The DOI matches its Crossref record; 186 of the 189 references it cites were found in a registry or an index.
Alzheimer's disease amyloid β-protein and synaptic function
Abstract
Alzheimer's disease (AD) is characterized neuropathologically by the deposition of different forms of amyloid beta-protein (A beta) including variable amounts of soluble species that correlate with severity of dementia. The extent of synaptic loss in the brain provides the best morphological correlate of cognitive impairment in clinical AD. Animal research on the pathophysiology of AD has therefore focussed on how soluble A beta disrupts synaptic mechanisms in vulnerable brain regions such as the hippocampus. Synaptic plasticity in the form of persistent activity-dependent increases or decreases in synaptic strength provide a neurophysiological substrate for hippocampal-dependent learning and memory. Acute treatment with human-derived or chemically prepared soluble A beta that contains certain oligomeric assemblies, potently and selectively disrupts synaptic plasticity causing inhibition of long-term potentiation (LTP) and enhancement of long-term depression (LTD) of glutamatergic transmission. Over time these and related actions of A beta have been implicated in reducing synaptic integrity. This review addresses the involvement of neurotransmitter intercellular signaling in mediating or modulating the synaptic plasticity disrupting actions of soluble A beta, with particular emphasis on the different roles of glutamatergic and cholinergic mechanisms. There is growing evidence to support the view that NMDA and possibly nicotinic receptors are critically involved in mediating t…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Previous reports consistently show that Aβ inhibits long-term potentiation (LTP) in the hippocampus (Ondrejcak et al., 2010), a widely accepted cellular model for learning and memory (Bliss and Collingridge, 1993)”
From Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice (2017) · cites this paper as Ondrejcak et al., 2010
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“…that certain forms of soluble Ab can trigger synaptic pruning in cultured neurons and brain slices in vitro (Roselli et al. 2005; Shankar et al. 2007) and cause cognitive impairment in the absence of neurodegeneration in animals (Cleary et al. 2005; Lesne et al. 2006; Haass and Selkoe 2007).”
BackgroundRetractedPhilosophical transactions of the Royal Society of London. B
Press, H. (1886) · Cited by 10,087
A JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
Lindemann, L., Jaeschke, G., Michalon, A., Vieira, E., Honer, M., Spooren, W., Porter, R., Hartung, T., Kolczewski, S., Büttelmann, B., et al. (1909) · JAMA · doi:10.1001/jama.1909.02550020033007 · Cited by 7,889
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Self-citationShankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Self-citationDiffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Long-Term Potentiation and Memory
Lynch, M. A. (2004) · Physiological Reviews · doi:10.1152/physrev.00014.2003 · Cited by 2,074
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644
Mattson, M. P., Cheng, B., Davis, D. G., Bryant, K., Lieberburg, I. M., & Rydel, R. E. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-02-00376.1992 · Cited by 1,633
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530
Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431
Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188
NMDA receptor trafficking in synaptic plasticity and neuropsychiatric disorders
Lau, C. G., & Zukin, R. S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2153 · Cited by 1,159 · cited 2×
“…the relative importance of the various soluble Ab assembly states in causing cognitive deficits has emphasized the importance of both low-n oligomers (such as dimers and trimers) and larger oligo- mers (including some that may form globular structures independent of Ab aggregation into fibrils).”
BackgroundClusters of Hyperactive Neurons Near Amyloid Plaques in a Mouse Model of Alzheimer’s Disease
Busche, M. A., Eichhoff, G., Adelsberger, H., Abramowski, D., Wiederhold, K.-H., Haass, C., Staufenbiel, M., Konnerth, A., & Garaschuk, O. (2008) · Science · doi:10.1126/science.1162844 · Cited by 1,125
AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042
Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., & Selkoe, D. (2009) · Neuron · doi:10.1016/j.neuron.2009.05.012 · Cited by 972
Chishti, M. A., Yang, D.-S., Janus, C., Phinney, A. L., Horne, P., Pearson, J., Strome, R., Zuker, N., Loukides, J., French, J., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100710200 · Cited by 955
Cholinergic systems in mammalian brain and spinal cord
WOOLF, N. (1991) · Progress in Neurobiology · doi:10.1016/0301-0082(91)90006-m · Cited by 948
Glutamate-mediated excitotoxicity and neurodegeneration in Alzheimer?s disease
HYND, M. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2004.03.007 · Cited by 938
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882
β-Amyloid1–42 Binds to α7 Nicotinic Acetylcholine Receptor with High Affinity
Wang, H.-Y., Lee, D. H. S., D’Andrea, M. R., Peterson, P. A., Shank, R. P., & Reitz, A. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5626 · Cited by 818
Metabotropic glutamate receptors: electrophysiological properties and role in plasticity
Anwyl, R. (1999) · Brain Research Reviews · doi:10.1016/s0165-0173(98)00050-2 · Cited by 799
Turner, P. R., O’Connor, K., Tate, W. P., & Abraham, W. C. (2003) · Progress in Neurobiology · doi:10.1016/s0301-0082(03)00089-3 · Cited by 796
Picomolar Amyloid-β Positively Modulates Synaptic Plasticity and Memory in Hippocampus
Puzzo, D., Privitera, L., Leznik, E., Fà, M., Staniszewski, A., Palmeri, A., & Arancio, O. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2692-08.2008 · Cited by 740
Synchronous Hyperactivity and Intercellular Calcium Waves in Astrocytes in Alzheimer Mice
Kuchibhotla, K. V., Lattarulo, C. R., Hyman, B. T., & Bacskai, B. J. (2009) · Science · doi:10.1126/science.1169096 · Cited by 729
Parsons, C. G., Stöffler, A., & Danysz, W. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.07.013 · Cited by 724
β-amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity
Zheng, H., Jiang, M., Trumbauer, M. E., SIRINATHSINGHJI, D. J. S., Hopkins, R., Smith, D. W., HEAVENS, R. P., Dawson, G. R., Boyce, S., Conner, M. W., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90073-x · Cited by 699
Bodick, N. C., Offen, W., Levey, A. I., Cutler, N. R., Gauthier, S. G., Satlin, A., Shannon, H. E., Tollefson, G. D., Rasmussen, K., Bymaster, F. P., et al. (1997) · Archives of Neurology · doi:10.1001/archneur.1997.00550160091022 · Cited by 697
Auld, D. S., Kornecook, T. J., Bastianetto, S., & Quirion, R. (2002) · Progress in Neurobiology · doi:10.1016/s0301-0082(02)00079-5 · Cited by 678
β-Amyloid protein increases the vulnerability of cultured cortical neurons to excitotoxic damage
Koh, J., Yang, L. L., & Cotman, C. W. (1990) · Brain Research · doi:10.1016/0006-8993(90)91355-k · Cited by 617
Wang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567
Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559
(2019) · Nature reviews. Neuroscience · doi:10.1038/41583.1471-0048 · Cited by 550
The significance of the cholinergic system in the brain during aging and in Alzheimer’s disease
Schliebs, R., & Arendt, T. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0579-2 · Cited by 548
Maurice, T., Lockhart, B. P., & Privat, A. (1996) · Brain Research · doi:10.1016/0006-8993(95)01032-7 · Cited by 530
Synaptic degeneration in Alzheimer's disease
Arendt, T. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0536-x · Cited by 517
Morris, R., Moser, E. I., Riedel, G., Martin, S. J., Sandin, J., Day, M., & O’Carroll, C. (2003) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2002.1264 · Cited by 493
Excitatory amino acids and Alzheimer's disease
Greenamyre, J. T., & Young, A. B. (1989) · Neurobiology of Aging · doi:10.1016/0197-4580(89)90143-7 · Cited by 485
Dineley, K. T., Westerman, M., Bui, D., Bell, K., Ashe, K. H., & Sweatt, J. D. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-12-04125.2001 · Cited by 462
Keller, J. N., Pang, Z., Geddes, J. W., Begley, J. G., Germeyer, A., Waeg, G., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69010273.x · Cited by 439 · cited 2×
“Possible mechanisms for the Ab-mediated enhanced excitotoxicity include the ability of Ab to reduce glutamate uptake (Harris et al. 1995; Keller et al. 1997; Harkany et al. 2000; Fernandez-Tome et al. 2004; Matos et al. 2008), or to increase glutamate release (Arias et al. 1995; Noda et al. 1999;…”
BackgroundAlbuquerque, E. X., Alkondon, M., Pereira, E. F. R., Castro, N. G., Schrattenholz, A. S., Barbosa, C. T. F., Bonfante-Cabarcas, R. A., Aracava, Y., Eisenberg, H. M., & Maelicke, A. (1997) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)36503-6 · Cited by 437
Wang, Q., Walsh, D. M., Rowan, M. J., Selkoe, D. J., & Anwyl, R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1633-03.2004 · Cited by 437
Self-citationTiming and Location of Nicotinic Activity Enhances or Depresses Hippocampal Synaptic Plasticity
Ji, D., Lape, R., & Dani, J. A. (2001) · Neuron · doi:10.1016/s0896-6273(01)00332-4 · Cited by 419
Effects of nicotinic stimulation on cognitive performance
NEWHOUSE, P. A. (2003) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2003.11.001 · Cited by 411
Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses
Almeida, C. G., Tampellini, D., Takahashi, R. H., Greengard, P., Lin, M. T., Snyder, E. M., & Gouras, G. K. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.02.008 · Cited by 397
Dawson, G. R., Seabrook, G. R., Zheng, H., Smith, D. W., Graham, S. J., O'Dowd, G., Bowery, B. J., Boyce, S., Trumbauer, M. E., Chen, H. Y., et al. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00410-2 · Cited by 394
Ring, S., Weyer, S. W., Kilian, S. B., Waldron, E., Pietrzik, C. U., Filippov, M. A., Herms, J., Buchholz, C., Eckman, C. B., Korte, M., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.1026-07.2007 · Cited by 390
The Production of Amyloid β Peptide Is a Critical Requirement for the Viability of Central Neurons
Plant, L. D., Boyle, J. P., Smith, I. F., Peers, C., & Pearson, H. A. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-13-05531.2003 · Cited by 326
Klyubin, I., Betts, V., Welzel, A. T., Blennow, K., Zetterberg, H., Wallin, A., Lemere, C. A., Cullen, W. K., Peng, Y., Wisniewski, T., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.5161-07.2008 · Cited by 321
Self-citationMüller, U. (1994) · Cell · doi:10.1016/0092-8674(94)90066-3 · Cited by 315
Zhang, S.-J., Steijaert, M. N., Lau, D., Schütz, G., Delucinge-Vivier, C., Descombes, P., & Bading, H. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.025 · Cited by 313
ROTH, M., TOMLINSON, B. E., & BLESSED, G. (1966) · Nature · doi:10.1038/209109a0 · Cited by 298
The Pathogenesis of Alzheimer Disease: An Alternative to the Amyloid Hypothesis
Terry, R. D. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199655100-00001 · Cited by 291
β-Amyloid 1–42 Peptide Directly Modulates Nicotinic Receptors in the Rat Hippocampal Slice
Pettit, D. L., Shao, Z., & Yakel, J. L. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-01-j0003.2001 · Cited by 291
Roselli, F., Tirard, M., Lu, J., Hutzler, P., Lamberti, P., Livrea, P., Morabito, M. A., & Almeida, O. F. X. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3034-05.2005 · Cited by 284
Harkany, T., Ábrahám, I. M., Timmerman, W., Laskay, G., Tóth, B., Sasvári, M., Kónya, C., Sebens, J. B., Korf, J., Nyakas, C. J., et al. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00164.x · Cited by 283
Seabrook, G. R., Smith, D. W., Bowery, B. J., Easter, A., Reynolds, T., Fitzjohn, S. M., Morton, R. A., Zheng, H., Dawson, G. R., SIRINATHSINGHJI, D. J. S., et al. (1999) · Neuropharmacology · doi:10.1016/s0028-3908(98)00204-4 · Cited by 281
Léveillé, F., Gaamouch, F. E., Gouix, E., Lecocq, M., Lobner, D., Nicole, O., & Buisson, A. (2008) · The FASEB Journal · doi:10.1096/fj.08-107268 · Cited by 280
Mg2+Imparts NMDA Receptor Subtype Selectivity to the Alzheimer's Drug Memantine
Kotermanski, S. E., & Johnson, J. W. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3703-08.2009 · Cited by 271
Nicotinic and muscarinic subtypes in the human brain: Changes with aging and dementia
Nordberg, A. K., Alafuzoff, I. I., & Winblad, B. G. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310115 · Cited by 270
β-Amyloid protein-induced Alzheimer's disease animal model
Nitta, A., Itoh, A., Hasegawa, T., & Nabeshima, T. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90239-9 · Cited by 269
Pathologically activated therapeutics for neuroprotection
Lipton, S. A. (2007) · Nature reviews. Neuroscience · doi:10.1038/nrn2229 · Cited by 268
Moloney, M. G. (1998) · Natural Product Reports · doi:10.1039/a815205y · Cited by 255
Jones, C. K., Brady, A. E., Davis, A. A., Xiang, Z., Bubser, M., Tantawy, M. N., Kane, A. S., Bridges, T. M., Kennedy, J. P., Bradley, S. R., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.1850-08.2008 · Cited by 248
Kelly, B. L., & Ferreira, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605081200 · Cited by 244
β-Amyloid Peptide Activates α7 Nicotinic Acetylcholine Receptors Expressed in Xenopus Oocytes
Dineley, K. T., Bell, K. A., Bui, D., & Sweatt, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200066200 · Cited by 242
Modulation of Hippocampus-Dependent Learning and Synaptic Plasticity by Nicotine
Kenney, J. W., & Gould, T. J. (2008) · Molecular Neurobiology · doi:10.1007/s12035-008-8037-9 · Cited by 242
Matos, M., Augusto, E., Oliveira, C. R., & Agostinho, P. M. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.08.022 · Cited by 239
Block of LTP in rat hippocampus in vivo by β-amyloid precursor protein fragments
Cullen, W. K., Suh, Y., Anwyl, R., & Rowan, M. J. (1997) · Neuroreport · doi:10.1097/00001756-199710200-00006 · Cited by 239
Self-citationShinoe, T., Matsui, M., Taketo, M. M., & Manabe, T. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2338-05.2005 · Cited by 237
Nicotinic receptor abnormalities in Alzheimer’s disease
COURT, J. A., Martin-Ruiz, C. M., Piggott, M. A., Spurden, D., Griffiths, M., & Perry, E. K. (2001) · Biological Psychiatry · doi:10.1016/s0006-3223(00)01116-1 · Cited by 232
Deshpande, A., Kawai, H., Metherate, R., Glabe, C. G., & Busciglio, J. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5980-08.2009 · Cited by 232
Stéphan, A., Laroche, S., & Davis, S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-15-05703.2001 · Cited by 228
Kang, J.-E., Cirrito, J. R., Dong, H., Csernansky, J. G., & Holtzman, D. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700148104 · Cited by 219
Synaptic plasticity in animal models of early Alzheimer's disease
Rowan, M. J., Klyubin, I. V., Cullen, W. K., & Anwyl, R. (2003) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2002.1240 · Cited by 206
Self-citationOriglia, N., Righi, M., Capsoni, S., Cattaneo, A., Fang, F., Stern, D. M., Chen, J. X., Schmidt, A. M., Arancio, O., Yan, S. D., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0204-08.2008 · Cited by 206
Acute and chronic nicotine exposure differentially facilitate the induction of LTP
Fujii, S., Ji, Z., Morita, N., & Sumikawa, K. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01982-4 · Cited by 204
Cholinergic Neuronal and Axonal Abnormalities Are Present Early in Aging and in Alzheimer Disease
Geula, C., Nagykery, N. G., Nicholas, A., & Wu, C. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31816a1df3 · Cited by 204
Taylor, C. J., Ireland, D. R., Ballagh, I. H., Bourne, K., Marechal, N. M., Turner, P. R., Bilkey, D. K., Tate, W. P., & Abraham, W. C. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.04.011 · Cited by 204
Hippocampal α7 and α4β2 nicotinic receptors and working memory
Levin, E. D., Bradley, A., Addy, N., & Sigurani, N. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00538-3 · Cited by 202
Dziewczapolski, G., Głogowski, M., Masliah, E., & Heinemann, S. F. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.6159-08.2009 · Cited by 199
Kim, J., Anwyl, R., Suh, Y., Djamgoz, M. B. A., & Rowan, M. J. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-04-01327.2001 · Cited by 186
Self-citationGu, Z., Liu, W., & Yan, Z. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806508200 · Cited by 185
RAGE and Alzheimer's Disease: A Progression Factor for Amyloid-β-Induced Cellular Perturbation?
Yan, S. D., Bierhaus, A., Nawroth, P. P., & Stern, D. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1030 · Cited by 184
Ishida, A., Furukawa, K., Keller, J. N., & Mattson, M. P. (1997) · Neuroreport · doi:10.1097/00001756-199707070-00009 · Cited by 177
Chen, Q.-S., Wei, W., Shimahara, T., & Xie, C.-W. (2002) · Neurobiology of Learning and Memory · doi:10.1006/nlme.2001.4034 · Cited by 176
Biton, B., Bergis, O. E., Galli, F., Alain, N., Lochead, A. W., Jegham, S., Godet, D., Lanneau, C., Santamaria, R., Chesney, F., et al. (2006) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301189 · Cited by 174
Wevers, A., Monteggia, L. M., Nowacki, S., Bloch, W., Schütz, U., Lindstrom, J. M., Pereira, E. F. R., Eisenberg, H. M., Giacobini, E., de Vos, R. A. I., et al. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00676.x · Cited by 159
Low-frequency activation of the NMDA receptor system can prevent the induction of LTP
Coan, E. J., Irving, A. J., & Collingridge, G. L. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90038-4 · Cited by 157
Synaptic memory mechanisms: Alzheimer's disease amyloid β-peptide-induced dysfunction
Rowan, M. J., Klyubin, I. V., Wang, Q., Hu, N., & Anwyl, R. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351219 · Cited by 154
Self-citationAmyloid Fibril Toxicity in Alzheimer's Disease and Diabetesa
Lorenzo, A., & Yankner, B. A. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34406.x · Cited by 151
Cacucci, F., Yi, M., Wills, T. J., Chapman, P. F., & O'Keefe, J. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802908105 · Cited by 148
Glutamate release from microglia via glutamate transporter is enhanced by amyloid-beta peptide
Noda, M., Nakanishi, H., & Akaike, N. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00036-6 · Cited by 144
Matsuyama, S., Matsumoto, A., Enomoto, T., & Nishizaki, T. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00259.x · Cited by 143
Frankiewicz, T., Potier, B., Bashir, Z. I., Collingridge, G. L., & Parsons, C. G. (1996) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1996.tb15245.x · Cited by 135
Yang, T., Knowles, J. K., Lu, Q., Zhang, H., Arancio, O., Moore, L. A., Chang, T., Wang, Q., Andreasson, K. I., Rajadas, J., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003604 · Cited by 134
The role of nicotinic acetylcholine receptors in Alzheimer’s disease
Oddo, S., & LaFerla, F. M. (2006) · Journal of Physiology-Paris · doi:10.1016/j.jphysparis.2005.12.080 · Cited by 132
Ge, S., & Dani, J. A. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0542-05.2005 · Cited by 132
Srivareerat, M., Tran, T. T., Alzoubi, K. H., & Alkadhi, K. A. (2008) · Biological Psychiatry · doi:10.1016/j.biopsych.2008.08.021 · Cited by 128
β-Amyloid selectively augments NMDA receptor-mediated synaptic transmission in rat hippocampus
Wu, J., Anwyl, R., & Rowan, M. J. (1995) · Neuroreport · doi:10.1097/00001756-199511270-00031 · Cited by 128
Self-citationSrivareerat, M., Tran, T. T., Salim, S., Aleisa, A. M., & Alkadhi, K. A. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.04.015 · Cited by 122
Soluble Arctic amyloid β protein inhibits hippocampal long‐term potentiation in vivo
Klyubin, I. V., Walsh, D. M., Cullen, W. K., Fadeeva, J. V., Anwyl, R., Selkoe, D. J., & Rowan, M. J. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03389.x · Cited by 121
Self-citationMa, H., Lesné, S., Kotilinek, L., Steidl-Nichols, J. V., Sherman, M. A., Younkin, L. H., Younkin, S. G., Forster, C. L., Sergeant, N., Delacourte, A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609521104 · Cited by 121
Phinney, A. L., Calhoun, M. E., Wolfer, D. P., Lipp, H., Zheng, H., & Jucker, M. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00645-9 · Cited by 120
Binding Sites of Amyloid β-Peptide in Cell Plasma Membrane and Implications for Alzheimers Disease
Verdier, Y., & Penke, B. (2004) · Current Protein and Peptide Science · doi:10.2174/1389203043486937 · Cited by 118
Welsby, P. J., Rowan, M. J., & Anwyl, R. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05187.x · Cited by 118
Self-citationWang, H., Song, L., Laird, F. M., Wong, P. C., & Lee, H. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2440-08.2008 · Cited by 116
Deregulation of NMDA-receptor function and down-stream signaling in APP[V717I] transgenic mice
Dewachter, I., Filipkowski, R. K., Priller, C., Ris, L., Neyton, J., Croes, S., Terwel, D., Gysemans, M., Devijver, H., Borghgraef, P., et al. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.06.011 · Cited by 116
Amyloid precursor protein knockout mice show age-dependent deficits in passive avoidance learning
Sénéchal, Y., Kelly, P. H., & Dev, K. K. (2007) · Behavioural Brain Research · doi:10.1016/j.bbr.2007.08.003 · Cited by 113
Harris‐White, M. E., Carney, J. M., Cole, P. S., Hensley, K., Howard, B. J., Martin, L., Bummer, P. M., Wang, Y., Pedigo, N. W., & Butterfield, D. A. (1995) · Neuroreport · doi:10.1097/00001756-199510020-00013 · Cited by 112
Zajaczkowski, W., Frankiewicz, T., Parsons, C. G., & Danysz, W. (1997) · Neuropharmacology · doi:10.1016/s0028-3908(97)00070-1 · Cited by 112
Chen, L., Yamada, K., Nabeshima, T., & Sokabe, M. (2005) · Neuropharmacology · doi:10.1016/j.neuropharm.2005.09.018 · Cited by 111
Long-Term Potentiation Is Increased in the CA1 Area of the Hippocampus of APPswe/ind CRND8 Mice
Jolas, T. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0557 · Cited by 100
Grassi, F., Palma, E., Tonini, R., Amici, M., Ballivet, M., & Eusebi, F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.035436 · Cited by 98
Role of Amyloid- Glycine 33 in Oligomerization, Toxicity, and Neuronal Plasticity
Harmeier, A., Wozny, C., Rost, B. R., Munter, L. M., Hua, H., Georgiev, O., Beyermann, M., Hildebrand, P. W., Weise, C., Schaffner, W., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1336-09.2009 · Cited by 97
Arias, C., Arrieta, I., & Tapia, R. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490410416 · Cited by 96
NMDA receptor regulation by amyloid-β does not account for its inhibition of LTP in rat hippocampus
Raymond, C. R., Ireland, D. R., & Abraham, W. C. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02269-8 · Cited by 94
Physiological Roles of Amyloid-?? and Implications for its Removal in Alzheimer???s Disease
Bishop, G. M., & Robinson, S. R. (2004) · Drugs & Aging · doi:10.2165/00002512-200421100-00001 · Cited by 94
Tietje, K. R., Anderson, D. J., Bitner, R., Blomme, E., Brackemeyer, P. J., Briggs, C., Browman, K. E., Bury, D., Curzon, P., Drescher, K., et al. (2008) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1527-3458.2008.00037.x · Cited by 91
Ventral hippocampal α4β2 nicotinic receptors and chronic nicotine effects on memory
Bancroft, A., & Levin, E. D. (2000) · Neuropharmacology · doi:10.1016/s0028-3908(00)00099-x · Cited by 89
Wevers, A., Burghaus, L., Moser, N., Witter, B., Steinlein, O. K., Schütz, U., Achnitz, B., Krempel, U., Nowacki, S., Pilz, K., et al. (2000) · Behavioural Brain Research · doi:10.1016/s0166-4328(00)00215-1 · Cited by 87
Hu, N., Smith, I. M., Walsh, D. M., & Rowan, M. J. (2008) · Brain · doi:10.1093/brain/awn174 · Cited by 87
Self-citationFernández-Tomé, P., Brera, B., Arévalo, M., & CEBALLOS, M. L. D. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.12.006 · Cited by 85
Effects of an exogenous β-amyloid peptide on retention for spatial learning
McDonald, M. P., Dahl, E. E., Overmier, J. B., Mantyh, P. W., & Cleary, J. P. (1994) · Behavioral and Neural Biology · doi:10.1016/s0163-1047(05)80059-7 · Cited by 83
Network dysfunction in Alzheimer's disease: does synaptic scaling drive disease progression?
Small, D. H. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.006 · Cited by 83
β-amyloid-(1–40) increases long-term potentiation in rat hippocampus in vitro
Wu, J., Anwyl, R., & Rowan, M. J. (1995) · European Journal of Pharmacology · doi:10.1016/0014-2999(95)00539-w · Cited by 80
Self-citationMann, E. O., & Greenfield, S. A. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.045492 · Cited by 79
Nicotinic Acetylcholine Receptors
Wiley, J., York, N., Colquhoun, D., Unwin, P. N. T., Shelley, C., Hatton, C., & Sivilotti, L. G. (2004) · Encyclopedic Dictionary of Genetics, Genomics and Proteomics · doi:10.1002/0471684228.egp08474 · Cited by 79
Ramsden, M., Plant, L. D., Webster, N. J., Vaughan, P. F. T., Henderson, Z., & Pearson, H. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00618.x · Cited by 76
α2β1 and αVβ1 integrin signaling pathways mediate amyloid-β-induced neurotoxicity
Wright, S., Malinin, N. L., Powell, K. A., Yednock, T. A., Rydel, R. E., & Griswold‐Prenner, I. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.12.002 · Cited by 75
Fodero, L. R., Mok, S. S., Lošić, D., Martin, L. L., Aguilar, M., Barrow, C. J., Livett, B. G., & Small, D. H. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02296.x · Cited by 75
Ye, C., Walsh, D. M., Selkoe, D. J., & Hartley, D. M. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.05.060 · Cited by 75
Bridging Physiology and Pathology in AD
Kim, D., & Tsai, L. (2009) · Cell · doi:10.1016/j.cell.2009.05.042 · Cited by 72
Aβ1–42 modulation of Akt phosphorylation via α7 nAChR and NMDA receptors
Abbott, J. J., Howlett, D. R., Francis, P. T., & Williams, R. J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.01.003 · Cited by 71
Protection against Aβ-mediated rapid disruption of synaptic plasticity and memory by memantine
Klyubin, I., Wang, Q., Reed, M. N., Irving, E. A., Upton, N., Hofmeister, J., Cleary, J. P., Anwyl, R., & Rowan, M. J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.04.005 · Cited by 69 · cited 5×
“Some of the strongest support for the hypothesis that Ab disrupts synaptic plasticity by increasing activation of NMDARs relies on the partial reduction of the Ab-mediated inhibition of LTP by memantine (Klyubin et al. 2009).”
BackgroundInfluentialSelf-citationCowburn, R. F., Wiehager, B., Trief, E., Mo, L., & Sundström, E. (1997) · Neurochemical Research · doi:10.1023/a:1021942109490 · Cited by 69
Compartmentalized NMDA receptor signalling to survival and death
Soriano, F. X., & Hardingham, G. E. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.138875 · Cited by 68
Lee, D. H. S., & Wang, H.-Y. (2003) · Journal of Neurobiology · doi:10.1002/neu.10203 · Cited by 67
Warpman, U., Alafuzoff, I., & Nordberg, A. (1993) · Neuroscience Letters · doi:10.1016/0304-3940(93)90103-r · Cited by 67
Bymaster, F. P., Shannon, H. E., Rasmussen, K., DeLapp, N. W., Mitch, C. H., Ward, J. S., Calligaro, D. O., Ludvigsen, T. S., Sheardown, M. J., Olesen, P. H., et al. (1998) · European Journal of Pharmacology · doi:10.1016/s0014-2999(98)00487-7 · Cited by 65
Cullen, W. K., Wu, J., Anwyl, R., & Rowan, M. J. (1996) · Neuroreport · doi:10.1097/00001756-199612200-00018 · Cited by 65
Self-citationCheng, L., Yin, W., Zhang, J., & Qi, J. (2008) · Synapse · doi:10.1002/syn.20599 · Cited by 65
Intracellular mechanisms underlying the nicotinic enhancement of LTP in the rat dentate gyrus
Welsby, P. J., Rowan, M. J., & Anwyl, R. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06562.x · Cited by 64
Self-citationThe Cholinergic Neuronal Phenotype in Alzheimer's Disease
Blusztajn, J. K., & Berse, B. (2000) · Metabolic Brain Disease · doi:10.1007/bf02680013 · Cited by 64
LAWLOR, B. A., & Davis, K. L. (1992) · Biological Psychiatry · doi:10.1016/0006-3223(92)90227-q · Cited by 63
Nicotinic receptors and Alzheimer's disease
Bourin, M., Ripoll, N., & Dailly, É. (2003) · Current Medical Research and Opinion · doi:10.1185/030079903125001631 · Cited by 62
Hu, M., Schurdak, M. E., Puttfarcken, P. S., Kouhen, R. E., Gopalakrishnan, M., & Li, J. (2007) · Brain Research · doi:10.1016/j.brainres.2007.03.051 · Cited by 60
Nicotinic receptor agonists and antagonists increase sAPPα secretion and decrease Aβ levels in vitro
Mousavi, M. T., & Hellström‐Lindahl, E. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.12.001 · Cited by 60
Domingues, A. M. D. J., Almeida, S., DACRUZESILVA, E., Oliveira, C. R., & Rego, A. C. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.03.001 · Cited by 60
Enhancement of NMDA responses by β-amyloid peptides in the hippocampus in vivo
Molnár, Z., Soós, K., Lengyel, I., Penke, B., Szegedi, V., & Budai, D. (2004) · Neuroreport · doi:10.1097/01.wnr.0000134471.06244.d2 · Cited by 60
Contribution of neural networks to Alzheimer disease's progression
Savioz, A., Leuba, G., Vallet, P. G., & Walzer, C. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.06.006 · Cited by 59
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
Chapter 12 Modulation of LTP induction by NMDA receptor activation and nitric oxide release
Zorumski, C. F., & Izumi, Y. (1998) · Progress in brain research · doi:10.1016/s0079-6123(08)63207-0 · Cited by 57
Teaktong, T., Graham, A. J., COURT, J. A., Perry, R. H., Jaros, E., Johnson, M., Hall, R., & Perry, E. K. (2004) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2004.06.015 · Cited by 57
Nicotinic Receptors Differentially Regulate N-Methyl-d-aspartate Damage in Acute Hippocampal Slices
Ferchmin, P. A., Pérez, D., Eterović, V. A., & de Vellis, J. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.048173 · Cited by 57
Chin, J. H., Ma, L., MacTavish, D., & Jhamandas, J. H. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1843-07.2007 · Cited by 56
β-Amyloid-related peptides potentiate K+-evoked glutamate release from adult rat hippocampal slices
Kabogo, D., Rauw, G. A., Amritraj, A., Baker, G. B., & Kar, S. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.08.009 · Cited by 55
Synaptic Retrogenesis and Amyloid-β in Alzheimer's Disease
Wasling, P., Daborg, J., Riebe, I., Andersson, M., Portelius, E., Blennow, K., Hanse, E., & Zetterberg, H. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0918 · Cited by 53
Dornan, W. A., Kang, D. E., McCampbell, A., & Kang, E. E. (1993) · Neuroreport · doi:10.1097/00001756-199311180-00018 · Cited by 51
Burn, J. H. (1968) · BMJ · doi:10.1136/bmj.1.5587.310-b · Cited by 50
Impairment of muscarinic transmission in transgenic APPswe/PS1dE9 mice
Machová, E., Jakubík, J., Michal, P., Oksman, M., Iivonen, H., Tanila, H., & Doležal, V. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.029 · Cited by 50
Gay, E. A., Giniatullin, R. A., Skorinkin, A., & Yakel, J. L. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.149492 · Cited by 49
Memory performance is related to amyloid and tau pathology in the hippocampus
Reitz, C., Honig, L. S., Vonsattel, J. P., Tang, M.-X., & Mayeux, R. P. (2009) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2008.154146 · Cited by 49
Stereospecific interactions are necessary for Alzheimer disease amyloid-β toxicity.
Ciccotosto, G., Tew, D., Drew, S., Smith, D. G., Johanssen, T., Lal, V., Lau, T., Perez, K., Curtain, C., Wade, J., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.018 · Cited by 48
Bobich, J. A., Zheng, Q., & Campbell, A. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6305 · Cited by 46
Wrighton, D. C., Baker, E. J., Chen, P. E., & Wyllie, D. J. A. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.143164 · Cited by 46
Freir, D. B., & Herron, C. E. (2003) · Journal of Neurophysiology · doi:10.1152/jn.00996.2002 · Cited by 45
The Role of β-Amyloid Protein in Synaptic Function: Implications for Alzheimers Disease Therapy
Peña‐Ortega, F., Gutiérrez-Lerma, A. I., Quiroz‐Baez, R., & Arias, C. (2006) · Current Neuropharmacology · doi:10.2174/157015906776359531 · Cited by 45
Sénéchal, Y., Larmet, Y., & Dev, K. K. (2006) · Neurodegenerative Diseases · doi:10.1159/000094772 · Cited by 43
αv integrins mediate beta-amyloid induced inhibition of long-term potentiation
Wang, Q., Klyubin, I., Wright, S., Griswold-Prenner, I., Rowan, M. J., & Anwyl, R. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.03.018 · Cited by 42
Self-citationGoto, Y., Niidome, T., Hongo, H., Akaike, A., Kihara, T., & Sugimoto, H. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.01.030 · Cited by 39
Szegedi, V., Juhász, G., Budai, D., & Penke, B. (2005) · Brain Research · doi:10.1016/j.brainres.2005.09.014 · Cited by 39
Beta-amyloid blocks high frequency stimulation induced LTP but not nicotine enhanced LTP
Welsby, P. J., Rowan, M. J., & Anwyl, R. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.05.013 · Cited by 39
Self-citationMartin, S. E., de Fiebre, N. E. C., & de Fiebre, C. M. (2004) · Brain Research · doi:10.1016/j.brainres.2004.07.016 · Cited by 39
Yamazaki, Y., Hamaue, N., & Sumikawa, K. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02935-9 · Cited by 39
Wu, M., He, Y., Guo, F., & Qi, J. (2008) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2008.06.005 · Cited by 30
(2017) · Elsevier eBooks · doi:10.1016/b978-0-323-47778-9.50239-7 · Cited by 22
Glutamatergic synaptic depression by synthetic amyloid β‐peptide in the medial septum
Santos‐Torres, J., de la Fuente, A., Criado, J. M., Riolobos, A. S., Heredia, M., & Yajeya, J. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21150 · Cited by 21
Li, S., Feig, L. A., & Hartley, D. M. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05760.x · Cited by 9
Pathogenesis of Alzheimer disease
Pavlović, D. M., Pavlovic, A. M., & Zugic, S. (2007) · Vojnosanitetski pregled · doi:10.2298/vsp0711765p · Cited by 8
Flagged first, then by citations
3 of the 189 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Wang, Q., Klyubin, I., Wright, S., Griswold-Prenner, I., Rowan, M. J., & Anwyl, R. (2008b). Alpha v integrins mediate beta-amyloid induced inhibition of long-term potentiation. Neurobiology of Aging, 29, 1485–1493. · DOI · Paper page
Cited by
Sorted by citations
Hippocampus in health and disease: An overview
Dhikav, V., & Anand, K. S. (2012) · Annals of Indian Academy of Neurology · doi:10.4103/0972-2327.104323 · Cited by 603
S-Glutathionylation: From Molecular Mechanisms to Health Outcomes
Xiong, Y., Uys, J. D., Tew, K. D., & Townsend, D. M. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3540 · Cited by 314
NMDA receptors in nervous system diseases
Zhou, Q., & Sheng, M. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.03.030 · Cited by 304
Resenberger, U. K., Harmeier, A., Woerner, A. C., Goodman, J. L., Müller, V., Krishnan, R., Vabulas, R. M., Kretzschmar, H. A., Lindquist, S. L., Hartl, F. U., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.86 · Cited by 250
The roles of TNF in brain dysfunction and disease
Clark, I. A., Alleva, L. M., & Vissel, B. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.08.007 · Cited by 239
Metadata
- Authors
- Ondrejcak, T., Klyubin, I., Hu, N.-W., Barry, A. E., Cullen, W. K., & Rowan, M. J.
- Affiliations
- Trinity College Dublin (IE)
- Corresponding author
- Rowan, Michael J.
- Venue
- NeuroMolecular Medicine
- Published
- 2009-09-16
- Volume
- 12
- Issue
- 1
- Pages
- 13-26
- ISSN
- 1535-1084 (ISSN-L)
- 1559-1174
- OpenAlex
- W2150302044
- Cited by
- 146
- References
- 189
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 7 · 2023: 2 · 2022: 7 · 2021: 6 · 2020: 5 · 2019: 5 · 2018: 7 · 2017: 16 · 2016: 5 · 2015: 7 · 2014: 10 · 2013: 13 · 2012: 18
- FWCI
- 10.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- NeuroMolecular Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Health Research Board
- Science Foundation Ireland
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta, soluble amyloid-beta oligomers, synaptic plasticity, long-term potentiation, long-term depression, glutamatergic neurotransmission, cholinergic mechanisms, NMDA receptor, nicotinic acetylcholine receptors, muscarinic receptors, hippocampus, synaptic loss, neurotransmitter signaling
- MeSH terms
- Acetylcholine, Alzheimer Disease, Animals, Humans, Synaptic Transmission, Receptors, Cholinergic, Synapses, Receptors, N-Methyl-D-Aspartate, Amyloid beta-Peptides, Long-Term Potentiation, Glutamic Acid, Long-Term Synaptic Depression
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