The Relationship between Amyloid and Tau

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Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

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Molecular basis of myotonic dystrophy: Expansion of a trinucleotide (CTG) repeat at the 3′ end of a transcript encoding a protein kinase family member

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Candidate gene for the chromosome 1 familial Alzheimer’s disease locus

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Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein

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Niemann-Pick C1 Disease Gene: Homology to Mediators of Cholesterol Homeostasis

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Amyloid, the presenilins and Alzheimer’s disease

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Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

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Lewy Bodies Contain Altered α-Synuclein in Brains of Many Familial Alzheimer's Disease Patients with Mutations in Presenilin and Amyloid Precursor Protein Genes

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Apolipoprotein E is essential for amyloid deposition in the <i>APP</i> ^V717F transgenic mouse model of Alzheimer's disease

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A stop-codon mutation in the BRI gene associated with familial British dementia

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Susceptibility Locus for Alzheimer's Disease on Chromosome 10

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Pathologic and biochemical studies of juvenile parkinsonism linked to chromosome 6q

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Capacitative Calcium Entry Deficits and Elevated Luminal Calcium Content in Mutant Presenilin-1 Knockin Mice

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Mutant prion proteins in Gerstmann-Sträussler-Scheinker disease with neurofibrillary tangles

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Lewy bodies in the brain of two members of a family with the 717 (Val to Ile) mutation of the amyloid precursor protein gene.

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Genetic variability at the amyloid-β precursor protein locus may contribute to the risk of late-onset Alzheimer's disease

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Pathways to Primary Neurodegenerative Disease

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The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics

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THE BIOCHEMISTRY OF PARKINSON'S DISEASE

Cookson, M. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133400 · Cited by 659 · see citing works

Tau phosphorylation in neuronal cell function and dysfunction

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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

Tau phosphorylation: physiological and pathological consequences

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Genetics of Parkinson's disease and parkinsonism

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Cdk5 deregulation in the pathogenesis of Alzheimer's disease

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Pivotal role of glycogen synthase kinase-3: A therapeutic target for Alzheimer's disease

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Donepezil-based multi-functional cholinesterase inhibitors for treatment of Alzheimer's disease

Li, Q., He, S., Chen, Y., Feng, F., Qu, W., & Sun, H. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.031 · Cited by 211 · see citing works

A Cdk5 inhibitory peptide reduces tau hyperphosphorylation and apoptosis in neurons

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Stem cell derived basal forebrain cholinergic neurons from Alzheimer’s disease patients are more susceptible to cell death

Duan, L., Bhattacharyya, B. J., Belmadani, A. A., Pan, L., Miller, R. J., & Kessler, J. A. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-3 · Cited by 159 · see citing works

Interaction between pathogenic proteins in neurodegenerative disorders

Jellinger, K. A. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01507.x · Cited by 128 · see citing works

Dual GSK-3β/AChE Inhibitors as a New Strategy for Multitargeting Anti-Alzheimer’s Disease Drug Discovery

Jiang, X.-Y., Chen, T.-K., Zhou, J.-T., He, S.-Y., Yang, H.-Y., Chen, Y., Qu, W., Feng, F., & Sun, H.-P. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00463 · Cited by 122 · see citing works

The emerging role of peptidyl‐prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease

Blair, L. J., Baker, J. D., Sabbagh, J. J., & Dickey, C. A. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13033 · Cited by 120 · see citing works

The Role of microRNAs in Alzheimer’s Disease and Their Therapeutic Potentials

Shaik, M. M., Tamargo, I. A., Abubakar, M. B., Kamal, M. A., Greig, N. H., & Gan, S. H. (2018) · Genes · doi:10.3390/genes9040174 · Cited by 114 · see citing works

Glycogen Synthase Kinase 3β Induces Caspase-cleaved Tau Aggregation in Situ

Cho, J., & Johnson, G. V. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403364200 · Cited by 116 · see citing works

Amyloid Fibril Formation of α-Synuclein Is Accelerated by Preformed Amyloid Seeds of Other Proteins

Yagi, H., Kusaka, E., Hongo, K., Mizobata, T., & Kawata, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508623200 · Cited by 111 · see citing works

c-Abl tyrosine kinase modulates tau pathology and Cdk5 phosphorylation in AD transgenic mice

Cancino, G. I., Perez de Arce, K., Castro, P. U., Toledo, E. M., von Bernhardi, R., & Alvarez, A. R. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.07.007 · Cited by 110 · see citing works

Discovery and Biological Evaluation of a Novel Highly Potent Selective Butyrylcholinsterase Inhibitor

Li, Q., Xing, S., Chen, Y., Liao, Q., Xiong, B., He, S., Lu, W., Liu, Y., Yang, H., Li, Q., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01129 · Cited by 106 · see citing works

Neurodegeneration in an Aβ‐induced model of Alzheimer’s disease: the role of Cdk5

Lopes, J. P., Oliveira, C. R., & Agostinho, P. M. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00536.x · Cited by 86 · see citing works

The binding affinity of anti-Aβ1-42 MAb-decorated nanoliposomes to Aβ1-42 peptides in vitro and to amyloid deposits in post-mortem tissue

Canovi, M., Markoutsa, E., Lazar, A. N., Pampalakis, G., Clemente, C., Re, F., Sesana, S., Masserini, M., Salmona, M., Duyckaerts, C. J., et al. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.04.020 · Cited by 83 · see citing works

Interactive Domains in the Molecular Chaperone Human αB Crystallin Modulate Microtubule Assembly and Disassembly

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Interaction between -Synuclein and Other Proteins in Neurodegenerative Disorders

Jellinger, K. A. (2011) · The Scientific World JOURNAL · doi:10.1100/2011/371893 · Cited by 63 · see citing works

Role of Cyclin-Dependent Kinase 5 in the Neurodegenerative Process Triggered by Amyloid-Beta and Prion Peptides: Implications for Alzheimer’s Disease and Prion-Related Encephalopathies

Lopes, J. P., Oliveira, C. R., & Agostinho, P. M. (2007) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-007-9224-3 · Cited by 63 · see citing works

Caspase-cleaved tau accumulation in neurodegenerative diseases associated with tau and α-synuclein pathology

Newman, J., Rissman, R. A., Sarsoza, F. M., Kim, R. C., Dick, M. B., Bennett, D. A., Cotman, C. W., Rohn, T. T., & Head, E. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1027-3 · Cited by 55 · see citing works

Neuroimaging and the Search for a Cure for Alzheimer Disease

Petrella, J. R. (2013) · Radiology · doi:10.1148/radiol.13122503 · Cited by 47 · see citing works

Pharmacological Findings on the Biochemical Bases of Memory Processes: A General View

Izquierdo, I., Cammarota, M., Medina, J., & Bevilaqua, L. (2004) · Journal of Neural Transplantation and Plasticity · doi:10.1155/np.2004.159 · Cited by 41 · see citing works

Toward Alzheimer Therapies Based on Genetic Knowledge

Hardy, J. (2004) · Annual Review of Medicine · doi:10.1146/annurev.med.55.091902.103607 · Cited by 41 · see citing works

Dictyostelium: An Important Source of Structural and Functional Diversity in Drug Discovery

Kubohara, Y., & Kikuchi, H. (2018) · Cells · doi:10.3390/cells8010006 · Cited by 39 · see citing works

Age-related increase in amyloid plaque burden is associated with impairment in conditioned fear memory in CRND8 mouse model of amyloidosis

Hanna, A., Iremonger, K., Das, P., Dickson, D., Golde, T., & Janus, C. (2012) · Alzheimer's Research &amp; Therapy · doi:10.1186/alzrt124 · Cited by 38 · see citing works

Alzheimer?s disease?a sum greater than its parts?

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S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions

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The end of Alzheimer's disease—From biochemical pharmacology to ecopsychosociology: A personal perspective

Whitehouse, P. J. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.11.017 · Cited by 30 · see citing works

Understanding Glycogen Synthase Kinase-3: A Novel Avenue for Alzheimer’s Disease

Sequeira, R. C., & Godad, A. P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03839-1 · Cited by 30 · see citing works

New insights into the role of the branched‐chain aminotransferase proteins in the human brain

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Some evolutionary perspectives on Alzheimer's disease pathogenesis and pathology

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Why Alzheimer's Disease Starts with a Memory Impairment: Neurophysiological Insight

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The Quest for Cellular Prion Protein Functions in the Aged and Neurodegenerating Brain

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Mechanism-based treatments for Alzheimer's disease

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Relative paucity of tau accumulation in the small areas with abundant Aβ42-positive capillary amyloid angiopathy within a given cortical region in the brain of patients with Alzheimer pathology

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Coexisting Cholinergic and Parahippocampal Degeneration: A Key to Memory Loss in Dementia and a Challenge for Transgenic Models?

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TRAIL‐related neurotoxicity implies interaction with the Wnt pathway in human neuronal cells in vitro

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The Amyloid β Protein

Lazo, N. D., Maji, S. K., Fradinger, E. A., Bitan, G., & Teplow, D. B. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch17 · Cited by 18 · see citing works

Investigation of the Flexibility of Protein Kinases Implicated in the Pathology of Alzheimer’s Disease

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A reaction–diffusion model of spatial propagation of A$$\beta $$ oligomers in early stage Alzheimer’s disease

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Inhibitory Effect of Piperlonguminine/Dihydropiperlonguminine on the Production of Amyloid β and APP in SK-N-SH Cells

Qi, H.-S. (2009) · The Chinese Journal of Physiology · doi:10.4077/cjp.2009.amh062 · Cited by 15 · see citing works

Isolation of short peptide fragments from α-synuclein fibril core identifies a residue important for fibril nucleation: A possible implication for diagnostic applications

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Reduced amyloidogenic processing of the amyloid β-protein precursor by the small-molecule Differentiation Inducing Factor-1

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Discovery of a highly selective BChE inhibitor with concomitant anti-neuroinflammatory activity for treating Alzheimer's disease

Zhao, Y., Wu, K., Luo, W., Zhao, Y., Zeng, J., Wu, J., Yang, C., Yang, M., Liu, J., Lei, Z., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118071 · Cited by 11 · see citing works

Inhibition of beta-amyloid precursor protein gene in SK-N-SH cells by piperlonguminine/dihydropiperlonguminine components separated from Chinese herbal medicine Futokadsura stem.

Xia, W. R., Zeng, J., Chen, L.-B., Jiang, A.-L., Xiang, L., Xu, J., Cui, X., & Han, E. (2007) · PubMed · Cited by 9 · see citing works

Caspases in Alzheimer’s Disease

Zhang, Y. (2013) · InTech eBooks · doi:10.5772/54627 · Cited by 8 · see citing works

Neuroprotective Effects of an Aqueous Extract of Futokadsura Stem in an Aβ-Induced Alzheimer's Disease-Like Rat Model

Xia, W. R. (2015) · The Chinese Journal of Physiology · doi:10.4077/cjp.2015.bad273 · Cited by 8 · see citing works

Reversal of Tau-Dependent Cognitive Decay by Blocking Adenosine A1 Receptors: Comparison of Transgenic Mouse Models with Different Levels of Tauopathy

Anglada‐Huguet, M., Endepols, H., Sydow, A., Hilgers, R., Neumaier, B., Drzezga, A. E., Kaniyappan, S., Mandelkow�, E., & Mandelkow, E.-M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119260 · Cited by 7 · see citing works

Tau Exon 10 Inclusion by PrPC through Downregulating GSK3β Activity

Lidón, L., Llaó-Hierro, L., Nuvolone, M., Aguzzi, A., Ávila, J., Ferrer, I., del Rı́o, J. A., & Gavı́n, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105370 · Cited by 6 · see citing works

Design, synthesis, and pharmacological characterization of sulfonylurea-based NLRP3 inhibitors: Towards an effective therapeutic strategy for Alzheimer's disease

Lyu, W., Gao, T., Shi, C., Lu, D., Chen, Y., Qin, H., Yu, R., Zhang, H., Zhou, X., Qiang, B., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116993 · Cited by 5 · see citing works

Effective Reduction of Tau Amyloid Aggregates in the Presence of Cyclophilin from Platanus orientalis Pollens; An Alternative Mechanism of Action of the Allergen

Mehrabi, M., Bijari, N., Akbari, V., Ranjbar, S., Karima, S., Sankian, M., Ojaghi, S., & Khodarahmi‬, R. (2023) · Current Protein and Peptide Science · doi:10.2174/1389203724666230530143704 · Cited by 5 · see citing works

IM-MS and ECD-MS/MS Provide Insight into Modulation of Amyloid Proteins Self-Assembly by Peptides and Small Molecules

Taha, H. B., Chawla, E., & Bitan, G. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00065 · Cited by 4 · see citing works

Summary of the Current Status of DNA Vaccination for Alzheimer Disease

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Amyloid Hypothesis and Alzheimer's Disease

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Neuroinflammation-Modulating Agent SB1617 Enhances LC3-Associated Phagocytosis to Mitigate Tau Pathology

Cho, H., Choi, B. Y., Shin, Y., Suh, S. W., & Park, S. B. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00508 · Cited by 4 · see citing works

Linking higher amyloid beta 1‐38 (Aβ(1‐38)) levels to reduced Alzheimer's disease progression risk

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Ultrasmall superparamagnetic iron oxide nanoparticles conjugated with Ile-Pro-Leu-Pro-Phe-Tyr-Asn

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Why Are Humans Vulnerable to Alzheimer’s Disease?

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Cardiovascular drugs and triazole based kinase inhibitors as a new strategies for the treatment of Alzheimer disease

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Different Inhibitors of Aβ42-Induced Toxicity Have Distinct Metal-Ion Dependency

Mason, A. J., Hurst, I., Malik, R., Siddique, I. A., Solomonov, I., Sagi, I., Klärner, F., Schrader, T. H., & Bitan, G. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00192 · Cited by 2 · see citing works

Utilizing fractional-order operator to Alzheimer’s disease dynamics

Nisar, K. S., & Farman, M. (2026) · Scientific Reports · doi:10.1038/s41598-025-33804-y · Cited by 1 · see citing works

Demenze degenerative primarie

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2-(4-(2-[18F]Fluoroethyl)piperidin-1-yl)benzo[4,5]imidazo[1,2-a]pyrimidine

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N-Methyl-[11C]-2-(4'-methylaminophenyl)-6-hydroxybenzothiasole

Leung, K. (2005) · National Center for Biotechnology Information (US) eBooks

Multivalent Synthetic Receptors for Proteins

Polkowska, J., Talbiersky, P., & Schrader, T. H. (2009) · Wiley eBooks · doi:10.1002/9783527627011.ch8

Effekte der Inhibition von ROCK und Rac1 auf Neuronen

Kosarev, S. (2013) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-16830

Observations on cerebral amyloid angiopathy and microvascular pathology in Alzheimer's disease and vascular dementia

Haglund, M. (2005) · Lund University Publications (Lund University)

(E)-3-(4-(Dimethylamino)phenyl)-1-(4-(2-(([18F]fluoroethoxy)ethoxy)ethoxy)phenyl)-2-propen-1-one

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2-(4-Aminophenyl)-6-(2-([18F]fluoroethoxy))quinoline

Leung, K. (2011) · Europe PMC (PubMed Central)

Trans-4-(N-Methylamino)-4´-{2-[2-(2-[18F]fluoro-ethoxy)-ethoxy]-ethoxy}-stilbene

Leung, K. (2009)

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Reversal of tau-dependent cognitive decay by blocking adenosine A1 receptors in mouse models of tauopathyPreprint

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Fluorinated Peptidomimetics : Synthesis, Conformational Studies and Evaluation as Amyloid Proteins Aggregation Modulators

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BindingDB Entry 50011055: Discovery and Biological Evaluation of a Novel Highly Potent Selective Butyrylcholinsterase Inhibitor.

BindingDB (2021) · UC San Diego · doi:10.7270/q2bp06c1

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BindingDB (2026) · UC San Diego · doi:10.7270/q2tf036g

BindingDB Entry 50003138: Donepezil-based multi-functional cholinesterase inhibitors for treatment of Alzheimer's disease.

BindingDB (2020) · UC San Diego · doi:10.7270/q26h4m3z

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BindingDB (2020) · UC San Diego · doi:10.7270/q2mg7s5f

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BindingDB (2017) · UC San Diego · doi:10.7270/q2th8ph8

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