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The neuropeptide PACAP promotes ?‐secretase pathway for processing Alzheimer amyloid precursor protein
Abstract
The neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) has neurotrophic as well as anti-apoptotic properties and is involved in learning and memory processes. Its specific G protein-coupled receptor PAC1 is expressed in several central nervous system (CNS) regions, including the hippocampal formation. Here we examined the effect of PAC1 receptor activation on alpha-secretase cleavage of the amyloid precursor protein (APP) and the production of secreted APP (APPsalpha). Stimulation of endogenously expressed PAC1 receptors with PACAP in human neuroblastoma cells increased APPsalpha secretion, which was completely inhibited by the PAC1 receptor specific antagonist PACAP-(6-38). In HEK cells stably overexpressing functional PAC1 receptors, PACAP-27 and PACAP-38 strongly stimulated alpha-secretase cleavage of APP. The PACAP-induced APPsalpha production was dose dependent and saturable. This increase of alpha-secretase activity was completely abolished by hydroxamate-based metalloproteinase inhibitors, including a preferential ADAM 10 inhibitor. By using several specific protein kinase inhibitors, we show that the MAP-kinase pathway [including extracellular-regulated kinase (ERK) 1 and ERK2] and phosphatidylinositol 3-kinase mediate the PACAP-induced alpha-secretase activation. Our findings provide evidence for a role of the neuropeptide PACAP in stimulation of the nonamyloidogenic pathway, which might be related to its neuroprotective properties.
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“ERK, a mitogen-activated protein kinase (MAPK), has been shown to suppress Aβ production in vitro and in vivo by altering secretase activity (24, 25).”
From Serotonin signaling is associated with lower amyloid-β levels and plaques in transgenic mice and humans (2011) · cites this paper as [25]
In the citing paper
“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 [25]
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Cites
A new generation of Ca2+ indicators with greatly improved fluorescence properties.
Grynkiewicz, G., Poenie, M., & Tsien, R. Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83641-4 · Cited by 21,562
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
Differential signal transduction by five splice variants of the PACAP receptor
Spengler, D., Waeber, C., Pantaloni, C., Holsboer, F., Bockaert, J., Seeburg, P. H., & Journot, L. (1993) · Nature · doi:10.1038/365170a0 · Cited by 1,182
Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: From Structure to Functions
Vaudry, D., Gonzalez, B. J., Basille, M., Yon, L., Fournier, A., & Vaudry, H. (2000) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01449-2 · Cited by 1,120
Lammich, S., Kojro, E., Postina, R., Gilbert, S., Pfeiffer, R., Jasionowski, M., Haass, C., & Fahrenholz, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3922 · Cited by 975
Self-citationBuxbaum, J. D., Liu, K.-N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., & Black, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27765 · Cited by 952
Nitsch, R. M., Slack, B. E., Wurtman, R. J., & Growdon, J. H. (1992) · Science · doi:10.1126/science.1411529 · Cited by 898
Sherwood, N. M., Krueckl, S. L., & McRory, J. E. (2000) · Endocrine Reviews · doi:10.1210/edrv.21.6.0414 · Cited by 733
Hundhausen, C., Misztela, D., Berkhout, T. A., BROADWAY, N. M., Säftig, P., Reiß, K., Hartmann, D., Fahrenholz, F., Postina, R., Matthews, V. B., et al. (2003) · Blood · doi:10.1182/blood-2002-12-3775 · Cited by 731
Self-citationStructure and function of phosphoinositide 3-kinases
Wymann, M. P., & Pirola, L. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s0005-2760(98)00139-8 · Cited by 667
Research works printed but not linked: 1
- 10.1210/er.21.6.619 · DOI
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Vaudry, D., Falluel‐Morel, A., Bourgault, S., Basille, M., Burel, D., Wurtz, O., Fournier, A., Chow, B., Hashimoto, H., Galas, L., et al. (2009) · Pharmacological Reviews · doi:10.1124/pr.109.001370 · Cited by 1,060
Kuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621
ADAM-17: the enzyme that does it all
Gooz, M. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003628015 · Cited by 377
Cirrito, J. R., Disabato, B. M., Restivo, J. L., Verges, D. K., Goebel, W. D., Sathyan, A., Hayreh, D., D'Angelo, G., Benzinger, T., Yoon, H., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107411108 · Cited by 377
Tamagno, E., Guglielmotto, M., Aragno, M., Borghi, R., Autelli, R., Giliberto, L., Muraca, G., Danni, O., Zhu, X., Smith, M. A., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05072.x · Cited by 342
The role of G protein-coupled receptors in the pathology of Alzheimer's disease
Thathiah, A., & De Strooper, B. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2977 · Cited by 288
Zhang, L., Bukulin, M., Kojro, E., Roth, A., Metz, V. V., Fahrenholz, F., Nawroth, P. P., Bierhaus, A., & Postina, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806948200 · Cited by 294
Self-citationZhao, Y., Calon, F., Julien, C., Winkler, J. W., Petasis, N. A., Lukiw, W. J., & Bazan, N. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015816 · Cited by 243
Lichtenthaler, S. F., Haass, C., & Steiner, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07248.x · Cited by 205
Bossers, K., Wirz, K. T. S., Meerhoff, G. F., Essing, A. H. W., van Dongen, J. W., Houba, P., Kruse, C. G., Verhaagen, J., & Swaab, D. F. (2010) · Brain · doi:10.1093/brain/awq258 · Cited by 230
The alpha secretase ADAM10: A metalloprotease with multiple functions in the brain
Säftig, P., & Lichtenthaler, S. F. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.10.003 · Cited by 223
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Robichaux, W. G., & Cheng, X. (2018) · Physiological Reviews · doi:10.1152/physrev.00025.2017 · Cited by 222
Alpha-secretase in Alzheimer’s disease: molecular identity, regulation and therapeutic potential
Lichtenthaler, S. F. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07081.x · Cited by 207
Jiménez, S., Torres, M., Vizuete, M., Sanchez-Varo, R. M., Sánchez‐Mejías, E., Trujillo‐Estrada, L., Carmona‐Cuenca, I., Caballero, C., Ruano, D., Gutiérrez, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209718 · Cited by 190
The Role of ADAM10 in Alzheimer’s Disease
Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160
Marcade, M., Bourdin, J., Loiseau, N., Peillon, H., Rayer, A., Drouin, D., Schweighoffer, F., & Désiré, L. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05396.x · Cited by 155
Zussy, C., Brureau, A., Delair, B., Marchal, S., Keller, E., IXART, G., Naert, G., Meunier, J., Chevallier, N., Maurice, T., et al. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.03.021 · Cited by 154
Rat, D., Schmitt, U., Tippmann, F., Dewachter, I., Theunis, C., Wieczerzak, E., Postina, R., LEUVEN, F. V., Fahrenholz, F., & Kojro, E. (2011) · The FASEB Journal · doi:10.1096/fj.10-180133 · Cited by 155
Self-citationSynaptic Therapy in Alzheimer's Disease: A CREB-centric Approach
Teich, A. F., Nicholls, R. E., Puzzo, D., Fiorito, J., Purgatorio, R., Fà, M., & Arancio, O. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0327-5 · Cited by 151
The metalloproteinase ADAM10: A useful therapeutic target?
Wetzel, S., Seipold, L., & Säftig, P. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.06.005 · Cited by 137
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Chen, X., Du, Y., & Chen, L. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00493 · Cited by 131
Obesity, leptin, and Alzheimer's disease
Lee, E. B. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06274.x · Cited by 126
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Mockett, B. G., Richter, M., Abraham, W. C., & Müller, U. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00030 · Cited by 127
Hwang, S. H., Shin, E., Shin, T., Lee, B., Choi, S.-H., Kang, J., Kim, H., Kwon, S., Jang, C., Lee, J., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120439 · Cited by 115
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Postina, R. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07459.x · Cited by 114
Self-citationG Protein-Coupled Receptors (GPCRs) in Alzheimer’s Disease: A Focus on BACE1 Related GPCRs
Zhao, J., Deng, Y., Jiang, Z., & Qing, H. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00058 · Cited by 112
Delarasse, C., Auger, R., Gonnord, P., Fontaine, B., & Kanellopoulos, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.200618 · Cited by 117
Cochet, M., Donneger, R., Cassier, E., Gaven, F., Lichtenthaler, S. F., Marin, P., Bockaert, J., Dumuis, A., & Claeysen, S. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300095t · Cited by 111
Blechman, J., & Levkowitz, G. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00055 · Cited by 105
Mao, S., Hua, R., Zhao, X., Qin, X., Sun, Z.-Q., Zhang, Y., Wu, Y.-Q., Jia, M., Cao, J., & Zhang, Y.-M. (2012) · Journal of Neurotrauma · doi:10.1089/neu.2011.2244 · Cited by 93
Alzheimer culprits: Cellular crossroads and interplay
Claeysen, S., Cochet, M., Donneger, R., Dumuis, A., Bockaert, J., & Giannoni, P. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.05.008 · Cited by 82
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Endres, K., & Fahrenholz, F. (2011) · Experimental Brain Research · doi:10.1007/s00221-011-2885-7 · Cited by 87
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Endres, K., & Fahrenholz, F. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07566.x · Cited by 79
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Fisher, J. R., Wallace, C. E., Tripoli, D. L., Sheline, Y. I., & Cirrito, J. R. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0112-5 · Cited by 79
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Vingtdeux, V., & Marambaud, P. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07477.x · Cited by 81
Lee, E. H., & Seo, S. R. (2014) · BMB Reports · doi:10.5483/bmbrep.2014.47.7.086 · Cited by 75
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Verges, D. K., Restivo, J. L., Goebel, W. D., Holtzman, D. M., & Cirrito, J. R. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0607-11.2011 · Cited by 74
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Wu, T., Ding, L., Cheng, Y., Jiang, S., Riaz, M. W., Fu, N., Mou, C., Ye, M., & Zheng, Y. (2022) · Aging and Disease · doi:10.14336/ad.2022.0412 · Cited by 81
Rácz, B., Gasz, B., Borsiczky, B., Gallyas, F., Tamás, A., Józsa, R., Lubics, A., Kiss, P., Rőth, E., Ferencz, A., et al. (2006) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2006.12.006 · Cited by 71
Qian, M., Shen, X., & Wang, H. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0232-4 · Cited by 71
Bandyopadhyay, S., Hartley, D. M., Cahill, C. M., Lahiri, D. K., Chattopadhyay, N., & Rogers, J. T. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20864 · Cited by 65
Induction of RAGE Shedding by Activation of G Protein-Coupled Receptors
Metz, V. V., Kojro, E., Rat, D., & Postina, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041823 · Cited by 65
Self-citationWang, Y., Tang, X. C., & Zhang, H. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22775 · Cited by 59
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Fahrenholz, F., & Postina, R. (2006) · Neurodegenerative Diseases · doi:10.1159/000095264 · Cited by 59
Self-citationChun, Y. S., Kim, M., Lee, S., Kim, M. J., Hong, T.-J., Jeon, J. K., Ganbat, D., Kim, H. T., Kim, S. S., Kam, T., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01713-5 · Cited by 56
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Alam, J., & Sharma, L. K. (2018) · Current Drug Targets · doi:10.2174/1389450119666180820104723 · Cited by 56
Dénes, V., Geck, P., Mester, A., & Gabriel, R. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8091488 · Cited by 59
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Kalueff, A. V. (2007) · Neural Plasticity · doi:10.1155/2007/78171 · Cited by 54
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Chen, W., Deng, W., & Goldys, E. M. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.04.015 · Cited by 53
Rosenbaum, D., & Säftig, P. (2023) · FEBS Journal · doi:10.1111/febs.16870 · Cited by 53
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Vincent, B. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.03.020 · Cited by 45
Kojro, E., Füger, P., Prinzen, C., Kanarek, A. M., Rat, D., Endres, K., Fahrenholz, F., & Postina, R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091621 · Cited by 49
Self-citationCong, L., & Jia, J. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.01.001 · Cited by 43
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Yang, R., Jiang, X. M., Ji, R., Meng, L., Liu, F., Chen, X., & Xin, Y. (2015) · Cellular & Molecular Biology Letters · doi:10.1515/cmble-2015-0008 · Cited by 43
Shieh, P.-C., Tsao, C.-W., Li, J.-S., Wu, H., Wen, Y.-J., Kou, D., & Cheng, J. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.12.032 · Cited by 43
Marks, N., & Berg, M. J. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0054-1 · Cited by 38
Zhang, L., Postina, R., & Wang, Y. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0121-4 · Cited by 40
Self-citationKojro, E., & Postina, R. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0998 · Cited by 40
Self-citationMaretzky, T., Evers, A., Gall, S. M. L., Alabi, R. O., Speck, N., Reiß, K., & Blobel, C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.603753 · Cited by 39
Metcalfe, M., Huang, Q., & Figueiredo‐Pereira, M. E. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.70 · Cited by 38
Reglődi, D., Jüngling, A., Longuespée, R., Kriegsmann, J., Casadonte, R., Kriegsmann, M., Juhász, T., Bardosi, S., Tamás, A., Fulop, B. D., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5100 · Cited by 38
Gardoni, F., Luca, M. D., Malinverno, M., Marcello, E. E., Verpelli, C., Sala, C., & Luca, M. D. (2012) · Journal of Cell Science · doi:10.1242/jcs.097576 · Cited by 33
Bajor, M., & Kaczmarek, L. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0919-6 · Cited by 33
Yamamoto, N., Tanida, M., Kasahara, R., Sobue, K., & Suzuki, K. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12828 · Cited by 30
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Marks, N., & Berg, M. J. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.06.020 · Cited by 30
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Musardo, S., Saraceno, C., Pelucchi, S., & Marcello, E. E. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.07.019 · Cited by 29
Dillen, K., & Annaert, W. G. (2006) · International review of cytology · doi:10.1016/s0074-7696(06)54005-7 · Cited by 29
Ciranna, L., & Costa, L. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00524 · Cited by 30
Marolda, R., Ciotti, M. T., Matrone, C., Possenti, R., Calissano, P., Cavallaro, S., & Severini, C. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.12.025 · Cited by 27
Joly, S., Lamoureux, S., & Pernet, V. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.02.004 · Cited by 24
Zhang, W., Smith, A. D., Liu, J., Cheung, N. S., Zhou, S., Liu, K., Li, Q., & Duan, W. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.10.008 · Cited by 24
Apostol, C. R., Bernard, K., Tanguturi, P., Molnar, G., Bartlett, M. J., Szabó, L., Liu, C., Ortiz, J. B., Saber, M., Giordano, K. R., et al. (2022) · Frontiers in Drug Discovery · doi:10.3389/fddsv.2021.818003 · Cited by 21
Sanchez, A. C., Rao, H. V., & Grammas, P. (2008) · Regulatory Peptides · doi:10.1016/j.regpep.2008.07.004 · Cited by 19
STC1 Induction by PACAP is Mediated Through cAMP and ERK1/2 but not PKA in Cultured Cortical Neurons
Holighaus, Y., Weihe, E., & Eiden, L. E. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9653-9 · Cited by 17
Potashkin, J. A., Bottero, V., Santiago, J. A., & Quinn, J. P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113787 · Cited by 17
Rose, C., Peoc’h, K., Chasseigneaux, S., Paquet, C., Dumurgier, J., Bourasset, F., Calon, F., Laplanche, J., Hugon, J., & Allinquant, B. (2012) · BMC Neuroscience · doi:10.1186/1471-2202-13-84 · Cited by 13
Khashali, H. A., Ray, R., Coleman, K.-L., Atali, S., Haddad, B., Wareham, J., Guthrie, J. W., Heyl, D., & Evans, H. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810746 · Cited by 13
Pecoraro, V., Sardone, L. M., Chisari, M., Licata, F., Volsi, G. L., Perciavalle, V., Ciranna, L., & Costa, L. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.10.061 · Cited by 12
Liao, H., Chou, L.-M., Chien, Y., Wu, C., Chang, J., Lin, C.-I., & Lin, S. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2017.02.013 · Cited by 12
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Toyn, J. H., Lin, X.-A., Thompson, M. W., Guss, V. L., Meredith, J. E., Sankaranarayanan, S., Barrezueta, N. X., Corradi, J., Majumdar, A., Small, D. L., et al. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-143 · Cited by 11
Pharmacological Treatment of Alzheimer`s Disease: Is it Progressing Adequately?
Robles, A. (2009) · The Open Neurology Journal · doi:10.2174/1874205x00903010027 · Cited by 11
Ohshima, R. (2015) · American Journal of BioScience · doi:10.11648/j.ajbio.20150301.13 · Cited by 10
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Subramaniam, V., Chuang, G. C., Xia, H., Burn, B. R., Bradley, J., Maderdrut, J. L., Coy, D. H., & Varner, K. J. (2017) · Peptides · doi:10.1016/j.peptides.2017.07.007 · Cited by 10
Alo, B., & Lamers, C. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00153 · Cited by 10
Kanarek, A. M., Wagner, A., Küppers, J., Gütschow, M., Postina, R., & Kojro, E. (2017) · FEBS Journal · doi:10.1111/febs.14015 · Cited by 9
Self-citationCunliffe, G., Lim, Y. T., Chae, W., & Jung, S. (2022) · Biomedicines · doi:10.3390/biomedicines10123064 · Cited by 6
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Pastore, F., Battistoni, M., Sollazzo, R., Renna, P., Paciello, F., Puma, D. D. L., Barone, E., Dağliyan, O., Ripoli, C., & Grassi, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020917 · Cited by 6
ADAM10: Function insights, disease implications, and promise of therapeutic targeting
Zhang, W., Xu, Y., & Fu, J. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104414 · Cited by 6
Schmidt, S. D., Zinn, C. G., Behling, J. A. K., Furian, A. F., Furini, C. R. G., Myskiw, J. D. C., & Izquierdo, I. (2021) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2021.107423 · Cited by 5
Watters, J. J., & Pocock, J. M. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1429-6_3 · Cited by 5
Galushkin, A., & Gozes, I. (2024) · Current Research in Biotechnology · doi:10.1016/j.crbiot.2024.100254 · Cited by 4
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Metadata
- Authors
- Kojro, E., Postina, R., Buro, C., Meiringer, C., Gehrig‐Burger, K., & Fahrenholz, F.
- Affiliations
- Institute of Biochemistry Johannes Gutenberg University D‐55128 Mainz Germany
- Johannes Gutenberg University Mainz (DE)
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2006-01-09
- Volume
- 20
- Issue
- 3
- Pages
- 512-514
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1984933995
- Cited by
- 118
- References
- 65
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 2 · 2020: 1 · 2019: 4 · 2018: 4 · 2017: 9 · 2016: 5 · 2015: 6 · 2014: 5 · 2013: 3 · 2012: 12
- FWCI
- 5.30
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (KO 2104/2-1)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
- Keywords
- PACAP, PAC1 receptor, amyloid precursor protein, alpha-secretase, ADAM10, non-amyloidogenic pathway, mitogen-activated protein kinase, ERK1/2, phosphatidylinositol 3-kinase, Alzheimer's disease, neuroprotection, G protein-coupled receptor signaling
- MeSH terms
- ADAM10 Protein, ADAM17 Protein, Wortmannin, Phosphoinositide-3 Kinase Inhibitors, Adenylyl Cyclases, Alzheimer Disease, Amino Acid Sequence, Androstadienes, Animals, Calcium, Cell Line, Enzyme Activation, Humans, Kidney, Membrane Proteins, Molecular Sequence Data, Neuroblastoma, Endopeptidases, Phosphorylation, Protein Kinase C, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Transfection, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, PC12 Cells, Cyclic AMP Response Element-Binding Protein, Cyclic AMP-Dependent Protein Kinases, Phosphatidylinositol 3-Kinases, Cell Line, Tumor, Extracellular Signal-Regulated MAP Kinases, Pituitary Adenylate Cyclase-Activating Polypeptide, Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I, Rats, ADAM Proteins, Amyloid Precursor Protein Secretases
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