{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T15:23:33Z","timestamp":1784561013826,"version":"3.55.0"},"reference-count":33,"publisher":"Japan Society of Histochemistry & Cytochemistry","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Acta Histochem. Cytochem.","Acta Histochemica et Cytochemica","Acta Histochem. Cytochem"],"published-print":{"date-parts":[[2023,12,28]]},"DOI":"10.1267\/ahc.23-00058","type":"journal-article","created":{"date-parts":[[2023,12,19]],"date-time":"2023-12-19T22:12:34Z","timestamp":1703023954000},"page":"87-94","source":"Crossref","is-referenced-by-count":6,"title":["Visualization of Amyloid Oligomers in the Brain of Patients with Alzheimer\u2019s Disease"],"prefix":"10.1267","volume":"56","author":[{"given":"Ikuo","family":"Tooyama","sequence":"first","affiliation":[{"name":"Medical Innovation Research Center, Shiga University of Medical Science"},{"name":"Molecular Neuroscience Research Center, Shiga University of Medical Science"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomoko","family":"Kato","sequence":"additional","affiliation":[{"name":"Medical Innovation Research Center, Shiga University of Medical Science"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyasu","family":"Taguchi","sequence":"additional","affiliation":[{"name":"Molecular Neuroscience Research Center, Shiga University of Medical Science"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yusuke","family":"Kageyama","sequence":"additional","affiliation":[{"name":"Medical Innovation Research Center, Shiga University of Medical Science"},{"name":"Education Center for Medicine and Nursing, Shiga University of Medical Science"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuhiro","family":"Irie","sequence":"additional","affiliation":[{"name":"Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yukie","family":"Hirahara","sequence":"additional","affiliation":[{"name":"Faculty of Nursing, Kansai Medical University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daijiro","family":"Yanagisawa","sequence":"additional","affiliation":[{"name":"Molecular Neuroscience Research Center, Shiga University of Medical Science"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"334","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"1 Abu Bakar, Z. H., Kato, T., Yanagisawa, D., Bellier, J. P., Mukaisho, K. and Tooyam, I. (2021) Immunohistochemical study of mitochondrial ferritin in the midbrain of patients with progressive supranuclear palsy. Acta Histochem. Cytochem. 54; 97\u2013104.","DOI":"10.1267\/ahc.21-00019"},{"key":"2","unstructured":"2 Alzheimer, A. (1907) u\u0308ber eine eigenartige Erkankung der Hirnrinde. Allgemeine Zeitschrift fur Psychiatrie under Psychisch-Gerichtliche Medizin. 64; 146\u2013148."},{"key":"3","doi-asserted-by":"crossref","unstructured":"3 Becker, R. E., Greig, N. H. and Giacobini, E. (2008) Why do so many drugs for Alzheimer\u2019s disease fail in development? Time for new methods and new practices? J. Alzheimers Dis. 15; 303\u2013325.","DOI":"10.3233\/JAD-2008-15213"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4 Braak, H. and Braak, E. (1996) Evolution of the neuropathology of Alzheimer\u2019s disease. Acta Neurol. Scand. Suppl. 165; 3\u201312.","DOI":"10.1111\/j.1600-0404.1996.tb05866.x"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5 Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., et al. (2005) Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat. Neurosci. 8; 79\u201384.","DOI":"10.1038\/nn1372"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6 Cline, E. M., Bicca, M. A., Viola, K. L. and Klein, W. M. (2018) The amyloid-oligomer hypothesis: beginning of the third decade. J. Alzheimer. Dis. 64; S567\u2013S610.","DOI":"10.3233\/JAD-179941"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7 Glenner, G. G. and Wong, C. W. (1984) Alzheimer\u2019s disease and Down\u2019s syndrome: Sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122; 1131\u20131135.","DOI":"10.1016\/0006-291X(84)91209-9"},{"key":"8","doi-asserted-by":"publisher","unstructured":"8 Goate, A., Chartier-Harlin, M. C., Mullan, M., Brown, J., Crawfold, F., Fidani, L., et al. (1991) Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer\u2019s disease. Nature 349; 704\u2013706.","DOI":"10.1038\/349704a0"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9 Hamaguchi, T., Ono, K. and Yamada, M. (2010) Review: Curcumin and Alzheimer\u2019s disease. CNS Neurosci. Ther. 16; 285\u2013297.","DOI":"10.1111\/j.1755-5949.2010.00147.x"},{"key":"10","doi-asserted-by":"publisher","unstructured":"10 Hardy, J. A. and Higgins, G. A. (1992) Alzheimer\u2019s disease: the amyloid cascade hypothesis. Science 256; 184\u2013185.","DOI":"10.1126\/science.1566067"},{"key":"11","doi-asserted-by":"publisher","unstructured":"11 Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer\u2019s disease: progress and problems on the road to therapeutics. Science 297; 353\u2013356.","DOI":"10.1126\/science.1072994"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12 Iqbal, K., Liu, F., Gong, C.-X. and Grundke-Iqbal, I. (2010) Tau in Alzheimer Disease and Related Tauopathies. Curr. Alzheimer Res. 7; 656\u2013664.","DOI":"10.2174\/156720510793611592"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13 Irie, K. (2020) New diagnostic method for Alzheimer\u2019s disease based on the toxic conformation theory of amyloid \u03b2. Biosci. Biotechnol. Biochem. 84; 1\u201316.","DOI":"10.1080\/09168451.2019.1667222"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14 Kageyama, Y., Irie, Y., Matsushima, Y., Segawa, T., Bellier, J. P., Hidaka, K., et al. (2021) Characterization of a conformation-restricted amyloid peptide and immunoreactivity of its antibody in human AD brain. ACS Chem. Neurosci. 12; 3418\u20133432.","DOI":"10.1021\/acschemneuro.1c00416"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15 Ko\u0308pke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K. and Grundke-Iqbal, I. (1993) Microtubule-associated protein tau. Abnormal phos-phorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268; 24374\u201324384.","DOI":"10.1016\/S0021-9258(20)80536-5"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16 Kuo, Y. M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., et al. (1996) Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains. J. Biol. Chem. 271; 4077\u20134081.","DOI":"10.1074\/jbc.271.8.4077"},{"key":"17","doi-asserted-by":"publisher","unstructured":"17 Long, J. M. and Holtzman, D. M. (2019) Alzheimer Disease: An Update on Pathobiology and Treatment Strategies. Cell 179; 312\u2013339.","DOI":"10.1016\/j.cell.2019.09.001"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18 Lue, L. F., Kuo, Y. M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., et al. (1999) Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer\u2019s disease. Am. J. Pathol. 155; 853\u2013862.","DOI":"10.1016\/S0002-9440(10)65184-X"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19 Masuda, Y., Uemura, S., Ohashi, R., Nakanishi, A., Takegoshi, K., Shimizu, T., et al. (2009) Identification of physiological and toxic conformations in Abeta42 aggregates. Chembiochem. 10; 287\u2013295.","DOI":"10.1002\/cbic.200800411"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20 Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L. and Beyreuther, K. (1985). Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl. Acad. Sci. U.S.A. 82; 4245\u20134249.","DOI":"10.1073\/pnas.82.12.4245"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21 Matsushima, Y., Yanagita, R. C. and Irie, K. (2020) Control of the toxic conformation of amyloid \u03b242 by intramolecular disulfide bond formation. Chem. Commun. 56; 4118\u20134121.","DOI":"10.1039\/D0CC01053G"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22 McLean, C. A., Cherny, R. A., Fraser, F. W., Fuller, S. J., Smith, M. J., Beyreuther, K., et al. (1999) Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer\u2019s disease. Ann. Neurol. 46; 860\u2013866.","DOI":"10.1002\/1531-8249(199912)46:6<860::AID-ANA8>3.0.CO;2-M"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23 Murakami, K., Hara, H., Masuda, Y., Ohigashi, H. and Irie, K. (2007) Distance measurement between Tyr10 and Met35 in amyloid beta by site-directed spin-labeling ESR spectroscopy: implications for the stronger neurotoxicity of Abeta42 than Abeta40. Chembiochem. 8; 2308\u20132314.","DOI":"10.1002\/cbic.200700240"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24 Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y., Masuda, Y., Kinoshita, N., et al. (2010) Monoclonal antibody against the turn of the 42-residue amyloid \u03b2-protein at positions 22 and 23. ACS Chem. Neurosci. 1; 747\u2013756.","DOI":"10.1021\/cn100072e"},{"key":"25","unstructured":"25 Prince, M., Albanese, E., Guerchet, M. and Prina, M. (2014) World Alzheimer Report 2014. Alzheimer\u2019s Disease International, London."},{"key":"26","unstructured":"26 Rueger, M. A., Kracht, L. W., Hilker, R., Thiel, A., Sobesky, J., Winkeler, A., et al. (2007) Role of in vivo imaging of the central nervous system for developing novel drugs. J. Nucl. Med. Mol. Imaging. 51; 164\u2013181."},{"key":"27","doi-asserted-by":"publisher","unstructured":"27 Sevigny, J., Chiao, P., Bussi\u00e8re, T., Weinreb, P. H., Williams, L., Maier, M., et al. (2016) The antibody aducanumab reduces A\u03b2 plaques in Alzheimer\u2019s disease. Nature 537; 50\u201356.","DOI":"10.1038\/nature19323"},{"key":"28","doi-asserted-by":"crossref","unstructured":"28 Tomiyama, T., Nagata, T., Shimada, H., Teraoka, R., Fukushima, A., Kanemitsu, H., et al. (2008) A new amyloid beta variant favoring oligomerization in Alzheimer\u2019s-type dementia. Ann. Neurol. 63; 377\u2013387.","DOI":"10.1002\/ana.21321"},{"key":"29","doi-asserted-by":"crossref","unstructured":"29 Tooyama, I., Yanagisawa, D., Taguchi, H., Kato, T., Hirao, K., Shirai, N., et al. (2016) Amyloid imaging using fluorine-19 magnetic resonance imaging (19F-MRI). Ageing Res. Rev. 30; 85\u201394.","DOI":"10.1016\/j.arr.2015.12.008"},{"key":"30","doi-asserted-by":"crossref","unstructured":"30 van Dyck, C. H., Swanson, C. J., Aisen, P., Bateman, R. J., Chen, C., Gee, M., et al. (2023) Lecanemab in Early Alzheimer\u2019s Disease. N. Eng. J. Med. 388; 9\u201321.","DOI":"10.1056\/NEJMoa2212948"},{"key":"31","doi-asserted-by":"publisher","unstructured":"31 Walsh, D. M. and Selkoe, D. J. (2004) Deciphering the molecular basis of memory failure in Alzheimer\u2019s disease. Neuron 44; 181\u2013193.","DOI":"10.1016\/j.neuron.2004.09.010"},{"key":"32","doi-asserted-by":"publisher","unstructured":"32 Yanagisawa, D., Shirai, N., Amatsubo, T., Taguchi, H., Hirao, K., Urushitani, M., et al. (2010) Relationship between the tautomeric structures of curcumin derivatives and their Abeta-binding activities in the context of therapies for Alzheimer\u2019s disease. Biomaterials 31; 4179\u20134185.","DOI":"10.1016\/j.biomaterials.2010.01.142"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33 Yanagisawa, D., Taguchi, H., Yamamoto, A., Shirai, N., Hirao, K. and Tooyama, I. (2011) Curcuminoids bind to Amyloid A\u00df1-42 oligomer and fibril. <i>J. Alzheimer Dis.<\/i> 24(supple 2); 33\u201342.","DOI":"10.3233\/JAD-2011-102100"}],"container-title":["ACTA HISTOCHEMICA ET CYTOCHEMICA"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/ahc\/56\/6\/56_23-00058\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,13]],"date-time":"2024-05-13T05:08:00Z","timestamp":1715576880000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/ahc\/56\/6\/56_23-00058\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,12,28]]},"references-count":33,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2023]]}},"URL":"https:\/\/doi.org\/10.1267\/ahc.23-00058","relation":{},"ISSN":["0044-5991","1347-5800"],"issn-type":[{"value":"0044-5991","type":"print"},{"value":"1347-5800","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,12,28]]},"article-number":"23-00058"}}