The DOI matches its Crossref record; 43 of the 44 references it cites were found in a registry or an index.
Aβ induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597–624)
Open accessAbstract
Amyloid beta-peptide (Abeta) is postulated to play a central role in the pathogenesis of Alzheimer's disease. We recently proposed a pathway of Abeta-induced toxicity that is APP dependent and involves the facilitation of APP complex formation by Abeta. The APP-dependent component requires cleavage of APP at position 664 in the cytoplasmic domain, presumably by caspases or caspase-like proteases, with release of a potentially cytotoxic C31 peptide. In this study we show that Abeta interacted directly and specifically with membrane-bound APP to facilitate APP homo-oligomerization. Using chimeric APP molecules, this interaction was shown to take place between Abeta and its homologous sequence on APP. Consistent with this finding, we demonstrated that Abeta also facilitated the oligomerization of beta-secretase cleaved APP C-terminal fragment (C99). We found that the YENPTY domain in the APP cytoplasmic tail and contained within C31 is critical for this cell death pathway. Deletion or alanine- scanning mutagenesis through this domain significantly attenuated cell death apparently without affecting either APP dimerization or cleavage at position 664. This indicated that sequences within C31 are required after its release from APP. As the YENPTY domain has been shown to interact with a number of cytosolic adaptor molecules, it is possible that the interaction of APP, especially dimeric forms of APP, with these molecules contribute to cell death.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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
“Remarkably, it was shown that extracellular Aβ1-42 was not toxic to APP knockout neurons [107] and that even point mutations in the NPXY motif in the C-terminus of APP block toxicity [169].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [169]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
Mattson, M. P. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.4.1081 · Cited by 1,006 · cited 1×
“Some biological properties have been attributed to APP, including adhesion, neuronal development, synaptogenesis, neurite outgrowth, neuroprotection, and stimulation of proliferation of neuronal progenitor cells (11).”
BackgroundSynaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954
The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
Selkoe, D. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01363-4 · Cited by 862
Gervais, F. G., Xu, D., Robertson, G. S., Vaillancourt, J. P., Zhu, Y., Huang, J., LeBlanc, A., Smith, D., Rigby, M., Shearman, M. S., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80748-5 · Cited by 674
Pathologic conformations of prion proteins.
Cohen, F., & Prusiner, S. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.793 · Cited by 533
Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 494
Sastre, M., Steiner, H., Fuchs, K. P., Capell, A., Multhaup, G., Condron, M. M., Teplow, D. B., & Haass, C. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve180 · Cited by 472
Cited by
Sorted by citations
Yankner, B. A., Lu, T., & Loerch, P. (2008) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.2.010506.092044 · Cited by 677
Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease
Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372
β-amyloid Peptides and Amyloid Plaques in Alzheimer's Disease
Gouras, G. K., Olsson, T. T., & Hansson, O. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0313-y · Cited by 346
Synaptic changes in Alzheimer’s disease and its models
Pozueta, J., Lefort, R., & Shelanski, M. L. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.050 · Cited by 319
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313
The role of metallobiology and amyloid-β peptides in Alzheimer's disease
Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07500.x · Cited by 266
Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds
Stefani, M., & Rigacci, S. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140612411 · Cited by 245
Amyloid β-Protein Toxicity and the Pathogenesis of Alzheimer Disease
Yankner, B. A., & Lu, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800018200 · Cited by 229
Amyloid-β causes memory impairment by disturbing the JAK2/STAT3 axis in hippocampal neurons
Chiba, T., Yamada, M., Sasabe, J., Terashita, K., Shimoda, M., Matsuoka, M., & Aiso, S. (2009) · Molecular Psychiatry · doi:10.1038/mp.2008.105 · Cited by 194
Kirouac, L., Rajic, A. J., Cribbs, D. H., & Padmanabhan, J. (2017) · eneuro · doi:10.1523/eneuro.0149-16.2017 · Cited by 207
Stefani, M. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.002 · Cited by 175
LTP and memory impairment caused by extracellular Aβ and Tau oligomers is APP-dependent
Puzzo, D., Piacentini, R., Fá, M., Gulisano, W., Li Puma, D. D., Staniszewski, A., Zhang, H., Tropea, M. R., Cocco, S., Palmeri, A., et al. (2017) · eLife · doi:10.7554/elife.26991 · Cited by 172
Bhattarai, P., Thomas, A. K., Cosacak, M. I., Papadimitriou, C., Mashkaryan, V., Froc, C., Reinhardt, S., Kurth, T., Dahl, A., Zhang, Y., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.075 · Cited by 151
Wang, Z., Jackson, R. J., Hong, W., Taylor, W. M., Corbett, G. T., Moreno, A. J., Liu, W., Li, S., Frosch, M. P., Slutsky, I., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2009-17.2017 · Cited by 157
Harris, J. A., Devidze, N., Halabisky, B., Lo, I., Thwin, M. T., Yu, G.-Q., Bredesen, D. E., Masliah, E., & Mucke, L. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5341-09.2010 · Cited by 146
Self-citationFogel, H., Frere, S., Segev, O., Bharill, S., Shapira, I., Gazit, N., O’Malley, T., Slomowitz, E., Berdichevsky, Y., Walsh, D. M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.024 · Cited by 138
“Next, we examined the importance of the Ab homologous sequence on APP, which has been suggested to directly bind Ab (Shaked et al., 2006), by replacing it with the cognate region from APLP2, the sequence of which is divergent from APP (APPAPLP2; Figure 6A).”
BackgroundInfluentialSaganich, M. J., Schroeder, B. E., Galván, V., Bredesen, D. E., Koo, E. H., & Heinemann, S. F. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4180-06.2006 · Cited by 139
Self-citationCholesterol in Alzheimers Disease: Unresolved Questions
Stefani, M., & Liguri, G. (2009) · Current Alzheimer Research · doi:10.2174/156720509787313899 · Cited by 136
Evangelisti, E., Cascella, R., Becatti, M., Marrazza, G., Dobson, C. M., Chiti, F., Stefani, M., & Cecchi, C. (2016) · Scientific Reports · doi:10.1038/srep32721 · Cited by 133
Tampellini, D., Rahman, N., Gallo, E. F., Huang, Z., Dumont, M., Capetillo-Zarate, E., Ma, T., Zheng, R., Lu, B., Nanus, D. M., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2292-09.2009 · Cited by 127
Ripoli, C., Cocco, S., Puma, D. D. L., Piacentini, R., Mastrodonato, A., Scala, F., Puzzo, D., D’Ascenzo, M., & Grassi, C. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1201-14.2014 · Cited by 131
Tampellini, D., Magrané, J., Takahashi, R. H., Li, F., Lin, M. T., Almeida, C. G., & Gouras, G. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700373200 · Cited by 118
Cecchi, C., & Stefani, M. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.06.003 · Cited by 117
Sosa, L. J., Cáceres, A., Dupraz, S., Oksdath, M., Quiroga, S., & Lorenzo, A. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14122 · Cited by 117
Gulisano, W., Melone, M., Ripoli, C., Tropea, M. R., Li Puma, D. D., Giunta, S., Cocco, S., Marcotulli, D., Origlia, N., Palmeri, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0163-19.2019 · Cited by 100
Caspase-2 is required for dendritic spine and behavioural alterations in J20 APP transgenic mice
Pozueta, J., Lefort, R., Ribé, E. M., Troy, C. M., Arancio, O., & Shelanski, M. L. (2013) · Nature Communications · doi:10.1038/ncomms2927 · Cited by 100
Eggert, S., Midthune, B., Cottrell, B. A., & Koo, E. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.038646 · Cited by 99
Self-citationNeurodegeneration in Alzheimer's disease: caspases and synaptic element interdependence
Bredesen, D. E. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-27 · Cited by 103
Self-citationAβ Internalization by Neurons and Glia
Mohamed, A., & Chaves, E. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/127984 · Cited by 94
Protein Folding and Misfolding on Surfaces
Stefani, M. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9122515 · Cited by 89
Pitt, J. E., Wilcox, K. C., Tortelli, V., Diniz, L. P., Oliveira, M. S., Dobbins, C., Yu, X., Nandamuri, S., Gomes, F. C. A., DiNunno, N., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0416 · Cited by 87
Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC
Javed, I., Zhang, Z., Adamčík, J., Andrikopoulos, N., Li, Y., Otzen, D. E., Lin, S., Mezzenga, R., Davis, T. P., Ding, F., et al. (2020) · Advanced Science · doi:10.1002/advs.202001299 · Cited by 83
Granic, A., Padmanabhan, J., Norden, M., & Potter, H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-10-0850 · Cited by 83
Pfundstein, G., Nikonenko, A. G., & Sytnyk, V. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.969547 · Cited by 89
Endogenous Aβ causes cell death via early tau hyperphosphorylation
Amadoro, G., Corsetti, V., Ciotti, M. T., Florenzano, F., Capsoni, S., Amato, G., & Calissano, P. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.06.005 · Cited by 74
Selective vulnerability in Alzheimer's disease: Amyloid precursor protein and p75NTR interaction
Fombonne, J., Rabizadeh, S., Banwait, S., Mehlen, P., & Bredesen, D. E. (2009) · Annals of Neurology · doi:10.1002/ana.21578 · Cited by 68
Self-citationAcquarone, E., Argyrousi, E. K., van den Berg, M., Gulisano, W., Fà, M., Staniszewski, A., Calcagno, E., Zuccarello, E., D'adamio, L., Deng, S.-X., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0326-4 · Cited by 71
Cecchi, C., Rosati, F., Pensalfini, A., Formigli, L., Nosi, D., Liguri, G., Dichiara, F., Morello, M., Danza, G., Pieraccini, G., et al. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00216.x · Cited by 70
Prion-like propagation of β-amyloid aggregates in the absence of APP overexpression
Ruiz‐Riquelme, A., Lau, H. H. C., Stuart, E., Goczi, A. N., Wang, Z., Schmitt‐Ulms, G., & Watts, J. C. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0529-x · Cited by 69
G Protein–Coupled Receptors, Cholinergic Dysfunction, and Aβ Toxicity in Alzheimer’s Disease
Thathiah, A., & Strooper, B. D. (2009) · Science Signaling · doi:10.1126/scisignal.293re8 · Cited by 59
Critical role of cPLA2 in Aβ oligomer-induced neurodegeneration and memory deficit
Desbène, C., Malaplate, C., Youssef, I., Garcia, P., Stenger, C., Sauvée, M., Fischer, N., Rimet, D., Koziel, V., Escanyé, M., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.008 · Cited by 64
Angulo, S. L., Orman, R., Neymotin, S. A., Liu, L., Buitrago, L., Cepeda-Prado, E., Stefanov, D. G., Lytton, W. W., Stewart, M., Small, S. A., et al. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.08.015 · Cited by 58
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
Mutant Presenilin 1 Increases the Expression and Activity of BACE1
Giliberto, L., Borghi, R., Piccini, A., Mangerini, R., Sorbi, S., Cirmena, G., Garuti, A., Ghetti, B. F., Tagliavini, F., Mughal, M. R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805685200 · Cited by 56
Synapses, synaptic activity and intraneuronal Aβ in Alzheimer’s disease
Tampellini, D. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00013 · Cited by 58
Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein
Park, S. A., Shaked, G. M., Bredesen, D. E., & Koo, E. H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.042 · Cited by 53
Self-citationTau is not necessary for amyloid-β–induced synaptic and memory impairments
Puzzo, D., Argyrousi, E. K., Staniszewski, A., Zhang, H., Calcagno, E., Zuccarello, E., Acquarone, E., Fà, M., Puma, D. D. L., Grassi, C., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci137040 · Cited by 53
Bignante, E. A., Heredia, F., Morfini, G. A., & Lorenzo, A. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.04.021 · Cited by 50
Pantelopulos, G. A., Straub, J. E., Thirumalai, D., & Sugita, Y. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.04.002 · Cited by 49
Banwait, S., Galván, V., Zhang, J., Gorostiza, O. F., Ataie, M., Huang, W., Crippen, D., Koo, E. H., & Bredesen, D. E. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13101 · Cited by 45
Self-citationSomatostatin binds to the human amyloid β peptide and favors the formation of distinct oligomers
Wang, H., Muiznieks, L. D., Ghosh, P., Williams, D., Solarski, M., Fang, A., Ruiz‐Riquelme, A., Pomès, R., Watts, J. C., Chakrabartty, A., et al. (2017) · eLife · doi:10.7554/elife.28401 · Cited by 46
Lipid rafts are primary mediators of amyloid oxidative attack on plasma membrane
Zampagni, M., Evangelisti, E., Cascella, R., Liguri, G., Becatti, M., Pensalfini, A., Uberti, D. L., Cenini, G., Memo, M., Bagnoli, S., et al. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0603-8 · Cited by 44
Galván, V., Zhang, J., Gorostiza, O. F., Banwait, S., Huang, W., Ataie, M., Tang, H., & Bredesen, D. E. (2008) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.03.035 · Cited by 43
Self-citationExamination of potential mechanisms of amyloid-induced defects in neuronal transport
Shah, S. B., Nolan, R. L., Davis, E., Stokin, G. B., Niesman, I. R., Canto, I., Glabe, C. G., & Goldstein, L. S. B. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.016 · Cited by 45
Membrane cholesterol enrichment prevents Aβ-induced oxidative stress in Alzheimer's fibroblasts
Pensalfini, A., Zampagni, M., Liguri, G., Becatti, M., Evangelisti, E., Fiorillo, C., Bagnoli, S., Cellini, E., Nacmias, B., Sorbi, S., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.010 · Cited by 43
Amyloid-β precursor protein mediates neuronal toxicity of amyloid β through Go protein activation
Vigo, F. S., Kedikian, G., Heredia, L., Heredia, F., Añel, A. D., Rosa, A. L., & Lorenzo, A. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.11.017 · Cited by 42
Liu, J., Wang, Y., Jing, G., Sun, J., & Qinfeng, S. (2020) · Aging · doi:10.18632/aging.103306 · Cited by 42
Granic, A., & Potter, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060718 · Cited by 40
Spilman, P. R., Corset, V., Gorostiza, O., Poksay, K. S., Galvan, V., Zhang, J., Rao, R., Peters-Libeu, C., Vincelette, J., McGeehan, A., et al. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-151046 · Cited by 39
Self-citationCholesterol and Lipid Rafts in the Biogenesis of Amyloid-β Protein and Alzheimer's Disease
Pantelopulos, G. A., Abraham, C. B., & Straub, J. E. (2024) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-062823-023436 · Cited by 43
Conjugated polythiophene probes target lysosome-related acidic vacuoles in cultured primary cells
Björk, P., Nilsson, K. P. R., Lenner, L., Kågedal, B., Persson, B., Inganäs, O., & Jonasson, J. (2007) · Molecular and Cellular Probes · doi:10.1016/j.mcp.2007.04.005 · Cited by 40
Lefort, R., Pozueta, J., & Shelanski, M. L. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6473-11.2012 · Cited by 41
Tropea, M. R., Puma, D. D. L., Melone, M., Gulisano, W., Arancio, O., Grassi, C., Conti, F., & Puzzo, D. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102154 · Cited by 42
Rolland, M., Powell, R., Jacquier‐Sarlin, M. R., Boisseau, S., Reynaud-Dulaurier, R., Hernández, J. M., André, L., Borel, E., Buisson, A., & Lanté, F. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2501-19.2020 · Cited by 41
The brain on time: links between development and neurodegeneration
Shabani, K., & Hassan, B. A. (2023) · Development · doi:10.1242/dev.200397 · Cited by 39
Dysfunction of amyloid precursor protein signaling in neurons leads to DNA synthesis and apoptosis
Neve, R. L., & McPhie, D. L. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.008 · Cited by 33
Decock, M., Haylani, L. E., Stanga, S., Dewachter, I., Octave, J., Smith, S. O., Constantinescu, S. N., & Kienlen‐Campard, P. (2015) · FEBS Open Bio · doi:10.1016/j.fob.2015.09.002 · Cited by 30
Willén, K. I., Sroka-Oleksiak, A., Takahashi, R. H., & Gouras, G. K. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170262 · Cited by 28
BACE: Lead Target for Orchestrated Therapy of Alzheimer's Disease
John, V. (2010) · doi:10.1002/9780470594087 · Cited by 27
Paradoxical Effect of TrkA Inhibition in Alzheimer's Disease Models
Zhang, Q., Descamps, O., Hart, M. J., Poksay, K. S., Spilman, P. R., Kane, D. J., Gorostiza, O. F., John, V., & Bredesen, D. E. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-130017 · Cited by 26
Self-citationShaked, G. M., Chauv, S., Ubhi, K. K., Hansen, L. A., & Masliah, E. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06997.x · Cited by 25
Self-citationOropesa‐Nuñez, R., Seghezza, S., Dante, S., Diaspro, A., Cascella, R., Cecchi, C., Stefani, M., Chiti, F., & Canale, C. (2016) · Oncotarget · doi:10.18632/oncotarget.10449 · Cited by 25
Association of TrkA and APP Is Promoted by NGF and Reduced by Cell Death-Promoting Agents
Canu, N., Pagano, I., Rosa, L. R. L., Pellegrino, M., Ciotti, M. T., Mercanti, D., Moretti, F., Sposato, V., Triaca, V., Petrella, C., et al. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00015 · Cited by 24
Matrone, C., Iannuzzi, F., & Annunziato, L. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.04.003 · Cited by 24
Cecchi, C., Pensalfini, A., Stefani, M., Baglioni, S., Fiorillo, C., Cappadona, S., Caporale, R., Nosi, D., Ruggiero, M., & Liguri, G. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0265-3 · Cited by 24
Wild-Type Neural Progenitors Divide and Differentiate Normally in an Amyloid-Rich Environment
Yetman, M. J., & Jankowsky, J. L. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1917-13.2013 · Cited by 24
Xl, C., & Mk, L. (2014) · PubMed · Cited by 23
Antonino, M., Marmo, P., Freites, C. L., Quassollo, G., Sánchez, M. F., Lorenzo, A., & Bignante, E. A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.852738 · Cited by 24
Zhang, J., Gorostiza, O. F., Tang, H., Bredesen, D. E., & Galván, V. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.09.013 · Cited by 22
Self-citationAmyloid precursor protein mediates monocyte adhesion in AD tissue and apoE−/− mice
Austin, S. A., & Combs, C. K. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.10.013 · Cited by 21
Interaction of ASK1 and the β-amyloid precursor protein in a stress-signaling complex
Galván, V., Banwait, S., Spilman, P. R., Gorostiza, O. F., Peel, A. L., Ataie, M., Crippen, D., Huang, W., Sidhu, G., Ichijo, H., et al. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.06.017 · Cited by 20
Self-citationThe Development of an in vivo γ-Secretase Assay using Zebrafish Embryos
Wilson, L., & Lardelli, M. T. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130332 · Cited by 18
Bignante, E. A., Ponce, N. E., Heredia, F., Musso, J., Krawczyk, M. C., Millan, J., Pigino, G. F., Inestrosa, N. C., Boccia, M. M., & Lorenzo, A. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.12.013 · Cited by 17
Kedikian, G., Heredia, F., Rozés‐Salvador, V., Raimunda, D., Isoardi, N. A., Heredia, L., & Lorenzo, A. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22347 · Cited by 17
Yoo, J.-Y., Kim, H.-B., Baik, T., Lee, J., & Woo, R. (2021) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2021.104622 · Cited by 17
Facchinetti, P., Dorard, E., Contremoulins, V., Gaillard, M., Déglon, N., Sazdovitch, V., Guihenneuc‐Jouyaux, C., Brouillet, E., Duyckaerts, C. J., & Allinquant, B. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.08.039 · Cited by 15
Libeu, C. P., Descamps, O., Zhang, Q., John, V., & Bredesen, D. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040027 · Cited by 15
Self-citationPark, S. S., Jung, H., Kim, Y., Park, T. K., Kim, C., Choi, H., Mook‐Jung, I. H., Koo, E. H., & Park, S. A. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12032 · Cited by 14
Self-citationTrillaud-Doppia, É., Paradis-Isler, N., & Boehm, J. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.02.016 · Cited by 13
The β amyloid peptide can act as a modular aggregation domain
Link, C. D., Fonte, V. G., Roberts, C. M., Hiester, B. G., Silverman, M. A., & Stein, G. H. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.08.003 · Cited by 13
Yamamoto, K., Yamamoto, R., & Kato, N. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.660319 · Cited by 13
Role of Drosophila Amyloid Precursor Protein in Memory Formation
Préat, T., & Goguel, V. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00142 · Cited by 13
Wang, S. S. ‐., & Liu, K.-N. (2008) · Journal of The Chinese Institute of Chemical Engineers · doi:10.1016/j.jcice.2008.03.001 · Cited by 13
LRP4-related signalling pathways and their regulatory role in neurological diseases
Chen, B., Lin, Z.-Y., Zeng, X.-X., Jiang, Y., & Geng, F. (2023) · Brain Research · doi:10.1016/j.brainres.2023.148705 · Cited by 12
Bourdet, I., Lampin-Saint-Amaux, A., Préat, T., & Goguel, V. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135741 · Cited by 13
Briand, S., Facchinetti, P., Clamagirand, C., Madeira, A., Pommet, J., Pimplikar, S. W., & Allinquant, B. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.021 · Cited by 12
Regulation of neuronal toxicity of β-amyloid oligomers by surface ATP synthase
Xing, S., Shen, D., Chen, C., WANG, J., Liu, T., & Yu, Z. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1722 · Cited by 11
Mechanisms of Microglial Activation by Amyloid Precursor Protein and its Proteolytic Fragments
Austin, S. A., & Combs, C. K. (2007) · Springer eBooks · doi:10.1007/978-0-387-73894-9_2 · Cited by 10
Re-Arranging the Puzzle between the Amyloid-Beta and Tau Pathology: An APP-Centric Approach
Haut, F., Argyrousi, E. K., & Arancio, O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010259 · Cited by 11
Kumasaka, D. K., Galván, V., Head, E., & Rohn, T. T. (2009) · PubMed Central · Cited by 9
Metadata
- Authors
- Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., Bredesen, D. E., Koo, E. H., Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., Bredesen, D. E., & Koo, E. H.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2006-04-24
- Volume
- 20
- Issue
- 8
- Pages
- 1254-1256
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- PMC
- PMC1847355
- OpenAlex
- W2108938583
- Cited by
- 132
- References
- 44
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 7 · 2023: 4 · 2022: 2 · 2021: 5 · 2020: 5 · 2019: 5 · 2018: 3 · 2017: 12 · 2016: 7 · 2015: 3 · 2014: 5 · 2013: 9 · 2012: 6
- FWCI
- 9.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (AG05131)
- Alzheimer's Association
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, Alzheimer's disease, APP, APP C-terminal fragments, caspase-like proteases, cell death
- MeSH terms
- Amino Acid Sequence, Animals, Membrane Proteins, Molecular Sequence Data, Peptide Fragments, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Cell Death, Protein Structure, Tertiary, Amino Acid Motifs, Cell Line, Tumor, Mice, 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
