Cited by 1,268Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.

Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline

Näslund, Jan·2000·JAMA

DOI 10.1001/jama.283.12.1571

Open this paper in CoChat — free account

Abstract

CONTEXT: Alzheimer disease (AD) is characterized neuropathologically by the presence of amyloid beta-peptide (Abeta)-containing plaques and neurofibrillary tangles composed of abnormal tau protein. Considerable controversy exists as to whether the extent of accumulation of Abeta correlates with dementia and whether Abeta alterations precede or follow changes in tau. OBJECTIVES: To determine whether accumulation of Abeta correlates with the earliest signs of cognitive deterioration and to define the relationship between Abeta accumulation and early tau changes. DESIGN, SETTING, AND PATIENTS: Postmortem cross-sectional study of 79 nursing home residents with Clinical Dementia Rating (CDR) scale scores of 0.0 to 5.0 who died between 1986 and 1997, comparing the levels of Abeta variants in the cortices of the subjects with no (CDR score, 0.0 [n = 16]), questionable (CDR score, 0.5 [n = 11]), mild (CDR score, 1.0 [n = 22]), moderate (CDR score, 2.0 [n = 15]), or severe (CDR score, 4.0 or 5.0 [n = 15]) dementia. MAIN OUTCOME MEASURES: Levels of total Abeta peptides with intact or truncated amino termini and ending in either amino acid 40 (A(beta)x-40) or 42 (A(beta)x-42) in 5 neocortical brain regions as well as levels of tau protein undergoing early conformational changes in frontal cortex, as a function of CDR score. RESULTS: The levels of both A(beta)x-40 and A(beta)x-42 were elevated even in cases classified as having questionable dementia (CDR score = 0.5), and increases of both peptides correlated with progression of dementia. Levels of the more fibril-prone A(beta)x-42 peptide were higher than those of A(beta)x-40 in nondemented cases and remained higher throughout progression of disease in all regions examined. Finally, increases in A(beta)x-40 and A(beta)x-42 precede significant tau pathology at least in the frontal cortex, an area chosen for examination because of the absence of neuritic changes in the absence of disease. CONCLUSIONS: In this study, levels of total A(beta)x-40 and A(beta)x-42 were elevated early in dementia and levels of both peptides were strongly correlated with cognitive decline. Of particular interest, in the frontal cortex, Abeta was elevated before the occurrence of significant tau pathology. These results support an important role for Abeta in mediating initial pathogenic events in AD dementia and suggest that treatment strategies targeting the formation, accumulation, or cytotoxic effects of Abeta should be pursued.

Integrity signals

Registry

Crossref · 10.1001/jama.283.12.1571

Cites

28 of 28 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?

A New Clinical Scale for the Staging of Dementia
Hughes, C. P., Berg, L., Danziger, W., Coben, L. A., & Martin, R. L. (1982) · British Journal of Psychiatry · doi:10.1192/bjp.140.6.566 · Cited by 7,056
The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668
Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
Amyloid, the presenilins and Alzheimer’s disease
Hardy, J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01030-2 · Cited by 1,370
Mechanisms of Neuronal Degeneration in Alzheimer's Disease
Yankner, B. A. (1996) · Neuron · doi:10.1016/s0896-6273(00)80115-4 · Cited by 953
Alzheimer's Disease--Genotypes, Phenotype, and Treatments
Selkoe, D. J. (1997) · Science · doi:10.1126/science.275.5300.630 · Cited by 879
Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
Haass, C., & Selkoe, D. J. (1993) · Cell · doi:10.1016/0092-8674(93)90312-e · Cited by 686
Tau protein pathology in neurodegenerative diseases
Spillantini, M. G., & Goedert, M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01337-x · Cited by 683
Neurochemical Correlates of Dementia Severity in Alzheimer's Disease: Relative Importance of the Cholinergic Deficits
Bierer, L. M., Haroutunian, V. H., Gabriel, S., Knott, P. J., Carlin, L. S., Purohit, D. P., Perl, D. P., Schmeidler, J., Kanof, P. D., & Davis, K. L. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64020749.x · Cited by 580

Show all 28 references

Sorted by citations

Items 201–300 of 1,000

Do CSF total tau, phosphorylated tau, and β-amyloid 42 help to predict progression of mild cognitive impairment to Alzheimer's disease? A systematic review and meta-analysis of the literature
Diniz, B. S., Pinto, J. A., & Forlenza, O. V. (2008) · The World Journal of Biological Psychiatry · doi:10.1080/15622970701535502 · Cited by 173
Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange
Kheterpal, I., Zhou, S., Cook, K. D., & Wetzel, R. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250288897 · Cited by 168
A neural cell adhesion molecule–derived peptide reduces neuropathological signs and cognitive impairment induced by Aβ25-35
Klementiev, B., Novikova, T. A., Novitskaya, V., Walmod, P. S., Dmytriyeva, O., Pakkenberg, B., Berezin, V., & Bock, E. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2006.11.060 · Cited by 166
Regulation of Bcl‐2 family proteins, neurotrophic factors, and APP processing in the neurorescue activity of propargylamine
Bar‐Am, O., Weinreb, O., Amit, T., & Youdim, M. B. H. (2005) · The FASEB Journal · doi:10.1096/fj.05-3794fje · Cited by 165
Age-dependent decline of neprilysin in Alzheimer's disease and normal brain: Inverse correlation with Aβ levels
Hellström‐Lindahl, E., Ravid, R., & Nordberg, A. K. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.010 · Cited by 167
Aluminum, copper, iron and zinc differentially alter amyloid-Aβ1–42 aggregation and toxicity
Bolognin, S., Luigi Messori, A., Drago, D., Gabbiani, C., Cendron, L., & Zatta, P. F. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.02.009 · Cited by 165
Immune hyporesponsiveness to amyloid β-peptide in amyloid precursor protein transgenic mice: Implications for the pathogenesis and treatment of Alzheimer's disease
Monsonego, A., Maron, R., Zota, V. E., Selkoe, D. J., & Weiner, H. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191118298 · Cited by 162
Coenzyme Q10 Decreases Amyloid Pathology and Improves Behavior in a Transgenic Mouse Model of Alzheimer's Disease
Dumont, M., Kipiani, K., Yu, F., Wille, E. J., Katz, M., Calingasan, N. Y., Gouras, G. K., Lin, M. T. S., & Beal, M. F. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110209 · Cited by 164
ALZHEIMER'S DISEASE AND RELATED DISORDERS
Raskind, M. A., & Peskind, E. R. (2001) · Medical Clinics of North America · doi:10.1016/s0025-7125(05)70341-2 · Cited by 161
The role of an astrocytic NADPH oxidase in the neurotoxicity of amyloid beta peptides
Abramov, A. Y., & Duchen, M. R. (2005) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1766 · Cited by 158
Amyloid‐ß‐directed immunotherapy for Alzheimer's disease
Lannfelt, L., Relkin, N. R., & Siemers, E. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12168 · Cited by 161
An amyloid-β protofibril-selective antibody prevents amyloid formation in a mouse model of Alzheimer's disease
Lord, A., Gumucio, A., Englund, H., Sehlin, D., Sundquist, V. S., Söderberg, L., Möller, C., Gellerfors, P., Lannfelt, L., Pettersson, F. E., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.08.007 · Cited by 158
Mapping synaptic glutamate transporter dysfunction in vivo to regions surrounding Aβ plaques by iGluSnFR two-photon imaging
Hefendehl, J. K., LeDue, J. M., Ko, R. W. Y., Mahler, J., Murphy, T. H., & MacVicar, B. A. (2016) · Nature Communications · doi:10.1038/ncomms13441 · Cited by 164
The molecular and genetic basis of AD: The end of the beginning
Rosenberg, R. N. (2000) · Neurology · doi:10.1212/wnl.54.11.2045 · Cited by 158
Bacopa monniera extract reduces amyloid levels in PSAPP mice
Holcomb, L. A., Dhanasekaran, M., Hitt, A. R., Young, K. A., Riggs, M., & Manyam, B. V. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9303 · Cited by 156
Immunotherapy for Alzheimer's disease
Gélinas, D. S., Silva, K. D., Fenili, D., George‐Hyslop, P. S., & McLaurin, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404866101 · Cited by 161
Animal models of Alzheimer’s disease: Applications, evaluation, and perspectives
Chen, Z.-Y., 北京大学生命科学学院膜生物学国家重点实验室, 北. 1., State Key Laboratory of Membrane Biology, C. O. L. S., & Zhang, Y. (2022) · Zoological Research · doi:10.24272/j.issn.2095-8137.2022.289 · Cited by 155
Amyloid-β immunisation for Alzheimer's disease
Wisniewski, T., & Konietzko, U. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70170-4 · Cited by 155
Melatonin Reverses the Profibrillogenic Activity of Apolipoprotein E4 on the Alzheimer Amyloid Aβ Peptide
Pöeggeler, B., Miravalle, L., Zagorski, M. G., Wısnıewskı, T., Chyan, Y., Zhang, Y., Shao, H., Bryant‐Thomas, T., Vidal, R., Frangione, B., et al. (2001) · Biochemistry · doi:10.1021/bi0114269 · Cited by 154
Aβ as a bioflocculant: implications for the amyloid hypothesis of Alzheimer’s disease
Robinson, S. R., & Bishop, G. M. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00342-6 · Cited by 155
BACE1 (β-secretase) transgenic and knockout mice: identification of neurochemical deficits and behavioral changes
Harrison, S. M., Harper, A. J., Hawkins, J., Duddy, G., Grau, E., Pugh, P. L., Winter, P. H., Shilliam, C. S., Hughes, Z. A., Dawson, L. A., et al. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(03)00227-6 · Cited by 152
Blood-brain barrier drug delivery of IgG fusion proteins with a transferrin receptor monoclonal antibody
Pardridge, W. M. (2015) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.2014.952627 · Cited by 152
Perspectives on future Alzheimer therapies: amyloid-β protofibrils - a new target for immunotherapy with BAN2401 in Alzheimer’s disease
Lannfelt, L., Möller, C., Basun, H., Osswald, G., Sehlin, D., Satlin, A., Logovinsky, V., & Gellerfors, P. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt246 · Cited by 153
Diagnostic Accuracy of Memory Measures in Alzheimer’s Dementia and Mild Cognitive Impairment: a Systematic Review and Meta-Analysis
Weissberger, G. H., Strong, J. V., Stefanidis, K. B., Summers, M. J., Bondi, M. W., & Stricker, N. H. (2017) · Neuropsychology Review · doi:10.1007/s11065-017-9360-6 · Cited by 169
Alzheimer’s Disease as a Membrane Disorder: Spatial Cross-Talk Among Beta-Amyloid Peptides, Nicotinic Acetylcholine Receptors and Lipid Rafts
Fabiani, C., & Antollini, S. S. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00309 · Cited by 158
Partial Purification and Characterization of γ-Secretase from Post-mortem Human Brain
Farmery, M. R., Tjernberg, L. O., Pursglove, S. E., Bergman, A., Winblad, B. G., & Näslund, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211992200 · Cited by 152
Self-citation
Association of increased cortical soluble Aβ42 levels with diffuse plaques after severe brain injury in humans
DeKosky, S. T., Abrahamson, E. E., Ciallella, J. R., Paljug, W. R., Wisniewski, S. R., Clark, R. S. B., & Ikonomovic, M. D. (2007) · Archives of Neurology · doi:10.1001/archneur.64.4.541 · Cited by 152
Large Aggregates Are the Major Soluble Aβ Species in AD Brain Fractionated with Density Gradient Ultracentrifugation
Sehlin, D., Englund, H., Simu, B., Karlsson, M., Ingelsson, M., Nikolajeff, F. K., Lannfelt, L., & Pettersson, F. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032014 · Cited by 150
Soluble pre-fibrillar tau and β-amyloid species emerge in early human Alzheimer’s disease and track disease progression and cognitive decline
Koss, D. J., Jones, G., Cranston, A., Gardner, H., Kanaan, N. M., & Platt, B. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1632-3 · Cited by 155
Multiple events lead to dendritic spine loss in triple transgenic Alzheimer’s disease mice
Bittner, T., Fuhrmann, M., Burgold, S., Ochs, S. M., Hoffmann, N., Mitteregger, G., Kretzschmar, H., LaFerla, F. M., & Herms, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015477 · Cited by 149
Amyloid β-Induced Nerve Growth Factor Dysmetabolism in Alzheimer Disease
Bruno, M. A., León, W., Fragoso, G., Mushynski, W. E., Almazán, G., & Cuello, A. C. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181aed9e6 · Cited by 152
Elevated plasma amyloid β-peptide 1–42 and onset of dementia in adults with Down syndrome
Schupf, N., Patel, B. N., Silverman, W. P., Zigman, W. B., Zhong, N., Tycko, B., Mehta, P. D., & Mayeux, R. P. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01657-3 · Cited by 148
Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains
Welander, H., Frånberg, J., Graff, C., Sundström, E., Winblad, B. G., & Tjernberg, L. O. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06170.x · Cited by 150
Targeting the Alpha 7 Nicotinic Acetylcholine Receptor to Reduce Amyloid Accumulation in Alzheimers Disease Pyramidal Neurons
D’Andrea, M. R., & Nagele, R. G. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206775474224 · Cited by 147
Neuroinflammation and anti-inflammatory therapy for Alzheimer’s disease
Moore, A. H., & O’Banion, M. K. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00162-x · Cited by 150
Cognition, glucose metabolism and amyloid burden in Alzheimer's disease
Furst, A. J., Rabinovici, G. D., Rostomian, A. H., Steed, T., Alkalay, A., Racine, C. A., Miller, B. L., & Jagust, W. J. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.03.011 · Cited by 153
Alzheimer's disease
Schachter, A. S., & Davis, K. L. (2000) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2000.2.2/asschachter · Cited by 153
Biochemically-defined pools of amyloid-β in sporadic Alzheimer’s disease: correlation with amyloid PET
Roberts, B. R., Lind, M., Wagen, A. Z., Rembach, A., Frugier, T., Li, Q.-X., Ryan, T. M., McLean, C. A., Doecke, J. D., Rowe, C. C., et al. (2017) · Brain · doi:10.1093/brain/awx057 · Cited by 143
Therapeutic Potential of γ -Secretase Inhibitors and Modulators
Imbimbo, B. (2008) · Current Topics in Medicinal Chemistry · doi:10.2174/156802608783334015 · Cited by 143
Wnt signaling in Alzheimer's disease: Up or down, that is the question
Boonen, R. A. C. M., van Tijn, P., & Živković, D. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2008.11.003 · Cited by 143
Quantification of Alzheimer pathology in ageing and dementia: age‐related accumulation of amyloid‐β(42) peptide in vascular dementia
Lewis, H. D., Beher, D., Cookson, N., Oakley, A. E., Piggott, M. A., Morris, C. M., Jaros, E., Perry, R., Ince, P. G., Kenny, R. A., et al. (2006) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00696.x · Cited by 143
Cell Biology of Prions and Prionoids: A Status Report
Aguzzi, A., & Lakkaraju, A. K. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.08.007 · Cited by 148
Place cell firing correlates with memory deficits and amyloid plaque burden in Tg2576 Alzheimer mouse model
Cacucci, F., Yi, M., Wills, T. J., Chapman, P. F., & O'Keefe, J. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802908105 · Cited by 148
Synaptotoxic Amyloid-β Oligomers: A Molecular Basis for the Cause, Diagnosis, and Treatment of Alzheimer's Disease?
Klein, W. L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129039 · Cited by 145
Role of calpain in apoptosis.
Momeni, H. R. (2011) · Europe PMC (PubMed Central) · Cited by 141
The neuropathological profile of mild cognitive impairment (MCI): a systematic review
Stephan, B. C. M., Hunter, S., Harris, D., Llewellyn, D. J., Siervo, M., Matthews, F. E., & Brayne, C. (2011) · Molecular Psychiatry · doi:10.1038/mp.2011.147 · Cited by 153
Biochemistry and Molecular Biology of Amyloid β‐Protein and the Mechanism of Alzheimer's Disease
(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(07)01223-7 · Cited by 137
Site-Specific Blockade of RAGE-VdPrevents Amyloid-β Oligomer Neurotoxicity
Sturchler, E., Galichet, A., Weibel, M., Leclerc, E., & Heizmann, C. W. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4878-07.2008 · Cited by 136
Associations between white matter microstructure and amyloid burden in preclinical Alzheimer’s disease: a multimodal imaging investigation.
Racine, A. M., Adluru, N., Alexander, A. L., Christian, B. T., Okonkwo, O. C., Oh, J., Cleary, C. A., Birdsill, A., Hillmer, A. T., Murali, D., et al. (2014) · NeuroImage: Clinical · doi:10.1016/j.nicl.2014.02.001 · Cited by 136
Overexpression of hAPPswe Impairs Rewarded Alternation and Contextual Fear Conditioning in a Transgenic Mouse Model of Alzheimer's Disease
Corcoran, K. A., Lu, Y., Turner, R. S., & Maren, S. (2002) · Learning & Memory · doi:10.1101/lm.51002 · Cited by 135
Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease
Lloret, A., Fuchsberger, T., Giraldo, E., & Viña, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.028 · Cited by 135
LRP in Amyloid‐β Production and Metabolism
Bu, G., Cam, J. A., & Zerbinatti, C. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.005 · Cited by 141
Pathophysiology of Alzheimer's Disease
Imbimbo, B. P., Lombard, J., & Pomara, N. (2005) · Neuroimaging Clinics of North America · doi:10.1016/j.nic.2005.09.009 · Cited by 137
Alzheimer's disease: insights from Drosophila melanogaster models
Moloney, A. M., Sattelle, D. B., Lomas, D. A., & Crowther, D. C. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.11.004 · Cited by 135
Properties of scyllo–inositol as a therapeutic treatment of AD-like pathology
Fenili, D., Brown, M., Rappaport, R. V., & McLaurin, J. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0156-7 · Cited by 136
The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species
Bien, J., Jefferson, T., Čaušević, M., Jumpertz, T., Munter, L., Multhaup, G., Weggen, S., Becker-Pauly, C., & Pietrzik, C. U. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.395608 · Cited by 136
Calcium Ions Promote Formation of Amyloid β-Peptide (1–40) Oligomers Causally Implicated in Neuronal Toxicity of Alzheimer's Disease
Itkin, A., Duprès, V., Dufrêne, Y. F., Bechinger, B., Ruysschaert, J., & Raussens, V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018250 · Cited by 131
Clioquinol Decreases Amyloid-β Burden and Reduces Working Memory Impairment in a Transgenic Mouse Model of Alzheimer's Disease
Grossi, C., Francese, S., Casini, A., Rosi, M. C., Luccarini, I., Fiorentini, A., Gabbiani, C., Luigi Messori, A., Moneti, G., & Casamenti, F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1063 · Cited by 131
Behavioral Assessment of Alzheimer's Transgenic Mice Following Long-Term A β Vaccination: Task Specificity and Correlations between A β Deposition and Spatial Memory
Arendash, G. W., Gordon, M. N., Diamond, D. M., Austin, L. A., Hatcher-Martin, J. M., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., & Morgan, D. (2001) · DNA and Cell Biology · doi:10.1089/10445490152717604 · Cited by 130
Dissociation of neuropathology from severity of dementia in late-onset Alzheimer disease
Prohovnik, I., Perl, D. P., Davis, K. L., Libow, L. S., Lesser, G. T., & Haroutunian, V. H. (2006) · Neurology · doi:10.1212/01.wnl.0000191298.68045.50 · Cited by 131
Amyloid imaging as a biomarker for cerebral β-amyloidosis and risk prediction for Alzheimer dementia
Klunk, W. E. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.006 · Cited by 131
Dementia Care in 9 OECD Countries
Moïse, P., Schwarzinger, M., & Um, M. Y. (2004) · OECD health working papers · doi:10.1787/485700737071 · Cited by 131
Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-β aggregation
Thomas, T., Nadackal, T. G., & Thomas, K. (2001) · Neuroreport · doi:10.1097/00001756-200110290-00024 · Cited by 128
Developmental vulnerability of synapses and circuits associated with neuropsychiatric disorders
Penzes, P., Buonanno, A., Passafaro, M., Sala, C., & Sweet, R. A. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12261 · Cited by 125
Amyloid-β, tau, and the cholinergic system in Alzheimer’s disease: seeking direction in a tangle of clues
Majdi, A., Sadigh‐Eteghad, S., Aghsan, S. R., Farajdokht, F., Vatandoust, S. M., Abbas-Abad, A. N., & Mahmoudi, J. (2020) · Reviews in the Neurosciences · doi:10.1515/revneuro-2019-0089 · Cited by 130
Alzheimer’s β-peptide oligomer formation at physiologic concentrations
LeVine, H. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.08.014 · Cited by 125
Soluble Aβ Promotes Wild-Type Tau Pathology In Vivo
Chabrier, M. A., Blurton-Jones, M., Agazaryan, A. A., Nerhus, J. L., Martinez-Coria, H., & LaFerla, F. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0172-12.2012 · Cited by 123
Apathy correlates with prefrontal amyloid deposition in Alzheimer's disease
Mori, T., Shimada, H., Shinotoh, H., Hirano, S., Eguchi, Y., Yamada, M., Fukuhara, R., Tanimukai, S., Zhang, M.-R., Kuwabara, S., et al. (2014) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2013-306110 · Cited by 122
Insulin degrading enzyme activity selectively decreases in the hippocampal formation of cases at high risk to develop Alzheimer's disease
Zhao, Z., Xiang, Z., Haroutunian, V. H., Buxbaum, J. D., Stetka, B., & Pasinetti, G. M. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.05.001 · Cited by 131
Kinetic characterization of amyloid-beta 1–42 aggregation with a multimethodological approach
Bartolini, M., Naldi, M., Fiori, J., Valle, F., Biscarini, F., Nicolau, D. V., & Andrisano, V. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.03.020 · Cited by 123
Alzheimer's Disease and the Amyloid β-Protein
Walsh, D. M., & Teplow, D. B. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00012-6 · Cited by 121
Membrane‐bound β‐amyloid oligomers are recruited into lipid rafts by a fyn‐dependent mechanism
Williamson, R., Usardi, A., Hanger, D. P., & Anderton, B. H. (2007) · The FASEB Journal · doi:10.1096/fj.07-9766com · Cited by 123
Transthyretin: A key gene involved in the maintenance of memory capacities during aging
Brouillette, J., & Quirion, R. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.007 · Cited by 130
Re-emphasizing early Alzheimer’s disease pathology starting in select entorhinal neurons, with a special focus on mitophagy
Kobro-Flatmoen, A., Lagartos-Donate, M. J., Aman, Y., Edison, P., Witter, M. P., & Fang, E. F. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101307 · Cited by 119
Alzheimer's disease drug discovery: in vivo screening using Caenorhabditis elegans as a model for β-amyloid peptide-induced toxicity
Lublin, A. L., & Link, C. D. (2012) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2012.02.002 · Cited by 119
Caloric restriction attenuates amyloid deposition in middle-aged dtg APP/PS1 mice
Mouton, P. R., Chachich, M. E., Quigley, C., Spangler, E. L., & Ingram, D. K. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.08.038 · Cited by 122
Hippocampal Aβ42 Levels Correlate with Spatial Memory Deficit in APP and PS1 Double Transgenic Mice
Puoliväli, J. T., Wang, J., Heikkinen, T., Heikkilä, M., Tapiola, T., van Groen, T., & Tanila, H. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0481 · Cited by 125
Insertion of Alzheimer’s Aβ40 Peptide into Lipid Monolayers
Ege, C., & Lee, K. Y. C. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.043265 · Cited by 118
Role of Cholesterol in APP Metabolism and Its Significance in Alzheimer’s Disease Pathogenesis
Maulik, M., Westaway, D. A., Jhamandas, J. H., & Kar, S. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8337-y · Cited by 121
Pharmacotherapy for Alzheimer's disease: progress and prospects
Palmer, A. M. (2002) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(02)02056-4 · Cited by 118
Effects of orexin-A on memory processing
Jaeger, L. B., Farr, S. A., Banks, W. A., & Morley, J. E. (2002) · Peptides · doi:10.1016/s0196-9781(02)00110-9 · Cited by 116
Acetyl-CoA the Key Factor for Survival or Death of Cholinergic Neurons in Course of Neurodegenerative Diseases
Szutowicz, A., Bielarczyk, H., Jankowska-Kulawy, A., Pawełczyk, T., & Ronowska, A. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1060-x · Cited by 117
Transcriptome analysis of synaptoneurosomes identifies neuroplasticity genes overexpressed in incipient Alzheimer's disease
Williams, C., Mehrian Shai, R., Wu, Y., Hsu, Y.-H., Sitzer, T., Spann, B., McCleary, C., Mo, Y., & Miller, C. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004936 · Cited by 116
Amyloid‐β Oligomers: Possible Roles as Key Neurotoxins in Alzheimer's Disease
Lublin, A. L., & Gandy, S. (2010) · Mount Sinai Journal of Medicine A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20160 · Cited by 116
Clinical and Neuropathological Features of the Arctic APP Gene Mutation Causing Early-Onset Alzheimer Disease
Basun, H., Bogdanovic, N., Ingelsson, M., Almkvist, O., Näslund, J., Axelman, K., Bird, T. D., Nochlin, D., Schellenberg, G. D., Wahlund, L.-O., et al. (2008) · Archives of Neurology · doi:10.1001/archneur.65.4.499 · Cited by 115
Self-citation
Oligomeropathies and pathogenesis of Alzheimer and Parkinson's diseases
Forloni, G., Artuso, V., Vitola, P. L., & Balducci, C. (2016) · Movement Disorders · doi:10.1002/mds.26624 · Cited by 116
Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1–42) compared to Aβ(1–40)
Wesén, E. V., Jeffries, G. D. M., Dzebo, M. M., & Esbjörner, E. K. (2017) · Scientific Reports · doi:10.1038/s41598-017-02227-9 · Cited by 115
MAPK recruitment by β‐amyloid in organotypic hippocampal slice cultures depends on physical state and exposure time
Bell, K. A., O’Riordan, K. J., Sweatt, J. D., & Dineley, K. T. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02722.x · Cited by 117
Insights into Alzheimer disease pathogenesis from studies in transgenic animal models
Schaeffer, E. L., Figueiró, M., & Gattaz, W. F. (2011) · Clinics · doi:10.1590/s1807-59322011001300006 · Cited by 114
Transcriptional vulnerability of brain regions in Alzheimer's disease and dementia
Haroutunian, V. H., Katsel, P., & Schmeidler, J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.07.021 · Cited by 113
Affinity-Based Inhibition of β-Amyloid Toxicity
Cairo, C. W., Strzelec, A., Murphy, R. M., & Kiessling, L. L. (2002) · Biochemistry · doi:10.1021/bi0156254 · Cited by 113
Overlapping profiles of Aβ peptides in the Alzheimer's disease and pathological aging brains
Moore, B. D., Chakrabarty, P., Levites, Y., Kukar, T. L., Baine, A.-M. T., Moroni, T., Ladd, T. B., Das, P., Dickson, D. W., & Golde, T. E. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt121 · Cited by 115
Synaptic Amyloid-β Oligomers Precede p-Tau and Differentiate High Pathology Control Cases
Bilousova, T., Miller, C. A., Poon, W. W., Vinters, H. V., Corrada, M., Kawas, C., Hayden, E. Y., Teplow, D. B., Glabe, C., Albay, R., et al. (2016) · The American Journal of Pathology · doi:10.1016/j.ajpath.2015.09.018 · Cited by 115
Silibinin ameliorates anxiety/depression-like behaviors in amyloid β-treated rats by upregulating BDNF/TrkB pathway and attenuating autophagy in hippocampus
Song, X., Liu, B., Cui, L., Zhou, B., Liu, W., Xu, F., Hayashi, T., Hattori, S., Ushiki‐Kaku, Y., Tashiro, S., et al. (2017) · Physiology & Behavior · doi:10.1016/j.physbeh.2017.07.023 · Cited by 112
Role of miRNAs in Alzheimer’s Disease and Possible Fields of Application
Silvestro, S., Bramanti, P., & Mazzon, E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20163979 · Cited by 113
Differential neuroimmune markers to the onset of Alzheimer's disease neurodegeneration and dementia: Autoantibodies to Aβ(25–35) oligomers, S100b and neurotransmitters
Алексеевна, Г. М., Davidova, T. B., Mališauskas, M., Sewell, R. D. E., Voskresenskaya, N. I., Wilhelm, K., Elistratova, E. I., Sherstnev, V. V., & Morozova‐Roche, L. A. (2007) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2007.03.023 · Cited by 112
Single intracerebroventricular administration of amyloid-beta (25–35) peptide induces impairment in short-term rather than long-term memory in rats
Stepanichev, M. Y., Moiseeva, Y. V., Лазарева, Н. А., Onufriev, M. V., & Gulyaeva, N. V. (2003) · Brain Research Bulletin · doi:10.1016/s0361-9230(03)00118-7 · Cited by 115
Investigating How Peptide Length and a Pathogenic Mutation Modify the Structural Ensemble of Amyloid Beta Monomer
Lin, Y.-S., Bowman, G. R., Beauchamp, K. A., & Pande, V. S. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.002 · Cited by 111
The Cysteine Protease Inhibitor, E64d, Reduces Brain Amyloid-β and Improves Memory Deficits in Alzheimer's Disease Animal Models by Inhibiting Cathepsin B, but not BACE1, β-Secretase Activity
Hook, G., HOOK, V. Y. H., & Kindy, M. S. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110101 · Cited by 114
Dysfunction of Wnt signaling and synaptic disassembly in neurodegenerative diseases
Purro, S. A., Galli, S., & Salinas, P. C. (2014) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt049 · Cited by 115

Authors: Näslund, J.
Affiliations: Rockefeller University (US)
Corresponding author: Näslund, Jan
Venue: JAMA
Publisher: American Medical Association (AMA)
Published: 2000-03-22
Volume: 283
Issue: 12
Pages: 1571
ISSN: 0002-9955 (ISSN-L)
0098-7484
DOI: 10.1001/jama.283.12.1571
OpenAlex: W2000706612
Cited by: 1,268
References: 28
Citations by year: 2026: 9 · 2025: 14 · 2024: 32 · 2023: 23 · 2022: 28 · 2021: 32 · 2020: 31 · 2019: 29 · 2018: 34 · 2017: 29 · 2016: 57 · 2015: 56 · 2014: 60 · 2013: 59 · 2012: 65
FWCI: 40.95
Type: journal article
Language: en
Open access: closed
Locations: JAMA (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG-02219, AG 05138, P50AG005138, AG 14996, P01AG002219)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta, Alzheimer's disease, cognitive decline, dementia progression, tau protein, amyloid-beta 42, Aβ40, frontal cortex, Clinical Dementia Rating, postmortem brain, neocortex, nursing home residents, amyloid plaques, neurofibrillary tangles
MeSH terms: Aged, Aged, 80 and over, Brain, Cognition Disorders, Cross-Sectional Studies, Dementia, Enzyme-Linked Immunosorbent Assay, Female, Frontal Lobe, Humans, Immunoenzyme Techniques, Male, Immunoblotting, Amyloid beta-Peptides, 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

Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks