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Interaction between Aβ Peptide and α Synuclein: Molecular Mechanisms in Overlapping Pathology of Alzheimer’s and Parkinson’s in Dementia with Lewy Body Disease
Abstract
Amyloidogenic proteins (Abeta peptide) in Alzheimer's disease (AD) and alpha-synuclein (alpha-Syn) in Parkinson's disease (PD) are typically soluble monomeric precursors, which undergo remarkable conformational changes and culminate in the form of aggregates in diseased condition. Overlap of clinical and neuropathological features of both AD and PD are observed in dementia with Lewy body (DLB) disease, the second most common form of dementia after AD. The identification of a 35-amino acid fragment of alpha-Syn in the amyloid plaques in DLB brain have raised the possibility that Abeta and alpha-Syn interact with each other. In this report, the molecular interaction of alpha-Syn with Abeta40 and/or Abeta42 are investigated using multidimensional NMR spectroscopy. NMR data in the membrane mimic environment indicate specific sites of interaction between membrane-bound alpha-Syn with Abeta peptide and vice versa. These Abeta-alpha-Syn interactions are demonstrated by reduced amide peak intensity or change in chemical shift of amide proton of the interacting proteins. Based on NMR results, the plausible molecular mechanism of overlapping pathocascade of AD and PD in DLB due to interactions between alpha-Syn and Abeta is described. To the best of our knowledge, it is the first report using multidimensional NMR spectroscopy that elucidates molecular interactions between Abeta and alpha-Syn which may lead to onset of DLB.
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“Evidence suggests that Aβ can directly affect α-synuclein toxicity, and it is also known that tau protein and α-synuclein can directly interact promoting their co-assembly [124–126].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [124]
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Cites
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
McKeith, I. G., Galasko, D., Kosaka, K., Perry, E. K., Dickson, D. W., Hansen, L. A., Salmon, D. P., Lowe, J., Mirra, S. S., Byrne, E. J., et al. (1996) · Neurology · doi:10.1212/wnl.47.5.1113 · Cited by 3,960
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
Piotto, M., Saudek, V., & Sklenář, V. (1992) · Journal of Biomolecular NMR · doi:10.1007/bf02192855 · Cited by 3,720
Marion, D., & Wüthrich, K. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)91093-8 · Cited by 3,160
University of California, San Francisco
(1974) · Medical History · doi:10.1017/s0025727300019682 · Cited by 2,218
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Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345
Self-citationThe neuropathological diagnosis of Alzheimer's disease
DeTure, M. A., & Dickson, D. W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0333-5 · Cited by 3,329
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Domínguez, L., Shea, J., Dokholyan, N. V., Simone, A. D., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 680
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Sakono, M., & Zako, T. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07568.x · Cited by 633
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Jellinger, K. A. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01010.x · Cited by 640
Clinton, L. K., Blurton-Jones, M., Myczek, K., Trojanowski, J. Q., & LaFerla, F. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.0490-10.2010 · Cited by 576
Shahnawaz, M., Tokuda, T., Waragai, M., Méndez, N., Ishii, R., Trenkwalder, C., Mollenhauer, B., & Soto, C. A. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.4547 · Cited by 485
Neuropathology of sporadic Parkinson's disease: Evaluation and changes of concepts
Jellinger, K. A. (2011) · Movement Disorders · doi:10.1002/mds.23795 · Cited by 480
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Spires‐Jones, T. L., Attems, J., & Thal, D. R. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1709-7 · Cited by 435
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Shi, M. Y., Bradner, J. M., Hancock, A. M., Chung, K. A., Quinn, J. F., Peskind, E. R., Galasko, D., Jankovic, J. J., Zabetian, C. P., Kim, H. M., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22311 · Cited by 422
α-synuclein in the pathophysiology of Alzheimer’s disease
Twohig, D., & Nielsen, H. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0320-x · Cited by 374
Crews, L. A., Spencer, B. J., Desplats, P., Patrick, C., Paulino, A., Rockenstein, E. M., Hansen, L. A., Adame, A., Galasko, D. R., & Masliah, E. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009313 · Cited by 379
Self-citationRetractedTsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003135 · Cited by 281
Self-citationRetractedRecent advances in our understanding of neurodegeneration
Jellinger, K. A. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0240-y · Cited by 274
Prevalence and impact of vascular and Alzheimer pathologies in Lewy body disease
Jellinger, K. A., & Attems, J. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0347-5 · Cited by 267
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Jellinger, K. A. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1821-9 · Cited by 277
Bassil, F., Brown, H. J., Pattabhiraman, S., Iwasyk, J. E., Maghames, C. M., Meymand, E. S., Cox, T. O., Riddle, D. M., Zhang, B., Trojanowski, J. Q., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.10.010 · Cited by 246
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Morales, R., Moreno‐González, I., & Soto, C. A. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003537 · Cited by 225
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Ono, K., Takahashi, R., Ikeda, T., & Yamada, M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07847.x · Cited by 222
Smith, C., Malek, N., Grosset, K. A., Cullen, B., Gentleman, S., & Grosset, D. G. (2019) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2019-321111 · Cited by 213
Confluence of α-Synuclein, Tau, and β-Amyloid Pathologies in Dementia With Lewy Bodies
Colom‐Cadena, M., Gelpí, E., Charif, S., Belbin, O., Blesa, R., Martí, M. J., Clarimón, J., & Lleó, A. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000018 · Cited by 188
Luca, C. M. G. D., Elia, A. E., Portaleone, S. M., Cazzaniga, F. A., Rossi, M., Bistaffa, E., Cecco, E. D., Narkiewicz, J., Salzano, G., Carletta, O., et al. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0164-x · Cited by 190
Simulation Studies of Amyloidogenic Polypeptides and Their Aggregates
Ilie, I. M., & Caflisch, A. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00731 · Cited by 181
Egawa, J., Pearn, M. L., Lemkuil, B. P., Patel, P. M., & Head, B. P. (2015) · The Journal of Physiology · doi:10.1113/jp270590 · Cited by 184
Lashley, T., Holton, J. L., Gray, E., Kirkham, K., O’Sullivan, S. S., Hilbig, A., Wood, N. W., Lees, A. J., & Révész, T. (2008) · Acta Neuropathologica · doi:10.1007/s00401-007-0336-0 · Cited by 172
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Oláh, J., Vincze, O., Virók, D., Simon, D., Bozsó, Z., Tőkési, N., Horváth, I., Hlavanda, E., Kovács, J., Magyar, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243907 · Cited by 137
Walker, D. G., Lue, L., Adler, C. H., Shill, H. A., Caviness, J. N., Sabbagh, M. N., Akiyama, H., Serrano, G. E., Sue, L. I., & Beach, T. G. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.11.020 · Cited by 153
Ivanova, M. I., Lin, Y., Lee, Y., Zheng, J., & Ramamoorthy, A. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106507 · Cited by 157
Goldman, J. G., Andrews, H., Amara, A. W., Naito, A., Alcalay, R. N., Shaw, L. M. J., Taylor, P., Xie, T., Tuite, P., Henchcliffe, C., et al. (2017) · Movement Disorders · doi:10.1002/mds.27232 · Cited by 149
Luo, J., Wärmländer, S. K. T. S., Gräslund, A., & Abrahams, J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.714576 · Cited by 142
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Marsh, S. E., & Blurton-Jones, M. M. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt109 · Cited by 140
Fundamentals of cross-seeding of amyloid proteins: an introduction
Ren, B., Zhang, Y., Zhang, M., Liu, Y., Zhang, D., Gong, X., Feng, Z., Tang, J., Chang, Y., & Zheng, J. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb01871a · Cited by 139
Spies, P. E., Slats, D., Sjögren, M. J. C., Kremer, B. P. H., Verhey, F. R. J., Rikkert, M. G. M. O., & Verbeek, M. M. (2010) · Current Alzheimer Research · doi:10.2174/156720510791383796 · Cited by 140
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Gold, A., Turkalp, Z. T., & Munoz, D. G. (2013) · Movement Disorders · doi:10.1002/mds.25298 · Cited by 132
Valera, E., Spencer, B. J., & Masliah, E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0397-z · Cited by 135
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Horvath, J. E., Herrmann, F. R., Burkhard, P. R., Bouras, C., & Kövari, E. (2013) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2013.05.010 · Cited by 124
Wang, Y., Hancock, A. M., Bradner, J. M., Chung, K. A., Quinn, J. F., Peskind, E. R., Galasko, D. R., Jankovic, J. J., Zabetian, C. P., Kim, H. M., et al. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.01.006 · Cited by 121
Barreto, G. E., Iarkov, A., & Echeverrı́a, V. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00340 · Cited by 119
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Subedi, S., Sasidharan, S., Nag, N., Saudagar, P., & Tripathi, T. (2022) · Molecules · doi:10.3390/molecules27061776 · Cited by 115
Tau and mTOR: The Hotspots for Multifarious Diseases in Alzheimer's Development
Mueed, Z., Tandon, P., Maurya, S. K., Deval, R., Kamal, M. A., & Poddar, N. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.01017 · Cited by 111
α-Synuclein modulates tau spreading in mouse brains
Bassil, F., Meymand, E. S., Brown, H. J., Xu, H. W., Cox, T. O., Pattabhiraman, S., Maghames, C. M., Wu, Q., Zhang, B., Trojanowski, J. Q., et al. (2020) · The Journal of Experimental Medicine · doi:10.1084/jem.20192193 · Cited by 109
Structural and Functional Insights into α-Synuclein Fibril Polymorphism
Mehra, S., Gadhe, L. G., Bera, R., Sawner, A. S., & Maji, S. K. (2021) · Biomolecules · doi:10.3390/biom11101419 · Cited by 111
Richman, M., Wilk, S., Chemerovski‐Glikman, M., Wärmländer, S. K. T. S., Wahlström, A., Gräslund, A., & Rahimipour, S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310064v · Cited by 108
Wang, C., Lau, C. Y., Ma, F., & Zheng, C. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106504118 · Cited by 106
Beyond the synucleinopathies: alpha synuclein as a driving force in neurodegenerative comorbidities
Visanji, N. P., Lang, A. E., & Kovács, G. G. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0172-x · Cited by 102
Cross-Seeding Interaction between β-Amyloid and Human Islet Amyloid Polypeptide
Hu, R., Zhang, M., Chen, H., Jiang, B., & Zheng, J. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00192 · Cited by 98
Swirski, M., Miners, J. S., de Silva, R., Lashley, T., Ling, H., Holton, J. L., Révész, T., & Love, S. (2014) · Alzheimer s Research & Therapy · doi:10.1186/s13195-014-0077-y · Cited by 98
Immunotherapies for Aging-Related Neurodegenerative Diseases—Emerging Perspectives and New Targets
Kwon, S., Iba, M., Kim, C., & Masliah, E. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00853-2 · Cited by 97
Self-citationMultiple pathogenic proteins implicated in neuronopathic Gaucher disease mice
Xu, Y., Xu, K., Sun, Y., Liou, B., Quinn, B., Li, R.-H., Xue, L., Zhang, W., Setchell, K. D. R., Witte, D. P., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu105 · Cited by 88
Role of Synucleins in Alzheimer’s Disease
Crews, L. A., Tsigelny, I. F., Hashimoto, M., & Masliah, E. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9073-6 · Cited by 85
Self-citationBaram, M., Atsmon‐Raz, Y., Ma, B., Nussinov, R., & Miller, Y. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp03338a · Cited by 81
γ-Synuclein: Seeding of α-Synuclein Aggregation and Transmission between Cells
Surgucheva, I. G., Sharov, V. S., & Surguchov, A. P. (2012) · Biochemistry · doi:10.1021/bi300478w · Cited by 86
Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro
Köppen, J., Schulze, A., Machner, L., Wermann, M., Eichentopf, R., Guthardt, M., Hähnel, A., Klehm, J., Kriegeskorte, M.-C., Hartlage‐Rübsamen, M., et al. (2020) · Molecules · doi:10.3390/molecules25030580 · Cited by 79
Regional Overlap of Pathologies in Lewy Body Disorders
Colom‐Cadena, M., Grau‐Rivera, O., Planellás, L., Cerquera‐Cleves, C., Morenas‐Rodríguez, E., Helgueta, S., Muñoz, L., Kulisevsky, J., Martı́, M. J., Tolosa, E. S., et al. (2017) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlx002 · Cited by 80
Alpha-synuclein potentiates Ca2+ influx through voltage-dependent Ca2+ channels
Adamczyk, A., & Strosznajder, J. B. (2006) · Neuroreport · doi:10.1097/wnr.0b013e3280115185 · Cited by 79
Jellinger, K. A. (2007) · Springer eBooks · doi:10.1007/978-3-211-73574-9_12 · Cited by 77
Significance of Brain Lesions in Parkinson Disease Dementia and Lewy Body Dementia
Jellinger, K. A. (2009) · Monographs in clinical neuroscience/Frontiers of neurology and neuroscience/Monographs in neural sciences · doi:10.1159/000197890 · Cited by 74
Overk, C., Cartier, A. E., Shaked, G. M., Rockenstein, E. M., Ubhi, K. K., Spencer, B. J., Price, D. L., Patrick, C., Desplats, P., & Masliah, E. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-18 · Cited by 73
Self-citationRetractedCross Currents in Protein Misfolding Disorders: Interactions and Therapy
Morales, R., Green, K., & Soto, C. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709789541998 · Cited by 72
Beishon, L., Batterham, A. P., Quinn, T. J., Nelson, C. P., Panerai, R. B., Robinson, T. G., & Haunton, V. J. (2019) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd013282.pub2 · Cited by 77
Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67
Kragh, C. L., Ubhi, K. K., Wyss‐Coray, T., & Masliah, E. (2011) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00545.x · Cited by 66
Self-citationLuo, X., Hou, L., Shi, H., Zhong, X., Zhang, Y., Zheng, D., Tan, Y., Guoyan, H., Mu, N., Chan, J., et al. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12331 · Cited by 66
Interaction between -Synuclein and Other Proteins in Neurodegenerative Disorders
Jellinger, K. A. (2011) · The Scientific World JOURNAL · doi:10.1100/2011/371893 · Cited by 64
Coskuner‐Weber, O., & Uversky, V. N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020336 · Cited by 71
A mechanistic survey of Alzheimer's disease
Tang, Y., Zhang, D., Gong, X., & Zheng, J. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106735 · Cited by 66
Giacomelli, C., Daniele, S., & Martini, C. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.01.017 · Cited by 71
Kayed, R., Dettmer, U., & Lesné, S. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-201965 · Cited by 63
Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid β Peptide
Luo, J., Wärmländer, S. K. T. S., Gräslund, A., & Abrahams, J. P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.574947 · Cited by 60
A novel PSEN2 mutation associated with a peculiar phenotype
Piscopo, P., Marcon, G., Piras, M. R., Crestini, A., Campeggi, L. M., Deiana, E., Cherchi, R., Tanda, F., Deplano, A., Vanacore, N., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000310643.53587.87 · Cited by 64
Ferman, T. J., & Boeve, B. F. (2007) · Neurologic Clinics · doi:10.1016/j.ncl.2007.03.001 · Cited by 68
Protein–protein interactions regulating α-synuclein pathology
Wang, J., Dai, L., Chen, S., Zhang, Z., Fang, X., & Zhang, Z. (2024) · Trends in Neurosciences · doi:10.1016/j.tins.2024.01.002 · Cited by 58
α-synuclein induced synapse damage is enhanced by amyloid-β1-42
Bate, C., Gentleman, S., & Williams, A. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-55 · Cited by 55
α-Synuclein enhances secretion and toxicity of amyloid beta peptides in PC12 cells
Wilkaniec, A., Strosznajder, J. B., & Adamczyk, A. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.08.004 · Cited by 59
α-Synuclein increases β-amyloid secretion by promoting β-/γ-secretase processing of APP
Hall‐Roberts, H., Schneider, B. L., & Brown, D. R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171925 · Cited by 55
Atsmon‐Raz, Y., & Miller, Y. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00204 · Cited by 56
Disease-modifying drugs and Parkinson's disease
Allain, H., Bentué‐Ferrer, D., & Akwa, Y. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.10.003 · Cited by 52
Piperidine-derived γ-secretase modulators
Hall, A., Elliott, R. L., Giblin, G. M. P., Hussain, I., Musgrave, J., Naylor, A., Sasse, R. Z., & Smith, B. B. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.08.072 · Cited by 51
Cerebrospinal Fluid Aβ42 Levels: When Physiological Become Pathological State
Martorana, A., Lorenzo, F. D., Belli, L., Sancesario, G., Toniolo, S., Sallustio, F., Sancesario, G. M., & Koch, G. (2015) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12476 · Cited by 51
Exploring pathological link between antimicrobial and amyloid peptides
Tang, Y., Zhang, Y., Zhang, D., Liu, Y., Nussinov, R., & Zheng, J. (2024) · Chemical Society Reviews · doi:10.1039/d3cs00878a · Cited by 53
Disordered Proteins: Biological Membranes as Two-Dimensional Aggregation Matrices
Byström, R., Aisenbrey, C., Borowik, T., Bokvist, M., Lindström, F., Sani, M., Olofsson, A., & Gröbner, G. (2008) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-008-9033-4 · Cited by 50
Cerebral amyloid angiopathy in Lewy body disease
Jellinger, K. A., & Attems, J. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-007-0856-8 · Cited by 50
Chemerovski‐Glikman, M., Rozentur‐Shkop, E., Richman, M., Grupi, A., Getler, A., Cohen, H. Y., Shaked, H., Wallin, C., Wärmländer, S. K. T. S., Haas, E., et al. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201601830 · Cited by 51
Absence of α-synuclein pathology in postencephalitic parkinsonism
Jellinger, K. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0537-9 · Cited by 49
Quantifying Co-Oligomer Formation by α-Synuclein
Iljina, M., Dear, A. J., Garcia, G. A., De, S., Tosatto, L., Flagmeier, P., Whiten, D. R., Michaels, T. C. T., Frenkel, D., Dobson, C. M., et al. (2018) · ACS Nano · doi:10.1021/acsnano.8b03575 · Cited by 51
Pellegrini, C., Daniele, S., Antonioli, L., Benvenuti, L., D’Antongiovanni, V., Piccarducci, R., Pietrobono, D., Citi, V., Piragine, E., Flori, L., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103523 · Cited by 49
Limegrover, C. S., Yurko, R., Izzo, N. J., LaBarbera, K. M., Rehak, C., Look, G., Rishton, G., Safferstein, H., & Catalano, S. M. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24782 · Cited by 43
Molecular simulation aspects of amyloid peptides at membrane interface
Liu, Y., Ren, B., Zhang, Y., Sun, Y. P., Chang, Y., Liang, G., Xu, L., & Zheng, J. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.02.004 · Cited by 43
Tosun, D., Hausle, Z., Thropp, P., Concha‐Marambio, L., Lamoureux, J., Lebovitz, R. M., Shaw, L. M. J., Singleton, A., Weiner, M. W., Initiative, T. A. D. N., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14276 · Cited by 42
Belostozky, A., Richman, M., Lisniansky, E., Tovchygrechko, A., Chill, J. H., & Rahimipour, S. (2018) · Chemical Communications · doi:10.1039/c8cc01233d · Cited by 41
Prabhu, S., Raman, B., Ramakrishna, T., & Rao, C. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029810 · Cited by 40
Daniele, S., Pietrobono, D., Fusi, J., Iofrida, C., Chico, L., Petrozzi, L., Gerfo, A. L., Baldacci, F., Galetta, F., Siciliano, G., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0523-5 · Cited by 41
Heterotypic Amyloid β interactions facilitate amyloid assembly and modify amyloid structure
Konstantoulea, K., Guerreiro, P. S., Ramakers, M., Louros, N. N., Aubrey, L. D., Houben, B., Michiels, E., Vleeschouwer, M. D., Lampi, Y., Ribeiro, L. F., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108591 · Cited by 39
Candreva, J., Chau, E., Rice, M. E., & Kim, J. R. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00655 · Cited by 39
Enzymatic degradation of RNA causes widespread protein aggregation in cell and tissue lysates
Aarum, J., Cabrera, C., Jones, T. A., Rajendran, S., Adiutori, R., Giovannoni, G., Barnes, M. R., Malaspina, A., & Sheer, D. (2020) · EMBO Reports · doi:10.15252/embr.201949585 · Cited by 38
Marciniuk, K., Taschuk, R., & Napper, S. (2013) · Clinical and Developmental Immunology · doi:10.1155/2013/473706 · Cited by 39
Metadata
- Authors
- Mandal, P. K., Pettegrew, J. W., Masliah, E., Hamilton, R. L., & Mandal, R.
- Affiliations
- University of Pittsburgh Medical Center (US)
- University of California San Diego (US)
- University of Pittsburgh (US)
- Corresponding author
- Mandal, Pravat K.
- Venue
- Neurochemical Research
- Published
- 2006-09
- Volume
- 31
- Issue
- 9
- Pages
- 1153-1162
- ISSN
- 0364-3190 (ISSN-L)
- 1573-6903
- OpenAlex
- W1965229261
- Cited by
- 219
- References
- 48
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 8 · 2023: 12 · 2022: 12 · 2021: 17 · 2020: 20 · 2019: 17 · 2018: 7 · 2017: 9 · 2016: 9 · 2015: 12 · 2014: 9 · 2013: 11 · 2012: 9
- FWCI
- 6.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neurochemical Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta, alpha-synuclein, dementia with Lewy bodies, Alzheimer's disease, Parkinson's disease, protein-protein interaction, Aβ40, amyloid-beta 42, amyloid plaques, protein aggregation, molecular pathogenesis
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Brain, Humans, Molecular Sequence Data, Parkinson Disease, Peptide Fragments, Amyloid beta-Peptides, Nuclear Magnetic Resonance, Biomolecular, Lewy Body Disease, alpha-Synuclein
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