Cited by 1,975Alzheimer's disease research and treatmentsNeuropeptides and Animal PhysiologyNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 29 of the 31 references it cites were found in a registry or an index, and 2 are not checked yet.

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Yankner, Bruce A., Duffy, Lawrence K., Kirschner, Daniel A.·1990·Science

DOI 10.1126/science.2218531

Open this paper in CoChat — free account

Abstract

The amyloid β protein is deposited in the brains of patients with Alzheimer's disease but its pathogenic role is unknown. In culture, the amyloid β protein was neurotrophic to undifferentiated hippocampal neurons at low concentrations and neurotoxic to mature neurons at higher concentrations. In differentiated neurons, amyloid β protein caused dendritic and axonal retraction followed by neuronal death. A portion of the amyloid β protein (amino acids 25 to 35) mediated both the trophic and toxic effects and was homologous to the tachykinin neuropeptide family. The effects of the amyloid β protein were mimicked by tachykinin antagonists and completely reversed by specific tachykinin agonists. Thus, the amyloid β protein could function as a neurotrophic factor for differentiating neurons, but at high concentrations in mature neurons, as in Alzheimer's disease, could cause neuronal degeneration.

Integrity signals

Registry

Crossref · 10.1126/science.2218531

Cites

29 of 31 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
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
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
The establishment of polarity by hippocampal neurons in culture.
Dotti, C., Sullivan, C., & Banker, G. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-04-01454.1988 · Cited by 1,862
Glutamate neurotoxicity in cortical cell culture
Choi, D. W., Maulucci-Gedde, M., & Kriegstein, A. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-02-00357.1987 · Cited by 1,506
Rat hippocampal neurons in dispersed cell culture.
Banker, G. A., & Cowan, W. M. (1977) · Brain Research · doi:10.1016/0006-8993(77)90594-7 · Cited by 1,110
Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels.
Masters, C. L., Multhaup, G., Simms, G., Pottgiesser, J., Martins, R. N., & Beyreuther, K. T. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04000.x · Cited by 1,048
Neurotoxicity of a Fragment of the Amyloid Precursor Associated with Alzheimer's Disease
Yankner, B. A., Dawes, L. R., Fisher, S., Villa-Komaroff, L., Oster-Granite, M. L., & Neve, R. L. (1989) · Science · doi:10.1126/science.2474201 · Cited by 907
Self-citation
Outgrowth-regulating actions of glutamate in isolated hippocampal pyramidal neurons
Mattson, M. P., Dou, P., & Kater, S. B. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-06-02087.1988 · Cited by 557
Tachykinins
Maggio, J. E. (1988) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.11.030188.000305 · Cited by 550

Show all 31 references

Research works printed but not linked: 2

Dayhoff, M. O., Atlas of Protein Sequence and Structure 5 3: 345 (1978).
GLENNER, G, BRANBURY REPORT 15: 137 (1983).

Sorted by citations

Items 801–900 of 1,008

Hematoxylin Inhibits Amyloid β-Protein Fibrillation and Alleviates Amyloid-Induced Cytotoxicity
Tu, Y., Ma, S., Liu, F., Sun, Y. P., & Dong, X. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b06878 · Cited by 58
Amyloid Beta 25–35 induces blood-brain barrier disruption in vitro
Cuevas, E., Rosas-Hernández, H., Burks, S. M., Ramirez-Lee, M. A., Guzmán, A., Imam, S. Z., Ali, S. F., & Sarkar, S. (2019) · Metabolic Brain Disease · doi:10.1007/s11011-019-00447-8 · Cited by 58
Isothermal titration calorimetry for studying interactions between peptides and lipid membranes
Wieprecht, T., & Seelig, J. (2002) · Current topics in membranes · doi:10.1016/s1063-5823(02)52004-4 · Cited by 58
Toxicity mediated by soluble oligomers of β‐amyloid(1–42) on cholinergic SN56.B5.G4 cells
Heinitz, K., Beck, M., Schliebs, R., & Perez-Polo, J. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04015.x · Cited by 58
Akt-dependent Expression of NAIP-1 Protects Neurons against Amyloid-β Toxicity
Lesné, S., Gabriel, C., Nelson, D. A., White, E., MacKenzie, E. T., Vivien, D., & Buisson, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413495200 · Cited by 58
Protective effect of benzothiazole derivative KHG21834 on amyloid β-induced neurotoxicity in PC12 cells and cortical and mesencephalic neurons
Choi, M., Kim, E.-A., Hahn, H., Nam, K. D., Yang, S.-J., Choi, S. Y., Kim, T. U., Cho, S. W., & Huh, J. (2007) · Toxicology · doi:10.1016/j.tox.2007.07.010 · Cited by 58
Chronic cognitive deficits and amyloid precursor protein elevation after selective immunotoxin lesions of the basal forebrain cholinergic system
Lin, L., Leblanc, C. J., Deacon, T. W., & Ole Isacson, A. (1998) · Neuroreport · doi:10.1097/00001756-199802160-00030 · Cited by 58
Self-Assembly of β-Amyloid 42 Is Retarded by Small Molecular Ligands at the Stage of Structural Intermediates
Bohrmann, B., Adrian, M., Dubochet, J., Kuner, P., Müller, F., Huber, W., Nordstedt, C., & Döbeli, H. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4241 · Cited by 58
Cognitive dysfunction induced by sequential injection of amyloid-β and ibotenate into the bilateral hippocampus; protection by memantine and MK-801
Nakamura, S., Murayama, N., Noshita, T., Katsuragi, R., & Ohno, T. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.07.049 · Cited by 58
Melatonin blocks rat hippocampal neuronal apoptosis induced by amyloid beta‐peptide 25–35
Shen, Y., Xu, S., Wei, W., Wang, X., Wang, H., & Sun, X. (2002) · Journal of Pineal Research · doi:10.1034/j.1600-079x.2002.1o839.x · Cited by 58
Localization of a Domain in Apolipoprotein E with both Cytostatic and Cytotoxic Activity
Clay, M. A., Anantharamaiah, G. M., Mistry, M. J., Balasubramaniam, A., & Harmony, J. A. K. (1995) · Biochemistry · doi:10.1021/bi00035a020 · Cited by 58
Cellular cofactors potentiating induction of stress and cytotoxicity by amyloid β-peptide
Yan, S. D., Roher, A. E., Chaney, M., Zloković, B. V., Schmidt, A. M., & Stern, D. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00041-7 · Cited by 58
Apoptosis, Neurotrophic Factors and Neurodegeneration
Dragunow, M., MacGibbon, G. A., Lawlor, P. A., Butterworth, N. J., Connor, B. J., Henderson, C. E., Walton, M. R., Woodgate, A.-M., Hughes, P. E., & Faull, R. L. M. (1997) · Reviews in the Neurosciences · doi:10.1515/revneuro.1997.8.3-4.223 · Cited by 58
Amyloid β-protein fragment 25–35 causes activation of cytoplasmic calcium in neurons
Joseph, R., & Han, E. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)80044-0 · Cited by 58
In 2024, the amyloid-cascade-hypothesis still remains a working hypothesis, no less but certainly no more
Behl, C. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1459224 · Cited by 57
Amyloid-β, Tau, and Dementia
Takashima, A. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1090 · Cited by 57
Effects of aging and β-amyloid on the properties of brain synaptic and mitochondrial membranes
Eckert, G. P., Wood, W. G., & Müller, W. E. G. (2001) · Journal of Neural Transmission · doi:10.1007/s007020170024 · Cited by 57
Calcium dyshomeostasis and neurotoxicity of Alzheimer’s β-amyloid protein
Kawahara, M., Kato‐Negishi, M., & Sadakane, Y. (2009) · Expert Review of Neurotherapeutics · doi:10.1586/ern.09.28 · Cited by 57
Protective effect of systemic l-kynurenine and probenecid administration on behavioural and morphological alterations induced by toxic soluble amyloid beta (25–35) in rat hippocampus
Carrillo‐Mora, P., Méndez-Cuesta, L. A., de la Cruz, V. P., van der Goes, T. I. F., & Santamarı́a, A. (2010) · Behavioural Brain Research · doi:10.1016/j.bbr.2010.02.041 · Cited by 57
β-Amyloid precursor protein and alzheimer's disease: The peptide plot thickens
Mattson, M. P., & Rydel, R. E. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90068-9 · Cited by 57
Transcriptional activation of Alzheimer's β-amyloid precursor protein gene by stress
Dewji, N. N., Do, C., & Bayney, R. M. (1995) · Molecular Brain Research · doi:10.1016/0169-328x(95)00131-b · Cited by 57
Neurocytopathic effects of beta-amyloid-stimulated monocytes: a potential mechanism for central nervous system damage in Alzheimer disease.
London, J. A., Biegel, D., & Pachter, J. S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4147 · Cited by 57
In‐vitro matured human macrophages express Alzheimer's βA4‐amyloid precursor protein indicating synthesis in microglial cells
Bauer, J., König, G., Strauss, S., Jonas, U., Ganter, U., Weidemann, A., Mönning, U., Masters, C. L., Volk, B., Berger, T., et al. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80508-z · Cited by 57
Racemization: Its Biological Significance on Neuropathogenesis of Alzheimer's Disease.
Mori, H., Ishii, K., Tomiyama, T., Furiya, Y., Sahara, N., Asano, S., Endo, N., Shirasawa, T., & Takio, K. (1994) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.174.251 · Cited by 56
Expression of the amyloid protein precursor of Alzheimer's disease in the developing rat olfactory system
Clarris, H. J., Key, B., Beyreuther, K. T., Masters, C. L., & Small, D. H. (1995) · Developmental Brain Research · doi:10.1016/0165-3806(95)00083-p · Cited by 56
Aβ1–42 reduces synapse number and inhibits neurite outgrowth in primary cortical and hippocampal neurons: A quantitative analysis
Evans, N. A., Facci, L., OWEN, D. E., Soden, P. E., Burbidge, S. A., Prinjha, R. K., Richardson, J. C., & Skaper, S. D. (2008) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2008.08.001 · Cited by 56
Stereoselectivities of enantiomers of huperzine A in protection against β-amyloid25–35-induced injury in PC12 and NG108-15 cells and cholinesterase inhibition in mice
Zhang, H., Liang, Y. Q., Tang, X. C., He, X., & Bai, D. L. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02437-5 · Cited by 56
Suppressed expression of nicotinic acetylcholine receptors by nanomolar β-amyloid peptides in PC12 cells
Guan, Z. Z., Miao, H., Tian, J., Unger, C., Nordberg, A. K., & Zhang, X. (2001) · Journal of Neural Transmission · doi:10.1007/s007020100017 · Cited by 56
Reduction in somatostatin and substance P levels and choline acetyltransferase activity in the cortex and hippocampus of the rat after chronic intracerebroventricular infusion of β-amyloid (1-40)
Nag, S., Yee, B. K., & Tang, F. M. K. (1999) · Brain Research Bulletin · doi:10.1016/s0361-9230(99)00196-3 · Cited by 56
Alzheimer's disease-like dystrophic neurites characteristically associated with senile plaques are not found within other neurodegenerative disease unless amyloid β-protein deposition is present
Benzing, W. C., Mufson, E. J., & Armstrong, D. M. (1993) · Brain Research · doi:10.1016/0006-8993(93)91563-8 · Cited by 56
β-Amyloid regulates gene expression of glial trophic substance S100β in C6 glioma and primary astrocyte cultures
Peña, L. A., Brecher, C. W., & Marshak, D. R. (1995) · Molecular Brain Research · doi:10.1016/0169-328x(95)00145-i · Cited by 56
Amyloid β up‐regulates brain‐derived neurotrophic factor production from astrocytes: Rescue from amyloid β‐related neuritic degeneration
Kimura, N., Takahashi, M., Tashiro, T., & Terao, K. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20984 · Cited by 55
Proteomic study of amyloid beta (25–35) peptide exposure to neuronal cells: Impact on APE1/Ref‐1's protein–protein interaction
Mantha, A. K., Dhiman, M., Taglialatela, G., Perez‐Polo, R. J., & MITRA, S. P. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23018 · Cited by 55
β-Amyloid Peptides Are Cytotoxic to Astrocytes in Culture: A Role for Oxidative Stress
Brera, B., Serrano, A., & CEBALLOS, M. L. D. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0313 · Cited by 55
Amyloid-β (25–35) increases activity of neuronal NO-synthase in rat brain
Stepanichev, M. Y., Onufriev, M. V., Yakovlev, A. A., Khrenov, A. I., Peregud, D., Vorontsova, O. N., Лазарева, Н. А., & Gulyaeva, N. V. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.11.009 · Cited by 55
Differential regional and cellular distribution of β-amyloid precursor protein messenger RNAs containing and lacking the kunitz protease inhibitor domain in the brain of human, rat and mouse
Solà, C., Mengod, G., Probst, A., & Palacios, J. M. (1993) · Neuroscience · doi:10.1016/0306-4522(93)90304-x · Cited by 55
Effects of tumor necrosis factor‐alpha central administration on hippocampal damage in rat induced by amyloid beta‐peptide (25–35)
Stepanichev, M. Y., Zdobnova, I. M., Yakovlev, A. A., Onufriev, M. V., Лазарева, Н. А., Zarubenko, I. I., & Gulyaeva, N. V. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10469 · Cited by 55
Long‐term deprivation of oestrogens by ovariectomy potentiates β‐amyloid‐induced working memory deficits in rats
Yamada, K., Tanaka, T., Zou, L., Senzaki, K., Yano, K., Osada, T., Olariu, A., Ren, X., Kameyama, T., & Nabeshima, T. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702811 · Cited by 55
Focusing on Formononetin: Recent Perspectives for its Neuroprotective Potentials
Tian, J., Wang, X.-Q., & Tian, Z. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.905898 · Cited by 54
Effects of baicalein on β-amyloid peptide-(25–35)-induced amnesia in mice
Wang, S.-Y., Wang, H., Chi, C., Chen, C., & Liao, J. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.10.029 · Cited by 54
Acetylcholinesterase Inhibitors: Structure Based Design, Synthesis, Pharmacophore Modeling, and Virtual Screening
Valasani, K. R., Chaney, M. O., Day, V. W., & Yan, S. S. (2013) · Journal of Chemical Information and Modeling · doi:10.1021/ci400196z · Cited by 54
Effect of amyloid beta peptide on poly(ADP-ribose) polymerase activity in adult and aged rat hippocampus.
Strosznajder, J. B., Jęśko, H. M., & Strosznajder, R. P. (2000) · Acta Biochimica Polonica · doi:10.18388/abp.2000_4003 · Cited by 54
Activation of Muscarinic Receptors Inhibits औ-Amyloid Peptide-induced Signaling in Cortical Slices
Gu, Z., Zhong, P., & Yan, Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209892200 · Cited by 54
Both oxidative stress-dependent and independent effects of amyloid β protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction assay
Abe, K., & Saitō, H. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01421-3 · Cited by 54
Prostaglandin E1 prevents apoptotic cell death in superficial dorsal horn of rat spinal cord
Kawamura, T., Akira, T., Watanabe, M., & Kagitani, Y. (1997) · Neuropharmacology · doi:10.1016/s0028-3908(97)00096-8 · Cited by 54
Relationship Between Multifunctional Protein "Clusterin" and Alzheimer Disease
Choi-Miura, N.-H., & Oda, T. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00106-6 · Cited by 54
Amyloid β peptide induces cytoplasmic accumulation of amyloid protein precursor via tau protein kinase I/glycogen synthase kinase-3β in rat hippocampal neurons
Takashima, A., Yamaguchi, H., Noguchi, K., Michel, G., Ishiguro, K., Sato, K., Hoshino, T., Hoshi, M. M., & Imahori, K. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11964-x · Cited by 54
β-amyloid increases choline conductance of PC12 cells: possible mechanism of toxicity in Alzheimer's disease
Galdzicki, Z., Fukuyama, R., Wadhwani, K. C., Rapoport, S. I., & Ehrenstein, G. (1994) · Brain Research · doi:10.1016/0006-8993(94)90101-5 · Cited by 54
Action of amyloid beta-protein on protein kinase C activity
Chauhan, A., Chauhan, V. P. S., Brockerhoff, H., & Wı́sniewski, H. M. (1991) · Life Sciences · doi:10.1016/0024-3205(91)90328-9 · Cited by 54
The β-Amyloid Precursor Protein and its Derivatives: From Biology to Learning and Memory Processes
Dodart, J., Mathis, C., & Ungerer, A. (2000) · Reviews in the Neurosciences · doi:10.1515/revneuro.2000.11.2-3.75 · Cited by 54
The older rabbit as an animal model: Implications for Alzheimer's disease
Woodruff‐Pak, D. S., & Trojanowski, J. Q. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(95)02064-0 · Cited by 54
Oxidative damage in Alzheimer’s disease
(2015) · Therapeutic Targets for Neurological Diseases · doi:10.14800/ttnd.246 · Cited by 54
A calcium-activated protease from Alzheimer's disease brain cleaves at the N-terminus of the amyloid β-protein
Abraham, C. R., Driscoll, J. J., Potter, H., Nostrand, W. E. V., & Tempst, P. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91487-w · Cited by 54
The muscarinic M1 agonist xanomeline increases soluble amyloid precursor protein release from chinese hamster ovary-m1 cells
Eckols, K., Bymaster, F. P., Mitch, C. H., Shannon, H. E., Ward, J. S., & DeLapp, N. W. (1995) · Life Sciences · doi:10.1016/0024-3205(95)02064-p · Cited by 53
Alzheimer’s Disease Animal Models: Elucidation of Biomarkers and Therapeutic Approaches for Cognitive Impairment
NAKAI, T., Yamada, K., & Mizoguchi, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115549 · Cited by 53
Lysophosphatidylcholine increases the neurotoxicity of Alzheimer’s amyloid β1-42 peptide: Role of oligomer formation
Sheikh, A. M., Michikawa, M., Kim, S. U., & Nagai, A. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.02.034 · Cited by 53
Mitochondrial Ferritin Deletion Exacerbates β‐Amyloid‐Induced Neurotoxicity in Mice
Wang, P., Wu, Q., Wu, W., Li, H., Guo, Y., Yu, P., Gao, G., Shi, Z., Zhao, B., & Chang, Y. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/1020357 · Cited by 53
Selective Antibody-Induced Cholinergic Cell and Synapse Loss Produce Sustained Hippocampal and Cortical Hypometabolism with Correlated Cognitive Deficits
Browne, S. E., Lin, L., Mattsson, A., Georgievska, B., & Ole Isacson, A. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7700 · Cited by 53
Aβ1–42 promotes cholinergic sprouting in patients with AD and Lewy body variant of AD
Masliah, E., Alford, M. F., Adame, A., Rockenstein, E. M., Galasko, D., Salmon, D. P., Hansen, L. A., & Thal, L. J. (2003) · Neurology · doi:10.1212/01.wnl.0000073987.79060.4b · Cited by 53
Neurotrophic factor mediated protection from excitotoxicity and disturbances in calcium and free radical metabolism
Mattson, M. P., Cheng, B., & Smith‐Swintosky, V. L. (1993) · Seminars in Neuroscience · doi:10.1016/s1044-5765(05)80035-1 · Cited by 53
Urine-Based Biomarkers for Alzheimer’s Disease Identified Through Coupling Computational and Experimental Methods
Yao, F., Hong, X., Li, S., Zhang, Y., Zhao, Q., Du, W., Wang, Y., & Ni, J. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180261 · Cited by 52
Chronic Apocynin Treatment Attenuates Beta Amyloid Plaque Size and Microglial Number in hAPP(751)SL Mice
Lull, M. E., Levesque, S., Surace, M. J., & Block, M. L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020153 · Cited by 53
Simultaneous Single-Molecule Fluorescence and Conductivity Studies Reveal Distinct Classes of Aβ Species on Lipid Bilayers
Schauerte, J. A., Wong, P., Wisser, K. C., Ding, H., Steel, D. G., & Gafni, A. (2010) · Biochemistry · doi:10.1021/bi901444w · Cited by 52
Genetic studies in Alzheimer's disease
Tang, Y., & Gershon, E. S. (2003) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2003.5.1/yptang · Cited by 52
Discovery of Potent Human Glutaminyl Cyclase Inhibitors as Anti-Alzheimer’s Agents Based on Rational Design
Hoang, V.-H., Tran, P., Cui, M., Ngo, V. T. H., Ann, J., Park, J., Lee, J., Choi, K., Cho, H., Kim, H., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00098 · Cited by 52
Clusterin Is Required for β-Amyloid Toxicity in Human iPSC-Derived Neurons
Robbins, J. P., Perfect, L., Ribé, E. M., Maresca, M., Dangla-Valls, A., Foster, E. M., Killick, R., Nowosiad, P., Reid, M. J., Polit, L. D., et al. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00504 · Cited by 53
Photoactive Bismuth Vanadate Structure for Light‐Triggered Dissociation of Alzheimer's β‐Amyloid Aggregates
Kim, K., Lee, S. H., Choi, D. S., & Park, C. B. (2018) · Advanced Functional Materials · doi:10.1002/adfm.201802813 · Cited by 52
β-Amyloid peptide toxicity in organotypic hippocampal slice culture involves Akt/PKB, GSK-3β, and PTEN
Nassif, M., Hoppe, J. B., Santin, K., Frozza, R. L., Zamin, L. L., Simão, F., Horn, A. P., & Salbego, C. G. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.08.008 · Cited by 52
Disruption of circadian regulation by brain grafts that overexpress Alzheimer beta/A4 amyloid.
Tate, B. A., Aboody-Guterman, K. S., Morris, A. M., Walcott, E. C., Majocha, R. E., & Marotta, C. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.15.7090 · Cited by 52
Fas and Fas ligand expression in Alzheimer's disease
Ferrer, I., Puig, B., Krupiński, J., Carmona, M., & Blanco, R. E. (2001) · Acta Neuropathologica · doi:10.1007/s004010000325 · Cited by 52
Proteolytic processing of amyloid β protein precursor (APP) by thrombin
Igarashi, K., Murai, H., & Asaka, J. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91726-7 · Cited by 52
Transgenic Animal Models for Alzheimer's Diseasea
Fukuchi, K., Ogburn, C. E., SMITH, A. C., Kunkel, D. D., Furlong, C. E., Deeb, S. S., Nochlin, D., Sumi, S. M., & Martin, G. M. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23055.x · Cited by 52
Studies of the Effects of Central Administration of β-Amyloid Peptide (25–35): Pathomorphological Changes in the Hippocampus and Impairment of Spatial Memory
Stepanichev, M. Y., Zdobnova, I. M., Zarubenko, I. I., Лазарева, Н. А., & Gulyaeva, N. V. (2005) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-005-0167-1 · Cited by 51
Amyloid beta plaque: a culprit for neurodegeneration
Gupta, A., & Goyal, R. (2016) · Acta Neurologica Belgica · doi:10.1007/s13760-016-0639-9 · Cited by 51
A resorcinarene for inhibition of Aβ fibrillation
Han, X., Park, J., Wu, W., Malagón, A., Wang, L., Vargas, É. F., Wikramanayake, A. H., Houk, K. N., & Leblanc, R. M. (2016) · Chemical Science · doi:10.1039/c6sc04854d · Cited by 51
Brain Amyloid — A Physicochemical Perspective
Maggie, J. E., & Mantyh, P. W. (1996) · Brain Pathology · doi:10.1111/j.1750-3639.1996.tb00797.x · Cited by 51
β-Amyloid Peptides Impair PKC-Dependent Functions of Metabotropic Glutamate Receptors in Prefrontal Cortical Neurons
Tyszkiewicz, J. P., & Yan, Z. (2005) · Journal of Neurophysiology · doi:10.1152/jn.00939.2004 · Cited by 51
Effects of endothelin B receptor agonists on amyloid β protein (25–35)-induced neuronal cell death
Yagami, T., Ueda, K., Asakura, K., Kuroda, T., Hata, S., Sakaeda, T., Kambayashi, Y., & Fujimoto, M. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02951-7 · Cited by 51
Alzheimer's disease: molecular concepts and therapeutic targets
Fassbender, K. C., Masters, C. L., & Beyreuther, K. T. (2001) · Die Naturwissenschaften · doi:10.1007/s001140100237 · Cited by 51
Changes in Protein Kinases in Brain Aging and Alzheimer??s Disease
Jin, L., & Saitoh, T. (1995) · Drugs & Aging · doi:10.2165/00002512-199506020-00006 · Cited by 51
Amyloid in Alzheimer's disease and prion-related encephalopathies: studies with synthetic peptides
Forloni, G., Tagliavini, F., Bugiani, O., & Salmona, M. (1996) · Progress in Neurobiology · doi:10.1016/0301-0082(96)00013-5 · Cited by 51
Amyloid beta-protein activates tachykinin receptors and inositol trisphosphate accumulation by synergy with glutamate.
Kimura, H., & Schubert, D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7508 · Cited by 51
Release of amino-terminal fragments from amyloid precursor protein reporter and mutated derivatives in cultured cells.
Sahasrabudhe, S. R., Spruyt, M. A., Muenkel, H. A., Blume, A. J., Vitek, M. P., & Jacobsen, J. S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74083-6 · Cited by 51
Mechanisms of cell death in Alzheimer’s disease
Bancher, C., Lassmann, H., Breitschopf, H., & Jellinger, K. A. (1997) · Journal of Neural Transmission. Supplementa · doi:10.1007/978-3-7091-6842-4_14 · Cited by 50
Pathogenesis of Alzheimer Disease: Role of Oxidative Stress, Amyloid-β Peptides, Systemic Ammonia and Erythrocyte Energy Metabolism
Kosenko, E. A., Solomadin, I., Tikhonova, L. A., Reddy, V. P., Aliev, G., & Kaminsky, Y. G. (2013) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/18715273113126660130 · Cited by 50
SAR110894, a potent histamine H3-receptor antagonist, displays procognitive effects in rodents
Griebel, G., Pichat, P., Pruniaux, M., Beeské, S., Lopez‐Grancha, M., Genet, E., Terranova, J.-P., Castro, A., Sánchez, J. A., Black, M. D., et al. (2012) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2012.04.004 · Cited by 50
Effects of glucocorticoids on oxidative stress-induced hippocampal cell death: implications for the pathogenesis of Alzheimer’s disease
Behl, C. (1998) · Experimental Gerontology · doi:10.1016/s0531-5565(98)00019-9 · Cited by 50
Olfactory neuroblasts from Alzheimer donors: Studies on APP processing and cell regulation
Wolozin, B. L., Lesch, K., Lebovics, R. S., & Sunderland, T. (1993) · Biological Psychiatry · doi:10.1016/0006-3223(93)90051-e · Cited by 50
Alzheimer's β-amyloid peptide as a source of neurotoxic free radicals: the role of structural effects
Pogocki, D. (2003) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2003-1463 · Cited by 50
Aggregation of Amyloid .BETA.-Protein and Its Neurotoxicity: Enhancement by Aluminum and Other Metals.
Kuroda, Y., & Kawahara, M. (1994) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.174.263 · Cited by 50
The Role of G Protein Activation in the Toxicity of Amyloidogenic Aβ-(1–40), Aβ-(25–35), and Bovine Calcitonin
Rymer, D. L., & Good, T. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005800200 · Cited by 50
Excitotoxic mechanisms in the pathogenesis of dementia
Dodd, P. R., Scott, H. L., & Westphalen, R. I. (1994) · Neurochemistry International · doi:10.1016/0197-0186(94)90064-7 · Cited by 50
Oleic acid ameliorates Aβ-induced inflammation by downregulation of COX-2 and iNOS via NFκB signaling pathway
Kim, H., Youn, K., Yun, E.-Y., Hwang, J.-S., Jeong, W., Ho, C., & Jun, M. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.01.027 · Cited by 49
Ligand–Receptor Interaction Catalyzes the Aggregation of Small Molecules To Induce Cell Necroptosis
Shi, J., Du, X., Yi, H., Zhou, J., Yuan, D., Wu, D., Zhang, Y., Haburcak, R., Epstein, I. R., & Xu, B. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5100417 · Cited by 49
Importance of Immunological and Inflammatory Processes in the Pathogenesis and THERAPY of Alzheimer's Disease
Popović, M., Caballero‐Bleda, M., Puelles, L., & Popović, N. (1998) · International Journal of Neuroscience · doi:10.3109/00207459809003341 · Cited by 49
Amyloid β-protein stimulates casein kinase I and casein kinase II activities
Chauhan, A., Chauhan, V. P. S., Murakami, N., Brockerhoff, H., & Wísniewski, H. M. (1993) · Brain Research · doi:10.1016/0006-8993(93)90479-7 · Cited by 49
Review
Verbeek, M. M., Ruiter, D. J., & de Waal, R. M. W. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.9.937 · Cited by 49
Assemblies of Alzheimer’s peptides Aβ25–35 and Aβ31–35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction
Bond, J. P., Deverin, S. P., Inouye, H., El‐Agnaf, O. M. A., Teeter, M. M., & Kirschner, D. A. (2003) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00625-1 · Cited by 49
Self-citation
Peripheral Transgene Expression of Plasma Gelsolin Reduces Amyloid in Transgenic Mouse Models of Alzheimer's Disease
Hirko, A. C., Meyer, E. M., King, M. A., & Hughes, J. A. (2007) · Molecular Therapy · doi:10.1038/sj.mt.6300253 · Cited by 49
Memory impairment and cholinergic dysfunction by centrally administered Aβ and carboxyl‐terminal fragment of Alzheimer's APP in mice
Choi, S. H., Park, C. H., Koo, J. W., Seo, J., Kim, H., Jeong, S., Lee, J., Kim, S. S., & Suh, Y. (2001) · The FASEB Journal · doi:10.1096/fj.00-0859fje · Cited by 49

Authors: Yankner, B. A., Duffy, L. K., & Kirschner, D. A.
Affiliations: Boston Children's Hospital (US)
University of Alaska Fairbanks (US)
ORCID: Yankner, Bruce A.
Duffy, Lawrence K.
Kirschner, Daniel A.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1990-10-12
Volume: 250
Issue: 4978
Pages: 279-282
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.2218531
OpenAlex: W2059214757
Cited by: 1,975
References: 31
Citations by year: 2026: 9 · 2025: 17 · 2024: 15 · 2023: 22 · 2022: 14 · 2021: 29 · 2020: 19 · 2019: 29 · 2018: 32 · 2017: 27 · 2016: 37 · 2015: 44 · 2014: 46 · 2013: 40 · 2012: 40
FWCI: 64.80
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG08572, R01AG008572)
National Institute of Neurological Disorders and Stroke (NS01240, K08NS001240)
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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta, Alzheimer's disease, neurotoxicity, neurotrophic effects, tachykinin antagonists, hippocampal neurons, neuronal differentiation, neuronal cell death, dendritic retraction, axonal retraction, neurotrophic factors
MeSH terms: Amino Acid Sequence, Animals, Cells, Cultured, Embryo, Mammalian, Hippocampus, Molecular Sequence Data, Neurons, Neurotoxins, Peptide Fragments, Tachykinins, Amyloid beta-Peptides, 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 ›

Are you an author, or do you see a problem with this page? Request a review

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks