Amyloid β-Protein and the Genetics of Alzheimer's Disease

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

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Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

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Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease.

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

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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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Hydrogen peroxide mediates amyloid β protein toxicity

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Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene

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The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022

The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor

Brown, M. S., & Goldstein, J. L. (1997) · Cell · doi:10.1016/s0092-8674(00)80213-5 · Cited by 3,834

Regulated Intramembrane Proteolysis

Brown, M. S., Ye, J., Rawson, R. B., & Goldstein, J. L. (2000) · Cell · doi:10.1016/s0092-8674(00)80675-3 · Cited by 1,329

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice

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Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide

Butterfield, D. A., Drake, J., Pocernich, C., & Castegna, A. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02173-6 · Cited by 1,114

Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

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Skeletal and CNS Defects in Presenilin-1-Deficient Mice

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The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease

Selkoe, D. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01363-4 · Cited by 862

Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity

Varadarajan, S., Yatin, S., Aksenova, M., & Butterfield, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4274 · Cited by 735

Progesterone receptors: form and function in brain

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Early Phenotypic Changes in Transgenic Mice That Overexpress Different Mutants of Amyloid Precursor Protein in Brain

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Neuronal SIRT1 Activation as a Novel Mechanism Underlying the Prevention of Alzheimer Disease Amyloid Neuropathology by Calorie Restriction

Qin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., Zhao, W., Thiyagarajan, M., MacGrogan, D., Rodgers, J. T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602909200 · Cited by 626

An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript

Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., Leiter, L., McPhee, J., Sarang, S. S., Utsuki, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207435200 · Cited by 551

Phenolic anti-inflammatory antioxidant reversal of Aβ-induced cognitive deficits and neuropathology

Frautschy, S. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00300-1 · Cited by 514

Sirtuin Functions in Health and Disease

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The glial glutamate transporter, GLT‐1, is oxidatively modified by 4‐hydroxy‐2‐nonenal in the Alzheimer's disease brain: the role of Aβ1–42

Lauderback, C. M., Hackett, J. M., Huang, F. F., Keller, J. N., Szweda, L. I., Markesbery, W. R., & Butterfield, D. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00451.x · Cited by 464

Signal peptidases.

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Complementation Cloning of , a Gene Encoding a Putative Metalloprotease Required for Intramembrane Cleavage of SREBPs

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Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer’s disease

D'Andrea, M. R., Nagele, R. G., Wang, H., Peterson, P. A., & Lee, D. H. S. (2001) · Histopathology · doi:10.1046/j.1365-2559.2001.01082.x · Cited by 390

Chapter 7 Protein Oxidation Processes in Aging Brain

Butterfield, D. A., & Stadtman, E. R. (1997) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60057-7 · Cited by 390

Ts1Cje, a partial trisomy 16 mouse model for Down syndrome, exhibits learning and behavioral abnormalities

Sago, H., Carlson, E. J., Smith, D. J., Kilbridge, J., Rubin, E. M., Mobley, W. C., Epstein, C. J., & Huang, T.-T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6256 · Cited by 382

The role of oxidative stress in the toxicity induced by amyloid β-peptide in Alzheimer’s disease

Miranda, S., Opazo, C., Larrondo, L. F., Muñoz, F. J., Ruiz, F., Leighton, F., & Inestrosa, N. C. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00015-0 · Cited by 369

β-Amyloid-Associated Free Radical Oxidative Stress and Neurotoxicity: Implications for Alzheimer’s Disease

Butterfield, D. A. (1997) · Chemical Research in Toxicology · doi:10.1021/tx960130e · Cited by 364

Different Mechanisms of Oxidative Stress and Neurotoxicity for Alzheimer‘s Aβ(1−42) and Aβ(25−35)

Varadarajan, S., Kanski, J., Aksenova, M., Lauderback, C., & Butterfield, D. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010452r · Cited by 346

Microglia and Alzheimer's disease pathogenesis

Streit, W. J. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20093 · Cited by 335

Comprehensive review of mechanisms of pathogenesis involved in Alzheimer’s disease and potential therapeutic strategies

Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331

A Human Stem Cell Model of Early Alzheimer’s Disease Pathology in Down Syndrome

Shi, Y., Kirwan, P., Smith, J., MacLean, G., Orkin, S. H., & Livesey, F. J. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003771 · Cited by 310

Intracellular Generation and Accumulation of Amyloid β-Peptide Terminating at Amino Acid 42

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Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia

Sondag, C. M., Dhawan, G., & Combs, C. K. (2009) · Journal of Neuroinflammation · doi:10.1186/1742-2094-6-1 · Cited by 295

Transport-Dependent Proteolysis of SREBP

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Amyloid β-induced Changes in Nitric Oxide Production and Mitochondrial Activity Lead to Apoptosis

Keil, U., Bonert, A., Marques, C. A., Scherping, I., Weyermann, J., Strosznajder, J. B., Müller-Spahn, F., Haass, C., Czech, C., Pradier, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405600200 · Cited by 287

Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer’s disease.

Zhang, Z., Song, M., Liu, X., Su Kang, S., Duong, D. M., Seyfried, N. T., Cao, X., Cheng, L., Sun, Y. E., Ping Yu, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9762 · Cited by 277

Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission

Moreno-Gonzalez, I., & Soto, C. (2011) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2011.04.002 · Cited by 252

Deficiency in BDNF/TrkB Neurotrophic Activity Stimulates δ-Secretase by Upregulating C/EBPβ in Alzheimer’s Disease

Wang, Z.-H., Xiang, J., Liu, X., Yu, S. P., Manfredsson, F. P., Sandoval, I. M., Wu, S., Wang, J.-Z., & Ye, K. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.054 · Cited by 238

Turnover of Amyloid β-Protein in Mouse Brain and Acute Reduction of Its Level by Phorbol Ester

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The X11α protein slows cellular amyloid precursor protein processing and reduces Aβ40 and Aβ42 secretion

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Interaction between Aβ(1−42) and Aβ(1−40) in Alzheimer's β-Amyloid Fibril Formation in Vitro

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Isolation, Chemical Characterization, and Quantitation of Aβ 3-Pyroglutamyl Peptide from Neuritic Plaques and Vascular Amyloid Deposits

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Iron dysregulation in Alzheimer's disease: Multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents

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Abnormal localization of iron regulatory protein in Alzheimer’s disease

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Amyloid-β Antibody Treatment Leads to Rapid Normalization of Plaque-Induced Neuritic Alterations

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Interaction of Nascent ApoE2, ApoE3, and ApoE4 Isoforms Expressed in Mammalian Cells with Amyloid Peptide β (1−40). Relevance to Alzheimer's Disease

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Second-site Cleavage in Sterol Regulatory Element-binding Protein Occurs at Transmembrane Junction as Determined by Cysteine Panning

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Histone deacetylase inhibitor valproic acid inhibits cancer cell proliferation via down-regulation of the alzheimer amyloid precursor protein

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Spines, plasticity, and cognition in Alzheimer's model mice

Spires-Jones, T., & Knafo, S. (2012) · Neural Plasticity · doi:10.1155/2012/319836 · Cited by 133

Neuroinflammation and fractalkine signaling in Alzheimer’s disease

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Deposition of Monomeric, Not Oligomeric, Aβ Mediates Growth of Alzheimer's Disease Amyloid Plaques in Human Brain Preparations

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The road ahead for health and lifespan interventions

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Ergothioneine rescues PC12 cells from β-amyloid-induced apoptotic death

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Presenilins and Alzheimer's disease

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ERK1/2 is an endogenous negative regulator of the γsecretase activity

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In Vivo Multiphoton Imaging of a Transgenic Mouse Model of Alzheimer Disease Reveals Marked Thioflavine-S-Associated Alterations in Neurite Trajectories

D'Amore, J. D., Kajdasz, S. T., McLellan, M. E., Bacskai, B. J., Stern, E. A., & Hyman, B. T. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.2.137 · Cited by 89

Oxidation of Aβ and Plaque Biogenesis in Alzheimer's Disease and Down Syndrome

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Impaired Modulation of GABAergic Transmission by Muscarinic Receptors in a Mouse Transgenic Model of Alzheimer's Disease

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Age, Alzheimer's disease and dementia in the Baltimore Longitudinal Study of Ageing

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Tau-induced pathology in epilepsy and dementia: notions from patients and animal models.

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Untitled work

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Prevention of the Neurotoxicity of the Amyloid Beta Protein by Genipin

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IGFBPL1 is a master driver of microglia homeostasis and resolution of neuroinflammation in glaucoma and brain tauopathy

Pan, L., Cho, K.-S., Wei, X., Xu, F., Lennikov, A., Hu, G., Tang, J., Guo, S., Chen, J., Kriukov, E., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112889 · Cited by 52

Neurofibrillary degeneration in Alzheimer's disease: from molecular mechanisms to identification of drug targets

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Promotion of β-amyloid production by C-reactive protein and its implications in the early pathogenesis of Alzheimer’s disease

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Pro-inflammatory effect of freshly solubilized β-amyloid peptides in the brain

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Regulation of the NMDA receptor-mediated synaptic response by acetylcholinesterase inhibitors and its impairment in an animal model of Alzheimer's disease

Chen, G., Chen, P., Tan, H., Ma, D., Dou, F., Feng, J., & Yan, Z. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.023 · Cited by 36

C/EBPβ/AEP Signaling Drives Alzheimer’s Disease Pathogenesis

Xiong, J., Zhang, Z., & Ye, K. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01025-w · Cited by 37

Axonal Terminals Exposed to Amyloid-β May Not Lead to Pre-Synaptic Axonal Damage

Sun, S.-W., Nishioka, C., Labib, W., & Liang, H.-F. (2015) · Journal of Alzheimer’s Disease · doi:10.3233/jad-142154 · Cited by 8