Serotonin 5-HT2a and 5-HT2c Receptors Stimulate Amyloid Precursor Protein Ectodomain Secretion

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619

Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment

Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397

Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein

Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516

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

Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757

An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp 717 ) Mutants

Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471

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

Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor

Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403

Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein

Weidemann, A., König, G., Bunke, D., Fischer, P. Q., Salbaum, J. M., Masters, C. L., & Beyreuther, K. T. (1989) · Cell · doi:10.1016/0092-8674(89)90177-3 · Cited by 1,233

Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor

Cai, X.-D., Golde, T. E., & Younkin, S. G. (1993) · Science · doi:10.1126/science.8424174 · Cited by 913

Androgens, ApoE, and Alzheimer's Disease

Raber, J. (2004) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2004.11.re2 · Cited by 48

Treatment of dementia with neurotransmission modulation

Doggrell, S. A., & Evans, S. (2003) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.12.10.1633 · Cited by 44

Muscarinic acetylcholine receptors activate the acetylcholinesterase gene promoter

Nitsch, R. M., Rossner, S., Albrecht, C., Mayhaus, M., Enderich, J., Schliebs, R., Wegner, M., Arendt, T., & von der Kammer, H. (1998) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(98)80029-6 · Cited by 44

Regulation of viral transcription elongation and termination during vaccinia virus infection

CONDIT, R. C., & Niles, E. G. (2002) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(02)00461-x · Cited by 44

GPR3 Stimulates Aβ Production via Interactions with APP and β-Arrestin2

Nelson, C. D., & Sheng, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0074680 · Cited by 42

Differences in regional and subcellular localization of Gq/11 and RGS4 protein levels in Alzheimer's disease: Correlation with muscarinic M1 receptor binding parameters

Muma, N. A., Mariyappa, R., Williams, K., & Lee, J. M. (2002) · Synapse · doi:10.1002/syn.10153 · Cited by 42

Regulated Proteolysis of RAGE and AβPP as Possible Link Between Type 2 Diabetes Mellitus and Alzheimer's Disease

Kojro, E., & Postina, R. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0998 · Cited by 40

GRK5 Deficiency Accelerates β-Amyloid Accumulation in Tg2576 Mice via Impaired Cholinergic Activity

Cheng, S., Li, L., He, S., Liu, J., Sun, Y., He, M., Grasing, K., Premont, R. T., & Suo, W. Z. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.170894 · Cited by 41

Metabotropic Glutamate Receptors Increase Amyloid Precursor Protein Processing in Astrocytes: Inhibition by Cyclic AMP

Lee, R. K. K., & Wurtman, R. J. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68051830.x · Cited by 40

Treatment of Alzheimer’s Disease: Current Approaches and Promising Developments

Small, G. W. (1998) · The American Journal of Medicine · doi:10.1016/s0002-9343(98)00027-8 · Cited by 41

Factors influencing the processing and function of the amyloid β precursor protein—a potential therapeutic target in Alzheimer's disease?

Coughlan, C. M. (2000) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(00)00036-x · Cited by 39

Imipramine and citalopram facilitate amyloid precursor protein secretion in vitro

PAKASKI, M., BJELIK, A., HUGYECZ, M., KASA, P., JANKA, Z., & KALMAN, J. (2005) · Neurochemistry International · doi:10.1016/j.neuint.2005.03.004 · Cited by 43

Interaction of Plasminogen Activator Inhibitor Type-1 (PAI-1) with Vitronectin (Vn): Mapping the Binding Sites on PAI-1 and Vn

Schroeck, F. R., de Prada, N. A., Sperl, S., Schmitt, M., & Magdolen, V. (2002) · Biological Chemistry · doi:10.1515/bc.2002.125 · Cited by 38

Metabotropic Glutamate Receptor Agonists Increase Release of Soluble Amyloid Precursor Protein Derivatives from Rat Brain Cortical and Hippocampal Slices

Ulus, İ. H., & Wurtman, R. J. (1997) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)36620-0 · Cited by 38

The Functions of the Amyloid Precursor Protein Gene

Panegyres, P. K. (2001) · Reviews in the Neurosciences · doi:10.1515/revneuro.2001.12.1.1 · Cited by 36

Cholinergic immunolesions by 192IgG‐saporin—a useful tool to simulate pathogenic aspects of alzheimer's disease

Roßner, S. (1997) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(97)00035-x · Cited by 36

Signal Transduction Therapeutics: Relevance for Alzheimer's Disease

Silva, O. A. B. D. C. E., Fardilha, M., Henriques, A. G., Rebelo, S., Vieira, S. I., & Silva, E. F. D. C. E. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:1-2:123 · Cited by 34

Regulation of APP Synthesis and Secretion by Neuroimmunophilin Ligands and Cyclooxygenase Inhibitors

Lee, R. K. K., & Wurtman, R. J. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06934.x · Cited by 33

Solution structure of recombinant somatomedin B domain from vitronectin produced in Pichia pastoris

Kjærgaard, M., Gårdsvoll, H., Hirschberg, D., Nielbo, S., Mayasundari, A., Peterson, C. B., Jansson, A., Jørgensen, T. J. D., Poulsen, F. M., & Ploug, M. (2007) · Protein Science · doi:10.1110/ps.072949607 · Cited by 31

Pathogenesis of Alzheimer’s Disease and Diversity of 1,2,3-Triazole Scaffold in Drug Development: Design Strategies, Structural Insights, and Therapeutic Potential

Singh, A., Singh, K., Kaur, J., Kaur, R., Sharma, A., Kaur, J., Kaur, U., Chadha, R., & Bedi, P. M. S. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00393 · Cited by 30

Association analysis of HTR6 and HTR2A polymorphisms in sporadic Alzheimer's disease

Thome, J., Retz, W., Baader, M., Pesold, B., Hu, M., Cowen, M. S., Durany, N., Adler, G., Henn, F. A., & Rösler, M. (2001) · Journal of Neural Transmission · doi:10.1007/s007020170007 · Cited by 30

A role for MAP kinase in regulating ectodomain shedding of APLP2 in corneal epithelial cells

Xu, K., Zoukhri, D., Zieske, J. D., Dartt, D. A., Sergheraert, C., Loing, E., & Yu, F. X. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.2.c603 · Cited by 30

Pimavanserin, a 5HT2A receptor inverse agonist, rapidly suppresses Aβ production and related pathology in a mouse model of Alzheimer’s disease

Yuede, C. M., Wallace, C. E., Davis, T. A., Gardiner, W. D., Hettinger, J. C., Edwards, H. M., Hendrix, R. D., Doherty, B. M., Yuede, K. M., Burstein, E. S., et al. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15260 · Cited by 29

Accumulation of the amyloid precursor-like protein APLP2 and reduction of APLP1 in retinoic acid-differentiated human neuroblastoma cells upon curcumin-induced neurite retraction.

Adlerz, L., Beckman, M., Holback, S., Tehranian, R., Toro, V. C., & Iverfeldt, K. (2003) · Brain Research. Molecular Brain Research · doi:10.1016/j.molbrainres.2003.08.014 · Cited by 34

The Application of Positron-Emitting Molecular Imaging Tracers in Alzheimer’s Disease

Cohen, R. M. (2007) · Molecular Imaging and Biology · doi:10.1007/s11307-007-0094-3 · Cited by 29

Serotonin 2A receptor-like immunoreactivity is detected in astrocytes but not in oligodendrocytes of rat spinal cord

Maxishima, M., Shiga, T., Shutoh, F., Hamada, S., Maeshima, T., & Okado, N. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03150-4 · Cited by 28

Protein Kinase C Activation Potentiates the Rapid Secretion of the Amyloid Precursor Protein from Rat Cortical Synaptosomes

McLaughlin, M., & Breen, K. C. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720273.x · Cited by 28

β‐Amyloid induced effects on cholinergic, serotonergic, and dopaminergic neurons is differentially counteracted by anti‐inflammatory drugs

Hochstrasser, T., Hohsfield, L. A., Sperner‐Unterweger, B., & Humpel, C. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23126 · Cited by 27

β-Amyloid and Cholinergic Neurons

Doležal, V., & Kašparová, J. (2003) · Neurochemical Research · doi:10.1023/a:1022865121743 · Cited by 27

Understanding How Physical Exercise Improves Alzheimer’s Disease: Cholinergic and Monoaminergic Systems

Zong, B., Yu, F., Zhang, X., Zhao, W., Sun, P., Li, S., & Li, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.869507 · Cited by 31

The Missing Piece? A Case for Microglia’s Prominent Role in the Therapeutic Action of Anesthetics, Ketamine, and Psychedelics

VanderZwaag, J., Halvorson, T., Dolhan, K., Šimončičová, E., Ben‐Azu, B., & Tremblay, M. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03772-0 · Cited by 28

Fleshing out the amyloid cascade hypothesis: the molecular biology of Alzheimer's disease

Lovestone, S. (2000) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2000.2.2/slovestone · Cited by 28

Motor impulsivity in APP-SWE mice: a model of Alzheimer??s disease

Adriani, W., Ognibene, E., Heuland, E., Ghirardi, O., Caprioli, A., & Laviola, G. (2006) · Behavioural Pharmacology · doi:10.1097/00008877-200609000-00019 · Cited by 26

Bradykinin-induced amyloid precursor protein secretion: a protein kinase C-independent mechanism that is not altered in fibroblasts from patients with sporadic Alzheimer's disease

Racchi, M., Ianna, P., Binetti, G. G., Trabucchi, M., & Govoni, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3301271 · Cited by 24

Association of the HTR6 polymorphism C267T with late-onset Alzheimer's disease in Chinese

Kan, R., Wang, B., Zhang, C., Yang, Z., Ji, S., Lu, Z., Zheng, C., Jin, F., & Wang, L. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.09.007 · Cited by 23

Mitogen-activated protein kinase is involved in N-methyl-d-aspartate receptor regulation of amyloid precursor protein cleavage

Mills, J., & Reiner, P. B. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00381-4 · Cited by 24

Phospholipase A2 is involved in muscarinic receptor-mediated sAPPα release independently of cyclooxygenase or lypoxygenase activity in SH-SY5Y cells

Cho, H.-W., Kim, J. H., Choi, S., & Kim, H.-J. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.12.014 · Cited by 23

5-HT Receptor Signal Transduction Pathways

Turner, J. H., Gelasco, A. K., Ayiku, H., Coaxum, S. D., Arthur, J. M., & Garnovskaya, M. N. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-080-5_5 · Cited by 23

Neuro-modulation, aminergic neuro-disinhibition and neuro-degeneration.

Schmitt, H. P. (2005) · Medical Hypotheses · doi:10.1016/j.mehy.2005.06.018 · Cited by 23

Serotonin Receptors as a Potential Target in the Treatment of Alzheimer’s Disease

Eremin, D. V., Kondaurova, E. M., Rodnyy, A. Y., Molobekova, C. A., Kudlay, D. A., & Naumenko, V. S. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923120064 · Cited by 23

Opportunities for multiscale computational modelling of serotonergic drug effects in Alzheimer's disease

Joshi, A., Wang, D., Watterson, S., McClean, P. L., Behera, C. K., Sharp, T., & Wong‐Lin, K. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108118 · Cited by 22

Capacitative Ca2+ entry is involved in regulating soluble amyloid precursor protein (sAPPα) release mediated by muscarinic acetylcholine receptor activation in neuroblastoma SH‐SY5Y cells

Kim, J. H., Choi, S., Jung, J., Roh, E.-J., & Kim, H. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03734.x · Cited by 22

Alzheimer's α‐secretase may be a calcium‐dependent protease

Chen, M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01214-3 · Cited by 21

New developments in the urokinase-type plasminogen activator system

Rosenberg, S. (2001) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.5.6.711 · Cited by 20

New players in old amyloid precursor protein‐processing pathways

Roßner, S. (2004) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2004.07.004 · Cited by 20

Differential Expression of Serotonin 5-HT2 Receptors during Rat Embryogenesis

Wu, C., Dias, P. B., Kumar, S., Lauder, J. M., & Singh, S. (1999) · Developmental Neuroscience · doi:10.1159/000017362 · Cited by 19

Cellular and ultra structural evidence for cytoskeletal localization of prolyl endopeptidase-like protein in neurons

Morawski, M., Nuytens, K., Juhász, T., Zeitschel, U., Seeger, G., Waelkens, E., Régal, L., Schulz, I., Arendt, T., Szeltner, Z., et al. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.02.038 · Cited by 17

Talsaclidine (WAL 2014 FU), a muscarinic M1 receptor agonist for the treatment of Alzheimer's disease

Wienrich, M., Ceci, A., Ensinger, H. A., Gaida, W., Mendla, K. D., Osugi, T., Raschig, A., & Weiser, T. W. (2002) · Drug Development Research · doi:10.1002/ddr.10085 · Cited by 17

Selective Serotonin Reuptake Inhibitor-Treatment Does Not Show Beneficial Effects on Cognition or Amyloid Burden in Cognitively Impaired and Cognitively Normal Subjects

Bouter, Y., & Bouter, C. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.883256 · Cited by 18

β-amyloid pathology is not associated with depression in a large community sample autopsy study

Saldanha, N. M., Suemoto, C. K., Rodriguez, R. D., Leite, R. E. P., Nascimento, C. F., Ferretti‐Rebustini, R. E. D. L., da Silva, M. M., Pasqualucci, C. A., Nitríni, R., Filho, W. J., et al. (2020) · Journal of Affective Disorders · doi:10.1016/j.jad.2020.09.062 · Cited by 16

Autism genes and the leukocyte transcriptome in autistic toddlers relate to pathogen interactomes, infection and the immune system. A role for excess neurotrophic sAPPα and reduced antimicrobial Aβ

Carter, C. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.03.007 · Cited by 15

Ghrelin system in Alzheimer's disease

Tian, J., Wang, T., & Du, H. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2022.102655 · Cited by 17

Reversal of neuronal tau pathology via adiponectin receptor activation

McGregor, E. R., Lasky, D. J., Rippentrop, O. J., Clark, J. P., Wright, S., Jones, M. V., & Anderson, R. M. (2025) · Communications Biology · doi:10.1038/s42003-024-07391-z · Cited by 14

Effects of Plasminogen Activator Inhibitor-1–Specific RNA Aptamers on Cell Adhesion, Motility, and Tube Formation

Brandal, S., Blake, C. M., Sullenger, B. A., & Fortenberry, Y. M. (2011) · Nucleic Acid Therapeutics · doi:10.1089/nat.2011.0320 · Cited by 14

Lu 25-109, a combined m1 agonist and m2 antagonist, modulates regulated processing of the amyloid precursor protein of Alzheimer's disease

Müller, D., Wiegmann, H., Langer, U., Lenz, S. M., & Nitsch, R. M. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050110 · Cited by 14

The plasminogen activator inhibitor system in colon cancer cell lines is influenced by the CO2 pneumoperitoneum

Krause, P., Bobisch, N. S., Thelen, P., Köhler, K., Koenig, S., Heinz Becker, A., & Leister, I. (2010) · International Journal of Colorectal Disease · doi:10.1007/s00384-010-1062-y · Cited by 12

Fibrillar beta-amyloid (Aβ) (1–42) elevates extracellular Aβ in cultured hippocampal neurons of adult rats

Majd, S., Rastegar, K., Zarifkar, A., & Takhshid, M. A. (2007) · Brain Research · doi:10.1016/j.brainres.2007.09.033 · Cited by 12

Serotonin Receptor Gene Polymorphisms Are Associated with Cerebrospinal Fluid, Genetic, and Neuropsychological Biomarkers of Alzheimer’s Disease

Leko, M. B., Perković, M. N., Španić, E., Štrac, D. Š., Pleić, N., Vogrinc, Ž., Gunjača, I., Bežovan, D., Erjavec, G. N., Klepac, N., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10123118 · Cited by 11

Modulators of the urokinase-type plasminogen activation system for cancer

Rosenberg, S. (2000) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.10.12.1843 · Cited by 11

Multi‐Targeting Ligands as Prospective Therapeutics for Alzheimer's Disease, a Prevalent Neurodegenerative Disorder: Mechanistic Insights, Emerging Targets and Drug Discovery Campaigns

Thakur, A., Rana, M., Vanjani, S., Liou, K.-C., Taliyan, R., Nepali, K., & Yang, C. (2026) · Medicinal Research Reviews · doi:10.1002/med.70047 · Cited by 10

The Combined Effects of Amyloidosis and Serotonin Deficiency by Tryptophan Hydroxylase-2 Knockout Impacts Viability of the APP/PS1 Mouse Model of Alzheimer’s Disease

von Linstow, C. U., Waider, J., Bergh, M. S., Anzalone, M., Madsen, C., Nicolau, A. B., Wirenfeldt, M., Lesch, K., & Finsen, B. R. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210581 · Cited by 9

Connecting Mind-Body Therapy-Mediated Effects to Pathological Features of Alzheimer’s Disease

Hüttenrauch, M., López‐Noguerola, J. S., & Castro‐Obregón, S. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200743 · Cited by 10

3,4-Methylenedioxymethamphetamine (MDMA), but not morphine, alters APP processing in the rat brain

Kalman, J. L., Bjelik, A., Hugyecz, M., Tímár, J., Gyarmati, Z., Zana, M., Fürst, Z., Janka, Z., Rakonczay, Z., Horváth, Z., et al. (2006) · The International Journal of Neuropsychopharmacology · doi:10.1017/s146114570600650x · Cited by 9

Efficacy and safety of negative allosteric modulators of 5-hydroxytryptamine 2A receptors in the treatment of Alzheimer’s disease psychosis: A systematic review and meta-analysis

Chen, Y., Sun, J., Yang, Z., & Bi, H. (2023) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/161159 · Cited by 9

The interaction between chronic low-level lead and the amyloid β precursor protein

Davey, F. D., & Breen, K. C. (1998) · Amyloid · doi:10.3109/13506129808995286 · Cited by 8

Cholinergic Modulation of Amyloid Processing and Dementia in Animal Models of Alzheimer's Disease

Ole Isacson, A., & Lin, L. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06940.x · Cited by 8

Random Peptide Bacteriophage Display as a Probe for Urokinase Receptor Ligands

Fong, S. K., DOYLE, M. V., Goodson, R. J., Drummond, R. J., Stratton, J., McGuire, L., Doyle, L. V., Chapman, H. A., & Rosenberg, S. (2002) · Biological Chemistry · doi:10.1515/bc.2002.015 · Cited by 8

Die Bedeutung depressiver Syndrome bei beginnender Demenz vom Alzheimer-Typ im höheren Lebensalter

Rapp, M. A., Hellweg, R., & Heinz, A. (2010) · Der Nervenarzt · doi:10.1007/s00115-010-3129-y · Cited by 7

Biological Characterization of Uncleavable Plasma Membrane-Anchored Human Macrophage Colony-Stimulating Factor

Deng, P., Wang, Y., Shahbazian, V. L., & Pattengale, P. K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3423 · Cited by 7

Chapter 12. The Urokinase-type Plasminogen Activator and Its Receptor in Cancer

Rosenberg, S. (1999) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(08)60574-6 · Cited by 7

β‐Amyloid Therapeutic Strategies for Alzheimer's Disease

Imbimbo, B. P., & Speroni, F. (2005) · Wiley eBooks · doi:10.1002/0471266949.bmc112 · Cited by 6

Amyloid β peptides activate the phosphoinositide signaling pathway in oocytes expressing rat brain RNA

Blitzer, R. D., Wong, T., Giovannini, M. G., Pangalos, M. N., Robakis, N. K. R. K., & Landau, E. M. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00340-x · Cited by 7

β-Adrenergic Receptor, Amyloid β-Peptide, and Alzheimer's Disease

Wang, D., & Xiang, Y. K. (2011) · Current topics in membranes · doi:10.1016/b978-0-12-384921-2.00010-0 · Cited by 6

Activation of 5-HT2C Receptor Promotes the Expression of Neprilysin in U251 Human Glioma Cells

Tian, X.-L., Yu, L., Li, W.-Q., Hu, Y. H., Yin, M., & Wang, Z. (2014) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0138-6 · Cited by 6

The status of plasminogen activator inhibitor-1 as a therapeutic target

Charlton, P. (1997) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.6.5.539 · Cited by 6

A Review of the Neurotrophic and Neuroprotective Properties of ONO‐1603: Comparison with Those of Tetrahydroaminoacridine, an Antidementia Drug

Katsube, N. C., & Ishitani, R. (2000) · CNS Drug Reviews · doi:10.1111/j.1527-3458.2000.tb00135.x · Cited by 6

Potential therapeutic targets for Alzheimer’s disease

McKeon‐O'Malley, C., Saunders, A. J., Bush, A. I., & Tanzi, R. E. (1998) · Emerging Therapeutic Targets · doi:10.1517/14728222.2.2.157 · Cited by 6

Effect of haloperidol and risperidone on amyloid precursor protein levels in vivo

Palotás, A., Pákáski, M., Palotás, M., Hugyecz, M., Molnár, J., Penke, B., Janka, Z., & Kalman, J. L. (2003) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2003.07.002 · Cited by 5

Computer-Aided Drug Design Approaches to Study Key Therapeutic Targets in Alzheimer’s Disease

Lemos, A., Melo, R., Moreira, I. S., & Cordeiro, M. N. D. S. (2017) · Neuromethods · doi:10.1007/978-1-4939-7404-7_3 · Cited by 4

Influência genética sobre a doença de Alzheimer de início tardio

Barros, A. C., Lucatelli, J. F., Maluf, S. W., & de Andrade, F. M. (2009) · Archives of Clinical Psychiatry (São Paulo) · doi:10.1590/s0101-60832009000100003 · Cited by 4

Amyloid beta: Functional protein or biological junk?

Koudinova, N. V., Koudinov, A. R., & Berezov, T. T. (2007) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s199075080703002x · Cited by 3

Regulation of Gene Expression by Muscarinic Acetylcholine Receptors: A Comprehensive Approach for the Identification of Regulated Genes

von der Kammer, H., Mayhaus, M., Albrecht, C., Andresen, B., Klaudiny, J., Demiralay, C., & Nitsch, R. M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06939.x · Cited by 3

Strategies to delay the onset of Alzheimer’s disease

Hüll, M. H., Fiebich, B. L., & Lieb, K. (2000) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-0348-8393-1_13 · Cited by 3

Cholinergic abnormalities in Alzheimer's disease: are there new targets for drug development?

Fodero, L. R., & Small, D. H. (2002) · Drug Development Research · doi:10.1002/ddr.10089 · Cited by 3

The Role of Integrin-Mediated Processes in the Biology of Metastasis

Marshall, J. F., & Davies, D. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-48388-2_2 · Cited by 3

GPCR, a rider of Alzheimer’s disease

Liu, X., & Zhao, J. (2011) · Frontiers in Biology · doi:10.1007/s11515-011-1129-3 · Cited by 3

Establishment and characterization of RNA-edited serotonin 2C receptor isoform cell models and alteration of amyloid precursor protein ectodomain secretion in HEK293 APPSwe cells

Guo, L., Zhang, J., Yan, Q.-X., & Yin, M. (2011) · Human Cell · doi:10.1007/s13577-011-0014-3 · Cited by 2

Muscarinic therapies in Alzheimer's disease; from palliative treatments to disease modification

Lovestone, S. (1997) · International Journal of Psychiatry in Clinical Practice · doi:10.3109/13651509709069201 · Cited by 2

Describing Brain Activity of Persons With AD and Depressive Symptoms

Holston, E. C. (2014) · Archives of Psychiatric Nursing · doi:10.1016/j.apnu.2014.09.002 · Cited by 2

Biological Basis for the Pharmacological Modulation of Amyloid Precursor Protein Metabolism

Racchi, M., Trabucchi, M., & Govoni, S. M. (1998) · KARGER eBooks · doi:10.1159/000061368 · Cited by 2

Paroxetine administration decreases AD-like pathology and reverses memory impairments in a transgenic model of Alzheimer disease

Bales, K. R. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.06.005 · Cited by 2

Neurotransmitter Receptor—G-Protein-Mediated Signal Transduction in Alzheimer’s Disease

Cowburn, R. F. (2000) · doi:10.1007/978-1-59259-019-3_5 · Cited by 2

L-glutamate and phorbol ester stimulate the release of secretory amyloid precursor protein from rat cortical synaptosomes

Kirazov, L., Kirazov, E. P., & Schliebs, R. (2005) · Acta Biologica Hungarica · doi:10.1556/abiol.56.2005.3-4.1 · Cited by 1

G protein-coupled receptors in neurodegenerative diseases

Guimarães, T. R., & Thathiah, A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816228-6.00017-9 · Cited by 1

Serotonin receptors - a potential target for the treatment of Alzheimer’s disease

Eremin, D. V., Kondaurova, E. M., Rodnyy, A. Y., Molobekova, K. A., Kudlay, D. A., & Naumenko, V. S. (2023) · Biochemistry (Moscow) · doi:10.31857/s0320972523120059 · Cited by 1

Chapter 14. Citalopram and Escitalopram

Shelton, R. C. (2024) · American Psychiatric Association Publishing eBooks · doi:10.1176/appi.books.9781615375523.as14 · Cited by 1

Functional neuroinflammatory- and serotonergic imaging in Alzheimer's disease: validation and preliminary clinical findings

Versijpt, J. J. (2003) · University of Groningen research database (University of Groningen / Centre for Information Technology) · Cited by 1

Basal Forebrain Cholinergic Lesion by 192 IgG-Saporin

Schliebs, R. (2005) · Humana Press eBooks · doi:10.1007/978-1-59259-896-0_4 · Cited by 1

Potential Role of Androgens and Androgen Receptors in Alzheimer's Disease

Raber, J. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-661-4_30 · Cited by 3

TRAFFICKING OF α-SECRETASE ADAM10: NEW INSIGHTS INTO THE MOLECULAR MECHANISM OF MODULATION

Farmacologiche, S., Farmacia, F. D., Farmacotossicologiche, S., & Ciclo, X. (2011)

The Human Serotonin 5-HT4 Receptor Regulates Secretion of Non-amyloidogenic Precursor Protein

Robert, S. J., Zugaza, J. L., Fischmeister, R., Gardier, A. M., & Lezoualc'h, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m109008200 · Cited by 104

Influence des récepteurs 5-HT4 de la sérotonine sur la maturation du précurseur de la protéine ß-amyloide associée à la maladie d'Alzheimer

Robert, S. J. (2004)

[5-HT2C receptor subtype modulate production of secretory beta-amyloid protein precursor in incubated rat hippocampal slices].

Zhang, G., Gao, D.-L., Cao, L.-G., & Yin, M. (2004) · PubMed

Regulation of Amyloid Precursor Protein Processing by Serotonin Signaling

Pimenova, A. A., Thathiah, A., Strooper, B. D., & Tesseur, I. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087014 · Cited by 50

Regulation of the amyloid precursor protein ectodomain shedding by the 5‐HT4 receptor and Epac

Robert, S. J., Maillet, M., Morel, É., Launay, J., Fischmeister, R., Mercken, L., & Lezoualc’h, F. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.010 · Cited by 58