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Evidence For and Against a Pathogenic Role of Reduced γ-Secretase Activity in Familial Alzheimer’s Disease

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Metabolic disorder in Alzheimer’s disease

Poddar, M. K., Banerjee, S., Chakraborty, A., & Dutta, D. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00673-z · Cited by 58

Folate/vitamin-B12 Prevents Chronic Hyperhomocysteinemia-Induced Tau Hyperphosphorylation and Memory Deficits in Aged Rats

Wei, W., Liu, Y., Zhang, C.-E., Wang, Q., Wei, Z., Mousseau, D. D., Wang, J., Tian, Q., & Liu, G. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110770 · Cited by 55

Exploration of the mechanism for LPFFD inhibiting the formation of β-sheet conformation of Aβ(1–42) in water

Cao, Y., Zhu, X., Li, J., & Shi, R. (2010) · Journal of Molecular Modeling · doi:10.1007/s00894-009-0594-y · Cited by 55

Aβ42 gene vaccine prevents Aβ42 deposition in brain of double transgenic mice

Qu, B., Xiang, Q., Li, L., Johnston, S. A., Hynan, L. S., & Rosenberg, R. N. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.05.012 · Cited by 55

Amyloid beta-protein and lipid metabolism

Zinser, E. G., Hartmann, T., & Grimm, M. O. W. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.014 · Cited by 55

A new structural model of Alzheimer’s Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling

Gu, L., Tran, J., Jiang, L., & Guo, Z. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.01.013 · Cited by 56

Ab initio model studies of copper binding to peptides containing a His–His sequence: relevance to the β-amyloid peptide of Alzheimer’s disease

Raffa, D. F., Gómez‐Balderas, R., Brunelle, P., Rickard, G. A., & Rauk, A. (2005) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-005-0038-9 · Cited by 56

Apolipoprotein E Genotype and Deposits of Aβ40 and Aβ42 in Alzheimer Disease

McNamara, M. J., Gómez‐Isla, T., & Hyman, B. T. (1998) · Archives of Neurology · doi:10.1001/archneur.55.7.1001 · Cited by 55

Search for dual function inhibitors for Alzheimer’s disease: Synthesis and biological activity of acetylcholinesterase inhibitors of pyridinium-type and their Aβ fibril formation inhibition capacity

Kapková, P., Alptüzün, V., Frey, P., Erciyas, E., & Holzgrabe, U. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.08.034 · Cited by 54

Modeling neurodegenerative diseases with patient-derived induced pluripotent cells: Possibilities and challenges

Poon, A., Zhang, Y., Chandrasekaran, A., Phanthong, P., Schmid, B., Nielsen, T. T., & Freude, K. (2017) · New Biotechnology · doi:10.1016/j.nbt.2017.05.009 · Cited by 54

Transgenic mice expressing the PS1-A246E mutation: effects on spatial learning, exploration, anxiety, and motor coordination

Lalonde, R., Qian, S., & Strazielle, C. (2002) · Behavioural Brain Research · doi:10.1016/s0166-4328(02)00230-9 · Cited by 54

Negative association between amyloid plaques and cerebral amyloid angiopathy in Alzheimer's disease

Tian, J., Shi, J., Bailey, K. L., & Mann, D. M. A. (2003) · Neuroscience Letters · doi:10.1016/j.neulet.2003.08.048 · Cited by 53

Ultrastructural evidence of early non-fibrillar Aβ42 in the capillary basement membrane of patients with hereditary cerebral hemorrhage with amyloidosis, Dutch type

Natté, R., Yamaguchi, H., Maat–Schieman, M. L. C., Prins, F. A., Neeskens, P., Roos, R. A. C., & van Duinen, S. G. (1999) · Acta Neuropathologica · doi:10.1007/s004010051121 · Cited by 54

N-truncated Abeta starting with position four: Early intraneuronal accumulation and rescue of toxicity using NT4X-167, a novel monoclonal antibody

Antonios, G., Saiepour, N., Bouter, Y., Richard, B. C., Paetau, A., Verkkoniemi-Ahola, A., Lannfelt, L., Ingelsson, M., Kovacs, G. G., Pillot, T., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-56 · Cited by 53

Proinflammatory cytokine interferon‐γ increases induction of indoleamine 2,3‐dioxygenase in monocytic cells primed with amyloid β peptide 1–42: implications for the pathogenesis of Alzheimer’s disease

Yamada, A., Akimoto, H., Kagawa, S., Guillemin, G. J., & Takikawa, O. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06175.x · Cited by 58

Alzheimer Patients Treated With an AchE Inhibitor Show Higher IL-4 and Lower IL-1β Levels and Expression in Peripheral Blood Mononuclear Cells

Gambi, F., Reale, M., Iarlori, C., Salone, A., Toma, L., Paladini, C., Luca, G. D., Feliciani, C., Salvatore, M., Salerno, R. M., et al. (2004) · Journal of Clinical Psychopharmacology · doi:10.1097/01.jcp.0000125683.74595.2f · Cited by 53

Amyloid-β peptide structure in aqueous solution varies with fragment size

Wise-Scira, O., Xu, L., Kitahara, T., Perry, G. L., & Coskuner‐Weber, O. (2011) · The Journal of Chemical Physics · doi:10.1063/1.3662490 · Cited by 53

Dietary lipids and their oxidized products in Alzheimer's disease

Corsinovi, L., Biasi, F., Poli, G., Leonarduzzi, G., & Isaia, G. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100208 · Cited by 54

Transmembrane Fragment Structures of Amyloid Precursor Protein Depend on Membrane Surface Curvature

Domı́nguez, L., Meredith, S. C., Straub, J. E., & Thirumalai, D. (2013) · Journal of the American Chemical Society · doi:10.1021/ja410958j · Cited by 53

Physiological and pathological roles of the γ-secretase complex

Carroll, C. M., & Li, Y. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.04.019 · Cited by 58

Clinical significance of fluid biomarkers in Alzheimer’s Disease

Lewczuk, P., Łukaszewicz‐Zając, M., Mroczko, P., & Kornhuber, J. (2020) · Pharmacological Reports · doi:10.1007/s43440-020-00107-0 · Cited by 56

The Swedish APP670/671 Alzheimer’s Disease Mutation: The First Evidence for Strikingly Increased Oxidative Injury in the Temporal Inferior Cortex

Bogdanović, N., Zilmer, M., Zilmer, K., Rehema, A., & Karelson, E. (2001) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000051282 · Cited by 53

Amyloid (Aβ) deposition in chromosome 1–linked Alzheimer's disease: The volga german families

Mann, D. M. A., Iwatsubo, T., Nochlin, D., Sumi, S. M., Levy‐Lahad, E., & Bird, T. D. (1997) · Annals of Neurology · doi:10.1002/ana.410410110 · Cited by 51

Long‐term deprivation of oestrogens by ovariectomy potentiates β‐amyloid‐induced working memory deficits in rats

Yamada, K., Tanaka, T., Zou, L., Senzaki, K., Yano, K., Osada, T., Olariu, A., Ren, X., Kameyama, T., & Nabeshima, T. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702811 · Cited by 55

Immunohistochemical analysis of COOH-termini of amyloid beta protein (Aβ) using end-specific antisera for Aβ40 and Aβ42 in Alzheimer's disease and normal aging

Yamaguchi, H., Sugihara, S., Ishiguro, K., Takashima, A., & Hirai, S. (1995) · Amyloid · doi:10.3109/13506129509031882 · Cited by 31

Amyloid β protein 1–42/43 (Aβ 1–42/43) in cerebellar diffuse plaques: enzyme-linked immunosorbent assay and immunocytochemical study

Tamaoka, A., Sawamura, N., Odaka, A., Suzuki, N., Mizusawa, H., Shoji, S., & Mori, H. (1995) · Brain Research · doi:10.1016/0006-8993(95)00162-j · Cited by 72

Amyloid β-protein ending at Thr43 is a minor component of some diffuse plaques in the Alzheimer's disease brain, but is not found in cerebrovascular amyloid

Iizuka, T., Shoji, M., Harigaya, Y., Kawarabayashi, T., Watanabe, M., Kanai, M., & Hirai, S. (1995) · Brain Research · doi:10.1016/0006-8993(95)01163-2 · Cited by 33

Amyloid beta protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance of A beta 42(43) and association of A beta 40 with cored plaques.

Fukumoto, H., Asami-Odaka, A., Suzuki, N., Shimada, H., Ihara, Y., & Iwatsubo, T. (1996) · Europe PMC (PubMed Central) · Cited by 108

Comparable amyloid β-protein (Aβ) 42(43) and Aβ40 deposition in the aged monkey brain

Kanemaru, K., Iwatsubo, T., & Ihara, Y. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)12893-7 · Cited by 27