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Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
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.
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“This Aβ peptide fragment contains the biologically active portion of Aβ (Yanker et al., 1990; Takadera et al., 1993).”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Yanker et al., 1990
Citations
Cites
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
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-citationOutgrowth-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
Maggio, J. E. (1988) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.11.030188.000305 · Cited by 550
Flagged first, then by citations
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).
Cited by
Sorted by citations
Items 401–500 of 1,008
Patil, S. P., Melrose, J., & Chan, C. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05797.x · Cited by 129
Neurofibrillary tangles and β-amyloid deposits in Alzheimer's disease
Goedert, M., Sisodia, S. S., & Price, D. L. (1991) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(91)90067-h · Cited by 128
Amyloid β peptide alters intracellular vesicle trafficking and cholesterol homeostasis
Liu, Y., Peterson, D. A., & Schubert, D. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13266 · Cited by 128
Zhang, L., Xing, G. Q., Barker, J. L., Chang, Y. H., Maric, D., Ma, W., Li, B., & Rubinow, D. R. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02205-4 · Cited by 128
An interaction of β‐amyloid with aluminium in vitro
Exley, C., Price, N. C., Kelly, S. M., & Birchall, J. D. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80137-j · Cited by 128
Transient receptor potential channels in Alzheimer's disease
Yamamoto, S., Wajima, T., Hara, Y., Nishida, M., & Mori, Y. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.03.006 · Cited by 127
Increased antioxidant enzyme activity in amyloid beta protein-resistant cells
Sagara, Y., Dargusch, R., Klier, F. G., Schubert, D. A., & Behl, C. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-02-00497.1996 · Cited by 127
Ionic effects of the Alzheimer's disease β-amyloid precursor protein and its metabolic fragments
Fraser, S. P., Suh, Y.-H., & Djamgoz, M. B. A. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)10079-5 · Cited by 127
Lack of alzheimer pathology after β-amyloid protein injections in rat brain
Games, D., Khan, K., Soriano, F., Keim, P. S., Davis, D. L., Bryant, K., & Lieberburg, I. M. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90057-5 · Cited by 127
Hormetic effect of amyloid-beta peptide in synaptic plasticity and memory.
Puzzo, D., Privitera, L., & Palmeri, A. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.12.020 · Cited by 95
Sex, Hormones, and Alzheimer's Disease
Baum, L. (2005) · The Journals of Gerontology Series A · doi:10.1093/gerona/60.6.736 · Cited by 127
Xu, J., Chen, S., Ku, G., Ahmed, S. H., Xu, J., Chen, H., & Hsu, C. Y. (2001) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200106000-00008 · Cited by 125
Mungarro‐Menchaca, X., Ferrera, P., Morán, J., & Arias, C. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10193 · Cited by 125
Schulze, H., Schuler, A., Stüber, D., Döbeli, H., Langen, H., & Huber, G. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb13420.x · Cited by 125
Kelly, J. W., & Lansbury, P. T. (1994) · Amyloid · doi:10.3109/13506129409148451 · Cited by 125
Mechanisms of Neuronal Cell Death in Wernicke's Encephalopathy
Hazell, A. S., Todd, K. G., & Butterworth, R. F. (1998) · Metabolic Brain Disease · doi:10.1023/a:1020657129593 · Cited by 124
Mattson, M. P., Begley, J. G., Mark, R. J., & Furukawa, K. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00824-x · Cited by 124
Galantamine modulates nicotinic receptor and blocks Aβ-enhanced glutamate toxicity
Kihara, T., Sawada, H., Nakamizo, T., Kanki, R., Yamashita, H., Maelicke, A., & Shimohama, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.132 · Cited by 124
Deregulated Cdk5 promotes oxidative stress and mitochondrial dysfunction
Sun, K., de Pablo, Y., Vincent, F., & Shah, K. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05616.x · Cited by 124
β-amyloid peptide decreases membrane fluidity
Müller, W. E., Koch, S., Eckert, A., Hartmann, H., & Scheuer, K. (1995) · Brain Research · doi:10.1016/0006-8993(94)01463-r · Cited by 124
May, P. C., Boggs, L. N., & Fuson, K. S. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07480.x · Cited by 124
Alzheimer’s disease due to loss of function: A new synthesis of the available data
Kepp, K. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.004 · Cited by 123
Exploring ER stress response in cellular aging and neuroinflammation in Alzheimer's disease
Uddin, M. S., Yu, W. S., & Lim, L. W. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101417 · Cited by 123
Arendt, T., Holzer, M., Grossmann, A., Zedlick, D., & Brückner, M. K. (1995) · Neuroscience · doi:10.1016/0306-4522(95)00146-a · Cited by 123
Reynolds, R., & Hardy, R. (1997) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19970301)47:5 · Cited by 261
Impairments of long-term potentiation in hippocampal slices of β-amyloid-infused rats
Itoh, A., Akaike, T., Sokabe, M., Nitta, A., Iida, R., Olariu, A., Yamada, K., & Nabeshima, T. (1999) · European Journal of Pharmacology · doi:10.1016/s0014-2999(99)00601-9 · Cited by 122
Ötvös, L., Szendrei, G. I., Lee, V. M.-Y., & Mantsch, H. H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb19893.x · Cited by 122
Beta-amyloid peptide blocks the fast-inactivating K+ current in rat hippocampal neurons
Good, T. A., Smith, D. O., & Murphy, R. M. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79570-x · Cited by 122
Zhou, L., Saksena, M. M., & Saksena, N. K. (2013) · Virology Journal · doi:10.1186/1743-422x-10-172 · Cited by 121
Global Effects of Mistranslation from an Editing Defect in Mammalian Cells
Nangle, L. A., Motta, C. M., & SCHIMMEL, P. R. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.08.011 · Cited by 121
New clues to Alzheimer's disease: Unraveling the roles of amyloid and tau
Yanker, B. A. (1996) · Nature Medicine · doi:10.1038/nm0896-850 · Cited by 120
Burdick, D., Kosmoski, J., Knauer, M. F., & Glabe, C. G. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01262-0 · Cited by 102
Kushima, Y., Hama, T., & Hatanaka, H. (1992) · Neuroscience Research · doi:10.1016/0168-0102(92)90039-f · Cited by 120
Expression of the low-affinity nerve growth factor receptor enhances beta-amyloid peptide toxicity.
Rabizadeh, S., Bitler, C. M., Butcher, L. L., & Bredesen, D. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10703 · Cited by 120
Axonal degeneration as a therapeutic target in the CNS
Lingor, P., Koch, J. C., Tönges, L., & Bähr, M. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1362-3 · Cited by 119
Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2008) · Biochemistry · doi:10.1021/bi8011093 · Cited by 119
Zussy, C., Brureau, A., Keller, E., Marchal, S., Blayo, C., Delair, B., IXART, G., Maurice, T., & Givalois, L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053117 · Cited by 118
Architecture of the Alzheimer?s A�P Ion Channel Pore
Arispe, N. J. (2004) · The Journal of Membrane Biology · doi:10.1007/s00232-003-0638-7 · Cited by 117
β‐Cyclodextrin interacts with the Alzheimer amyloid β‐A4 peptide
Camilleri, P., Haskins, N. J., & Hewlett, D. R. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80467-2 · Cited by 117
Solá, S., Castro, R. E., Laires, P. A., Steer, C. J., & Rodrigues, C. M. P. (2003) · Molecular Medicine · doi:10.2119/2003-00042.rodrigues · Cited by 117
β-amyloid peptide in vitro toxicity: Lot-to-lot variability
May, P. C., Gitter, B. D., Waters, D. C., Simmons, L. K., Becker, G. W., Small, J. S., & Robison, P. M. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90064-5 · Cited by 117
Mark, R. J., Ashford, J. W., Goodman, Y., & Mattson, M. P. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00150-2 · Cited by 117
Neurodegeneration mediated by glutamate and β-amyloid peptide: a comparison and possible interaction
Gray, C. W., & Patel, A. J. (1995) · Brain Research · doi:10.1016/0006-8993(95)00669-h · Cited by 117
The keystone of Alzheimer pathogenesis might be sought in Aβ physiology
Puzzo, D., Gulisano, W., Arancio, O., & Palmeri, A. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.08.039 · Cited by 116
A Novel Neurotrophic Drug for Cognitive Enhancement and Alzheimer's Disease
Chen, Q., Prior, M., Dargusch, R., Roberts, A. J., Riek, R., Eichmann, C., Chiruta, C., Akaishi, T., Abe, K., Maher, P. A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027865 · Cited by 116
Tohda, C., Tamura, T., Matsuyama, S., & Komatsu, K. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706865 · Cited by 116
Klein, A., Kowall, N. W., & Ferrante, R. J. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07845.x · Cited by 115
A broadly neuroprotective derivative of curcumin
Liu, Y., Dargusch, R., Maher, P. A., & Schubert, D. A. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05236.x · Cited by 115
Cofilin-mediated neurodegeneration in alzheimer’s disease and other amyloidopathies
Maloney, M. T., & Bamburg, J. R. (2007) · Molecular Neurobiology · doi:10.1007/bf02700622 · Cited by 115
Stepanichev, M. Y., Moiseeva, Y. V., Лазарева, Н. А., Onufriev, M. V., & Gulyaeva, N. V. (2003) · Brain Research Bulletin · doi:10.1016/s0361-9230(03)00118-7 · Cited by 115
Magrané, J., Rosen, K. M., Smith, R. C., Walsh, K. X., Gouras, G. K., & Querfurth, H. W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1723-05.2005 · Cited by 115
Passage of human amyloid β-protein 1–40 across the murine blood-brain barrier
Maness, L. M., Banks, W. A., Podlisny, M. B., Selkoe, D. J., & Kastin, A. J. (1994) · Life Sciences · doi:10.1016/0024-3205(94)00331-9 · Cited by 97
Amyloid-β-Induced Ion Flux in Artificial Lipid Bilayers and Neuronal Cells: Resolving a Controversy
Capone, R. F., Quiroz, F. G., Prangkio, P., Saluja, I., Sauer, A., Bautista, M. R., Turner, R. S., Yang, J., & Mayer, M. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9033-1 · Cited by 114
Expression analysis of glycogen synthase kinase‐3 in human tissues
Lau, K., Miller, C. C. J., Anderton, B. H., & Shaw, P. C. (1999) · Journal of Peptide Research · doi:10.1034/j.1399-3011.1999.00083.x · Cited by 114
Hirakura, Y., Carreras, I., Sipe, J. D., & Kagan, B. L. (2002) · Amyloid · doi:10.3109/13506120209072440 · Cited by 114
Hiruma, H., Katakura, T., Takahashi, S., Ichikawa, T., & Kawakami, T. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08967.2003 · Cited by 114
Grace, E. A., & Busciglio, J. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-02-00493.2003 · Cited by 113
Stepwise dynamics of epitaxially growing single amyloid fibrils
Kellermayer, M., Karsai, Á., Benke, M., Soós, K., & Penke, B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704305105 · Cited by 113
Araujo, D. M., & Lapchak, P. A. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90398-0 · Cited by 113
Canning, D. R., Höke, A., Malemud, C. J., & Silver, J. (1996) · International Journal of Developmental Neuroscience · doi:10.1016/0736-5748(96)00004-4 · Cited by 113
Chen, K. S., Masliah, E., Mallory, M. E., & Gage, F. H. (1995) · Neuroscience · doi:10.1016/0306-4522(95)00099-5 · Cited by 113
Association between vascular basement membrane components and the lesions of Alzheimer's disease
Perlmutter, L. S., Barrón, E., Saperia, D., & Chui, H. C. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490300411 · Cited by 113
Activation of nuclear factor-κB by β-amyloid peptides and interferon-γ in murine microglia
Bonaiuto, C., McDonald, P. P., Rossi, F., & Cassatella, M. A. (1997) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00054-4 · Cited by 112
Yatin, S. M., Aksenov, M. Y., & Butterfield, D. A. (1999) · Neurochemical Research · doi:10.1023/a:1020997903147 · Cited by 112
β-Amyloid neurotoxicity: A discussion of in vitro findings
Cotman, C. W., Pike, C. J., & Copani, A. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90060-b · Cited by 112
Astroglia in Alzheimer's disease
Frederickson, R. C. A. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90036-w · Cited by 111
Frim, D. M., Short, M. P., Rosenberg, W. S., Simpson, J. R., Breakefield, X. O., & Ole Isacson, A. (1993) · Journal of neurosurgery · doi:10.3171/jns.1993.78.2.0267 · Cited by 111
Dikalov, S., Vitek, M. P., & Mason, R. P. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.11.004 · Cited by 110
Klegeris, A., Walker, D. G., & McGeer, P. L. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01229-2 · Cited by 110
Amyloid Beta-Induced Neuronal Death is Bax-Dependent but Caspase-Independent
Selznick, L. A., Zheng, T. S., Flavell, R. A., RAKIC, P. T., & Roth, K. A. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.4.271 · Cited by 110
Altered Calcium Signaling and Neuronal Injury: Stroke and Alzheimer's Disease as Examplesa
Mattson, M. P., Rydel, R. E., Lieberburg, I. M., & Smith‐Swintosky, V. L. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb18285.x · Cited by 110
The role of amyloid β in the pathogenesis of Alzheimer's disease
Gilbert, B. J. (2013) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2013-201515 · Cited by 109
Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109
Ho, J. Y. S., Yu, M.-S., Lai, C. S.-W., So, K., Yuen, W.-H., & Chang, R. C. (2007) · Brain Research · doi:10.1016/j.brainres.2007.04.075 · Cited by 109
Jhala, S. S., & Hazell, A. S. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.11.019 · Cited by 109
Murtomäki, S., Risteli, J., Risteli, L., Koivisto, U., Johansson, S., & Liesi, P. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490320216 · Cited by 109
Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2008) · Neurochemical Research · doi:10.1007/s11064-007-9469-8 · Cited by 108
Cahill, C. M., Lahiri, D. K., Huang, X., & Rogers, J. T. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.12.001 · Cited by 108
Whitcomb, D. J., Hogg, E. L., Regan, P. L., Piers, T. M., Narayan, P. S., Whitehead, G., Winters, B. L., Kim, D.-H., Kim, E., George‐Hyslop, P. S., et al. (2015) · Scientific Reports · doi:10.1038/srep10934 · Cited by 108
The SEC receptor recognizes a pentapeptide neodomain of alpha 1-antitrypsin-protease complexes
Joslin, G., Fallon, R. J., Bullock, J., Adams, S. P., & Perlmutter, D. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99160-x · Cited by 108
Alzheimer Aβ neurotoxicity: Promotion by antichymotrypsin, ApoE4; inhibition by Aβ-related peptides
Ma, J., Brewer, H. B., & Potter, H. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00112-1 · Cited by 108
The cellular model for Alzheimer's disease research: PC12 cells
Xie, D., Deng, T., Zhai, Z., Sun, T., & Xu, Y. D. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1016559 · Cited by 107
Harkany, T., O’Mahony, S. M., Kelly, J. P., Soós, K., Törõ, I., Penke, B., Luiten, P. G. M., Nyakas, C. J., Gulya, K., & Leonard, B. E. (1998) · Behavioural Brain Research · doi:10.1016/s0166-4328(97)00091-0 · Cited by 107
Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid β-peptide
Jao, S., Ma, K., Talafous, J., Orlando, R., & Zagorski, M. G. (1997) · Amyloid · doi:10.3109/13506129709003835 · Cited by 107
Cam (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-8 · Cited by 106
Clementi, M. E., Pezzotti, M., Orsini, F., Sampaolese, B., Mezzogori, D., Grassi, C., Giardina, B., & Misiti, F. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.137 · Cited by 105
Is the Amyloid Hypothesis of Alzheimer's disease therapeutically relevant?
Teich, A. F., & Arancio, O. (2012) · Biochemical Journal · doi:10.1042/bj20120653 · Cited by 105
Novel Genetic Tools Reveal Cdk5's Major Role in Golgi Fragmentation in Alzheimer's Disease
Sun, K.-H., de Pablo, Y., Vincent, F., Johnson, E. O., Chavers, A. K., & Shah, K. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-11-1106 · Cited by 105
Neurovascular Pathways and Alzheimer Amyloid β-peptide
Zlokovic, B. V., Deane, R., Sallstrom, J., Chow, N., & Miano, J. M. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00103.x · Cited by 104
Thal, D. R., Papassotiropoulos, A., Saido, T. C., Griffin, W. S. T., Mrak, R. E., Kölsch, H., Tredici, K. D., Attems, J., & Ghebremedhin, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0707-9 · Cited by 103
The amyloid‐β peptide and its role in Alzheimer's disease
Clippingdale, A. B., Wade, J. D., & Barrow, C. J. (2001) · Journal of Peptide Science · doi:10.1002/psc.324 · Cited by 103
Norman, J. P., Perry, S. W., Reynolds, H. M., Kiebala, M., Bentley, K. L. D. M., Trejo, M., Volsky, D. J., Maggirwar, S. B., Dewhurst, S., Masliah, E., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003731 · Cited by 103
Nicotinic receptor–mediated protection against β-amyloid neurotoxicity
Shimohama, S., & Kihara, T. (2001) · Biological Psychiatry · doi:10.1016/s0006-3223(00)01100-8 · Cited by 103
Small heat shock proteins inhibit in vitro Aβ1–42 amyloidogenesis
Kudva, Y. C., Hiddinga, H. J., Butler, P. C., Mueske, C. S., & Eberhardt, N. L. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01180-0 · Cited by 103
Scarborough, P. E., Dunn, B. M., Guruprasad, K., Topham, C. M., Blundell, T. L., Richo, G. R., & Conner, G. E. (1993) · Protein Science · doi:10.1002/pro.5560020215 · Cited by 103
Amyloid-beta peptide, substance P, and bombesin bind to the serpin-enzyme complex receptor.
Joslin, G., Krause, J. E., Hershey, A. D., Adams, S., Fallon, R. J., & Perlmutter, D. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54721-9 · Cited by 103
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Metadata
- Authors
- Yankner, B. A., Duffy, L. K., & Kirschner, D. A.
- Affiliations
- Boston Children's Hospital (US)
- University of Alaska Fairbanks (US)
- Venue
- Science
- Published
- 1990-10-12
- Volume
- 250
- Issue
- 4978
- Pages
- 279-282
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- 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
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