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β-Amyloid Accumulation Impairs Multivesicular Body Sorting by Inhibiting the Ubiquitin-Proteasome System
Open accessAbstract
Increasing evidence links intraneuronal β-amyloid (Aβ 42 ) accumulation with the pathogenesis of Alzheimer’s disease (AD). In Aβ precursor protein (APP) mutant transgenic mice and in human AD brain, progressive intraneuronal accumulation of Aβ 42 occurs especially in multivesicular bodies (MVBs). We hypothesized that this impairs the MVB sorting pathway. We used the trafficking of the epidermal growth factor receptor (EGFR) and TrkB receptor to investigate the MVB sorting pathway in cultured neurons. We report that, during EGF stimulation, APP mutant neurons demonstrated impaired inactivation, degradation, and ubiquitination of EGFR. EGFR degradation is dependent on translocation from MVB outer to inner membranes, which is regulated by the ubiquitin-proteasome system (UPS). We provide evidence that Aβ accumulation in APP mutant neurons inhibits the activities of the proteasome and deubiquitinating enzymes. These data suggest a mechanism whereby Aβ accumulation in neurons impairs the MVB sorting pathway via the UPS in AD.
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“In this model, Ab accumulates along the endosomal/lysomal pathway that leads to dysfunction of multivesicular bodies, causing impairment of the ubiquitin-proteasome system, 9 which also controls the fate of NMDARs undergoing endocytic vesicular trafficking.50”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [9]
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“These cultures are characterized by progressive buildup of intraneuronal Ab, which is derived from endogenous Ab escaping exocytosis after cleavage of the APP SW mutant.9,49”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [9]
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“A number of studies have associated intraneuronal Ab buildup with hyperphosphorylation of tau protein, 8 disturbed protein trafficking and sorting, 9 reduced expression of synaptic proteins, 10 and mitochondrial dysfunction.11,12”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [9]
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“In one study, Aβ-induced abnormalities in MVB endocytic sorting were demonstrated in APP mutant neurons, which appeared to be due to impairment of the ubiquitin proteasome system (UPS; [2]).”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [2]
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“The study went on to provide evidence that abnormalities in MVB sorting were due to Aβ-dependent alterations in the ubiquitin-proteasome system (UPS).”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [2]
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“Using the well established endocytosis of the epidermal growth factor receptor (EGFR), this study demonstrated that specifically the MVB sorting pathway, and not internalization or the recycling pathway, was altered in Aβ accumulating neurons.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [2]
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Cites
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
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
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
Self-citationMukherjee, S., Ghosh, R. K., & Maxfield, F. R. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.3.759 · Cited by 1,299
Receptor downregulation and multivesicular-body sorting
Katzmann, D. J., Odorizzi, G., & Emr, S. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm973 · Cited by 1,201
Intraneuronal 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
Self-citationActivity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
Ehlers, M. D. (2003) · Nature Neuroscience · doi:10.1038/nn1013 · Cited by 977
The Rab5 effector EEA1 is a core component of endosome docking
Christoforidis, S., McBride, H. M., Burgoyne, R. D., & Zerial, M. (1999) · Nature · doi:10.1038/17618 · Cited by 854
Impaired Proteasome Function in Alzheimer's Disease
Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848
Evidence that production and release of amyloid beta-protein involves the endocytic pathway
Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 829
Research works printed but not linked: 1
- (2005), Methods Mol Biol, 301, 207
Cited by
Sorted by citations
Intracellular 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
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000
Biogenesis and Function of Multivesicular Bodies
Piper, R. C., & Katzmann, D. J. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123319 · Cited by 771
Autophagy, amyloidogenesis and Alzheimer disease
Nixon, R. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.019265 · Cited by 749
He, Z., Guo, J. L., McBride, J. D., Narasimhan, S., Kim, H., Changolkar, L., Zhang, B., Gathagan, R. J., Yue, C., Dengler, C., et al. (2018) · Nature Medicine · doi:10.1038/nm.4443 · Cited by 645
Amyloid oligomers: formation and toxicity of Aβ oligomers
Sakono, M., & Zako, T. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07568.x · Cited by 628
Lee, W., Loo, C., Bebawy, M., Luk, F., Mason, R. S., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 549
The Role of NMDA Receptors in Alzheimer’s Disease
Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535
Biogenesis and function of ESCRT-dependent extracellular vesicles
Juan, T., & Fürthauer, M. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.08.022 · Cited by 479
Eimer, W. A., & Vassar, R. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-2 · Cited by 425
“Intraneuronal Aβ42 localization to endosomes and lysosomes is also supported by previous studies that have proposed a mechanism in which the ubiquitin-proteasome system is disrupted, causing impaired protein degradation and increased Aβ accumulation [39,40].”
BackgroundGong, B., Cao, Z., Zheng, P., Vitolo, O. V., Liu, S., Staniszewski, A., Moolman, D. L., Zhang, H., Shelanski, M. L., & Arancio, O. (2006) · Cell · doi:10.1016/j.cell.2006.06.046 · Cited by 425
Molecular Mechanisms of Amyloid Oligomers Toxicity
Kayed, R., & Lasagna‐Reeves, C. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129001 · Cited by 438
Aβ inhibits the proteasome and enhances amyloid and tau accumulation
Tseng, B. P., Green, K. N., Chan, J. L., Blurton-Jones, M., & LaFerla, F. M. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.014 · Cited by 384
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
Self-citationPlaque formation and the intraneuronal accumulation of β‐amyloid in Alzheimer's disease
Takahashi, R. H., Nagao, T., & Gouras, G. K. (2017) · Pathology International · doi:10.1111/pin.12520 · Cited by 354
Self-citationDantuma, N. P., & Bott, L. C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00070 · Cited by 354
Exercise Plays a Preventive Role Against Alzheimer's Disease
Radak, Z. O., Hart, N., Sarga, L., Koltai, E., Atalay, M., Ohno, H., & Boldogh, I. R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091531 · Cited by 331
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
Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 316
Sannerud, R., Esselens, C., Ejsmont, P., Mattera, R., Rochin, L., Tharkeshwar, A. K., De Baets, G., De Wever, V., Habets, R., Baert, V., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.020 · Cited by 299
Deconstruction for Reconstruction: The Role of Proteolysis in Neural Plasticity and Disease
Bingol, B., & Sheng, M. (2011) · Neuron · doi:10.1016/j.neuron.2010.11.006 · Cited by 275
Umeda, T., Tomiyama, T., Sakama, N., Tanaka, S., Lambert, M. P., Klein, W. L., & Mori, H. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22640 · Cited by 270
The ubiquitin‐proteasome system in Alzheimer's disease
Oddo, S. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00276.x · Cited by 267
Exosomal transfer of proteins and RNAs at synapses in the nervous system
Smalheiser, N. R. (2007) · Biology Direct · doi:10.1186/1745-6150-2-35 · Cited by 256
Kurup, P. K., Zhang, Y., Xu, J., Venkitaramani, D. V., Haroutunian, V. H., Greengard, P., Nairn, A. C., & Lombroso, P. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0157-10.2010 · Cited by 228
Mysterious oligomerization of the amyloidogenic proteins
Uversky, V. N. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07721.x · Cited by 219
Dual roles for autophagy: Degradation and secretion of Alzheimer's disease Aβ peptide
Nilsson, P., & Saido, T. C. (2014) · BioEssays · doi:10.1002/bies.201400002 · Cited by 206
β-Amyloid impairs axonal BDNF retrograde trafficking
Poon, W. W., Blurton-Jones, M. M., Tu, C. H., Feinberg, L. M., Chabrier, M. A., Harris, J. W., Jeon, N. L., & Cotman, C. W. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.012 · Cited by 203
Multivesicular bodies in neurons: Distribution, protein content, and trafficking functions
von Bartheld, C. S., & Altick, A. L. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.01.003 · Cited by 207
Epidermal growth factor receptor is a preferred target for treating Amyloid-β–induced memory loss
Wang, L., Chiang, H.-C., Wu, W., Liang, B., Xie, Z., Yao, X., Ma, W., Du, S., & Zhong, Y. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208011109 · Cited by 190
Membrane Trafficking Pathways in Alzheimer's Disease
Rajendran, L., & Annaert, W. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01332.x · Cited by 171
Role of the ubiquitin proteasome system in Alzheimer's disease
Upadhya, S. C., & Hegde, A. N. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-s1-s12 · Cited by 187
Effects of in vivo conditions on amyloid aggregation
Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 180
Khandelwal, P. J., Herman, A. M., Hoe, H., Rebeck, G. W., & Moussa, C. E. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr091 · Cited by 185
Peptidyl-prolyl cis–trans isomerase Pin1 in ageing, cancer and Alzheimer disease
Lee, T. H., Pastorino, L., & Lu, K. P. (2011) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411001906 · Cited by 184
Reactive glia show increased immunoproteasome activity in Alzheimer’s disease
Orre, M., Kamphuis, W., Dooves, S., Kooijman, L., Chan, E. T., Kirk, C. J., Dimayuga Smith, V., Koot, S., Mamber, C., Jansen, A. H., et al. (2013) · Brain · doi:10.1093/brain/awt083 · Cited by 180
Schierle, G. S. K., van de Linde, S., Erdélyi, M., Esbjörner, E. K., Klein, T., Rees, E. J., Bertoncini, C. W., Dobson, C. M., Sauer, M., & Kaminski, C. F. (2011) · Journal of the American Chemical Society · doi:10.1021/ja201651w · Cited by 170
Bin1 and CD2AP polarise the endocytic generation of beta‐amyloid
Ubelmann, F., Burrinha, T., Salavessa, L., Gomes, R., Ferreira, C., Moreno, N., & Guimas Almeida, C. (2017) · The EMBO Reports · doi:10.15252/embr.201642738 · Cited by 165
Self-citationLaulagnier, K., Javalet, C., Hemming, F. J., Chivet, M., Lachenal, G., Blot, B., Chatellard, C., & Sadoul, R. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2664-0 · Cited by 164
Peric, A., & Annaert, W. G. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1379-7 · Cited by 172
Relationship between amyloid-beta and the ubiquitin–proteasome system in Alzheimer’s disease
Hong, L., Huang, H., & Jiang, Z.-F. (2013) · Neurological Research · doi:10.1179/1743132813y.0000000288 · Cited by 165
Bassoon and Piccolo maintain synapse integrity by regulating protein ubiquitination and degradation
Waites, C. L., Leal‐Ortiz, S., Okerlund, N. D., Dalke, H., Fejtová, A., Altrock, W. D., Gundelfinger, E. D., & Garner, C. C. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.27 · Cited by 156
PLD3 affects axonal spheroids and network defects in Alzheimer’s disease
Yuan, P., Zhang, M., Tong, L., Morse, T. M., McDougal, R. A., Ding, H., Chan, D., Cai, Y., & Grutzendler, J. (2022) · Nature · doi:10.1038/s41586-022-05491-6 · Cited by 155
Co-occurrence of Alzheimer's disease β-amyloid and tau pathologies at synapses
Takahashi, R. H., Capetillo-Zarate, E., Lin, M. T., Milner, T. A., & Gouras, G. K. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.07.021 · Cited by 150
Self-citationXu, J., Chatterjee, M., Baguley, T. D., Brouillette, J., Kurup, P. K., Ghosh, D., Kanyo, J. E., Zhang, Y., Seyb, K. I., Ononenyi, C., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001923 · Cited by 144
Alzheimer's APP mangles mitochondria
Lin, M. T., & Beal, M. F. (2006) · Nature Medicine · doi:10.1038/nm1106-1241 · Cited by 143
Signal pathways in the treatment of Alzheimer’s disease with traditional Chinese medicine
Ding, M.-R., Qu, Y.-J., Hu, B., & An, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113208 · Cited by 145
A Reassessment of the Neuropathology of Frontotemporal Dementia Linked to Chromosome 3
Holm, I. E., Englund, E. M., Mackenzie, I. R., Johannsen, P., & Isaacs, A. M. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181567f02 · Cited by 136
The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy
John, J. S. (2007) · Frontiers in bioscience · doi:10.2741/2714 · Cited by 135
Intracellular amyloid toxicity induces oxytosis/ferroptosis regulated cell death
Huang, L., McClatchy, D. B., Maher, P. A., Liang, Z., Diedrich, J. K., Soriano‐Castell, D., Goldberg, J., Shokhirev, M. N., Yates, J. R., Schubert, D. A., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03020-9 · Cited by 130
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
Self-citationFunctional Protein Delivery into Neurons Using Polymeric Nanoparticles
Hasadsri, L., Kreuter, J., Hattori, H., Iwasaki, T., & George, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805956200 · Cited by 129
The role of amyloid oligomers in neurodegenerative pathologies
Wells, C., Brennan, S. E., Keon, M., & Ooi, L. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.03.113 · Cited by 128
Oddo, S., Caccamo, A., Tseng, B., Cheng, D., Vasilevko, V., Cribbs, D. H., & LaFerla, F. M. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2464-08.2008 · Cited by 124
Accumulation of intraneuronal Aβ correlates with ApoE4 genotype
Christensen, D. Z., Schneider-Axmann, T., Lucassen, P. J., Bayer, T. A., & Wirths, O. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0666-1 · Cited by 120
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
Self-citationMiranda, M., Dionne, K. R., Sorkina, T., & Sorkin, A. D. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-08-0704 · Cited by 117
The role of intracellular amyloid β in Alzheimer's disease
Li, M. C., Chen, L., Lee, D. H. S., Yu, L., & Zhang, Y. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.08.002 · Cited by 118
Kabir, M. T., Sufian, M. A., Uddin, M. S., Begum, M. M., Akhter, S., Islam, A., Mathew, B., Islam, M. S., Amran, M. S., & Ashraf, G. M. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666191011102444 · Cited by 121
Proteotoxic stress and the ubiquitin proteasome system
Kandel, R., Jung, J., & Neal, S. E. (2023) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2023.08.002 · Cited by 123
Reconsider Alzheimer's disease by the ‘calpain–cathepsin hypothesis’—A perspective review
Yamashima, T. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.02.004 · Cited by 109
Exosomal Secretion of Cytoplasmic Prostate Cancer Xenograft-derived Proteins
Jansen, F. H., Krijgsveld, J., van Rijswijk, A., van den Bemd, G.-J., van den Berg, M. S., van Weerden, W. M., Willemsen, R., Dekker, L. J., Luider, T. M., & Jenster, G. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800443-mcp200 · Cited by 107
Synaptic transmission block by presynaptic injection of oligomeric amyloid beta
Moreno, H., Yu, E., Pigino, G. F., Hernandez, A. I., Kim, N., Moreira, J. E., Sugimori, M., & Llinás, R. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900944106 · Cited by 113
Protein Homeostasis, Aging and Alzheimer’s Disease
Morawe, T., Hiebel, C., Kern, A., & Behl, C. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8246-0 · Cited by 105
Mitra, S. S., Tsvetkov, A. S., & Finkbeiner, S. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806269200 · Cited by 107
Distinct Pools of β-Amyloid in Alzheimer Disease–Affected Brain: A Clinicopathologic Study
Steinerman, J. R., Irizarry, M., Scarmeas, N., Raju, S., Brandt, J., Albert, M., Blacker, D., Hyman, B., & Stern, Y. (2008) · Archives of Neurology · doi:10.1001/archneur.65.7.906 · Cited by 104
Structure, Dynamics and Function of the 26S Proteasome
Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 110
Torres, M., Jiménez, S., Sanchez-Varo, R. M., Navarro, V., Trujillo‐Estrada, L., Sánchez‐Mejías, E., Carmona, I., Dávila, J. C., Vizuete, M., Gutiérrez, A., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-59 · Cited by 103
Protein folding diseases and neurodegeneration: Lessons learned from yeast
Winderickx, J., Delay, C., Vos, A. D., Klinger, H., Pellens, K., Vanhelmont, T., LEUVEN, F. V., & Zabrocki, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.020 · Cited by 108
Bustamante, H. A., González, A., Cerda‐Troncoso, C., Shaughnessy, R., Carola Otth, L., Soza, A., & Burgos, P. V. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00126 · Cited by 102
The Proteasome and Oxidative Stress in Alzheimer's Disease
Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99
Poon, W. W., Carlos, A. J., Aguilar, B. L., Berchtold, N. C., Kawano, C. K., Zograbyan, V., Yaopruke, T., Shelanski, M. L., & Cotman, C. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463711 · Cited by 101
Role of ubiquitin–proteasome-mediated proteolysis in nervous system disease
Hegde, A. N., & Upadhya, S. C. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.07.006 · Cited by 96
Salahuddin, P., Fatima, M. T., Abdelhameed, A. S., Nusrat, S., & Khan, R. H. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.02.065 · Cited by 95
The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer’s Disease
Sulistio, Y. A., & Heese, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9063-4 · Cited by 93
Miles, A. L., Burr, S. P., Grice, G. L., & Nathan, J. A. (2017) · eLife · doi:10.7554/elife.22693 · Cited by 91
Bortezomib in the treatment of AL amyloidosis: targeted therapy?
Sitia, R., Palladini, G. O., & Merlini, G. (2007) · Haematologica · doi:10.3324/haematol.12136 · Cited by 91
The proteasome and its role in the nervous system
Türker, F., Cook, E. K., & Margolis, S. S. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.003 · Cited by 101
Aβ Internalization by Neurons and Glia
Mohamed, A., & Chaves, E. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/127984 · Cited by 94
Kuszczyk, M. A., Sanchez, S., Pankiewicz, J., Kim, J., Duszczyk, M., Guridi, M., Asuni, A. A., Sullivan, P. M., Holtzman, D. M., & Sadowski, M. J. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.01.034 · Cited by 89
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Metadata
- Authors
- Almeida, C. G., Takahashi, R. H., & Gouras, G. K.
- Affiliations
- Cornell University (US)
- Corresponding author
- Gouras, Gunnar K.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2006-04-19
- Volume
- 26
- Issue
- 16
- Pages
- 4277-4288
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6673997
- OpenAlex
- W2168538246
- Cited by
- 316
- References
- 59
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 11 · 2023: 26 · 2022: 18 · 2021: 12 · 2020: 17 · 2019: 20 · 2018: 14 · 2017: 15 · 2016: 14 · 2015: 15 · 2014: 10 · 2013: 20 · 2012: 18
- FWCI
- 11.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- Alzheimer's Association
- American Health Assistance Foundation
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01NS045677, NS 045677)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- amyloid-beta deposition, multivesicular bodies, ubiquitin-proteasome system, Alzheimer's disease, epidermal growth factor receptor, TrkB receptor, receptor degradation, ubiquitination, deubiquitinase, proteasome inhibition
- MeSH terms
- Animals, Cells, Cultured, Epidermal Growth Factor, Hippocampus, Humans, Male, Mice, Transgenic, Synaptic Vesicles, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Rats, Sprague-Dawley, Ubiquitin, Proteasome Endopeptidase Complex, Mice, Rats, Proteasome Inhibitors, ErbB Receptors
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