Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Barage, Sagar H.; Sonawane, Kailas D.

doi:10.1016/j.npep.2015.06.008

Cited by 588Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchCholinesterase and Neurodegenerative Diseases

Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Barage, Sagar H., Sonawane, Kailas D.·2015·Neuropeptides

DOI 10.1016/j.npep.2015.06.008

Open this paper in CoChat — free account

Abstract

Alzheimer's disease is an irreversible, progressive neurodegenerative disorder. Various therapeutic approaches are being used to improve the cholinergic neurotransmission, but their role in AD pathogenesis is still unknown. Although, an increase in tau protein concentration in CSF has been described in AD, but several issues remains unclear. Extensive and accurate analysis of CSF could be helpful to define presence of tau proteins in physiological conditions, or released during the progression of neurodegenerative disease. The amyloid cascade hypothesis postulates that the neurodegeneration in AD caused by abnormal accumulation of amyloid beta (Aβ) plaques in various areas of the brain. The amyloid hypothesis has continued to gain support over the last two decades, particularly from genetic studies. Therefore, current research progress in several areas of therapies shall provide an effective treatment to cure this devastating disease. This review critically evaluates general biochemical and physiological functions of Aβ directed therapeutics and their relevance.

Integrity signals

Registry

Crossref · 10.1016/j.npep.2015.06.008

Cites

367 of 367 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Low levels of corticotrophin-releasing hormone (CRH), somatostatin and neuropeptide Y, and higher levels of Angiotensin II, are likely involved in either irregular cleavage of APP or impaired removal of Aβ1-42 fragment.
“Apart from the genetic mutations, many neuropeptides are likely to be involved in the formation of the plaque for e.g. low levels of corticotrophin-releasing hormone (CRH), somatostatin and neuropeptide Y levels whereas higher levels of Angiotensin II are likely to be involved in either irregular cleavage of the APP or impaired removal of Aβ1-42 fragment [2].”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [2]
Aβ plaque comprises Aβ peptides obtained from amyloid precursor protein (APP) by enzymatic cleavage via secretases (α, β and γ).
“The Aβ plaque comprises of Aβ peptides obtained from amyloid precursor protein (APP) by the enzymatic cleavage via secretases (α, β and γ) [2].”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [2]

A novel potent vasoconstrictor peptide produced by vascular endothelial cells
Yanagisawa, M., Kurihara, H., Kimura, S., Tomobe, Y. I., Kobayashi, M., Mitsui, Y., Yazaki, Y., Goto, K., & Masaki, T. (1988) · Nature · doi:10.1038/332411a0 · Cited by 10,716 · see citing works
Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429 · see citing works
Mild Cognitive Impairment: Clinical Characterization and Outcome
Petersen, R. C., Smith, G. E., Waring, S. C., Ivnik, R. J., Tangalos, E. G., & Kokmen, E. (1999) · Archives of Neurology · doi:10.1001/archneur.56.3.303 · Cited by 8,980 · see citing works
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works
The cholinergic hypothesis of geriatric memory dysfunction
Bartus, R. T., Dean, R. L., Beer, B., & Lippa, A. S. (1982) · Science · doi:10.1126/science.7046051 · Cited by 5,545 · see citing works
2016 Alzheimer's disease facts and figures
Alzheimer's Association (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.001 · Cited by 5,069 · see citing works
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
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 · see citing works
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 · see citing works
Alzheimer’s disease
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · see citing works
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051 · see citing works
Apolipoprotein E: Cholesterol Transport Protein with Expanding Role in Cell Biology
Mahley, R. W. (1988) · Science · doi:10.1126/science.3283935 · Cited by 4,028 · see citing works
β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · cited 2× · see citing works
“Inhibition of β-secretase. β-Secretase is a novel transmembrane aspartate protease BACE-1, also called Asp2 and memapsin2 (Vassar et al., 1999).”
SELECTIVE LOSS OF CENTRAL CHOLINERGIC NEURONS IN ALZHEIMER'S DISEASE
DAVIES, P. (1976) · The Lancet · doi:10.1016/s0140-6736(76)91936-x · Cited by 3,565 · see citing works
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149 · see citing works
Alzheimer’s disease
Blennow, K., de Leon, M. J., & Zetterberg, H. (2006) · The Lancet · doi:10.1016/s0140-6736(06)69113-7 · Cited by 3,134 · see citing works
Candidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577 · see citing works
Molecular and Biotechnological Aspects of Microbial Proteases
Rao, M. B., Tanksale, A. M., Ghatge, M. S., & DESHPANDE, V. V. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.3.597-635.1998 · Cited by 2,274 · see citing works
The cholinergic hypothesis of Alzheimer’s disease: A review of progress
Francis, P. T., Palmer, A. M., Snape, M., & Wilcock, G. K. (1999) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.66.2.137 · Cited by 2,198 · cited 1× · see citing works
“Moreover, the adverse effects like gastrointestinal, cardiovascular, neuromuscular risks associated with these inhibitors are not negligible (Francis et al., 1999; Raschetti et al., 2007).”
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · see citing works
Alzheimer Disease in the US Population: Prevalence Estimates Using the 2000 Census
Hebert, L. E., Scherr, P. A., Bienias, J. L., Bennett, D. A., & Evans, D. A. (2003) · Archives of Neurology · doi:10.1001/archneur.60.8.1119 · Cited by 2,168 · see citing works
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,106 · see citing works
Decreased Clearance of CNS β-Amyloid in Alzheimer’s Disease
Mawuenyega, K. G., Sigurdson, W., Ovod, V., Munsell, L., Kasten, T., Morris, J. C., Yarasheski, K. E., & Bateman, R. J. (2010) · Science · doi:10.1126/science.1197623 · Cited by 2,078 · see citing works
Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature
Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · cited 1× · see citing works
“Also, the demonstrating direct Aβ-peptide neurotoxicity has beendifficult inmost animalmodel revealed the existence of key intermediate between amyloidosis and neurodegeneration (Nelson et al., 2012; Serrano-Pozo et al., 2013).”
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938 · see citing works
Angiotensin II cell signaling: physiological and pathological effects in the cardiovascular system
Mehta, P. K., & Griendling, K. K. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00287.2006 · Cited by 1,924 · see citing works
Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., & Selkoe, D. J. (1999) · Nature · doi:10.1038/19077 · Cited by 1,913 · see citing works
Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849 · see citing works
Apolipoprotein E: Far More Than a Lipid Transport Protein
Mahley, R. W., & Rall, S. C. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.507 · Cited by 1,836 · see citing works
Alzheimer Mechanisms and Therapeutic Strategies
Huang, Y., & Mucke, L. (2012) · Cell · doi:10.1016/j.cell.2012.02.040 · Cited by 1,758 · see citing works
Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
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 · see citing works
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 · see citing works
Practice parameter: Management of dementia (an evidence-based review) [RETIRED]
Doody, R. S., Stevens, J. E., Beck, C., Dubinsky, R., Kaye, J. A., Gwyther, L. P., Mohs, R. C., Thal, L. J., Whitehouse, P. J., DeKosky, S. T., et al. (2001) · Neurology · doi:10.1212/wnl.56.9.1154 · Cited by 1,703 · see citing works
Epidemiology of Alzheimer disease
Reitz, C., Brayne, C., & Mayeux, R. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.2 · Cited by 1,675 · see citing works
Phase 3 Trials of Solanezumab for Mild-to-Moderate Alzheimer's Disease
Doody, R. S., Thomas, R. G., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., Raman, R., Sun, X., Aisen, P. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1312889 · Cited by 1,668 · see citing works
The role of apolipoprotein E in Alzheimer's disease
Kim, J., Basak, J. M., & Holtzman, D. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.06.026 · Cited by 1,661 · see citing works
Somatostatin and Its Receptor Family
Patel, Y. (1999) · Frontiers in Neuroendocrinology · doi:10.1006/frne.1999.0183 · Cited by 1,648 · see citing works
A 24-week, double-blind, placebo-controlled trial of donepezil in patients with Alzheimer's disease
Rogers, S. L., Farlow, M. R., Doody, R. S., Mohs, R., Friedhoff, L. T., & Donepezil Study Group* (1998) · Neurology · doi:10.1212/wnl.50.1.136 · Cited by 1,618 · see citing works
Purification and cloning of amyloid precursor protein β-secretase from human brain
Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612 · see citing works
Translating cell biology into therapeutic advances in Alzheimer's disease
Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,588 · see citing works
An english translation of alzheimer’s 1907 paper, “über eine eigenartige erkankung der hirnrinde”
Stelzmann, R. A., Norman Schnitzlein, H., & Reed Murtagh, F. (1995) · Clinical Anatomy · doi:10.1002/ca.980080612 · Cited by 1,455 · see citing works
Tau is a candidate gene for chromosome 17 frontotemporal dementia
Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374 · see citing works
Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo
Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E., Frosch, M., Eckman, C., Tanzi, R., Selkoe, D., & Guénette, S. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0230450100 · Cited by 1,361 · see citing works
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324 · see citing works
NEUROTRANSMITTER-RELATED ENZYMES AND INDICES OF HYPOXIA IN SENILE DEMENTIA AND OTHER ABIOTROPHIES
Bowen, D. M., Smith, C. B., White, P., & DAVISON, A. N. (1976) · Brain · doi:10.1093/brain/99.3.459 · Cited by 1,313 · see citing works
APRIORITY
Asher, R. (1961) · The Lancet · doi:10.1016/s0140-6736(61)91217-x · Cited by 1,293 · see citing works
The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases
MCGEER, P., & MCGEER, E. (1995) · Brain Research Reviews · doi:10.1016/0165-0173(95)00011-9 · Cited by 1,287 · see citing works
Alzheimer’s disease: Clinical trials and drug development
Mangialasche, F., Solomon, A., Winblad, B., Mecocci, P., & Kivipelto, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70119-8 · Cited by 1,217 · see citing works
The ADAM metalloproteinases
Edwards, D. R., Handsley, M. M., & Pennington, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,165 · see citing works
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111 · see citing works
A phase 1 clinical trial of nerve growth factor gene therapy for Alzheimer disease
Tuszynski, M. H., Thal, L., Pay, M., Salmon, D. P., U, H. S., Bakay, R., Patel, P., Blesch, A., Vahlsing, H. L., Ho, G., et al. (2005) · Nature Medicine · doi:10.1038/nm1239 · Cited by 1,050 · see citing works
Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.
Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037 · see citing works
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
Mattson, M. P. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.4.1081 · Cited by 1,006 · cited 2× · see citing works
“precursor protein (APP) and releases soluble APP which has neuroprotective and memory enhancing effects (Roberts et al., 1994; Mattson, 1997).”
Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17
Hong, M. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,003 · see citing works
2012 Alzheimer's disease facts and figures Alzheimer's Association ∗
Thies, W. H., & Bleiler, L. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.02.001 · Cited by 984 · see citing works
APP processing in Alzheimer’s disease.
Zhang, Y.-W., Thompson, R., Zhang, H., & Xu, H. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-3 · Cited by 983 · see citing works
ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1
Xu, D. L., Emoto, N., Giaid, A., Slaughter, C. A., Kaw, S., deWit, D., & Yanagisawa, M. (1994) · Cell · doi:10.1016/0092-8674(94)90425-1 · Cited by 923 · see citing works
A 5-month, randomized, placebo-controlled trial of galantamine in AD
Tariot, P. N., Solomon, P. R., Morris, J. C., Kershaw, P. R., Lilienfeld, S., Ding, C., & the Galantamine USA- Study Group (2000) · Neurology · doi:10.1212/wnl.54.12.2269 · Cited by 915 · see citing works
Metabolic Regulation of Brain Aβ by Neprilysin
Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N., Gerard, C., Hama, E., Lee, H., & Saido, T. (2001) · Science · doi:10.1126/science.1059946 · Cited by 894 · see citing works
Crystal structure of the human angiotensin-converting enzyme–lisinopril complex
NATESH, R., Schwager, S. L. U., Sturrock, E. D., & Acharya, K. R. (2003) · Nature · doi:10.1038/nature01370 · Cited by 891 · see citing works
ApoE Promotes the Proteolytic Degradation of Aβ
Jiang, Q., Lee, C. Y. D., Mandrekar, S., Wilkinson, B., Cramer, P., Zelcer, N., Mann, K., Lamb, B., Willson, T. M., Collins, J. L., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.010 · Cited by 876 · see citing works
Brain-derived neurotrophic factor in the control human brain, and in Alzheimer’s disease and Parkinson’s disease
Murer, M. G., Yan, Q., & Raisman-Vozari, R. (2001) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00014-9 · Cited by 874 · see citing works
Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
Ma, J., Yee, A., Brewer, H. B., Das, S., & Potter, H. (1994) · Nature · doi:10.1038/372092a0 · Cited by 871 · see citing works
Identification of the major Aβ1–42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
Iwata, N., Tsubuki, S., Takaki, Y., Watanabe, K., Sekiguchi, M., Hosoki, E., Kawashima-Morishima, M., Lee, H.-J., Hama, E., Sekine-Aizawa, Y., et al. (2000) · Nature Medicine · doi:10.1038/72237 · Cited by 867 · see citing works
Alzheimer's disease
Burns, A., & Iliffe, S. (2009) · BMJ · doi:10.1136/bmj.b158 · Cited by 859 · see citing works
Apolipoprotein E in Alzheimer’s disease and other neurological disorders
Verghese, P. B., Castellano, J. M., & Holtzman, D. M. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70325-2 · Cited by 857 · cited 1× · see citing works
“The in vitro and in vivo studies showed that ApoE3 and ApoE4 forms a stable complex with Aβ peptides whereas ApoE4 forming complexeswith Aβ peptidesmore rapidly and effectively than ApoE3 (Jiang et al., 2008; Huang, 2010; Verghese et al., 2011).”
The Genetics of Alzheimer Disease: Back to the Future
Bertram, L., Lill, C. M., & Tanzi, R. E. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.013 · Cited by 834 · see citing works
Neuropathology of Alzheimer's Disease
Perl, D. P. (2010) · Mount Sinai Journal of Medicine: A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20157 · Cited by 825 · see citing works
Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
Selkoe, D. J., & Schenk, D. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140248 · Cited by 816 · see citing works
A Familial Alzheimer's Disease Locus on Chromosome 1
Levy‐Lahad, E., Wijsman, E. M., Nemens, E. J., Anderson, L., Goddard, K. A. B., Weber, J. L., Bird, T. D., & Schellenberg, G. D. (1995) · Science · doi:10.1126/science.7638621 · Cited by 811 · see citing works
Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
Kojro, E., Gimpl, G., Lammich, S., März, W., & Fahrenholz, F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081612998 · Cited by 804 · see citing works
Some morphometric aspects of the brain in senile dementia of the alzheimer type
Terry, R. D., Peck, A., DeTeresa, R., Schechter, R., & Horoupian, D. S. (1981) · Annals of Neurology · doi:10.1002/ana.410100209 · Cited by 801 · see citing works
Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.
Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works
Human E apoprotein heterogeneity. Cysteine-arginine interchanges in the amino acid sequence of the apo-E isoforms.
Weisgraber, K. H., Rall, S. C., & Mahley, R. W. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52510-8 · Cited by 777 · see citing works
The Pathogenesis of Senile Plaques
DICKSON, D. W. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199704000-00001 · Cited by 753 · see citing works
A phase 2 multiple ascending dose trial of bapineuzumab in mild to moderate Alzheimer disease
Salloway, S., Sperling, R., Gilman, S., Fox, N. C., Blennow, K., Raskind, M., Sabbagh, M., Honig, L. S., Doody, R., van Dyck, C. H., et al. (2009) · Neurology · doi:10.1212/wnl.0b013e3181c67808 · Cited by 753 · see citing works
Alzheimer's Disease: A Central Role for Amyloid
Selkoe, D. J. (1994) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199409000-00003 · Cited by 752 · see citing works
Thirty years of Alzheimer's disease genetics: the implications of systematic meta-analyses
Bertram, L., & Tanzi, R. E. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2494 · Cited by 747 · see citing works
A learning deficit related to age and β-amyloid plaques in a mouse model of Alzheimer's disease
Chen, G., Chen, K. S., Knox, J., Inglis, J., Bernard, A., Martin, S. J., Justice, A., McConlogue, L., Games, D., Freedman, S. B., et al. (2000) · Nature · doi:10.1038/35050103 · Cited by 740 · see citing works
Inhibition of Cyclin‐Dependent Kinases by Purine Analogues
de Azevedo, W. F., Leclerc, S., Meijer, L., Havlı́ček, L., Strnad, M., & Kim, S. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.0518a.x · Cited by 733 · see citing works
DEFECTIVE BRAIN MICROTUBULE ASSEMBLY IN ALZHEIMER'S DISEASE
Iqbal, K., Zaidi, T., Wen, G. Y., Grundke, I., MERZ, P. A., Shaikh, S., Wisniewski, H., Alafuzoff, I. I., & Winblad, B. G. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92134-3 · Cited by 727 · see citing works
Treatment of Alzheimer's disease; current status and new perspectives
Scarpini, E. A., Scheltens, P., & Feldman, H. (2003) · The Lancet Neurology · doi:10.1016/s1474-4422(03)00502-7 · Cited by 720 · see citing works
Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs
Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y. (2004) · Nature Medicine · doi:10.1038/nm1113 · Cited by 715 · see citing works
Presenilin 1 is required for Notch 1 and Dll1 expression in the paraxial mesoderm
Wong, P. C., Zheng, H., Chen, H., Bêcher, M. W., SIRINATHSINGHJI, D. J. S., Trumbauer, M. E., Chen, H. Y., Price, D. L., der Ploeg, L. H. T. V., & Sisodia, S. S. (1997) · Nature · doi:10.1038/387288a0 · Cited by 712 · see citing works
Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
Levitan, D. J., & Greenwald, I. (1995) · Nature · doi:10.1038/377351a0 · Cited by 709 · see citing works
Enhanced Proteolysis of β-Amyloid in APP Transgenic Mice Prevents Plaque Formation, Secondary Pathology, and Premature Death
Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 708 · see citing works
Apolipoprotein E and Alzheimer disease.
Strittmatter, W. J., & Roses, A. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.4725 · Cited by 699 · see citing works
Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. Cohen
Kirkitadze, M. D., Condron, M. M., & Teplow, D. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4970 · Cited by 684 · see citing works
Expression of Concern: Potent anti‐amyloidogenic and fibril‐destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease
Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., & Yamada, M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01976.x · Cited by 681 · see citing works
Unusual spectral energy distribution of a galaxy previously reported to be at redshift 6.68
Chen, H., Lanzetta, K. M., Pascarelle, S. M., & Yahata, N. (2000) · RePEc: Research Papers in Economics · Cited by 680 · see citing works
Hyperphosphorylation of Microtubule-Associated Protein Tau: A Promising Therapeutic Target for Alzheimer Disease
Gong, C., & Iqbal, K. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708785909111 · Cited by 649 · see citing works
Diet‐induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease
Ho, L., Qin, W., Pompl, P., Xiang, Z.-M., Wang, J., Zhao, Z., Peng, Y., Cambareri, G., Rocher, A., Mobbs, C., et al. (2004) · The FASEB Journal · doi:10.1096/fj.03-0978fje · Cited by 646 · see citing works
A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20864 · Cited by 638 · see citing works
Structure and novel exons of the human .tau. gene
Andreadis, A., Brown, W. M., & Kosik, K. S. (1992) · Biochemistry · doi:10.1021/bi00158a027 · Cited by 625 · see citing works
Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.
Brandt, R., Léger, J. G., & Lee, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.5.1327 · Cited by 624 · see citing works
Practice parameter: Management of dementia (an evidence-based review)
Oken, B. (2001) · Neurology · doi:10.1212/wnl.57.12.2323 · Cited by 578 · see citing works
Autosomal-dominant Alzheimer's disease: a review and proposal for the prevention of Alzheimer's disease
Bateman, R. J., Aisen, P. S., De Strooper, B., Fox, N. C., Lemere, C. A., Ringman, J. M., Salloway, S., Sperling, R. A., Windisch, M., & Xiong, C. (2010) · Alzheimer's Research & Therapy · doi:10.1186/alzrt59 · Cited by 573 · see citing works
Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
Neve, R. L., Harris, P. K. W., Kosik, K. S., Kurnit, D. M., & Donlon, T. A. (1986) · Molecular Brain Research · doi:10.1016/0169-328x(86)90033-1 · Cited by 565 · see citing works
Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones 1
Erdös, E. G., & Skidgel, R. A. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.2.2521610 · Cited by 558 · see citing works
Neuropathologic changes in Alzheimer's disease.
Wenk, G. L. (2003) · PubMed · Cited by 554 · see citing works
Interactions between ANG II, sympathetic nervous system, and baroreceptor reflexes in regulation of blood pressure
Reid, I. A. (1992) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1992.262.6.e763 · Cited by 553 · see citing works
Alzheimer's disease
Wilcock, G. K., Esiri, M. M., Bowen, D. M., & Smith, C. C. T. (1982) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(82)90045-4 · Cited by 553 · see citing works
Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
Wang, J., Grundke, I., & Iqbal, K. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05226.x · Cited by 553 · see citing works
Review of insulin and insulin-like growth factor expression, signaling, and malfunction in the central nervous system: Relevance to Alzheimer's disease
de la Monte, S. M., & Wands, J. R. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-7106 · Cited by 552 · see citing works
Alzheimer–associated presenilins 1 and 2 : Neuronal expression in brain and localization to intracellular membranes in mammalian cells
Kovacs, D. M., Fausett, H. J., Page, K. J., Kim, T., Moir, R. D., Merriam, D. E., Hollister, R. D., Hallmark, O. G., Mancini, R., Felsenstein, K. M., et al. (1996) · Nature Medicine · doi:10.1038/nm0296-224 · Cited by 551 · see citing works
Amnestic MCI or prodromal Alzheimer's disease?
Dubois, B., & Albert, M. L. (2004) · The Lancet Neurology · doi:10.1016/s1474-4422(04)00710-0 · Cited by 543 · see citing works
Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency
Herreman, A., Hartmann, D., Annaert, W. G., Säftig, P., Craessaerts, K., Serneels, L., Umans, L., Schrijvers, V., Checler, F., Vanderstichele, H., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.21.11872 · Cited by 518 · see citing works
Apolipoprotein E mRNA is abundant in the brain and adrenals, as well as in the liver, and is present in other peripheral tissues of rats and marmosets.
Elshourbagy, N. A., Liao, W. S. ‐., Mahley, R. W., & Taylor, J. M. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.1.203 · Cited by 509 · see citing works
Regulation of APP cleavage by α‐, β‐ and γ‐secretases
Nunan, J., & Small, D. H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02076-7 · Cited by 509 · see citing works
The microtubule binding domain of tau protein
Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500 · see citing works
Role of Protein Aggregation in Mitochondrial Dysfunction and Neurodegeneration in Alzheimer's and Parkinson's Diseases
Hashimoto, M., Rockenstein, E. M., Crews, L. A., & Masliah, E. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:21 · Cited by 498 · see citing works
Neurons Regulate Extracellular Levels of Amyloid β-Protein via Proteolysis by Insulin-Degrading Enzyme
Vekrellis, K., Ye, Z., Qiu, W. Q., Walsh, D. M., Hartley, D. M., Chesneau, V., Rosner, M. R., & Selkoe, D. J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-05-01657.2000 · Cited by 495 · see citing works
The presenilin hypothesis of Alzheimer’s disease: Evidence for a loss-of-function pathogenic mechanism.
Shen, J., & Kelleher, R. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608332104 · Cited by 485 · see citing works
Intracerebroventricular Infusion of Nerve Growth Factor in Three Patients with Alzheimer’s Disease
Jönhagen, M. E., Nordberg, A. K., Amberla, K., Bäckman, L., Ebendal, T., Meyerson, B. A., Olson, L., Seiger, Å., Shigeta, M., Theodorsson, E., et al. (1998) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000017069 · Cited by 472 · see citing works
A randomized trial evaluating the efficacy and safety of ENA 713 (rivastigmine tartrate), a new acetylcholinesterase inhibitor, in patients with mild to moderately severe Alzheimer's disease
Corey-Bloom, J. (1998) · Medical Entomology and Zoology · Cited by 467 · see citing works
Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease.
Mueller-Steiner, S., Zhou, Y.-G., Arai, H., Roberson, E., Sun, B.-G., Chen, J., Wang, X., Yu, G.-Q., Esposito, L., Mucke, L., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.027 · Cited by 466 · see citing works
Presenilins and -Secretase: Structure, Function, and Role in Alzheimer DiseasePreprint
Strooper, B. D., Iwatsubo, T., & Wolfe, M. S. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006304 · Cited by 465 · see citing works
New Frontiers in Alzheimer's Disease Genetics
Tanzi, R. E., & Bertram, L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00476-7 · Cited by 464 · see citing works
Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases
Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459 · see citing works
The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function
Turner, A. J., Isaac, R. E., & Coates, D. (2001) · BioEssays · doi:10.1002/1521-1878(200103)23:3 · Cited by 450 · see citing works
Unusual spectral energy distribution of a galaxy previously reported to be at redshift 6.68
Chen, H., Lanzetta, K. M., Pascarelle, S., & Yahata, N. (2000) · Nature · doi:10.1038/35046031 · Cited by 447 · see citing works
Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro.
(1994) · PubMed Central · Cited by 441 · see citing works
Inflammation and Alzheimer's disease pathogenesis
Rogers, J., Webster, S. D., Lue, L., Brachova, L., CIVIN, W. H., Emmerling, M. R., Shivers, B. D., Walker, D. G., & McGeer, P. L. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00115-7 · Cited by 441 · see citing works
Mutations causing neurodegenerative tauopathies
Goedert, M., & Jakes, R. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.007 · Cited by 438 · see citing works
Proposed nomenclature of apoE isoproteins, apoE genotypes, and phenotypes
Zannis, V. I., Breslow, J. L., Utermann, G., Mahley, R. W., Weisgraber, K. H., Havel, R. J., Goldstein, J. L., Brown, M. S., Schonfeld, G., Hazzard, W. R., et al. (1982) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38094-9 · Cited by 436 · see citing works
Clearance of Alzheimer's Aβ Peptide
Tanzi, R. E., Moir, R. D., & Wagner, S. L. (2004) · Neuron · doi:10.1016/j.neuron.2004.08.024 · Cited by 431 · see citing works
The “A Disintegrin And Metalloprotease” (ADAM) family of sheddases: Physiological and cellular functions
Reiß, K., & Säftig, P. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.11.002 · Cited by 424 · see citing works
Presynaptic Cholinergic Dysfunction in Patients with Dementia
Sims, N. R., Bowen, D. M., Allen, S. J., Smith, C., Neary, D., Thomas, D. J., & DAVISON, A. N. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb11311.x · Cited by 421 · see citing works
Psychiatric Phenomena in Alzheimer's Disease. I: Disorders of Thought Content
Burns, A. S., Jacoby, R. J., & Levy, R. (1990) · The British Journal of Psychiatry · doi:10.1192/bjp.157.1.72 · Cited by 420 · see citing works
M1 Receptors Play a Central Role in Modulating AD-like Pathology in Transgenic Mice
Caccamo, A., Oddo, S., Billings, L. M., Green, K. N., Martinez-Coria, H., Fisher, A., & LaFerla, F. M. (2006) · Neuron · doi:10.1016/j.neuron.2006.01.020 · Cited by 417 · see citing works
Presenilin clinical mutations can affect γ‐secretase activity by different mechanisms
Bentahir, M., Nyabi, O., Verhamme, J., Tolia, A., Horré, K., Wiltfang, J., Esselmann, H., & Strooper, B. D. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03578.x · Cited by 412 · see citing works
Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX
Turner, A. J., & Tanzawa, K. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.5.9141502 · Cited by 405 · see citing works
Alzheimer's β‐amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
Kurochkin, I. V., & Goto, S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00387-4 · Cited by 401 · see citing works
Apolipoprotein E fragments present in Alzheimer's disease brains induce neurofibrillary tangle-like intracellular inclusions in neurons
Huang, Y., Liu, X. Q., Wyss-Coray, T., Brecht, W. J., Sanan, D. A., & Mahley, R. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151254698 · Cited by 392 · see citing works
Regulation of the Phosphorylation State and Microtubule-Binding Activity of Tau by Protein Phosphatase 2A
Sontag, E., Nunbhakdi‐Craig, V., Lee, G. S., Bloom, G. S., & Mumby, M. C. (1996) · Neuron · doi:10.1016/s0896-6273(00)80250-0 · Cited by 391 · see citing works
The Presenilins in Alzheimer's Disease--Proteolysis Holds the Key
Haass, C., & Strooper, B. D. (1999) · Science · doi:10.1126/science.286.5441.916 · Cited by 388 · see citing works
The two homologous domains of human angiotensin I-converting enzyme are both catalytically active
Wei, L., Alhenc‐Gelas, F., Corvol, P. L., & Clauser, É. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31543-6 · Cited by 383 · see citing works
Galantamine
Scott, L. J., & Goa, K. L. (2000) · Drugs · doi:10.2165/00003495-200060050-00008 · Cited by 383 · see citing works
Cholinesterase Inhibitors: A New Class of Psychotropic Compounds
Cummings, J. L. (2000) · American Journal of Psychiatry · doi:10.1176/ajp.157.1.4 · Cited by 383 · see citing works
SYMPOSIUM: Clearance of Aβ from the Brain in Alzheimer's Disease: Aβ‐Degrading Enzymes in Alzheimer's Disease
Miners, J. S., Baig, S., Palmer, J. C., Palmer, L. E., Kehoe, P. G., & Love, S. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00132.x · Cited by 380 · see citing works
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
Shen, Y., Joachimiak, A., Rosner, M. R., & Tang, W. (2006) · Nature · doi:10.1038/nature05143 · Cited by 375 · see citing works
The history of the cholinergic hypothesis
Contestabile, A. (2010) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.12.044 · Cited by 373 · see citing works
Axonal transport defects: a common theme in neurodegenerative diseases
Roy, S., Zhang, B., Lee, V. M. ‐., & Trojanowski, J. Q. (2005) · Acta Neuropathologica · doi:10.1007/s00401-004-0952-x · Cited by 372 · see citing works
Protein Topology of Presenilin 1
Doan, A., Thinakaran, G., Borchelt, D., Slunt, H. H., Ratovitski, T., Podlisny, M. B., Selkoe, D. J., Seeger, M., Gandy, S., Price, D. L., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80232-9 · Cited by 371 · see citing works
Somatostatin regulates brain amyloid β peptide Aβ42 through modulation of proteolytic degradation
Saito, T., Iwata, N., Tsubuki, S., Takaki, Y., Takano, J., Huang, S.-M., Suemoto, T., Higuchi, M., & Saido, T. C. (2005) · Nature Medicine · doi:10.1038/nm1206 · Cited by 361 · see citing works
Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease
Kisilevsky, R., Lemieux, L. J., Fraser, P. E., Kong, X., Hultin, P. G., & Szarek, W. A. (1995) · Nature Medicine · doi:10.1038/nm0295-143 · Cited by 360 · see citing works
Reduced neprilysin in high plaque areas of Alzheimer brain: a possible relationship to deficient degradation of β-amyloid peptide
Yasojima, K., Akiyama, H., McGeer, E. G., & McGeer, P. L. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01675-x · Cited by 357 · see citing works
The roles of microtubule-associated proteins in brain morphogenesis: a review
Tucker, R. P. (1990) · Brain Research Reviews · doi:10.1016/0165-0173(90)90013-e · Cited by 356 · see citing works
A Novel ε-Cleavage within the Transmembrane Domain of the Alzheimer Amyloid Precursor Protein Demonstrates Homology with Notch Processing
Weidemann, A., Eggert, S., Reinhard, F. B. M., Vogel, M., Paliga, K., Baier, G., Masters, C. L., Beyreuther, K. T., & Evin, G. M. (2002) · Biochemistry · doi:10.1021/bi015794o · Cited by 352 · see citing works
A variant of Alzheimer's disease with spastic paraparesis and unusual plaques due to deletion of exon 9 of presenilin 1
Crook, R., Verkkoniemi, A., Pérez‐Tur, J., Mehta, N. D., Baker, M. C., Houlden, H., Farrer, M. J., Hutton, M., Lincoln, S., Hardy, J., et al. (1998) · Nature Medicine · doi:10.1038/nm0498-452 · Cited by 347 · see citing works
Current Pharmacotherapy for Alzheimer's Disease
Lleó, A., Greenberg, S. M., & Growdon, J. H. (2005) · Annual Review of Medicine · doi:10.1146/annurev.med.57.121304.131442 · Cited by 346 · see citing works
Degradation of the Alzheimer's Amyloid β Peptide by Endothelin-converting Enzyme*
Eckman, E., Reed, D. K., & Eckman, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007579200 · Cited by 345 · see citing works
Inhibition of Alzheimer β-Fibrillogenesis by Melatonin
Pappolla, M. A., Bozner, P., Soto, C. A., Shao, H., Robakis, N. K., Zagorski, M. G., Frangione, B., & Ghiso, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7185 · Cited by 338 · see citing works
Neurotrophic factors in Alzheimer’s disease: role of axonal transport
Schindowski, K., Bélarbi, K., & Buée, L. (2008) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00378.x · Cited by 335 · see citing works
Alzheimer's disease associated with mutations in presenilin 2 is rare and variably penetrant.
Sherrington, R., Froelich, S., Sorbi, S., Campion, D., Chi, H., Rogaeva, E., Lévesque, G., Rogaev, E., Lin, C.-P., Liang, Y., et al. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.7.985 · Cited by 335 · see citing works
[Angiotensin I converting enzyme].
NAKAI, K., Syoh, T., & Hiramori, K. (1995) · PubMed · Cited by 334 · see citing works
Cathepsin B
Mort, J. S., & Buttle, D. J. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(96)00152-5 · Cited by 333 · see citing works
Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1–40).
Backstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-24-07910.1996 · Cited by 331 · cited 2× · see citing works
“…2006;Wang et al., 2012), aminopeptidase (Sevalle et al., 2009; Dhanavade and Sonawane, 2014), gelatinase A (Yamada et al., 1995b; Jalkute et al., 2015), matrix metalloendopeptidase-9 (Backstrom et al., 1996), coagulation factor Xia (Saporito-Irwin and Van Nostrand, 1995), antibody light chain c23.”
Amyloid β-Protein Is Degraded by Cellular Angiotensin-converting Enzyme (ACE) and Elevated by an ACE Inhibitor
Hemming, M. L., & Selkoe, D. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508460200 · Cited by 330 · see citing works
Cholinesterase Inhibitors in Mild Cognitive Impairment: A Systematic Review of Randomised Trials
Raschetti, R., Albanese, E., Vanacore, N., & Maggini, M. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040338 · Cited by 322 · see citing works
The Endosomal-Lysosomal System of Neurons in Alzheimer's Disease Pathogenesis: A Review
Nixon, R. A., Cataldo, A. M., & Mathews, P. M. (2000) · Neurochemical Research · doi:10.1023/a:1007675508413 · Cited by 315 · see citing works
Thermozymes and Their Applications: A Review of Recent Literature and Patents
Bruins, M. E., Janssen, A. E. M., & Boom, R. M. (2001) · Applied Biochemistry and Biotechnology · doi:10.1385/abab:90:2:155 · Cited by 313 · see citing works
Aging and disease: connections to sirtuins
Dönmez, G., & Guarente, L. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00548.x · Cited by 312 · see citing works
Targeting soluble Aβ peptide with Tramiprosate for the treatment of brain amyloidosis
Gervais, F., Paquette, J., Morissette, C., Krzywkowski, P., Yu, M. W. N., Azzi, M., Lacombe, D., Kong, X., Aman, A. M., Laurin, J., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.02.015 · Cited by 308 · see citing works
Angiotensin-converting Enzyme Degrades Alzheimer Amyloid β-Peptide (Aβ); Retards Aβ Aggregation, Deposition, Fibril Formation; and Inhibits Cytotoxicity*
Hu, J.-G., Igarashi, A., Kamata, M., & Nakagawa, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104068200 · Cited by 307 · see citing works
Physiological Functions of APP Family ProteinsPreprint
Müller, U., & Zheng, H. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006288 · Cited by 307 · see citing works
Current Advances on Different Kinases Involved in Tau Phosphorylation, and Implications in Alzheimers Disease and Tauopathies
Ferrer, I., Gómez‐Isla, T., Puig, B., Freixes, M., Ribé, E. M., Dalfó, E., & Ávila, J. (2005) · Current Alzheimer Research · doi:10.2174/1567205052772713 · Cited by 302 · see citing works
CHARACTERIZATION OF A DIPEPTIDE HYDROLASE (KININASE II: ANGIOTENSIN I CONVERTING ENZYME)
Yang, H., ERDÖS, E. O., & Levin, Y. (1971) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)28878-4 · Cited by 296 · see citing works
Tramiprosate in mild-to-moderate Alzheimer's disease — a randomized, double-blind, placebo-controlled, multi-centre study (the Alphase Study)
Aisen, P. S., Gauthier, S., Ferris, S. H., Saumier, D., Haine, D., Garceau, D., Duong, A., Suhy, J., Oh, J., Lau, W. C., et al. (2011) · Archives of Medical Science · doi:10.5114/aoms.2011.20612 · Cited by 295 · see citing works
P1‐071: Intensity of dementia through latent variable modelling (I‐DeLV) in the AIBL cohort
Burnham, S. C., Graham, P. L., Wilson, B., Ames, D. J., Macaulay, L. S., Martins, R. N., Masters, C. L., Maruff, P. T., Rowe, C. C., Szoeke, C. E. I., et al. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.347 · Cited by 292 · see citing works
Inflammatory mechanisms in Alzheimer's disease
Eikelenboom, P., Zhan, S., van Gool, W. A., & Allsop, D. (1994) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(94)90057-4 · Cited by 291 · see citing works
Phosphorylation, Subcellular Localization, and Membrane Orientation of the Alzheimer's Disease-associated Presenilins
Strooper, B. D., Beullens, M., Contreras, B., Lévesque, L., Craessaerts, K., Cordell, B., Moechars, D., Bollen, M., Fraser, P., George‐Hyslop, P. S., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3590 · Cited by 286 · see citing works
Reply to: 'Clearance of amyloid β-peptide from brain: transport or metabolism?'
Iwata, N., Tsubuki, S., Hama, E., Takaki, Y., Shirotani, K., & Saido, T. C. (2000) · Nature Medicine · doi:10.1038/77399 · Cited by 285 · see citing works
Accelerated filament formation from tau protein with specific FTDP‐17 missense mutations
Nacharaju, P., Lewis, J. M., Easson, C., Yen, S. H., Hackett, J., Hutton, M., & Yen, S.-H. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00294-x · Cited by 283 · see citing works
Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon 1 1Edited by R. Huber
Oefner, C., D'Arcy, A., Hennig, M., Winkler, F. K., & Dale, G. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3492 · Cited by 282 · see citing works
Evidence That Nonsteroidal Anti-inflammatory Drugs Decrease Amyloid β42 Production by Direct Modulation of γ-Secretase Activity
Weggen, S., Eriksen, J. L., Sagi, S. A., Pietrzik, C. U., Ozols, V. V., Fauq, A. H., Golde, T. E., & Koo, E. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303592200 · Cited by 280 · see citing works
Mutations of the presenilin I gene in families with early-onset Alzheimer's disease
Campion, D., Flaman, J., Brice, A., Hannequin, D., Dubois, B., Martin, C., Moreau, V., Charbonnier, F., Didierjean, O., Tardieu, S., et al. (1995) · Human Molecular Genetics · doi:10.1093/hmg/4.12.2373 · Cited by 277 · see citing works
Developing β‐secretase inhibitors for treatment of Alzheimer’s disease
Ghosh, A. K., Brindisi, M., & Tang, J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07476.x · Cited by 272 · see citing works
Nicotinic and muscarinic subtypes in the human brain: Changes with aging and dementia
Nordberg, A. K., Alafuzoff, I. I., & Winblad, B. G. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310115 · Cited by 270 · see citing works
Fibrillogenesis in Alzheimer's disease of amyloid <i>β</i> peptides and apolipoprotein E
Castano, E. M., Prelli, F., Wisniewski, T., Golabek, A., Kumar, R. A., Soto, C., & Frangione, B. (1995) · Biochemical Journal · doi:10.1042/bj3060599 · Cited by 267 · see citing works
A locus for familial early–onset Alzhelmer's disease on the long arm of chromosome 14, proximal to the α1–antichymotrypsin gene
Mullan, M., Houlden, H., Windelspecht, M., Fidani, L., Lombardi, C., Diaz, P., Rossor, M. N., Crook, R., Hardy, J., Duff, K., et al. (1992) · Nature Genetics · doi:10.1038/ng1292-340 · Cited by 267 · see citing works
Alzheimer's Disease β-Amyloid Peptide Is Increased in Mice Deficient in Endothelin-converting Enzyme
Eckman, E. A., Watson, M., Marlow, L. A., Sambamurti, K., & Eckman, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200642200 · Cited by 263 · see citing works
Variation in DCP1, encoding ACE, is associated with susceptibility to Alzheimer disease
Kehoe, P. G., Russ, C., McIlroy, S., Williams, H., Holmans, P., Holmes, C., Liolitsa, D., Vahidassr, D., Powell, J., McGleenon, B., et al. (1999) · Nature Genetics · doi:10.1038/5009 · Cited by 260 · cited 2× · see citing works
“of Angiotensin II has been implicated in AD (Kehoe et al., 1999).”
β‐Amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases?
Carson, J. A., & Turner, A. J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00855.x · Cited by 259 · see citing works
Genomic organization of the human amyloid beta-protein precursor gene
Yoshikai, S.-I., Sasaki, H., Doh‐ura, K., Furuya, H., & Sakaki, Y. (1990) · Gene · doi:10.1016/0378-1119(90)90310-n · Cited by 259 · see citing works
Donepezil: an update
Seltzer, B. (2007) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.8.7.1011 · Cited by 256 · see citing works
Neurovascular Dysfunction and Faulty Amyloid -Peptide Clearance in Alzheimer Disease
Sagare, A. P., Bell, R. D., & Zlokovic, B. V. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011452 · Cited by 251 · see citing works
Clearance mechanisms of Alzheimer's amyloid-β peptide: implications for therapeutic design and diagnostic tests
Bates, K. A., Verdile, G., Li, Q.-X., Ames, D., Hudson, P., Masters, C. L., & Martins, R. N. (2009) · Molecular Psychiatry · doi:10.1038/mp.2008.96 · Cited by 247 · see citing works
Conformational transition of amyloid β-peptide
Xu, Y., Shen, J., Luo, X., Zhu, W., Chen, K., Ma, J., & Jiang, H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501218102 · Cited by 247 · see citing works
The amyloid deposits in Alzheimer's disease: their nature and pathogenesis.
Glenner, G. G., Wong, C. W., Quaranta, V., & Eanes, E. D. (1984) · PubMed · Cited by 244 · see citing works
Substrate and Inhibitor Profile of BACE (β-Secretase) and Comparison with Other Mammalian Aspartic Proteases
Grüninger-Leitch, F., Schlatter, D., Küng, E., Nelböck, P., & Döbeli, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109266200 · Cited by 243 · see citing works
Inhibition of Toxicity in the β-Amyloid Peptide Fragment β-(25–35) Using N-Methylated Derivatives
Hughes, E., Burke, R. M., & Doig, A. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003554200 · Cited by 238 · see citing works
Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments.
Księżak-Reding, H., Liu, W.-K., & Shu, H.-Y. C. (1992) · Brain Research · doi:10.1016/0006-8993(92)91476-u · Cited by 237 · see citing works
Novel Research Horizons for Presenilins and γ-Secretases in Cell Biology and Disease
Strooper, B. D., & Annaert, W. G. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104117 · Cited by 233 · see citing works
Cystatin C-Cathepsin B Axis Regulates Amyloid Beta Levels and Associated Neuronal Deficits in an Animal Model of Alzheimer's Disease
Sun, B., Zhou, Y., Halabisky, B., Lo, I., Cho, S.-H., Mueller-Steiner, S., Devidze, N., Wang, X., Grubb, A., & Gan, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.001 · Cited by 231 · see citing works

Flagged first, then by citations

4 of the 371 references couldn’t be matched to a known paper.

Sorted by citations

Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease
Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820 · see citing works
“The Aβ plaque comprises of Aβ peptides obtained from amyloid precursor protein (APP) by the enzymatic cleavage via secretases (α, β and γ) [2].”
Background
Pathophysiologic relationship between Alzheimer's disease, cerebrovascular disease, and cardiovascular risk: A review and synthesis
Santos, C. Y., Snyder, P. J., Wu, W., Zhang, M., Echeverria, A., & Alber, J. (2017) · Alzheimer's & Dementia: Diagnosis, Assessment & Disease Monitoring · doi:10.1016/j.dadm.2017.01.005 · Cited by 431 · see citing works
Early long-term administration of the CSF1R inhibitor PLX3397 ablates microglia and reduces accumulation of intraneuronal amyloid, neuritic plaque deposition and pre-fibrillar oligomers in 5XFAD mouse model of Alzheimer’s disease
Sosna, J., Philipp, S., Albay, R., Reyes-Ruiz, J. M., Baglietto-Vargas, D., LaFerla, F. M., & Glabe, C. G. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0244-x · Cited by 406 · see citing works
Shaping the Nrf2-ARE-related pathways in Alzheimer’s and Parkinson’s diseases
Fão, L., Mota, S. I., & Rego, A. C. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100942 · Cited by 270 · see citing works
Plasma neuronal exosomes serve as biomarkers of cognitive impairment in HIV infection and Alzheimer’s disease
Pulliam, L., Sun, B., Mustapić, M., Chawla, S., & Kapogiannis, D. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-018-0695-4 · Cited by 246 · see citing works
Therapies for Prevention and Treatment of Alzheimer’s Disease
Mendiola-Precoma, J., Berumen, L. C., Padilla, K., & García‐Alcocer, G. (2016) · BioMed Research International · doi:10.1155/2016/2589276 · Cited by 245 · see citing works
MAP/ERK Signaling in Developing Cognitive and Emotional Function and Its Effect on Pathological and Neurodegenerative Processes
Albert‐Gascó, H., Ros‐Bernal, F., Castillo-Gómez, E., & Olucha-Bordonau, F. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124471 · Cited by 241 · see citing works
Natural Compounds for Alzheimer’s Disease Therapy: A Systematic Review of Preclinical and Clinical Studies
Andrade, S., Ramalho, M. J., Loureiro, J. A., & Pereira, M. D. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092313 · Cited by 240 · see citing works
Insulin Resistance in Alzheimer's Disease
Ferreira, L. S. S., Fernandes, C., Vieira, M. N. N., & Felice, F. G. D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00830 · Cited by 229 · see citing works
RETRACTED ARTICLE: Neuroprotective Effect of Fisetin Against Amyloid-Beta-Induced Cognitive/Synaptic Dysfunction, Neuroinflammation, and Neurodegeneration in Adult Mice
Ahmad, A., Ali, T., Park, H. Y., Badshah, H., Rehman, S. U., & Kim, M. O. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9795-4 · Cited by 216 · see citing works
Retracted
Deficits in cholinergic neurotransmission and their clinical correlates in Parkinson’s disease
Perez‐Lloret, S., & Barrantes, F. J. (2016) · npj Parkinson s Disease · doi:10.1038/npjparkd.2016.1 · Cited by 212 · see citing works
GABAergic Inhibitory Interneuron Deficits in Alzheimer’s Disease: Implications for Treatment
Xu, Y., Zhao, M., Han, Y., & Zhang, H. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00660 · Cited by 203 · see citing works
Hesperetin Confers Neuroprotection by Regulating Nrf2/TLR4/NF-κB Signaling in an Aβ Mouse Model
Ikram, M. A., Muhammad, T., Rehman, S. U., Khan, A., Jo, M. G., Ali, T., & Kim, M. O. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1512-7 · Cited by 194 · see citing works
Alzheimer’s Disease: The Link Between Amyloid-β and Neurovascular Dysfunction
Solis, E., Hascup, K. N., & Hascup, E. R. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200473 · Cited by 186 · see citing works
The Role of ADAM10 in Alzheimer’s Disease
Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160 · see citing works
Amyloid β-42 induces neuronal apoptosis by targeting mitochondria
Han, X., Hu, Y., Yang, Z., Jiang, L., Shi, S.-L., Li, Y.-R., Guo, M., Wu, H., & Wan, Y. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7203 · Cited by 144 · see citing works
Pathophysiology and management of alzheimer’s disease: an overview
Thakur, A. K., Kamboj, P., Goswami, K., & Ahuja, K. (2018) · Journal of Analytical & Pharmaceutical Research · doi:10.15406/japlr.2018.07.00230 · Cited by 142 · see citing works
Drug development for alzheimer’s disease: Microglia induced neuroinflammation as a target
Dong, Y., Li, X., Cheng, J., & Hou, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030558 · Cited by 136 · see citing works
FFPM, a PDE4 inhibitor, reverses learning and memory deficits in APP/PS1 transgenic mice via cAMP/PKA/CREB signaling and anti-inflammatory effects
Guo, H., Cheng, Y., Wang, C., Wu, J., Zou, Z., Niu, B., Yu, H. M., Wang, H., & Xu, J. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.01.004 · Cited by 133 · see citing works
Neurotransmitters in Prevention and Treatment of Alzheimer’s Disease
Yang, Z., Zou, Y., & Wang, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043841 · Cited by 132 · see citing works
Future Therapeutic Perspectives into the Alzheimer’s Disease Targeting the Oxidative Stress Hypothesis
Teixeira, J. P., de Castro, A. A., Soares, F. V., da Cunha, E. F. F., & Ramalho, T. C. (2019) · Molecules · doi:10.3390/molecules24234410 · Cited by 122 · see citing works
The Many Faces of Astrocytes in Alzheimer's Disease
Monterey, M. D., Wei, H., Wu, X., & Wu, J. Q. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.619626 · Cited by 117 · see citing works
Nose-to-brain drug delivery: from bench to bedside
Drath, I., Richter, F., & Feja, M. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00481-w · Cited by 128 · see citing works
Novel tacrine-tryptophan hybrids: Multi-target directed ligands as potential treatment for Alzheimer's disease
Chalupova, K., Korabecny, J., Bartolini, M., Monti, B., Lamba, D., Caliandro, R., Pesaresi, A., Brazzolotto, X., Gastellier, A.-J., Nachon, F., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.02.021 · Cited by 118 · see citing works
Tackling neuroinflammation and cholinergic deficit in Alzheimer's disease: Multi-target inhibitors of cholinesterases, cyclooxygenase-2 and 15-lipoxygenase
AlFadly, E. D., Elzahhar, P. A., Tramarin, A., Elkazaz, S., Shaltout, H. A., Abu-Serie, M. M., Janočková, J., Soukup, O., Ghareeb, D. A., EL‐Yazbi, A. F., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.02.012 · Cited by 108 · see citing works
Application of Iron Oxide Nanoparticles in the Diagnosis and Treatment of Neurodegenerative Diseases With Emphasis on Alzheimer’s Disease
Luo, S., Ma, C., Zhu, M., Ju, W.-N., Yu, Y., & Wang, X. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00021 · Cited by 109 · see citing works
Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane
Fatafta, H., Khaled, M., Owen, M. C., Sayyed–Ahmad, A., & Strodel, B. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106210118 · Cited by 108 · see citing works
Natural Phytochemicals in the Treatment and Prevention of Dementia: An Overview
Libro, R., Giacoppo, S., Soundara Rajan, T., Bramanti, P., & Mazzon, E. (2016) · Molecules · doi:10.3390/molecules21040518 · Cited by 107 · see citing works
T Lymphocytes and Inflammatory Mediators in the Interplay between Brain and Blood in Alzheimer’s Disease: Potential Pools of New Biomarkers
Mietelska‐Porowska, A., & Wojda, U. (2017) · Journal of Immunology Research · doi:10.1155/2017/4626540 · Cited by 107 · see citing works
Advances in developing therapeutic strategies for Alzheimer's disease
Nguyen, T. T., Nguyen, T. T. D., Nguyen, T. K. O., Vo, T. K., & Giau, V. V. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111623 · Cited by 107 · see citing works
Role of Amyloid Precursor Protein (APP) and Its Derivatives in the Biology and Cell Fate Specification of Neural Stem Cells
Coronel, R., Bernabeu-Zornoza, A., Palmer, C., Moreno, M. D. M. M., Zambrano, A., Cano, E., & Liste, I. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0914-2 · Cited by 104 · see citing works
Brain‐Penetration and Neuron‐Targeting DNA Nanoflowers Co‐Delivering miR‐124 and Rutin for Synergistic Therapy of Alzheimer's Disease
Ouyang, Q., Liu, K., Zhu, Q., Deng, H., Le, Y., Ouyang, W., Yan, X., Zhou, W., & Tong, J. (2022) · Small · doi:10.1002/smll.202107534 · Cited by 103 · see citing works
Early pathologic amyloid induces hypersynchrony of BOLD resting‐state networks in transgenic mice and provides an early therapeutic window before amyloid plaque deposition
Shah, D., Praet, J., Latif‐Hernandez, A., Höfling, C., Anckaerts, C., Bard, F., Morawski, M., Detrez, J. R., Prinsen, E., Villa, A. M., et al. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.03.010 · Cited by 100 · see citing works
Design, synthesis and biological evaluation of new phthalimide and saccharin derivatives with alicyclic amines targeting cholinesterases, beta-secretase and amyloid beta aggregation
Panek, D., Więckowska, A., Wichur, T., Bajda, M., Godyń, J., Jończyk, J., Mika, K., Janočková, J., Soukup, O., Knez, D., et al. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.09.078 · Cited by 98 · see citing works
Oligodendrocyte progenitor cells in Alzheimer's disease: from physiology to pathology
Zou, P., Wu, C., Liu, T. C.-Y., Duan, R., & Yang, L. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00385-7 · Cited by 97 · see citing works
Pharmacotherapy Evolution in Alzheimer’s Disease: Current Framework and Relevant Directions
Miculas, D. C., Negru, P. A., Bungau, S. G., Behl, T., Hassan, S. S. U., & Tit, D. M. (2022) · Cells · doi:10.3390/cells12010131 · Cited by 96 · see citing works
Harnessing endophenotypes and network medicine for Alzheimer's drug repurposing
Fang, J., Pieper, A. A., Nussinov, R., Lee, G., Bekris, L. M., Leverenz, J. B., Cummings, J. L., & Cheng, F. (2020) · Medicinal Research Reviews · doi:10.1002/med.21709 · Cited by 93 · see citing works
Current Progress on Peroxisome Proliferator-activated Receptor Gamma Agonist as an Emerging Therapeutic Approach for the Treatment of Alzheimer's Disease: An Update
Khan, M. A., Alam, Q., Haque, A., Ashafaq, M., Khan, M. J., Ashraf, G. M., & Ahmad, M. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180828100002 · Cited by 90 · see citing works
Long-term exercise pre-training attenuates Alzheimer’s disease–related pathology in a transgenic rat model of Alzheimer’s disease
Yang, L., Wu, C., Li, Y., Dong, Y., Wu, C. Y., Lee, R. H., Brann, D. W., Lin, H. W., & Zhang, Q. (2022) · GeroScience · doi:10.1007/s11357-022-00534-2 · Cited by 93 · see citing works
Fenugreek Seed Powder Attenuated Aluminum Chloride-Induced Tau Pathology, Oxidative Stress, and Inflammation in a Rat Model of Alzheimer’s Disease1
Prema, A., Justin Thenmozhi, A., Manivasagam, T., Mohamed Essa, M., & Guillemin, G. J. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161103 · Cited by 90 · see citing works
Microbiota-gut-brain axis and toll-like receptors in Alzheimer’s disease
Lin, C., Zhao, S., Zhu, Y., Fan, Z., Wang, J., Zhang, B., & Chen, Y. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.09.008 · Cited by 91 · see citing works
Essential Oils as Treatment Strategy for Alzheimerʼs Disease: Current and Future Perspectives
Benny, A., & Thomas, J. (2018) · Planta Medica · doi:10.1055/a-0758-0188 · Cited by 89 · see citing works
Ginsenoside Re Inhibits ROS/ASK-1 Dependent Mitochondrial Apoptosis Pathway and Activation of Nrf2-Antioxidant Response in Beta-Amyloid-Challenged SH-SY5Y Cells
Liu, M., Bai, X., Yu, S., Zhao, W., Qiao, J., Liu, Y., Zhao, D., Wang, J., & Wang, S. (2019) · Molecules · doi:10.3390/molecules24152687 · Cited by 88 · see citing works
Potential application of endocannabinoid system agents in neuropsychiatric and neurodegenerative diseases—focusing on FAAH/MAGL inhibitors
Ren, S., Wang, Z., Zhang, Y., & Chen, N. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0385-7 · Cited by 88 · see citing works
Design, Synthesis, and Evaluation of Novel Ferulic Acid Derivatives as Multi-Target-Directed Ligands for the Treatment of Alzheimer’s Disease
Sang, Z., Wang, K., Han, X., Cao, M., Tan, Z., & Liu, W. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00530 · Cited by 87 · see citing works
Antidiabetic Drugs for the Risk of Alzheimer Disease in Patients With Type 2 DM Using FAERS
Akimoto, H., Negishi, A., Oshima, S., Wakiyama, H., Okita, M., Horii, N., Inoue, N., Ohshima, S., & Kobayashi, D. (2020) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317519899546 · Cited by 89 · see citing works
Near-Infrared Fluorescent Probes as Imaging and Theranostic Modalities for Amyloid-Beta and Tau Aggregates in Alzheimer’s Disease
Rai, H., Gupta, S., Kumar, S., Yang, J., Singh, S. K., Ran, C., & Modi, G. P. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01619 · Cited by 86 · see citing works
Wnt signaling loss accelerates the appearance of neuropathological hallmarks of Alzheimer's disease in J20‐ APP transgenic and wild‐type mice
Tapia‐Rojas, C., & Inestrosa, N. C. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14278 · Cited by 87 · see citing works
Sirtuin 1 and Alzheimer's disease: An up-to-date review
Rizzi, L., & Roriz‐Cruz, M. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.07.001 · Cited by 83 · see citing works
Nanomaterials toward the treatment of Alzheimer’s disease: Recent advances and future trends
Zeng, H., Qi, Y., Zhang, Z., Liu, C., Peng, W., & Zhang, Y. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.01.014 · Cited by 82 · see citing works
Alzheimer’s Disease: Pathogenesis and Therapeutic Interventions
Ogbodo, J. O., Agbo, C. P., Njoku, U. O., Ogugofor, M. O., Egba, S. I., Ihim, S. A., Echezona, A. C., Brendan, K. C., Upaganlawar, A. B., & Upasani, C. D. (2021) · Current Aging Science · doi:10.2174/1874609814666210302085232 · Cited by 84 · see citing works
Natural Therapeutics in Aid of Treating Alzheimer’s Disease: A Green Gateway Toward Ending Quest for Treating Neurological Disorders
Bhat, B. A., Almilaibary, A., Mir, R. A., Aljarallah, B. M., Mir, W. R., Ahmad, F., & Mir, M. A. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.884345 · Cited by 85 · see citing works
Mitochondrial Bioenergetics Is Altered in Fibroblasts from Patients with Sporadic Alzheimer's Disease
Maria Jose Perez, J., Ponce, D. P., Osorio‐Fuentealba, C., Behrens, M. I., & Quintanilla, R. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00553 · Cited by 80 · see citing works
Protective Effects of Pioglitazone on Cognitive Impairment and the Underlying Mechanisms: A Review of Literature
Alhowail, A. H., Alsikhan, R. S., Alsaud, M. M., Aldubayan, M. A., & Rabbani, S. I. (2022) · Drug Design Development and Therapy · doi:10.2147/dddt.s367229 · Cited by 80 · see citing works
Longitudinal Assessment of Tau Pathology in Patients with Alzheimer’s Disease Using [18F]THK-5117 Positron Emission Tomography
Ishiki, A., Okamura, N., Furukawa, K., Furumoto, S., Harada, R., Tomita, N., Hiraoka, K., Watanuki, S., Ishikawa, Y., Tago, T., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140311 · Cited by 77 · see citing works
Bioactive Food Abates Metabolic and Synaptic Alterations by Modulation of Gut Microbiota in a Mouse Model of Alzheimer’s Disease
Syeda, T., Sánchez‐Tapia, M., Pinedo‐Vargas, L., Granados, O., Cuervo-Zanatta, D., Rojas-Santiago, E., Díaz-Cintra, S. Y., Torres, N., & Perez‐Cruz, C. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180556 · Cited by 78 · see citing works
AMPK activation does not enhance autophagy in neurons in contrast to MTORC1 inhibition: different impact on β-amyloid clearance
Benito‐Cuesta, I., Ordóñez‐Gutiérrez, L., & Wandosell, F. G. (2020) · Autophagy · doi:10.1080/15548627.2020.1728095 · Cited by 76 · see citing works
When Good Kinases Go Rogue: GSK3, p38 MAPK and CDKs as Therapeutic Targets for Alzheimer’s and Huntington’s Disease
D’Mello, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115911 · Cited by 77 · see citing works
Synaptic Mitochondria: An Early Target of Amyloid-β and Tau in Alzheimer’s Disease
Torres, A. K., Jara, C., Park-Kang, H. S., Polanco, C. M., Tapia, D., Alarcón, F., de la Peña, A., Llanquinao, J., Vargas-Mardones, G., Álvarez‐Indo, J., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215139 · Cited by 79 · see citing works
Pyrazoline Containing Compounds as Therapeutic Targets for Neurodegenerative Disorders
Ahsan, M. J., Ali, A., Ali, A., Thiriveedhi, A., Bakht, M. A., Yusuf, M., Salahuddin, S., Afzal, O., & Altamimi, A. S. A. (2022) · ACS Omega · doi:10.1021/acsomega.2c05339 · Cited by 75 · see citing works
Discovery and validation of plasma proteomic biomarkers relating to brain amyloid burden by SOMAscan assay
Shi, L., Westwood, S., Baird, A. L., Winchester, L. M., Dobričić, V., Kilpert, F., Hong, S., Franke, A., Hye, A., Ashton, N. J., et al. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.06.4951 · Cited by 74 · see citing works
Nanocarrier mediated drug delivery as an impeccable therapeutic approach against Alzheimer’s disease
Taliyan, R., Kakoty, V., Sarathlal, K. C., Kharavtekar, S. S., Karennanavar, C. R., Choudhary, Y. K., Singhvi, G., Riadi, Y., Dubey, S. K., & Kesharwani, P. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.01.044 · Cited by 76 · see citing works
Signaling Mechanisms of Selective PPARγ Modulators in Alzheimer’s Disease
Govindarajulu, M., Pinky, P. D., Bloemer, J., Ghanei, N., Suppiramaniam, V. D., & Amin, R. (2018) · PPAR Research · doi:10.1155/2018/2010675 · Cited by 75 · see citing works
Commonalities between Copper Neurotoxicity and Alzheimer’s Disease
Patel, R., & Aschner, M. (2021) · Toxics · doi:10.3390/toxics9010004 · Cited by 73 · see citing works
Neurotransmission systems in Parkinson’s disease
Moghaddam, H. S., Zare-Shahabadi, A., Rahmani, F., & Rezaei, N. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0068 · Cited by 76 · see citing works
Environment-Sensitive Near-Infrared Probe for Fluorescent Discrimination of Aβ and Tau Fibrils in AD Brain
Zhou, K., Yuan, C., Dai, B., Wang, K., Chen, Y., Ma, D., Dai, J., Liang, Y., Tan, H., & Cui, M. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00672 · Cited by 73 · see citing works
Roflumilast ameliorates cognitive impairment in APP/PS1 mice via cAMP/CREB/BDNF signaling and anti-neuroinflammatory effects
Feng, H., Wang, C., He, W., Wu, X.-J., Li, S., Zeng, Z., Wei, M., & He, B. (2019) · Metabolic Brain Disease · doi:10.1007/s11011-018-0374-4 · Cited by 72 · see citing works
Therapeutic Actions of the Thiazolidinediones in Alzheimer’s Disease
Maria Jose Perez, J., & Quintanilla, R. A. (2015) · PPAR Research · doi:10.1155/2015/957248 · Cited by 72 · see citing works
Profiling donepezil template into multipotent hybrids with antioxidant properties
Mezeiová, E., Špilovská, K., Nepovimová, E., Górecki, L., Soukup, O., Doležal, R., Maliňák, D., Janočková, J., Jun, D., Kuča, K., et al. (2018) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1443326 · Cited by 74 · see citing works
MicroRNA in Alzheimer’s disease revisited: implications for major neuropathological mechanisms
Dehghani, R., Rahmani, F., & Rezaei, N. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0042 · Cited by 72 · see citing works
Functionalised Carbon Nanotubes Enhance Brain Delivery of Amyloid-Targeting Pittsburgh Compound B (PiB)-Derived Ligands
Costa, P. M., Wang, J. T.-W., Morfin, J., Khanum, T., To, W., Sosabowski, J. K., Tóth, É., & Al‐Jamal, K. T. (2018) · Nanotheranostics · doi:10.7150/ntno.23125 · Cited by 71 · see citing works
Metal-involved theranostics: An emerging strategy for fighting Alzheimer’s disease
Wang, X., Wang, X., & Guo, Z. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.03.010 · Cited by 71 · see citing works
Mitochondrial Abnormalities and Synaptic Loss Underlie Memory Deficits Seen in Mouse Models of Obesity and Alzheimer’s Disease
Martins, I. V. A., Rivers‐Auty, J., Allan, S. M., & Lawrence, C. B. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160640 · Cited by 70 · see citing works
Low Phytanic Acid-Concentrated DHA Prevents Cognitive Deficit and Regulates Alzheimer Disease Mediators in an ApoE−/− Mice Experimental Model
Ruiz-Roso, M. B., Echeverry‐Alzate, V., Ruiz‐Roso, B., Quintela, J. C., Ballesteros, S., Lahera, V., Heras, N. D. L., López‐Moreno, J. A., & Martín‐Fernández, B. (2018) · Nutrients · doi:10.3390/nu11010011 · Cited by 70 · see citing works
Microbial BMAA elicits mitochondrial dysfunction, innate immunity activation, and Alzheimer’s disease features in cortical neurons
Silva, D. F., Candeias, E., Esteves, A. R., Magalhães, J. D., Ferreira, I. L., Nunes‐Costa, D., Rego, A. C., Empadinhas, N., & Cardoso, S. M. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-02004-y · Cited by 70 · see citing works
Dietary Polyphenols as Therapeutic Intervention for Alzheimer’s Disease: A Mechanistic Insight
Bukhari, S. N. A. (2022) · Antioxidants · doi:10.3390/antiox11030554 · Cited by 70 · see citing works
Caffeic acid loaded into engineered lipid nanoparticles for Alzheimer's disease therapy
Andrade, S., Pereira, M. D. C., & Loureiro, J. A. (2023) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2023.113270 · Cited by 68 · see citing works
Role of Fluid Biomarkers and PET Imaging in Early Diagnosis and its Clinical Implication in the Management of Alzheimer’s Disease
Hameed, S., Fuh, J., Senanarong, V., Ebenezer, E. G. M., Looi, I., Dominguez, J. C., Park, K. W., Karanam, A. K., & Simon, O. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-190143 · Cited by 67 · see citing works
Amyloid β-Targeted Metal Complexes for Potential Applications in Alzheimer's Disease
Liu, H., Qu, Y., & Wang, X. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0248 · Cited by 66 · see citing works
A Primer on the Evolution of Aducanumab: The First Antibody Approved for Treatment of Alzheimer’s Disease
Mukhopadhyay, S., & Banerjee, D. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215065 · Cited by 66 · see citing works
Synthesis and metabolism of methylglyoxal, S-D-lactoylglutathione and D-lactate in cancer and Alzheimer’s disease. Exploring the crossroad of eternal youth and premature aging
Lidia de, B. A. R. I., Atlante, A., Armeni, T., & Kalapos, M. P. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100915 · Cited by 66 · see citing works
Thermodynamics and kinetics of the amyloid-β peptide revealed by Markov state models based on MD data in agreement with experiment
Paul, A., Samantray, S., Anteghini, M., Khaled, M., & Strodel, B. (2020) · bioRxiv · doi:10.1039/d0sc04657d · Cited by 43 · see citing works
Neuroprotective Effects of Metformin Through the Modulation of Neuroinflammation and Oxidative Stress
Reed, S., Taka, E., Darling‐Reed, S., & Soliman, K. F. A. (2025) · Cells · doi:10.3390/cells14141064 · Cited by 71 · see citing works
Amyloid β production is regulated by β2-adrenergic signaling-mediated post-translational modifications of the ryanodine receptor
Bussiere, R., Lacampagne, A., Reiken, S. R., Liu, X., Scheuermann, V., Zalk, R., Martin, C., Checler, F., Marks, A. R., & Chami, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.743070 · Cited by 66 · see citing works
Deep Brain Stimulation for Alzheimer's Disease: Stimulation Parameters and Potential Mechanisms of Action
Luo, Y., Sun, Y., Tian, X., Zheng, X., Wang, X., Li, W., Wu, X., Shu, B., & Hou, W. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.619543 · Cited by 65 · see citing works
Differential Phenotypes of Myeloid-Derived Suppressor and T Regulatory Cells and Cytokine Levels in Amnestic Mild Cognitive Impairment Subjects Compared to Mild Alzheimer Diseased Patients
Page, A. Y. L., Garneau, H., Dupuis, G., Frost, E. H., Larbi, A., Witkowski, J. M., Pawelec, G., & Fülöp, T. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00783 · Cited by 65 · see citing works
Newly Developed Drugs for Alzheimer’s Disease in Relation to Energy Metabolism, Cholinergic and Monoaminergic Neurotransmission
Korábečný, J., Nepovimová, E., Cikánková, T., Špilovská, K., Vašková, L., Mezeiová, E., Kuča, K., & Hroudová, J. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2017.06.034 · Cited by 64 · see citing works
Curcumin improves memory deficits by inhibiting HMGB1‐RAGE/TLR4‐NF‐κB signalling pathway in APPswe/PS1dE9 transgenic mice hippocampus
Han, Y., Chen, R., Lin, Q., Liu, Y., Ge, W., Cao, H., & Li, J. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16855 · Cited by 62 · see citing works
Synthesis and evaluation of frentizole-based indolyl thiourea analogues as MAO/ABAD inhibitors for Alzheimer’s disease treatment
Hroch, L., Guest, P. N., Benek, O., Soukup, O., Janočková, J., Doležal, R., Kuča, K., Aitken, L., Smith, T., Gunn‐Moore, F. J., et al. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.12.029 · Cited by 62 · see citing works
Early functional connectivity deficits and progressive microstructural alterations in the TgF344-AD rat model of Alzheimer’s Disease: A longitudinal MRI study
Anckaerts, C., Blockx, I., Summer, P., Michael, J., Hamaide, J., Kreutzer, C., Boutin, H., Couillard‐Després, S., Verhoye, M., & der Linden, A. V. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.010 · Cited by 62 · see citing works
GSK-3β as a target for apigenin-induced neuroprotection against Aβ 25–35 in a rat model of Alzheimer's disease
Alireza, M. S., Nikbakht, F., Nia, H. H., Golab, F., Khadem, Y., Barati, M., & Vazifekhah, S. (2021) · Neuropeptides · doi:10.1016/j.npep.2021.102200 · Cited by 61 · see citing works
Aromatherapy and Aromatic Plants for the Treatment of Behavioural and Psychological Symptoms of Dementia in Patients with Alzheimer’s Disease: Clinical Evidence and Possible Mechanisms
Scuteri, D., Morrone, L. A., Rombolà, L., Avato, P., Bilia, A. R., Corasaniti, M. T., Sakurada, S., Sakurada, T., & Bagetta, G. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/9416305 · Cited by 59 · see citing works
Design, Synthesis, and Biological Evaluation of 1-Benzylamino-2-hydroxyalkyl Derivatives as New Potential Disease-Modifying Multifunctional Anti-Alzheimer’s Agents
Panek, D., Więckowska, A., Jończyk, J., Godyń, J., Bajda, M., Wichur, T., Pasieka, A., Knez, D., Pišlar, A. H., Korábečný, J., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00461 · Cited by 58 · see citing works
Role of Specialized Pro-resolving Mediators in Reducing Neuroinflammation in Neurodegenerative Disorders
Ponce, J., Ulu, A., Hanson, C., Cameron‐Smith, E., Bertoni, J. M., Wuebker, J., Fisher, A. L., Siu, K., Marmelat, V., Adamec, J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.780811 · Cited by 57 · see citing works
Glycogen Synthase Kinase 3β Involvement in Neuroinflammation and Neurodegenerative Diseases
Gianferrara, T., Cescon, E., Grieco, I., Spalluto, G., & Federico, S. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220216113517 · Cited by 58 · see citing works
The role of Cdk5‐mediated Drp1 phosphorylation in Aβ1‐42 induced mitochondrial fission and neuronal apoptosis
Guo, M., Shang, L., Hu, Y., Jiang, L., Wan, Y., Zhou, Q., Zhang, K., Liao, H., Yi, J., & Han, X. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26680 · Cited by 56 · see citing works
Peptide‐Functionalized Prussian Blue Nanomaterial for Antioxidant Stress and NIR Photothermal Therapy against Alzheimer's Disease
Song, X., Ding, Q., Wei, W., Zhang, J., Sun, R., Yin, L., Liu, S., & Pu, Y. (2023) · Small · doi:10.1002/smll.202206959 · Cited by 55 · see citing works
Alzheimer’s disease in people with Down’s syndrome: the prospects for and the challenges of developing preventative treatments
Castro, P., Zaman, S. H., & Holland, A. J. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8308-8 · Cited by 55 · see citing works
Molecular Insights into Destabilization of Alzheimer’s Aβ Protofibril by Arginine Containing Short Peptides: A Molecular Modeling Approach
Barale, S. S., Parulekar, R. S., Fandilolu, P. M., Dhanavade, M. J., & Sonawane, K. D. (2019) · ACS Omega · doi:10.1021/acsomega.8b02672 · Cited by 55 · see citing works
Self-citation
Synthesis and evaluation of novel GSK-3β inhibitors as multifunctional agents against Alzheimer's disease
Shi, X., Wu, J., Liu, P., & Liu, Z. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.02.001 · Cited by 55 · see citing works

Advances in the pathogenesis of Alzheimer’s disease: a re-evaluation of amyloid cascade hypothesis
Dong, S., Duan, Y., Hu, Y., & Zhao, Z. (2012) · Translational Neurodegeneration · doi:10.1186/2047-9158-1-18 · Cited by 139 · see citing works
Tau and beta-amyloid in Alzheimer’s Disease: Theories, treatments strategies, and future directions
Colautti, J., & Nagales, K. (2021) · The Meducator · doi:10.35493/medu.37.12
The Aβ Hypothesis: Leading Us to Rationally-Designed Therapeutic Strategies for the Treatment or Prevention of Alzheimer Disease
Golde, T. E. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00104.x · Cited by 98 · see citing works
Tau in Alzheimer’s Disease: Pathological Alterations and an Attractive Therapeutic Target
Gu, J., & Liu, F. (2020) · Current Medical Science · doi:10.1007/s11596-020-2282-1 · Cited by 38 · see citing works
A critical analysis of the ‘amyloid cascade hypothesis’
A. Armstrong, R. (2014) · Folia Neuropathologica · doi:10.5114/fn.2014.45562 · Cited by 110 · see citing works

Authors: Barage, S. H., & Sonawane, K. D.
Affiliations: Shivaji University (IN)
Corresponding author: Sonawane, Kailas D.
ORCID: Barage, Sagar H.
Sonawane, Kailas D.
Venue: Neuropeptides
Publisher: Elsevier BV
Published: 2015-08
Volume: 52
Pages: 1-18
ISSN: 0143-4179 (ISSN-L)
DOI: 10.1016/j.npep.2015.06.008
OpenAlex: W2099751992
Cited by: 579
References: 371
Citations by year: 2026: 22 · 2025: 57 · 2024: 75 · 2023: 69 · 2022: 58 · 2021: 67 · 2020: 59 · 2019: 58 · 2018: 51 · 2017: 33 · 2016: 24 · 2015: 5 · 2012: 1
FWCI: 4.66
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neuropeptides (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
Keywords: Alzheimer's disease, amyloid hypothesis, amyloid-beta, amyloid plaques, tau protein, cerebrospinal fluid biomarkers, cholinergic neurotransmission, neurodegeneration, Alzheimer's disease therapeutics, genetic risk factors
MeSH terms: Acetylcholine, Alzheimer Disease, Animals, Brain, Humans, Signal Transduction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Neurofibrillary Tangles, tau Proteins

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

Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks