Cited by 1,316Alzheimer's disease research and treatmentsParkinson's Disease Mechanisms and TreatmentsNeuroinflammation and Neurodegeneration Mechanisms

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The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

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Iwai, Akihiko, Masliah, Eliezer, Yoshimoto, Makoto, Ge, Nianfeng, Flanagan, Lisa, Rohan de Silva, H.A, Kittel, Agnes, Saitoh, Tsunao·1995·Neuron

DOI 10.1016/0896-6273(95)90302-x

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Abstract

Non-A beta component of Alzheimer's disease amyloid (NAC) is the second component in the amyloid from brain tissue of patients affected with Alzheimer's disease. Its precursor protein (NACP) was shown to be a brain-specific protein. In rat brain, NACP was more abundant in the neocortex, hippocampus, olfactory bulb, striatum, thalamus, and cerebellum and less abundant in the brain stem. Confocal laser microscopy analysis revealed that anti-NACP immunostaining was colocalized with synaptophysin-immunoreactive presynaptic terminals. Ultrastructural analysis showed that NACP immunoreactivity was associated with synaptic vesicles. NACP sequence showed 95% identity with that of rat synuclein 1, a synaptic/nuclear protein previously identified in rat brain, and good homology with Torpedo synuclein from the electric organ synapse and bovine phosphoneuroprotein 14 (PNP-14), a brain-specific protein present in synapses. Therefore, NACP is a synaptic protein, suggesting that synaptic aberration observed in senile plaques might be involved in amyloidogenesis in Alzheimer's disease.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
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
Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
Self-citation
Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease.
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,646
Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles
Wiedenmann, B. J., & Franke, W. W. (1985) · Cell · doi:10.1016/s0092-8674(85)80082-9 · Cited by 1,432
Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation
Kagawa, Y., & Racker, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61930-1 · Cited by 1,361
Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
Kennelly, P. J., & Krebs, E. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98436-x · Cited by 1,331

Show all 48 references

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(1998) · Europe PMC (PubMed Central) · Cited by 1,594
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Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,622
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Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105343200 · Cited by 1,103
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Wong, Y. C., & Krainc, D. (2017) · Nature Medicine · doi:10.1038/nm.4269 · Cited by 897
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Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, A., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 911
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George, J. M., Jin, H., Woods, W. S., & Clayton, D. F. (1995) · Neuron · doi:10.1016/0896-6273(95)90040-3 · Cited by 844
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Clayton, D. F., & George, J. M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01213-7 · Cited by 793
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Hsu, L. J., Sagara, Y., Arroyo, A., Rockenstein, E. M., Sisk, A., Mallory, M. E., Wong, J., Takenouchi, T., Hashimoto, M., & Masliah, E. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64553-1 · Cited by 737
Self-citation
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Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641
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Wakabayashi, K., Yoshimoto, M., Tsuji, S., & Takahashi, H. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00407-8 · Cited by 643
Self-citation
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Self-citation
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Choi, I., Zhang, Y., Seegobin, S. P., Pruvost, M., Wang, Q., Purtell, K., Zhang, B., & Yue, Z. (2020) · Nature Communications · doi:10.1038/s41467-020-15119-w · Cited by 549
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Self-citation
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Lo Bianco, C., Ridet, J.-L., Schneider, B. L., Déglon, N., & Aebischer, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152339799 · Cited by 482
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Okochi, M., Walter, J., Koyama, A., Nakajo, S., Baba, M., Iwatsubo, T., Meijer, L., Kahle, P. J., & Haass, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.390 · Cited by 535
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Rockenstein, E., Mallory, M., Hashimoto, M., Song, D., Shults, C. W., Lang, I., & Masliah, E. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10231 · Cited by 502
Self-citation
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Hashimoto, M., Rockenstein, E. M., Crews, L. A., & Masliah, E. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:21 · Cited by 508
Self-citation
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Jao, C. C., Hegde, B. G., Chen, J., Haworth, I. S., & Langen, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807826105 · Cited by 501
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Wakabayashi, K., Tanji, K., Odagiri, S., Miki, Y., Mori, F., & Takahashi, H. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8280-y · Cited by 507
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Kamp, F., Exner, N., Lutz, A. K., Wender, N., Hegermann, J., Brunner, B., Nuscher, B., Bartels, T., Giese, A., Beyer, K., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.223 · Cited by 504
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Burré, J., Sharma, M., & Südhof, T. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416598111 · Cited by 510
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Kam, T.-I., Mao, X., Park, H., Chou, S.-C., Karuppagounder, S. S., Umanah, G. E., Yun, S. P., Brahmachari, S., Panicker, N., Chen, R., et al. (2018) · Science · doi:10.1126/science.aat8407 · Cited by 476
Lewy bodies
Shults, C. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509567103 · Cited by 495
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Li, W., West, N. C., Colla, E., Pletniková, O., Troncoso, J. C., Marsh, L., Dawson, T. M., Jäkälä, P., Hartmann, T., Price, D. L., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406976102 · Cited by 479
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Uversky, V. N., Li, J., Souillac, P. O., Millett, I. S., Doniach, S., Jakes, R., Goedert, M., & Fink, A. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109541200 · Cited by 473
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Braak, H., Sastre, M., & Del Tredici, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0244-3 · Cited by 462
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Goldberg, M. S., & Lansbury, P. T. (2000) · Nature Cell Biology · doi:10.1038/35017124 · Cited by 459
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Lee, F. J. S., Liu, F., Pristupa, Z. B., & Niznik, H. B. (2001) · The FASEB Journal · doi:10.1096/fj.00-0334com · Cited by 463
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Lee, H.-J., Choi, C., & Lee, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107045200 · Cited by 462
Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models
Karpinar, D. P., Balija, M. B. G., Kügler, S., Opazo, F., Rezaei‐Ghaleh, N., Wender, N., Kim, H., Taschenberger, G., Falkenburger, B. H., Heise, H., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.257 · Cited by 432
NACP/α-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson’s disease brains
Wakabayashi, K., Hayashi, S., Yoshimoto, M., Kudo, H., & Takahashi, H. (2000) · Acta Neuropathologica · doi:10.1007/pl00007400 · Cited by 451
Self-citation
Interaction of Human α-Synuclein and Parkinson's Disease Variants with Phospholipids
Perrin, R. J., Woods, W. S., Clayton, D. F., & George, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004851200 · Cited by 444
The toxicity in vitro of β-amyloid protein
Iversen, L. L., Mortishire‐Smith, R. J., Pollack, S. J., & Shearman, M. S. (1995) · Biochemical Journal · doi:10.1042/bj3110001 · Cited by 428
Decreased α-synuclein in cerebrospinal fluid of aged individuals and subjects with Parkinson’s disease
Tokuda, T., Salem, S. A., Allsop, D., Mizuno, T., Nakagawa, M., Qureshi, M. M., Locascio, J. J., Schlossmacher, M. G., & El-Agnaf, O. M. A. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.024 · Cited by 425
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Masliah, E., Rockenstein, E. M., Mante, M., Crews, L. A., Spencer, B. J., Adame, A., Patrick, C., Trejo, M., Ubhi, K. K., Rohn, T. T., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019338 · Cited by 422
Self-citation
Retracted
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Larsen, K. E., Schmitz, Y., Troyer, M. D., Mosharov, E. V., Dietrich, P., Quazi, A. Z., Savalle, M., Nemani, V. M., Chaudhry, F. A., Edwards, R. H., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3821-06.2006 · Cited by 424
Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders.
Takeda, A., Mallory, M. E., Sundsmo, M. P., Honer, W. G., Hansen, L. A., & Masliah, E. (1998) · Europe PMC (PubMed Central) · Cited by 403
Self-citation
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Ishizawa, T., Mattila, P. M., Davies, P., Wang, D., & Dickson, D. W. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.4.389 · Cited by 402
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Vila, M., Vukosavić, S., Jackson-Lewis, V. R., Neystat, M., Jakowec, M. W., & Przedborski, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.740721.x · Cited by 394
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Middleton, E. R., & Rhoades, E. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.056 · Cited by 392
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Jensen, P. H., Hager, H., Nielsen, M. S., Højrup, P., Gliemann, J., & Jakes, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25481 · Cited by 377
Multiple Tight Phospholipid-Binding Modes of α-Synuclein Revealed by Solution NMR Spectroscopy
Bodner, C. R., Dobson, C. M., & Bax, A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.066 · Cited by 378
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Twohig, D., & Nielsen, H. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0320-x · Cited by 374
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Braak, H., & Del Tredici, K. (2017) · Journal of Parkinson’s Disease · doi:10.3233/jpd-179001 · Cited by 372
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Greenbaum, E. A., Graves, C. L., Mishizen-Eberz, A. J., Lupoli, M. A., Lynch, D. R., Englander, S. W., Axelsen, P. H., & Giasson, B. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411638200 · Cited by 388
Iron Toxicity in Diseases of Aging: Alzheimer's Disease, Parkinson's Disease and Atherosclerosis
Altamura, S., & Muckenthaler, M. U. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1010 · Cited by 369
The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
Munishkina, L. A., Cooper, E. M., Uversky, V. N., & Fink, A. L. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.699 · Cited by 355
Pathological roles of α-synuclein in neurological disorders
Vekrellis, K., Xilouri, M., Emmanouilidou, E., Rideout, H. J., & Stefanis, L. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70213-7 · Cited by 382
Effect of Mutant α-Synuclein on Dopamine Homeostasis in a New Human Mesencephalic Cell Line
Lotharius, J., Barg, S., Wiekop, P., Lundberg, C., Raymon, H. K., & Brundin, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205518200 · Cited by 368
Accumulation of α-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy
Wakabayashi, K., Hayashi, S., Kakita, A., Yamada, M., Toyoshima, Y., Yoshimoto, M., & Takahashi, H. (1998) · Acta Neuropathologica · doi:10.1007/s004010050918 · Cited by 347
Self-citation
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Microglia Phenotypes in Aging and Neurodegenerative Diseases
Wendimu, M. Y., & Hooks, S. B. (2022) · Cells · doi:10.3390/cells11132091 · Cited by 336
Astrocytic expression of Parkinson's disease-related A53T α-synuclein causes neurodegeneration in mice
Gu, X., Long, C.-X., Sun, L., Xie, C., Lin, X. Z., & Cai, H. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-12 · Cited by 351
Antibody-Aided Clearance of Extracellular α-Synuclein Prevents Cell-to-Cell Aggregate Transmission
Bae, E.-J., Lee, H.-J., Rockenstein, E., Ho, D.-H., Park, E.-B., Yang, N.-Y., Desplats, P., Masliah, E., & Lee, S.-J. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1292-12.2012 · Cited by 339
Self-citation
Copper(II)-induced self-oligomerization of α-synuclein
Paik, S. R., Shin, H.-J., Lee, J., Chang, C., & Kim, J. (1999) · Biochemical Journal · doi:10.1042/bj3400821 · Cited by 340
Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation
Flagmeier, P., Meisl, G., Vendruscolo, M., Knowles, T. P. J., Dobson, C. M., Buell, A. K., & Galvagnion, C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604645113 · Cited by 336
NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease
Wakabayashi, K., Matsumoto, K., Takayama, K., Yoshimoto, M., & Takahashi, H. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00891-4 · Cited by 331
Self-citation
α-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins
Sharon, R., Goldberg, M. S., Bar-Josef, I., Betensky, R. A., Shen, J., & Selkoe, D. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171300598 · Cited by 340
Impaired dopamine metabolism in Parkinson’s disease pathogenesis
Masato, A., Plotegher, N., Boassa, D., & Bubacco, L. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0332-6 · Cited by 350
Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling
Der-Sarkissian, A., Jao, C. C., Chen, J., & Langen, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305266200 · Cited by 337
Understanding the molecular causes of Parkinson's disease
Wood‐Kaczmar, A., Gandhi, S., & Wood, N. W. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.09.007 · Cited by 334
Reducing C-Terminal-Truncated Alpha-Synuclein by Immunotherapy Attenuates Neurodegeneration and Propagation in Parkinson's Disease-Like Models
Games, D., Valera, E., Spencer, B. J., Rockenstein, E. M., Mante, M., Adame, A., Patrick, C., Ubhi, K. K., Nuber, S., Sacayon, P., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5314-13.2014 · Cited by 329
Self-citation
Biophysics of Parkinsons Disease: Structure and Aggregation of α- Synuclein
Uversky, V. N., & Eliezer, D. (2009) · Current Protein and Peptide Science · doi:10.2174/138920309789351921 · Cited by 325
The Synuclein FamilyPreprint
Lavedan, C. N. (1998) · Genome Research · doi:10.1101/gr.8.9.871 · Cited by 323
Expression of Concern: Antioxidant compounds have potent anti‐fibrillogenic and fibril‐destabilizing effects for α‐synuclein fibrils in vitro
Ono, K., & Yamada, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03707.x · Cited by 325

Authors: Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T.
Affiliations: University of California San Diego (US)
ORCID: Masliah, Eliezer
Flanagan, Lisa
Venue: Neuron
Publisher: Elsevier BV
Published: 1995-02
Volume: 14
Issue: 2
Pages: 467-475
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/0896-6273(95)90302-x
OpenAlex: W2059261643
Cited by: 1,316
References: 48
Citations by year: 2026: 21 · 2025: 23 · 2024: 34 · 2023: 36 · 2022: 60 · 2021: 56 · 2020: 69 · 2019: 59 · 2018: 62 · 2017: 49 · 2016: 53 · 2015: 61 · 2014: 52 · 2013: 41 · 2012: 47
FWCI: 12.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6741 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: American Health Assistance Foundation
National Institutes of Health
National Institute on Aging (AG10689, AG05131, R01AG010689, P50AG005131)
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
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: presynaptic proteins, synaptic vesicles, synaptophysin, amyloidogenesis, amyloid plaques, brain distribution, Alzheimer's disease
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Animals, Antibodies, Antibody Specificity, Brain, Cattle, Humans, Molecular Sequence Data, Oligopeptides, Organ Specificity, Recombinant Proteins, Torpedo, Blotting, Western, Microscopy, Immunoelectron, Amyloid beta-Protein Precursor, Synaptophysin, Rats, Sprague-Dawley, Sequence Homology, Amino Acid, Microscopy, Confocal, Rats

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The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

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