Autophagy, amyloidogenesis and Alzheimer disease
Abstract
Autophagy is the sole pathway for organelle turnover in cells and is a vital pathway for degrading normal and aggregated proteins, particularly under stress or injury conditions. Recent evidence has shown that the amyloid beta peptide is generated from amyloid beta precursor protein (APP) during autophagic turnover of APP-rich organelles supplied by both autophagy and endocytosis. Abeta generated during normal autophagy is subsequently degraded by lysosomes. Within neurons, autophagosomes and endosomes actively form in synapses and along neuritic processes but efficient clearance of these compartments requires their retrograde transport towards the neuronal cell body, where lysosomes are most concentrated. In Alzheimer disease, the maturation of autophagolysosomes and their retrograde transport are impeded, which leads to a massive accumulation of ;autophagy intermediates' (autophagic vacuoles) within large swellings along dystrophic and degenerating neurites. The combination of increased autophagy induction and defective clearance of Abeta-generating autophagic vacuoles creates conditions favorable for Abeta accumulation in Alzheimer disease.
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Insufficient degradation of protein aggregates and chronic inflammation are driving forces of AD and PD brain pathology.
“Growing evidence indicates that insufficient degradation of protein aggregates and chronic inflammation are driving forces of AD and PD brain pathology [30–32].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [31]
Chronic disturbance of the autophagic/endosome-lysosome system is thought to contribute to protein accumulation and neurodegeneration.
“Consistent with this, the autophagic system and endosome/lysosome pathways are compromised in AD brains, and chronic disturbance of this system is thought to contribute to protein accumulation and neurodegeneration [85–87].”
The autophagic system and endosome/lysosome pathways are compromised in AD brains.
“Consistent with this, the autophagic system and endosome/lysosome pathways are compromised in AD brains, and chronic disturbance of this system is thought to contribute to protein accumulation and neurodegeneration [85–87].”
Cites
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · cited 4× · see citing works
“A transmembrane aspartyl protease that has optimal activity at low pH distributes predominantly to endosomes (Vassar et al., 1999; Capell et al., 2000; Walter et al., 2001), where CTF has been shown to be generated (Grbovic, 2003; Mathews et al., 2002), although additional BACE is found in the TGN…”
BackgroundInfluentialCandidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577 · see citing works
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · cited 1× · see citing works
“Notably APP and synuclein, a protein implicated in Parkinson disease, contain this targeting sequence (Massey et al., 2004), and impaired CMA-mediated degradation contributes to accumulation of mutant -synuclein in the disease (Cuervo et al., 2004).”
BackgroundIntracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942 · see citing works
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 · see citing works
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268 · see citing works
Molecular dissection of autophagy: two ubiquitin-like systems
Ohsumi, Y. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056522 · Cited by 1,240 · cited 1× · see citing works
“This process has been reviewed in detail (Shintani and Klionsky, 2004; Levine and Klionsky, 2004; Seglen and Bohley, 1992; Dunn, 1994; Ohsumi, 2001; Mizushima et al., 2002).”
MethodIntraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991 · see citing works
Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain
Takahashi, R. H., Almeida, C. G., Kearney, P. F., Yu, F., Lin, M. T., Milner, T. A., & Gouras, G. K. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5167-03.2004 · Cited by 445 · see citing works
Cataldo, A. M., Barnett, J. L., Pieroni, C., & Nixon, R. A. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-16-06142.1997 · Cited by 393 · see citing works
Self-citationIsolation and Characterization of Rat Liver Amphisomes
Berg, T. O., Fengsrud, M., Strømhaug, P. E., Berg, T., & Seglen, P. O. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21883 · Cited by 385 · see citing works
Cataldo, A. M., Barnett, J. L., Berman, S. A., Li, J., Quarless, S., Bursztajn, S., Lippa, C., & Nixon, R. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90324-0 · Cited by 379 · see citing works
Self-citationAlmeida, C. G., Takahashi, R. H., & Gouras, G. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5078-05.2006 · Cited by 316 · see citing works
Physiological roles for amyloid β peptides
Pearson, H. A., & Peers, C. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.111203 · Cited by 286 · see citing works
Prelysosomal convergence of autophagic and endocytic pathways
Gordon, P. B., & Seglen, P. O. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(88)90556-6 · Cited by 281 · cited 1× · see citing works
“Digestion of sequestered material within autophagosomes is initiated when lysosomes fuse with the outer membrane of the autophagosome, although, as discussed earlier, late endosomes can also fuse with autophagosomes (Gordon and Seglen, 1988; Liou et al., 1997).”
BackgroundYu, W. H., Kumar, A., Peterhoff, C., Shapiro Kulnane, L., Uchiyama, Y., Lamb, B. T., Cuervo, A. M., & Nixon, R. A. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.05.010 · Cited by 279 · see citing works
Self-citationKanazawa, T., Taneike, I., Akaishi, R., Yoshizawa, F., Furuya, N., Fujimura, S., & Kadowaki, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306337200 · Cited by 208 · see citing works
Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia
Suzuki, K., & Terry, R. D. (1967) · Acta Neuropathologica · doi:10.1007/bf00688828 · Cited by 169 · see citing works
Flagged first, then by citations
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Sorted by citations
Dong, X.-X., Wang, Y., & Qin, Z.-H. (2009) · Acta Pharmacologica Sinica · doi:10.1038/aps.2009.24 · Cited by 1,297 · see citing works
Trafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works
Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044 · see citing works
Spilman, P., Podlutskaya, N., Hart, M. J., Debnath, J., Gorostiza, O., Bredesen, D., Richardson, A., Strong, R., & Galvan, V. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009979 · Cited by 1,033 · see citing works
Lee, J.-H., Yang, D.-S., Goulbourne, C. N., Im, E., Stavrides, P., Pensalfini, A., Chan, H., Bouchet-Marquis, C., Bleiwas, C., Berg, M. J., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01084-8 · Cited by 638 · see citing works
Self-citationMechanisms of Aβ Clearance and Degradation by Glial Cells
Ries, M., & Sastre, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00160 · Cited by 527 · see citing works
“It was hypothesized that a defective clearance of Aβ-generating autophagic vacuoles creates conditions favorable for Aβ accumulation in AD and this is supported by data indicating that increasing autophagy by rapamycin reduces amyloid burden in vivo (Nixon, 2007).”
BackgroundAβ Secretion and Plaque Formation Depend on Autophagy
Nilsson, P., Loganathan, K., Sekiguchi, M., Matsuba, Y., Hui, K., Tsubuki, S., Tanaka, M., Iwata, N., Saito, T., & Saido, T. C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.042 · Cited by 459 · see citing works
Lee, C. Y. D., Daggett, A., Gu, X., Jiang, L.-L., Langfelder, P., Li, X., Wang, N., Zhao, Y., Park, C. S., Cooper, Y., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.02.002 · Cited by 396 · see citing works
Gowrishankar, S., Yuan, P., Wu, Y., Schrag, M., Paradise, S., Grutzendler, J., De Camilli, P., & Ferguson, S. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510329112 · Cited by 406 · see citing works
Yang, D.-S., Stavrides, P., Mohan, P. S., Kaushik, S., Kumar, A., Ohno, M., Schmidt, S. D., Wesson, D., Bandyopadhyay, U., Jiang, Y., et al. (2011) · Brain · doi:10.1093/brain/awq341 · Cited by 429 · see citing works
Self-citationNixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400 · see citing works
Self-citationLee, J.-H., McBrayer, M. K., Wolfe, D. M., Haslett, L. J., Kumar, A., Sato, Y., Lie, P. P. Y., Mohan, P., Coffey, E. E., Kompella, U., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.050 · Cited by 358 · see citing works
Self-citationIntraneuronal 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 · see citing works
Autophagy and the ubiquitin-proteasome system: Collaborators in neuroprotection
Nedelsky, N. B., Todd, P. K., & Taylor, J. P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.002 · Cited by 351 · see citing works
Bordi, M., Berg, M. J., Mohan, P. S., Peterhoff, C. M., Alldred, M. J., Che, S., Ginsberg, S. D., & Nixon, R. A. (2016) · Autophagy · doi:10.1080/15548627.2016.1239003 · Cited by 353 · see citing works
Self-citationHuman Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes
Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0983-17.2017 · Cited by 339 · see citing works
Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306 · see citing works
Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity
Friedrich, R. P., Tepper, K., Rönicke, R., Soom, M., Westermann, M., Reymann, K., Kaether, C., & Fändrich, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904532106 · Cited by 303 · see citing works
Role of tau protein in Alzheimer’s disease: The prime pathological player
Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278 · see citing works
Immunotherapy Targeting Pathological Tau Prevents Cognitive Decline in a New Tangle Mouse Model
Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4363-10.2010 · Cited by 272 · see citing works
Tsvetkov, A. S., Miller, J., Arrasate, M., Wong, J. S., Pleiss, M. A., & Finkbeiner, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004498107 · Cited by 266 · see citing works
Alzheimer's disease and type 2 diabetes: a critical assessment of the shared pathological traits
Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270 · see citing works
Piras, A., Collin, L., Grüninger, F., Graff, C., & Rönnbäck, A. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0292-9 · Cited by 271 · see citing works
Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease
Overk, C. R., & Masliah, E. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.015 · Cited by 242 · see citing works
Kandalepas, P. C., Sadleir, K. R., Eimer, W. A., Zhao, J., Nicholson, D. A., & Vassar, R. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1152-3 · Cited by 240 · see citing works
Amyloidosis in Alzheimer’s Disease: Pathogeny, Etiology, and Related Therapeutic Directions
Ma, C., Hong, F., & Yang, S. (2022) · Molecules · doi:10.3390/molecules27041210 · Cited by 243 · see citing works
Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
Rothenberg, C., Srinivasan, D., Mah, L., Kaushik, S., Peterhoff, C. M., Ugolino, J., Fang, S., Cuervo, A. M., Nixon, R. A., & Monteiro, M. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq231 · Cited by 225 · see citing works
Self-citationRostami, J., Mothes, T., Kolahdouzan, M., Eriksson, O., Moslem, M., Bergström, J., Ingelsson, M., O’Callaghan, P., Healy, L. M., Falk, A., et al. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02158-3 · Cited by 224 · see citing works
Sanchez-Varo, R., Trujillo-Estrada, L., Sanchez-Mejias, E., Torres, M., Baglietto-Vargas, D., Moreno-Gonzalez, I., De Castro, V., Jimenez, S., Ruano, D., Vizuete, M., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0896-x · Cited by 222 · see citing works
Morel, E., Chamoun, Z., Lasiecka, Z. M., Chan, R. B., Williamson, R. L., Vetanovetz, C., Dall’Armi, C., Simoes, S., Point Du Jour, K. S., McCabe, B. D., et al. (2013) · Nature Communications · doi:10.1038/ncomms3250 · Cited by 222 · see citing works
Bartlett, B. J., Isakson, P., Lewerenz, J., Sanchez, H., Kotzebue, R. W., Cumming, R. C., Harris, G. L., Nezis, I. P., Schubert, D. R., Simonsen, A., et al. (2011) · Autophagy · doi:10.4161/auto.7.6.14943 · Cited by 215 · see citing works
Disrupted autophagy after spinal cord injury is associated with ER stress and neuronal cell death
Liu, S., Sarkar, C., Dinizo, M., Faden, A. I., Koh, E. Y., Lipinski, M. M., & Wu, J. (2015) · Cell Death & Disease · doi:10.1038/cddis.2014.527 · Cited by 209 · see citing works
Increased Accumulation of Intraneuronal Amyloid β in HIV-Infected Patients
HNRC, Achim, C. L., Adame, A., Dumaop, W., Everall, I. P., & Masliah, E. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9152-8 · Cited by 205 · see citing works
The Autophagy Lysosomal Pathway and Neurodegeneration
Finkbeiner, S. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033993 · Cited by 196 · see citing works
A Self-Destructive Nanosweeper That Captures and Clears Amyloid β-Peptides
Luo, Q., Lin, Y.-X., Yang, P.-P., Wang, Y., Qi, G.-B., Qiao, Z.-Y., Li, B.-N., Zhang, K., Zhang, J.-P., Wang, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04255-z · Cited by 191 · see citing works
Tai, L. M., Bilousova, T., Jungbauer, L., Roeske, S. K., Youmans, K. L., Yu, C., Poon, W. W., Cornwell, L. B., Miller, C. A., Vinters, H. V., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442103 · Cited by 165 · see citing works
Neuropathological role of PI3K/Akt/mTOR axis in Down syndrome brain
Perluigi, M., Pupo, G., Tramutola, A., Cini, C., Coccia, R., Barone, E., Head, E., Butterfield, D. A., & Di Domenico, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.04.007 · Cited by 155 · see citing works
Cell “Self‐Eating” (Autophagy) Mechanism in Alzheimer's Disease
Funderburk, S. F., Marcellino, B. K., & Yue, Z. (2010) · Mount Sinai Journal of Medicine: A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20161 · Cited by 139 · see citing works
Implication of the Immune System in Alzheimer's Disease: Evidence from Genome-Wide Pathway Analysis
Lambert, J.-C., Grenier-Boley, B., Chouraki, V., Heath, S., Zelenika, D., Fievet, N., Hannequin, D., Pasquier, F., Hanon, O., Brice, A., et al. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100018 · Cited by 144 · see citing works
Annunziata, I., Patterson, A., Helton, D., Hu, H., Moshiach, S., Gomero, E., Nixon, R., & d’Azzo, A. (2013) · Nature Communications · doi:10.1038/ncomms3734 · Cited by 146 · see citing works
Self-citationChandra, S., Jana, M., & Pahan, K. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.0054-18.2018 · Cited by 134 · see citing works
Silva, D. F., Selfridge, J. E., Lu, J., E, L., Roy, N., Hutfles, L., Burns, J. M., Michaelis, E. K., Yan, S., Cardoso, S. M., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt247 · Cited by 133 · see citing works
Noncanonical function of an autophagy protein prevents spontaneous Alzheimer’s disease
Heckmann, B. L., Teubner, B. J. W., Boada-Romero, E., Tummers, B., Guy, C., Fitzgerald, P., Mayer, U., Carding, S., Zakharenko, S. S., Wileman, T., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb9036 · Cited by 114 · see citing works
Ultrastructural evidence of microglial heterogeneity in Alzheimer’s disease amyloid pathology
El Hajj, H., Savage, J. C., Bisht, K., Parent, M., Vallières, L., Rivest, S., & Tremblay, M.-È. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1473-9 · Cited by 119 · see citing works
Nogalska, A., D'Agostino, C., Terracciano, C., Engel, W. K., & Askanas, V. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.100050 · Cited by 114 · see citing works
Di Domenico, F., Barone, E., Perluigi, M., & Butterfield, D. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6759 · Cited by 114 · see citing works
Western, D., Timsina, J., Wang, L., Wang, C., Yang, C., Phillips, B., Wang, Y., Liu, M., Ali, M., Beric, A., et al. (2024) · Nature Genetics · doi:10.1038/s41588-024-01972-8 · Cited by 111 · see citing works
Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., & Iijima, K. M. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005917 · Cited by 105 · see citing works
Sequential formation of different layers of dystrophic neurites in Alzheimer’s brains
Sharoar, M. G., Hu, X., Ma, X.-M., Zhu, X., & Yan, R. (2019) · Molecular Psychiatry · doi:10.1038/s41380-019-0396-2 · Cited by 87 · see citing works
Amyloid‐β impairs the phagocytosis of dystrophic synapses by astrocytes in Alzheimer's disease
Sanchez‐Mico, M. V., Jimenez, S., Gomez‐Arboledas, A., Muñoz‐Castro, C., Romero‐Molina, C., Navarro, V., Sanchez‐Mejias, E., Nuñez‐Diaz, C., Sanchez‐Varo, R., Galea, E., et al. (2021) · Glia · doi:10.1002/glia.23943 · Cited by 93 · see citing works
Di Domenico, F., Tramutola, A., Foppoli, C., Head, E., Perluigi, M., & Butterfield, D. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.009 · Cited by 89 · see citing works
Cholinotrophic basal forebrain system alterations in 3xTg-AD transgenic mice
Perez, S. E., He, B., Muhammad, N., Oh, K.-J., Fahnestock, M., Ikonomovic, M. D., & Mufson, E. J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.10.002 · Cited by 80 · see citing works
Im, E., Jiang, Y., Stavrides, P. H., Darji, S., Erdjument-Bromage, H., Neubert, T. A., Choi, J. Y., Wegiel, J., Lee, J.-H., & Nixon, R. A. (2023) · Science Advances · doi:10.1126/sciadv.adg1925 · Cited by 80 · see citing works
Self-citationSharoar, M. G., Palko, S., Ge, Y., Saido, T. C., & Yan, R. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00464-1 · Cited by 78 · see citing works
Chong, C.-M., Ke, M., Tan, Y., Huang, Z., Zhang, K., Ai, N., Ge, W., Qin, D., Lu, J.-H., & Su, H. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0945-7 · Cited by 66 · see citing works
Decourt, B., D’Souza, G. X., Shi, J., Ritter, A., Suazo, J., & Sabbagh, M. N. (2022) · Aging and disease · doi:10.14336/ad.2021.0529 · Cited by 69 · see citing works
Activation of PPARα enhances astroglial uptake and degradation of β-amyloid
Raha, S., Ghosh, A., Dutta, D., Patel, D. R., & Pahan, K. (2021) · Science Signaling · doi:10.1126/scisignal.abg4747 · Cited by 63 · see citing works
Pharmacological modulation of autophagy for Alzheimer's disease therapy: Opportunities and obstacles
Deng, Z., Dong, Y., Zhou, X., Lu, J.-H., & Yue, Z. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.009 · Cited by 58 · see citing works
Aducanumab anti-amyloid immunotherapy induces sustained microglial and immune alterations
Cadiz, M. P., Gibson, K. A., Todd, K. T., Nascari, D. G., Massa, N., Lilley, M. T., Olney, K. C., Al-Amin, M. M., Jiang, H., Holtzman, D. M., et al. (2024) · Journal of Experimental Medicine · doi:10.1084/jem.20231363 · Cited by 55 · see citing works
The contribution of altered neuronal autophagy to neurodegeneration
Filippone, A., Esposito, E., Mannino, D., Lyssenko, N., & Praticò, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108178 · Cited by 55 · see citing works
- Authors
- Nixon, R. A.
- Affiliations
- Nathan Kline Institute for Psychiatric Research (US)
- Corresponding author
- Nixon, Ralph A.
- ORCID
- Nixon, Ralph A.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2007-12-01
- Volume
- 120
- Issue
- 23
- Pages
- 4081-4091
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2097631517
- Cited by
- 749
- References
- 18
- Citations by year
- 2026: 13 · 2025: 29 · 2024: 39 · 2023: 39 · 2022: 36 · 2021: 46 · 2020: 45 · 2019: 60 · 2018: 45 · 2017: 34 · 2016: 48 · 2015: 46 · 2014: 39 · 2013: 40 · 2012: 54
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- autophagy, amyloid-beta, amyloid precursor protein, Alzheimer's disease, autophagolysosomes, retrograde transport, autophagosomes, lysosomal degradation, endocytosis, neurite degeneration, protein aggregation
- MeSH terms
- Alzheimer Disease, Animals, Autophagy, Disease Models, Animal, Endocytosis, Humans, Lysosomes, Models, Biological, Neurons, Amyloid beta-Peptides, Amyloid beta-Protein Precursor
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 ›
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