The DOI matches its Crossref record; 47 of the 48 references it cites were found in a registry or an index.
The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
Open accessAbstract
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“αSyn is predominantly expressed within the presynaptic terminals of neurons [141–143]”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [141]
Citations
Cites
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
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
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-citationStrittmatter, 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
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
Kennelly, P. J., & Krebs, E. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98436-x · Cited by 1,331
Cited by
Sorted by citations
Items 901–1,000 of 1,000
Crossroads between copper ions and amyloid formation in Parkinson’s disease
Wittung-Stafshede, P. E. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220043 · Cited by 18
Jahan, I., Ahmad, A., & Deep, S. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140951 · Cited by 18
Chatterjee, P., & Sengupta, N. (2012) · European Biophysics Journal · doi:10.1007/s00249-012-0803-y · Cited by 18
α‐Synuclein Oligomers: A Study in Diversity
van Diggelen, F., Tepper, A. W. J. W., Apetri, M. M., & Otzen, D. E. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600116 · Cited by 18
Kong, C., Xie, H., Gao, Z., Shao, M., Li, H., Shi, R., Cai, L., Gao, S., Sun, T., & Li, C. (2019) · Virologica Sinica · doi:10.1007/s12250-019-00124-1 · Cited by 18
CCAAT/enhancer binding protein δ is a transcriptional repressor of α-synuclein
Valente, T., Dentesano, G., Ezquerra, M., Fernández‐Santiago, R., Martinez-Martin, J., Gallastegui, E., Domuro, C., Compta, Y., Martı́, M. J., Bachs, O., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0368-8 · Cited by 18
Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy
Kim, D.-H., Lee, J., Mok, K. H., Lee, J., & Han, K. (2020) · Biomolecules · doi:10.3390/biom10030428 · Cited by 18
Current experimental disease-modifying therapeutics for multiple system atrophy
Lemos, M., Wenning, G. K., & Stefanova, N. (2021) · Journal of Neural Transmission · doi:10.1007/s00702-021-02406-z · Cited by 17
Martín, E. D., Gonzalez-Garcia, C., Milán, M., Fariñas, I., & Ceña, V. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03801.x · Cited by 18
Gupta, V. R., Salim, S., Hmila, I., Vaikath, N. N., Sudhakaran, I. P., Ghanem, S. S., Majbour, N. K., Abdulla, S. A., Emara, M. M., Abdesselem, H., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-65035-8 · Cited by 18
Windisch, M., Hutter‐Paier, B., Schreiner, E., & Wronski, R. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:24:1:155 · Cited by 18
Pham-Lake, C., Aronoff, E. B., Camp, C. R., Vester, A. I., Peters, S. J., & Caudle, W. M. (2017) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2017.02.003 · Cited by 17
Li, X., Zhang, Y., Fu, Y., Zhang, H., Li, H.-X., Li, Q., Li, H., Tan, R., Jiang, C.-X., Jiang, W., et al. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-00605-0 · Cited by 18
Ziółkowska, B., Gieryk, A., Wawrzczak‐Bargieła, A., KROWKA, T., Kamińska, D., Korkosz, A., Bieńkowski, P., & Przewłocki, R. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.04.001 · Cited by 17
Kowalik‐Jankowska, T., Rajewska, A., Jankowska, E., & Grzonka, Z. (2008) · Dalton Transactions · doi:10.1039/b714440g · Cited by 17
Loss of α-Synuclein Does Not Affect Mitochondrial Bioenergetics in Rodent Neurons
Pathak, D., Berthet, A., Bendor, J., Yu, K., Sellnow, R. C., Orr, A. L., Nguyen, M. K., Edwards, R. H., Manfredsson, F. P., & Nakamura, K. (2017) · eNeuro · doi:10.1523/eneuro.0216-16.2017 · Cited by 16
Pathology of Parkinson's Disease
Halliday, G. M., & Murphy, K. (2009) · Blue books of neurology · doi:10.1016/b978-1-4160-6641-5.00009-x · Cited by 17
Sakamoto, M., Uchihara, T., Nakamura, A., Mizutani, T., & Mizusawa, H. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1066-9 · Cited by 17
Hellman, N. E., Grant, E., & Goate, A. (1998) · Annals of Neurology · doi:10.1002/ana.410440223 · Cited by 17
Parkin and 𝛂-Synuclein: Opponent Actions in The Pathogenesis of Parkinson’S Disease
Baptista, M. J., Cookson, M., & Miller, D. W. (2004) · The Neuroscientist · doi:10.1177/1073858403260392 · Cited by 17
Flowers, J. M., Leigh, P. N., Davies, A. M., Ninkina, N. N., Buchman, V. L., Vaughan, J. R., Wood, N. W., & Powell, J. F. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00673-4 · Cited by 17
Synaptic vesicle-omics in mice captures signatures of aging and synucleinopathy
Gao, V., Chlebowicz, J., Gaskin, K., Briano, J. A., Komer, L. E., Pineda, A., Jhalani, S., Ahmad, S., Uwaifo, E., Black, L. S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59441-7 · Cited by 18
Role of Lipids in the Pathogenesis of Parkinson’s Disease
Kamano, S., Ozawa, D., Ikenaka, K., & Nagai, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168935 · Cited by 15
The loss of inhibitory C‐terminal conformations in disease associated P123H β‐synuclein
Janowska, M. K., & Baum, J. (2015) · Protein Science · doi:10.1002/pro.2798 · Cited by 16
The interactome of stabilized α‐synuclein oligomers and neuronal proteins
van Diggelen, F., Frank, S. A., Somavarapu, A. K., Scavenius, C., Apetri, M. M., Nielsen, J., Tepper, A. W. J. W., Enghild, J. J., & Otzen, D. E. (2019) · FEBS Journal · doi:10.1111/febs.15124 · Cited by 16
Alpha-Synuclein-Specific Naturally Occurring Antibodies Inhibit Aggregation In Vitro and In Vivo
Braczynski, A. K., Sevenich, M. M., Gering, I., Kupreichyk, T., Agerschou, E. D., Kronimus, Y., Habib, P., Stoldt, M., Willbold, D., Schulz, J. B., et al. (2022) · Biomolecules · doi:10.3390/biom12030469 · Cited by 17
Modulation effect of filamentous phage on α-synuclein aggregation
Dimant, H., Sharon, N., & Solomon, B. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.04.048 · Cited by 16
Chermenina, M., Chorell, E., Pokrzywa, M., Antti, H., Almqvist, F., Strömberg, I., & Wittung-Stafshede, P. E. (2015) · npj Parkinson s Disease · doi:10.1038/npjparkd.2015.24 · Cited by 16
Effects of small-molecule amyloid modulators on a Drosophila model of Parkinson’s disease
Pokrzywa, M., Pawełek, K., Kucia, W. E., Sarbak, S., Chorell, E., Almqvist, F., & Wittung-Stafshede, P. E. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184117 · Cited by 15
Are we listening to everything the PARK genes are telling us?
Benson, D. L., & Huntley, G. W. (2019) · The Journal of Comparative Neurology · doi:10.1002/cne.24642 · Cited by 17
Brown, D. F. (1999) · Annals of Medicine · doi:10.3109/07853899909115977 · Cited by 16
Baldensperger, T., Preissler, M., & Becker, C. F. W. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00221k · Cited by 17
Tanji, K., Mori, F., Kito, K., Kakita, A., Mimura, J., Itoh, K., Takahashi, H., Kamitani, T., & Wakabayashi, K. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182303745 · Cited by 16
The Role ofα-Synuclein and LRRK2 in Tau Phosphorylation
Kawakami, F., & Ichikawa, T. (2015) · Parkinson s Disease · doi:10.1155/2015/734746 · Cited by 15
Amyloidosis and Longevity: A Lesson from Plants
Surguchov, A. P., Emamzadeh, F. N., & Surguchev, A. A. (2019) · Biology · doi:10.3390/biology8020043 · Cited by 14
Raman spectral imaging of 13C2H15N-labeled α-synuclein amyloid fibrils in cells
Watson, M., Flynn, J. D., & Lee, J. C. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106528 · Cited by 14
Kim, T., Newman, A. J., Imberdis, T., Brontesi, L., Tripathi, A., Ramalingam, N., Fanning, S., Selkoe, D. J., & Dettmer, U. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab188 · Cited by 17
Modelling the functional genomics of Parkinson’s disease inCaenorhabditis elegans:LRRK2and beyond
Chandler, R. J., Cogo, S., Lewis, P. A., & Kevei, É. (2021) · Bioscience Reports · doi:10.1042/bsr20203672 · Cited by 16
Rocha, S., Kumar, R., Nordén, B., & Wittung-Stafshede, P. E. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05344 · Cited by 15
α-Synuclein-positive structures induced in leupeptin-infused rats
Nakajima, T., Takauchi, S., Ohara, K., Kokai, M., Nishii, R., Maeda, S., Takanaga, A., Tanaka, T., Takeda, M., Seki, M., et al. (2005) · Brain Research · doi:10.1016/j.brainres.2005.01.099 · Cited by 15
Ruiz, R., Biea, I. A., & Tabares, L. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.032 · Cited by 15
Yoon, D.-K., Hwang, I. K., Yoo, K., Lee, Y.-B., Lee, J.-J., Kim, J., Kang, T., Lee, B., Sohn, H.-S., & Won, M. H. (2006) · Neuroscience Research · doi:10.1016/j.neures.2006.04.014 · Cited by 15
Gentile, A., Amadoro, G., Corsetti, V., Ciotti, M. T., Serafino, A., & Calissano, P. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13205 · Cited by 15
Hirohata, M., Ono, K., Morinaga, A., Ikeda, T., & Yamada, M. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.01.005 · Cited by 15
Rogers, D. A., & Schor, N. F. (2009) · Annals of Neurology · doi:10.1002/ana.21841 · Cited by 15
Small molecule-based fluorescent probes for the detection of α-Synuclein aggregation states
Haque, R., & Maity, D. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129257 · Cited by 15
The Effects of Lipids on α-Synuclein Aggregation In Vitro
Ramirez, J., Pancoe, S. X., Rhoades, E. R., & Petersson, E. J. (2023) · Biomolecules · doi:10.3390/biom13101476 · Cited by 15
α -Synuclein Trafficking in Parkinson’s Disease: Insights From Fly and Mouse Models
Cheng, J., Lu, Q., Li, S., & Ho, M. S.-C. (2018) · ASN NEURO · doi:10.1177/1759091418812587 · Cited by 14
Sumoylated α-synuclein translocates into the nucleus by karyopherin α6
Ryu, S., Baek, I., & Liew, H. (2018) · Molecular & Cellular Toxicology · doi:10.1007/s13273-019-0012-1 · Cited by 14
Stefanovic, A. N. D., Claessens, M. M. A. E., Blum, C., & Subramaniam, V. (2015) · Small · doi:10.1002/smll.201402674 · Cited by 14
Frandsen, P. M., Madsen, L. B., Bendixen, C., & Larsen, K. (2008) · Molecular Biology Reports · doi:10.1007/s11033-008-9270-z · Cited by 14
Neuroproteases in Peptide Neurotransmission and Neurodegenerative Diseases
HOOK, V. Y. H. (2006) · BioDrugs · doi:10.2165/00063030-200620020-00005 · Cited by 15
Alpha-synuclein levels in patients with multiple system atrophy: a meta-analysis
Yang, F., Li, W.-J., & Huang, X. (2017) · International Journal of Neuroscience · doi:10.1080/00207454.2017.1394851 · Cited by 15
Spinocerebellar ataxia type 2 with glial cell cytoplasmic inclusions
Probst‐Cousin, S. (2004) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2003.011825 · Cited by 14
Lee, J., Shin, H.-J., Chang, C., & Paik, S. R. (1998) · Neurochemical Research · doi:10.1023/a:1020711025418 · Cited by 14
Caminati, G., Martina, M. R., Menichetti, S., & Procacci, P. (2019) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2019.1667342 · Cited by 13
miR-101a-3p Impairs Synaptic Plasticity and Contributes to Synucleinopathy
Xylaki, M., Paiva, I., Al‐Azzani, M., Gerhardt, E., Jain, G., Islam, R., Vasili, E., Wassouf, Z., Schulze-Hentrich, J. M., Fischer, A., et al. (2023) · Journal of Parkinson s Disease · doi:10.3233/jpd-225055 · Cited by 13
Calogero, A. M., Basellini, M. J., Isilgan, H. B., Longhena, F., Bellucci, A., Mazzetti, S., Rolando, C., Pezzoli, G., & Cappelletti, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512287 · Cited by 13
Sano, T., Nagata, T., Ebihara, S., Yoshida‐Tanaka, K., Nakamura, A., Sasaki, A., Shimozawa, A., Mochizuki, H., Uchihara, T., Hasegawa, M., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01766-3 · Cited by 16
Mekala, S., Wu, Y., & Li, Y. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00576g · Cited by 13
Ramalingam, M., Jang, S., & Jeong, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052322 · Cited by 14
Franco, A., Cuéllar, J., Fernández-Higuero, J. Á., de la Arada, I., Orozco, N., Valpuesta, J., Prado, A., & Muga, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312983 · Cited by 13
The Therapeutic Potential of LRRK2 and α-Synuclein in Parkinson's Disease
Sen, S., & West, A. B. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2430 · Cited by 12
Solmaz, V., Özlece, H. K., Eroğlu, H. A., Aktuğ, H., Erbaş, O., & Taşkıran, D. (2017) · Neurology Research International · doi:10.1155/2017/5952149 · Cited by 13
Zhang, S., Feng, R., Li, Y., Gan, L., Zhou, F., Meng, S., Li, Q., & Wen, T. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.03.010 · Cited by 13
The Paradoxical Cell Biology of α-Synucle
Roy, S. (2009) · Results and problems in cell differentiation · doi:10.1007/400_2009_23 · Cited by 13
α-Synuclein protein is not scavenged in neuronal loss induced by kainic acid or focal ischemia
Kitamura, Y., Ishida, Y., Takata, K., Kakimura, J., Mizutani, H., Shimohama, S., Akaike, A., & Taniguchi, T. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02159-x · Cited by 13
Sukhanova, A. V., Poly, S., Shemetov, A. A., Bronstein, I. B., & Nabiev, I. R. (2012) · Biopolymers · doi:10.1002/bip.22055 · Cited by 14
The Biochemistry of Alzheimer??s Disease
Stege, G. J. J., & Bosman, G. J. C. G. M. (1999) · Drugs & Aging · doi:10.2165/00002512-199914060-00004 · Cited by 13
Target-binding behavior of IDPs via pre-structured motifs
Kim, D.-H., & Han, K. (2021) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2021.07.031 · Cited by 12
Exploring the effect of APOE ε4 on biomarkers of neurodegeneration in Alzheimer’s disease
Agnello, L., Gambino, C. M., Ciaccio, A. M., Piccoli, T., Blandino, V., Scazzone, C., Sasso, B. L., Ben, F. D., & Ciaccio, M. (2024) · Clinica Chimica Acta · doi:10.1016/j.cca.2024.119876 · Cited by 12
Bharathi, P., Nagabhushan, P. N., & Rao, K. S. J. (2008) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2008.08.008 · Cited by 12
Levigoureux, E., Bouillot, C., Baron, T., Zimmer, L., & Lancelot, S. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12978 · Cited by 12
Downregulation of α-Synuclein Protein Levels by an Intracellular Single-Chain Antibody
Chen, Y., Yu, S., Wu, K., Wang, Y.-S., Tsai, H.-M., Liao, L.-W., Chen, S., Hsieh, W., Chen, H., Hsu, S., et al. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-191787 · Cited by 12
Initiative, A. D. N., Li, J., Bi, Y., Shen, X., Wang, H.-F., Xu, W., Tan, C., Dong, Q., Wang, Y., Tan, L., et al. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00222-1 · Cited by 12
α-Synuclein and neuronal membranes: Conformational flexibilities in health and disease
Bozelli, J. C., Kamski‐Hennekam, E. R., Melacini, G., & Epand, R. M. (2021) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2020.105034 · Cited by 13
C-terminal truncation of α -synuclein alters DNA structure from extension to compaction
Jiang, K., Rocha, S., Kumar, R., Westerlund, F., & Wittung-Stafshede, P. E. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.06.059 · Cited by 12
Buffering capacity is determinant for restoring early α-synuclein aggregation
Saraiva, M. A., & Florêncio, M. H. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106760 · Cited by 12
The Synucleins and the Astrocyte
Myers, A. J., Brahimi, A., Jenkins, I. J., & Koob, A. O. (2023) · Biology · doi:10.3390/biology12020155 · Cited by 12
The metabolomics of alpha-synuclein (SNCA) gene deletion and mutation in mouse brain
Musgrove, R. E., Horne, J., Wilson, R., King, A. E., Edwards, L. M., & Dickson, T. C. (2013) · Metabolomics · doi:10.1007/s11306-013-0561-6 · Cited by 12
Alternative Structures of α-Synuclein
Dułak, D., Gadzała, M., Banach, M., Konieczny, L., & Roterman, I. (2020) · Molecules · doi:10.3390/molecules25030600 · Cited by 12
“Janus-Faced” α-Synuclein: Role in Parkinson’s Disease
Ray, B., Mahalakshmi, A. M., Tuladhar, S., Bhat, A., Srinivasan, A., Pellegrino, C., Kannan, A., Bolla, S. R., Chidambaram, S. B., & Sakharkar, M. K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.673395 · Cited by 14
Examining the Toxicity of α-Synuclein in Neurodegenerative Disorders
Shan, F. Y., Fung, K., Zieneldien, T., Kim, J., Cao, C., & Huang, J. H. (2021) · Life · doi:10.3390/life11111126 · Cited by 13
Caenorhabditis Elegans as a Model for Human Synucleopathies
Vartiainen, S. (2007) · Cited by 12
The Gut–Brain Axis in Parkinson's DiseasePreprint
Gao, V., Crawford, C. V., & Burré, J. (2024) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041618 · Cited by 15
Pieger, K., Schmitt, V., Gauer, C., Gießl, N., Prots, I., Winner, B., Winkler, J., Brandstätter, J. H., & Xiang, W. (2022) · Biomolecules · doi:10.3390/biom12081108 · Cited by 11
Devi, S., Garg, D. K., & Bhat, R. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140917 · Cited by 11
Kubo, S. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1086340 · Cited by 11
Latchoumycandane, C., Brahadeeswaran, S., & Lateef, M. (2022) · Current Molecular Medicine · doi:10.2174/1566524022666220203163631 · Cited by 11
Lysophospholipids: A Potential Drug Candidates for Neurodegenerative Disorders
Karaki, T., Haniu, H., Matsuda, Y., & Tsukahara, T. (2022) · Biomedicines · doi:10.3390/biomedicines10123126 · Cited by 11
Vinueza‐Gavilanes, R., Bravo-González, J. J., Basurco, L., Boncristiani, C., Fernández‐Irigoyen, J., Santamaría, E., Marcilla, I., Pérez‐Mediavilla, A., Luquín, M. R., Vales, Á., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106166 · Cited by 11
Arévalo-Villalobos, J. I., Govea‐Alonso, D. O., Monreal‐Escalante, E., Zarazúa, S., & Rosales‐Mendoza, S. (2017) · Planta · doi:10.1007/s00425-017-2675-y · Cited by 11
Dedic, J., Rocha, S., Okur, H. İ., Wittung-Stafshede, P. E., & Roke, S. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b11096 · Cited by 12
Dong, C., Garen, C., Mercier, P., Petersen, N., & Woodside, M. (2019) · Protein Science · doi:10.1002/pro.3684 · Cited by 10
Protein Folding and Aggregation in in vitro Models of Parkinson's Disease
Eliezer, D. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374028-1.00042-7 · Cited by 11
α-Synuclein Aggregation and Parkinson’s Disease
Uversky, V. N. (2007) · Springer eBooks · doi:10.1007/978-0-387-36534-3_4 · Cited by 11
Mattson, M. (1999) · doi:10.1002/(sici)1097-4547(19991001)58:1
Goodrum (2000) · doi:10.1002/(sici)1097-4547(20000215)59:4
Louis (1999) · doi:10.1002/1531-8257(199905)14:3
Metadata
- 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)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1995-02
- Volume
- 14
- Issue
- 2
- Pages
- 467-475
- ISSN
- 0896-6273 (ISSN-L)
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review