The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
Abstract
To learn about the carboxy-terminal extent of amyloid beta-protein (A beta) composition of senile plaques (SPs) in the brain affected with Alzheimer's disease (AD), we employed two end-specific monoclonal antibodies as immunocytochemical probes: one is specific for A beta 40, the carboxyl terminus of A beta 1-40, while the other is specific for A beta 42(43). In the AD cortex, all SPs that were labeled with an authentic antibody were A beta 42(43) positive, while only one-third of which, on the average, were A beta 40 positive. There was a strong correlation between A beta 40 positivity and mature plaques. Two familial AD cortices with the mutation of beta-amyloid protein precursor 717 (beta APP717) (Val to Ile) showed a remarkable predominance of A beta 42(43)-positive, A beta 40-negative plaques. Diffuse plaques, representing the earliest stage of A beta deposition, were exclusively positive for A beta 42(43), but completely negative for A beta 40.
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In the citing paper
“These observations indicate that Aps ending at Ap42(43), which are a minor component of the Ap in human cerebrospinal fluid and plasma, are critically important in AD where they deposit selectively in plaques of all kinds.”
From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [21]
In the citing paper
“The immunocytochemical results shown here and in a recent report by Iwatsubo et al. (21) demonstrate that BC-05 intensely stains all types of senile plaques, that vessels are stained by both BC-OS and BA-27, and that BA-27 stains plaques poorly, in many cases only faintly staining occasional cored plaques (Fig. 3).”
From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [21]
In the citing paper
“From studies of trisomy 21 brains (Iwatsubo et al., 1994), it is generally believed that, in human AD, A deposition begins with the formation of diffuse plaques.”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“there is good evidence that A1-42 is deposited early and selectively in senile plaques (Iwatsubo et al., 1994).”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“In contrast, Aβ40, the major Aβ peptide secreted by cells, appears to be the predominant species deposited in the amyloid deposits in the cerebral vasculature (congophillic angiopathy, CAA) (Gravina et al., 1995; Iwatsubo et al., 1994).”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“These data provide definitive in vivo confirmation of predictions inferred from (1) in vitro studies of Aβ aggregation, (2) effects of PS and certain APP mutations on Aβ production and deposition, and (3) analyses of Aβ peptides in the human AD brain (Gravina et al., 1995; Iwatsubo et al., 1994).”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“Indeed, Aβ42 is the main component of amyloid plaques and is shown to be neurotoxic [30].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [30]
In the citing paper
“the slightly longer Aβ42 species that is specifically linked with FAD is also the first Aβ species deposited in cerebral plaques [82].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [82]
In the citing paper
“The subsequent development of antibodies directed at the free C-terminal ends of Aβ40 or Aβ42 [82] led to the ability to differentiate Aβ from APP labeling”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [82]
Citations
Cites
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
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
The molecular pathology of Alzheimer's disease
Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708
Diagnosis of Alzheimer's Disease
Khachaturian, Z. S. (1985) · Archives of Neurology · doi:10.1001/archneur.1985.04060100083029 · Cited by 2,499
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
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Choucair, A., Chakrapani, M., Chakravarthy, B., Katsaras, J., & Johnston, L. J. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.005 · Cited by 105
APP Function and Lipids: A Bidirectional Link
Grimm, M. O. W., Mett, J., Grimm, H. S., & Hartmann, T. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00063 · Cited by 104
Head, E., Azizeh, B. Y., Lott, I. T., Tenner, A. J., Cotman, C. W., & Cribbs, D. H. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0380 · Cited by 103
van Horssen, J., Otte‐Höller, I., David, G., Maat–Schieman, M. L. C., van den Heuvel, L. P., Wesseling, P., de Waal, R. M., & Verbeek, M. M. (2001) · Acta Neuropathologica · doi:10.1007/s004010100414 · Cited by 103
Ferreira, L. K., & Busatto, G. F. (2011) · Clinics · doi:10.1590/s1807-59322011001300003 · Cited by 102
Alexandru, A., Jagla, W., Graubner, S., Becker, A., Bäuscher, C., Kohlmann, S., Sedlmeier, R., Raber, K. A., Cynis, H., Rönicke, R., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.1794-11.2011 · Cited by 102
Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1–42) and Amyloid Beta(1–40)
Zheng, W., Tsai, M., & Wolynes, P. G. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b08089 · Cited by 102
The cellular model for Alzheimer's disease research: PC12 cells
Xie, D., Deng, T., Zhai, Z., Sun, T., & Xu, Y. D. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1016559 · Cited by 107
Cardiac Disorders as Risk Factors for Alzheimer's Disease
Alves, T. C. T. F., Ferreira, L. K., Wajngarten, M., & Busatto, G. F. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091561 · Cited by 107
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Pan, L., & Patterson, J. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070681 · Cited by 102
Presenilins are not required for Aβ42 production in the early secretory pathway
Wilson, C., Doms, R. W., Zheng, H., & Lee, V. M. ‐. (2002) · Nature Neuroscience · doi:10.1038/nn898 · Cited by 101
Styrylbenzoxazole Derivatives forIn VivoImaging of Amyloid Plaques in the Brain
Okamura, N., Suemoto, T., Shimadzu, H., Suzuki, M., Shiomitsu, T., Akatsu, H., Yamamoto, T., Staufenbiel, M., Yanai, K., Arai, H., et al. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4456-03.2004 · Cited by 100
Protein coding of neurodegenerative dementias: the neuropathological basis of biomarker diagnostics
Kovács, G. G., Botond, G., & Budka, H. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0658-1 · Cited by 102
Panza, F., Solfrizzi, V., Imbimbo, B. P., Tortelli, R., Santamato, A., & Logroscino, G. (2014) · Expert Review of Clinical Immunology · doi:10.1586/1744666x.2014.883921 · Cited by 103
α-Helix Mimetics as Modulators of Aβ Self-Assembly
Kumar, S., & Hamilton, A. D. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b09734 · Cited by 99
Li, X., & Buxbaum, J. N. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-79 · Cited by 104
Hiruma, H., Katakura, T., Takahashi, S., Ichikawa, T., & Kawakami, T. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08967.2003 · Cited by 114
Is there still any hope for amyloid-based immunotherapy for Alzheimer's disease?
Panza, F., Logroscino, G., Imbimbo, B. P., & Solfrizzi, V. (2014) · Current Opinion in Psychiatry · doi:10.1097/yco.0000000000000041 · Cited by 101
Active γ‐secretase is localized to detergent‐resistant membranes in human brain
Hur, J., Welander, H., Behbahani, H., Aoki, M., Frånberg, J., Winblad, B. G., Frykman, S., & Tjernberg, L. O. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06278.x · Cited by 100
The JNK/c-Jun cascade and Alzheimer's disease
Okazawa, H., & Estus, S. (2002) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/153331750201700209 · Cited by 98
Shin, R., Ogino, K., Kondo, A., Saido, T. C., Trojanowski, J. Q., Kitamoto, T., & Tateishi, J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-21-08187.1997 · Cited by 96
Miyashita, N., Straub, J. E., & Thirumalai, D. (2009) · Journal of the American Chemical Society · doi:10.1021/ja905457d · Cited by 98
Binding of Gelsolin, a Secretory Protein, to Amyloid β-Protein
Chauhan, V. P. S., Ray, I., Chauhan, A., & Wı́sniewski, H. M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0623 · Cited by 98
Boada, M., Anaya, F., Ortiz, P., Olazarán, J., Shua-Haim, J. R., Obisesan, T. O., Hernández, I., Muñoz, J., Buendia, M., Alegret, M., et al. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160565 · Cited by 94
Talking Point on the role of presenilin mutations in Alzheimer disease
Strooper, B. D. (2007) · Cited by 97
Notarachille, G., Arnesano, F., Calò, V., & Meleleo, D. (2014) · BioMetals · doi:10.1007/s10534-014-9719-6 · Cited by 97
AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species
Ruggeri, F. S., Habchi, J., Cerreta, A., & Dietler, G. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160518141911 · Cited by 92
Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Ohashi, R., Takegoshi, K., Nagao, M., Shimizu, T., & Shirasawa, T. (2005) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.99.437 · Cited by 104
Cerebral amyloid angiopathy: pathogenetic mechanisms and link to dense amyloid plaques
Kumar‐Singh, S. (2008) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00380.x · Cited by 101
Galimberti, D., Venturelli, E., Fenoglio, C., Guidi, I., Villa, C., Bergamaschini, L. C., Cortini, F., Scalabrini, D., Baron, P., Vergani, C., et al. (2008) · Journal of Neurology · doi:10.1007/s00415-008-0737-6 · Cited by 94
Amadoro, G., Corsetti, V., Atlante, A., Florenzano, F., Capsoni, S., Bussani, R., Mercanti, D., & Calissano, P. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.08.001 · Cited by 95
Clinical, Pathological, and Biochemical Spectrum of Alzheimer Disease Associated With PS-1 Mutations
Lleó, A., Berezovska, O., Growdon, J. H., & Hyman, B. T. (2004) · American Journal of Geriatric Psychiatry · doi:10.1097/00019442-200403000-00006 · Cited by 94
Mann, D. M. A., Iwatsubo, T., Pickering-Brown, S. M., Owen, F., Saido, T. C., & Perry, R. H. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(96)13294-8 · Cited by 91
Self-citationGM1 Ganglioside-Bound Amyloid β-Protein in Alzheimer’s Disease Brain
Yanagisawa, K., & Ihara, Y. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00032-3 · Cited by 90
Self-citationBiological function of Presenilin and its role in AD pathogenesis
Zhang, S., Zhang, M., Cai, F., & Song, W. (2013) · Translational Neurodegeneration · doi:10.1186/2047-9158-2-15 · Cited by 97
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Tokuda, T., Fukushima, T., Ikeda, S., Sekijima, Y., Shoji, S., Yanagisawa, N., & Tamaoka, A. (1997) · Annals of Neurology · doi:10.1002/ana.410410220 · Cited by 92
Tomita, T., Watabiki, T., Takikawa, R., Morohashi, Y., Takasugi, N., Kopan, R., Strooper, B. D., & Iwatsubo, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011152200 · Cited by 92
Self-citationKanatsu, K., Morohashi, Y., Suzuki, M., Kuroda, H., Watanabe, T., Tomita, T., & Iwatsubo, T. (2014) · Nature Communications · doi:10.1038/ncomms4386 · Cited by 99
Self-citationβ-Amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes
Deb, S., Wenjun Zhang, J., & Gottschall, P. E. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02344-8 · Cited by 81
Muñoz, F. J., & Inestrosa, N. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00468-8 · Cited by 91
Yamaguchi, H., Maat–Schieman, M. L. C., van Duinen, S. G., Prins, F. A., Neeskens, P., Natté, R., & Roos, R. A. C. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.8.723 · Cited by 91
Positron Emission Tomography Radiopharmaceuticals for Imaging Brain Beta-Amyloid
Vallabhajosula, S. (2011) · Seminars in Nuclear Medicine · doi:10.1053/j.semnuclmed.2011.02.005 · Cited by 95
Short Aβ peptides attenuate Aβ42 toxicity in vivo
Moore, B. D., Martin, J., de Mena, L., Sánchez, J., Cruz, P. E., Ceballos‐Diaz, C., Ladd, T. B., Ran, Y., Levites, Y., Kukar, T. L., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20170600 · Cited by 89
ANCA: A Family of Fluorescent Probes that Bind and Stain Amyloid Plaques in Human Tissue
Chang, W. M., Dakanali, M., Capule, C. C., Sigurdson, C. J., Yang, J., & Theodorakis, E. A. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200018v · Cited by 90
Cerebrospinal Fluid Aβ to Tau Ratio and Postoperative Cognitive Change
Xie, Z., McAuliffe, S., Swain, C. A., Ward, S. A. P., Crosby, C. A., Zheng, H., Sherman, J. C., Dong, Y., Zhang, Y., Sunder, N., et al. (2013) · Annals of Surgery · doi:10.1097/sla.0b013e318298b077 · Cited by 92
Sohma, Y., Hayashi, Y., Kimura, M., Chiyomori, Y., Taniguchi, A., Sasaki, M., Kimura, T., & Kiso, Y. (2005) · Journal of Peptide Science · doi:10.1002/psc.649 · Cited by 90
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Yamada, K., Tanaka, T., Mamiya, T., Shiotani, T., Kameyama, T., & Nabeshima, T. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702309 · Cited by 92
Chen, J., Armstrong, A. H., Koehler, A. N., & Hecht, M. H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja107552s · Cited by 89
Strack, S., Zaucha, J. A., Ebner, F. F., Colbran, R. J., & Wadzinski, B. E. (1998) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19980323)392:4 · Cited by 181
Correlation Between Aβx-40–, Aβx-42–, and Aβx-43–Containing Amyloid Plaques and Cognitive Decline
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Golde, T. E. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00523-1 · Cited by 98
Kurt, M. A., Davies, D. C., Kidd, M., Duff, K., Rolph, S. C., JENNINGS, K. H., & Howlett, D. R. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7717 · Cited by 89
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Horsburgh, K. J., Cole, G. M., Yang, F., Savage, M. J., Greenberg, B., Gentleman, S. M., Graham, D. I., & Nicoll, J. A. R. (2000) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2000.026002124.x · Cited by 88
Sharma, B., Singh, N., & Singh, M. (2008) · Journal of Psychopharmacology · doi:10.1177/0269881107081553 · Cited by 88
Ishii, K., Tamaoka, A., Mizusawa, H., Shoji, S.-I., Ohtake, T., Fraser, P. E., Takahashi, H., Tsuji, S., Gearing, M., Mizutani, T., et al. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01363-7 · Cited by 85
Self-citationRecent developments in biological aspects of chalcones: the odyssey continues
Rani, A., Ȧnand, A., Kumar, K., & Kumar, V. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1573812 · Cited by 87
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Murphy, M. P., Beckett, T. L., Ding, Q., Patel, E., Markesbery, W. R., Clair, D. K. S., LeVine, H., & Keller, J. N. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.06.002 · Cited by 87
Ordóñez‐Gutiérrez, L., Re, F., Bereczki, E., Ioja, E., Gregori, M., Andersen, A. J., Antón, M., Moghimi, S. M., Pei, J.-J., Masserini, M., et al. (2014) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2014.09.015 · Cited by 86
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Theuns, J. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.16.2383 · Cited by 89
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Dezutter, N. A., Dom, R., de Groot, T., Bormans, G., & Verbruggen, A. (1999) · European Journal of Nuclear Medicine · doi:10.1007/s002590050470 · Cited by 73
Potter, H. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00308-6 · Cited by 87
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Roher, A. E., Baudry, J. Y., Chaney, M. O., Kuo, Y., Stine, W. B., & Emmerling, M. R. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00030-2 · Cited by 89
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Sawamura, N., Morishima‐Kawashima, M., Waki, H., Kobayashi, K., Kuramochi, T., Frosch, M. P., Ding, K., Ito, M., Kim, T., Tanzi, R. E., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004308200 · Cited by 89
Self-citationTian, L., Guo, R., Yue, X., Lv, Q., Ye, X., Wang, Z., Chen, Z., Wu, B., Xu, G., & Liu, X. (2012) · Brain Research · doi:10.1016/j.brainres.2011.12.059 · Cited by 84
Schmidt, M. L., Schuck, T., Sheridan, S., Kung, M., Kung, H. F., Zhuang, Z., Bergeron, C., Lamarche, J. S., Skovronsky, D., Giasson, B. I., et al. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61769-5 · Cited by 86
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Lichtenthaler, S. F., Ida, N., Multhaup, G., Masters, C. L., & Beyreuther, K. T. (1997) · Biochemistry · doi:10.1021/bi971071m · Cited by 86
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Tycko, R. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00123-x · Cited by 86
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Harman, D. (1995) · AGE · doi:10.1007/bf02436085 · Cited by 87
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Mochizuki, A., Tamaoka, A., Shimohata, A., Komatsuzaki, Y., & Shoji, S. (2000) · The Lancet · doi:10.1016/s0140-6736(99)04937-5 · Cited by 85
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Usui, K., Hulleman, J. D., Paulsson, J. F., Siegel, S. J., Powers, E. T., & Kelly, J. W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804758106 · Cited by 84
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Takasugi, N., Sasaki, T., Ebinuma, I., Osawa, S., Isshiki, H., Takeo, K., Tomita, T., & Iwatsubo, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064050 · Cited by 85
Self-citationLandman, N., & Kim, T. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2004.04.001 · Cited by 85
Steiner, H., Révész, T., Neumann, M., Romig, H., Grim, M. G., Pesold, B., Kretzschmar, H. A., Hardy, J., Holton, J. L., Baumeister, R., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007183200 · Cited by 89
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Ikonomović, M. D., Klunk, W. E., Abrahamson, E. E., Wuu, J., Mathis, C. A., Scheff, S. W., Mufson, E. J., & DeKosky, S. T. (2011) · Neurology · doi:10.1212/wnl.0b013e3182231419 · Cited by 82
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Sani, S., Traul, D., Klink, A., Niaraki, N., Gonzalo-Ruiz, A., Wu, C.-K., & Geula, C. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0626-5 · Cited by 83
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Chauhan, N. B., & Sandoval, J. (2007) · Phytotherapy Research · doi:10.1002/ptr.2122 · Cited by 86
Histopathological studies of senile plaques and cerebral amyloidosis in cynomolgus monkeys
Nakamura, S., Nakayama, H., Naoaki, G. O. T. O., Ono, F., Sakakibara, I., & Yoshikawa, Y. (1998) · Journal of Medical Primatology · doi:10.1111/j.1600-0684.1998.tb00244.x · Cited by 84
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Guerra, B., Díaz, M. L., Alonso, R., & Marín, R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02695.x · Cited by 82
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Andreasen, N., & Blennow, K. (2002) · Peptides · doi:10.1016/s0196-9781(02)00056-6 · Cited by 86
Ratan, Y., Rajput, A., Maleysm, S., Pareek, A., Jain, V. K., Pareek, A., Kaur, R., & Singh, G. (2023) · Biomedicines · doi:10.3390/biomedicines11051398 · Cited by 89
Schlenzig, D., Rönicke, R., Cynis, H., Ludwig, H., Scheel, E., Reymann, K. G., Saido, T. C., Hause, G., Schilling, S., & Demuth, H. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07707.x · Cited by 83
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Savonenko, A. V., Xu, G. M., Price, D. L., Borchelt, D. R., & Markowska, A. L. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(02)00012-8 · Cited by 63
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Mak, K., Yang, F., Vinters, H. V., Frautschy, S. A., & Cole, G. M. (1994) · Brain Research · doi:10.1016/0006-8993(94)91725-6 · Cited by 80
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Janciauskiene, S. M., de Frutos, P. G., Carlemalm, E., Dahlbäck, B., & Eriksson, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.44.26041 · Cited by 82
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Capurro, V., Busquet, P., Lopes, J. P., Bertorelli, R., Tarozzo, G., Bolognesi, M. L., Piomelli, D., Reggiani, A. M., & Cavalli, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056870 · Cited by 79
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Olofsson, A., Lindhagen‐Persson, M., Sauer-Eriksson, A. E., & Öhman, A. (2007) · Biochemical Journal · doi:10.1042/bj20061561 · Cited by 80
Metadata
- Authors
- Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y.
- Affiliations
- Takeda (Japan) (JP)
- The University of Tokyo (JP)
- University of Tsukuba (JP)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1994-07
- Volume
- 13
- Issue
- 1
- Pages
- 45-53
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1991435932
- Cited by
- 1,774
- References
- 41
- Citations by year
- 2026: 30 · 2025: 41 · 2024: 53 · 2023: 49 · 2022: 49 · 2021: 55 · 2020: 68 · 2019: 49 · 2018: 41 · 2017: 49 · 2016: 52 · 2015: 45 · 2014: 68 · 2013: 69 · 2012: 66
- FWCI
- 35.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, Aβ40, amyloid plaques, Alzheimer's disease, familial Alzheimer's disease, plaque maturation, diffuse plaques, immunocytochemistry
- MeSH terms
- Adult, Aged, Aged, 80 and over, Alzheimer Disease, Antibodies, Monoclonal, Brain, Cerebral Cortex, Female, Humans, Immunoenzyme Techniques, Male, Middle Aged, Mutation, Peptide Fragments, Amyloid beta-Peptides
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