbol Esters, Pregnancy, Protein Kinase C, Signal Transduction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, PC12 Cells, Rats, Sprague-Dawley, Receptors, Nerve Growth Factor, Calcium-Calmodulin-Dependent Protein Kinases, Rats
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 ›
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