Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside
Open accessAbstract
Alzheimer’s disease is the most common cause of dementia. Over the last three decades, research has advanced dramatically and provided a detailed understanding of the molecular events underlying the pathogenesis of Alzheimer’s disease. In parallel, assays for the detection of biomarkers that reflect the typical Alzheimer’s disease-associated pathology have been developed and validated in myriads of clinical studies. Such biomarkers complement clinical diagnosis and improve diagnostic accuracy. The use of biomarkers will become even more important with the advent of disease-modifying therapies. Such therapies will likely be most beneficial when administered early in the disease course. Here, we summarise the development of the core Alzheimer’s disease cerebrospinal fluid biomarkers: amyloid-β and tau. We provide an overview of their role in cellular physiology and Alzheimer’s disease pathology, and embed their development as cerebrospinal fluid biomarkers into the historical context of Alzheimer’s disease research. Finally, we summarise recommendations for their use in clinical practice, and outline perspectives for novel cerebrospinal fluid candidate biomarkers.
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An ELISA assay called INNOTEST has been used for two decades for quantification of t-tau, p-tau and Aβ42 in CSF, giving a unique 'Alzheimer's CSF profile' where an increased level of t-tau and p-tau is observed with decreased Aβ42 level.
“An ELISA assay called as INNOTEST has been used for two decades for quantification of t-tau, p-tau and Aβ42 in CSF which gives a unique ‘Alzheimer’s CSF profile’ where an increased level of t-tau and p-tau is observed with decreased Aβ42 level [45, 46].”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [46]
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1 retracted
RETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009) · Nature · doi:10.1038/nature07767 · Cited by 992 · see citing works
RetractedMcKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915 · see citing works
McKhann, G. M., Knopman, D. S., Chertkow, H., Hyman, B. T., Jack, C. R., Kawas, C. H., Klunk, W. E., Koroshetz, W. J., Manly, J. J., Mayeux, R., et al. (2011) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.03.005 · Cited by 18,657 · see citing works
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 1× · see citing works
“The sequence of atrophy progression on MRI is highly similar to the spatial spreading of neurofibrillary tangles in histopathological studies [5,162,166].”
BackgroundAmyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Albert, M. S., DeKosky, S. T., Dickson, D., Dubois, B., Feldman, H. H., Fox, N. C., Gamst, A., Holtzman, D. M., Jagust, W. J., Petersen, R. C., et al. (2011) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.03.008 · Cited by 10,152 · 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
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404 · 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
Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade
Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70299-6 · Cited by 4,806 · see citing works
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
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · 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
Research criteria for the diagnosis of Alzheimer's disease: revising the NINCDS–ADRDA criteria
Dubois, B., Feldman, H. H., Jacova, C., DeKosky, S. T., Barberger-Gateau, P., Cummings, J., Delacourte, A., Galasko, D., Gauthier, S., Jicha, G., et al. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70178-3 · Cited by 4,411 · see citing works
Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396 · see citing works
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676 · see citing works
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498 · see citing works
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · see citing works
Advancing research diagnostic criteria for Alzheimer's disease: the IWG-2 criteria
Dubois, B., Feldman, H. H., Jacova, C., Hampel, H., Molinuevo, J. L., Blennow, K., DeKosky, S. T., Gauthier, S., Selkoe, D., Bateman, R., et al. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70090-0 · Cited by 3,321 · see citing works
Scheltens, P., Blennow, K., Breteler, M. M. B., de Strooper, B., Frisoni, G. B., Salloway, S., & Van der Flier, W. M. (2016) · The Lancet · doi:10.1016/s0140-6736(15)01124-1 · Cited by 3,125 · see citing works
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089 · see citing works
The molecular pathology of Alzheimer's disease
Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708 · see citing works
Albert, M., DeKosky, S. T., Dickson, D. W., Dubois, B., Feldman, H., Fox, N. C., Gamst, A. C., Holtzman, D. M., Jagust, W. J., Petersen, R. C., et al. (2013) · FOCUS The Journal of Lifelong Learning in Psychiatry · doi:10.1176/appi.focus.11.1.96 · Cited by 2,630 · see citing works
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538 · see citing works
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492 · see citing works
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · see citing works
Cerebrospinal fluid biomarker signature in Alzheimer's disease neuroimaging initiative subjects
Shaw, L. M., Vanderstichele, H., Knapik‐Czajka, M., Clark, C. M., Aisen, P. S., Petersen, R. C., Blennow, K., Soares, H., Simon, A., Lewczuk, P., et al. (2009) · Annals of Neurology · doi:10.1002/ana.21610 · Cited by 2,065 · see citing works
Olsson, B., Lautner, R., Andreasson, U., Öhrfelt, A., Portelius, E., Bjerke, M., Hölttä, M., Rosén, C., Olsson, C., Strobel, G., et al. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00070-3 · Cited by 2,049 · see citing works
Preclinical Alzheimer’s Disease: Definition, Natural History, and Diagnostic Criteria
Dubois, B., Hampel, H., Feldman, H. H., Scheltens, P., Aisen, P., Andrieu, S., Bakardjian, H., Benali, H., Bertram, L., Blennow, K., et al. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.02.002 · Cited by 1,925 · see citing works
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921 · see citing works
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Metabolic reduction in the posterior cingulate cortex in very early Alzheimer's disease
Minoshima, S., Giordani, B., Berent, S., Frey, K. A., Foster, N. L., & Kuhl, D. E. (1997) · Annals of Neurology · doi:10.1002/ana.410420114 · Cited by 1,802 · see citing works
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · 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
Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693 · see citing works
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588 · see citing works
Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474 · see citing works
Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,462 · 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
Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease
Ittner, L. M., & Götz, J. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2967 · Cited by 1,357 · see citing works
Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,333 · see citing works
Fagan, A. M., Mintun, M. A., Mach, R. H., Lee, S., Dence, C. S., Shah, A. R., LaRossa, G. N., Spinner, M. L., Klunk, W. E., Mathis, C. A., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20730 · Cited by 1,246 · see citing works
A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60
Cao, X., & Südhof, T. C. (2001) · Science · doi:10.1126/science.1058783 · Cited by 1,202 · see citing works
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works
Beach, T. G., Monsell, S. E., Phillips, L. E., & Kukull, W. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31824b211b · Cited by 1,103 · cited 1× · see citing works
“However, in comparison with neuropathological diagnosis, accuracy is limited with a sensitivity of 71–87% and a specificity of 44–71% [153,155].”
BackgroundTrafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works
Review: history of the amyloid fibril.
Sipe, J., & Cohen, A. B. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4221 · Cited by 1,037 · see citing works
Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease
KIDD, M. (1963) · Nature · doi:10.1038/197192b0 · Cited by 1,012 · see citing works
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012 · see citing works
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000 · see citing works
Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965 · see citing works
Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915 · see citing works
Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works
Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899 · see citing works
Tapiola, T., Alafuzoff, I., Herukka, S.-K., Parkkinen, L., Hartikainen, P., Soininen, H., & Pirttilä, T. (2009) · Archives of Neurology · doi:10.1001/archneurol.2008.596 · Cited by 896 · see citing works
Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881 · see citing works
Brain Imaging in Alzheimer Disease
Johnson, K. A., Fox, N. C., Sperling, R. A., & Klunk, W. E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006213 · Cited by 875 · see citing works
Biochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint
Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 839 · see citing works
X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
Eanes, E. D., & Glenner, G. G. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.11.673 · Cited by 823 · see citing works
Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., & Wisniewski, H. M. (1989) · Brain Research · doi:10.1016/0006-8993(89)91396-6 · Cited by 818 · see citing works
Blennow, K., Wallin, A., Ågren, H., Spenger, C., Siegfried, J., & Vanmechelen, E. (1995) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815140 · Cited by 789 · see citing works
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
Al-Atrache, Z., Cader, A., & Appelt, D. M. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.06.894 · Cited by 765 · see citing works
Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 749 · see citing works
Scahill, R. I., Schott, J. M., Stevens, J., Rossor, M. N., & Fox, N. C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052587399 · Cited by 748 · see citing works
Precursor of amyloid protein in Alzheimer disease undergoes fast anterograde axonal transport.
Koo, E. H., Sisodia, S. S., Archer, D. R., Martin, L. J., Weidemann, A., Beyreuther, K., Fischer, P., Masters, C. L., & Price, D. L. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1561 · Cited by 733 · see citing works
Greenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 732 · see citing works
PET imaging of amyloid deposition in patients with mild cognitive impairment
Forsberg, A., Engler, H., Almkvist, O., Blomquist, G., Hagman, G., Wall, A. E., Ringheim, A., Långström, B., & Nordberg, A. K. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.03.029 · Cited by 725 · see citing works
Consensus Report of the Working Group on: “Molecular and Biochemical Markers of Alzheimer’s Disease”
The Ronald and Nancy Reagan Research Institute of the Alzheimer’s Association and, & National Institute on Aging Working Group (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00022-0 · Cited by 702 · see citing works
Motter, R., Vigo‐Pelfrey, C., Kholodenko, D., Barbour, R., Johnson‐Wood, K., Galasko, D., Chang, L., Miller, B., Clark, C., Green, R., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410380413 · Cited by 701 · see citing works
The characterization of soluble amyloid prepared in water
Pras, M., Zucker‐Franklin, D., Rimon, A., & Franklin, E. C. (1968) · Journal of Clinical Investigation · doi:10.1172/jci105784 · Cited by 643 · see citing works
Electron Microscopic Observations on a Fibrous Component in Amyloid of Diverse Origins
Cohen, A. S., & Calkins, E. (1959) · Nature · doi:10.1038/1831202a0 · Cited by 638 · see citing works
Cell adhesion molecules: signalling functions at the synapse
Dalva, M. B., McClelland, A. C., & Kayser, M. S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2075 · Cited by 620 · see citing works
CSF Aβ 42 levels correlate with amyloid-neuropathology in a population-based autopsy study
Strozyk, D., Blennow, K., White, L. R., & Launer, L. J. (2003) · Neurology · doi:10.1212/01.wnl.0000046581.81650.d0 · Cited by 604 · see citing works
Morris, J. C., Storandt, M., McKeel, D. W., Rubin, E. H., Price, J. L., Grant, E. A., & Berg, L. (1996) · Neurology · doi:10.1212/wnl.46.3.707 · Cited by 603 · see citing works
Amyloid Fibril Proteins: Proof of Homology with Immunoglobulin Light Chains by Sequence Analyses
Glenner, G. G., Terry, W., Harada, M., et al. (1971) · Science · doi:10.1126/science.172.3988.1150 · Cited by 590 · see citing works
Matsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588 · see citing works
Buerger, K., Ewers, M., Pirttila, T., Zinkowski, R., Alafuzoff, I., Teipel, S. J., DeBernardis, J., Kerkman, D., McCulloch, C., Soininen, H., et al. (2006) · Brain · doi:10.1093/brain/awl269 · Cited by 586 · see citing works
A Neuronal Antigen in the Brains of Alzheimer Patients
Wolozin, B. L., Pruchnicki, A., Dickson, D. W., & Davies, P. (1986) · Science · doi:10.1126/science.3083509 · Cited by 585 · see citing works
The Neuropsychological Profile of Alzheimer DiseasePreprint
Weıntraub, S., Wicklund, A. H., & Salmon, D. P. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006171 · Cited by 569 · see citing works
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
Foster, N. L., Chase, T. N., Fedio, P., Patronas, N. J., Brooks, R. A., & Chiro, G. D. (1983) · Neurology · doi:10.1212/wnl.33.8.961 · Cited by 540 · see citing works
Phosphorylated Tau Protein Is Integrated into Paired Helical Filaments in Alzheimer's Disease1
Ihara, Y., Nukina, N., Miura, R., & OGAWARA, M. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135662 · Cited by 527 · see citing works
Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., Mandelkow, E., & Zweckstetter, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504081112 · Cited by 524 · see citing works
Cerebrospinal fluid protein biomarkers for Alzheimer’s disease
Blennow, K. (2004) · Neurotherapeutics · doi:10.1602/neurorx.1.2.213 · Cited by 487 · see citing works
Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472 · see citing works
Sastre, M., Steiner, H., Fuchs, K. P., Capell, A., Multhaup, G., Condron, M. M., Teplow, D. B., & Haass, C. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve180 · Cited by 472 · see citing works
Transient increase in total tau but not phospho-tau in human cerebrospinal fluid after acute stroke
Hesse, C., Rosengren, L., Andreasen, N., Davidsson, P., Vanderstichele, H., Vanmechelen, E., & Blennow, K. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01697-9 · Cited by 450 · see citing works
Nuclear Tau, a Key Player in Neuronal DNA Protection
Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421 · cited 1× · see citing works
“Additionally, aggregated tau has lost its ability to enter the nucleus, which may result in DNA damage, due to the loss of the DNA-protective function of tau [80,105].”
BackgroundPhosphorylation determines two distinct species of tau in the central nervous system
Papasozomenos, S. C., & Binder, L. I. (1987) · Cell Motility · doi:10.1002/cm.970080303 · Cited by 420 · see citing works
Genetic linkage studies suggest that Alzheimer's disease is not a single homogeneous disorder
George‐Hyslop, P. S., Haines, J. L., Farrer, L. A., Polinsky, R. J., Broeckhoven, C. V., Goate, A., McLachlan, D. R. C., Orr, H. T., Bruni, A. C., Sorbi, S., et al. (1990) · Nature · doi:10.1038/347194a0 · Cited by 392 · see citing works
Clinical, imaging, and pathological heterogeneity of the Alzheimer's disease syndrome
Lam, B., Masellis, M., Freedman, M., Stuss, D. T., & Black, S. E. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt155 · Cited by 386 · see citing works
CSF biomarker variability in the Alzheimer's Association quality control program
Mattsson, N., Andréasson, U., Persson, S., Carrillo, M. C., Collins, S. J., Chalbot, S., Cutler, N. E., Dufour‐Rainfray, D., Fagan, A. M., Heegaard, N. H. H., et al. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.01.010 · Cited by 383 · see citing works
Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375 · see citing works
Proteolytic Degradation of Amyloid -Protein
Saido, T., & Leissring, M. A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006379 · Cited by 368 · see citing works
Hua, X., Leow, A., Parikshak, N., Lee, S., Chiang, M.-C., Toga, A. W., Jack, C. R., Weiner, M. W., & Thompson, P. M. (2008) · NeuroImage · doi:10.1016/j.neuroimage.2008.07.013 · Cited by 359 · see citing works
Vanderstichele, H., Bibl, M., Engelborghs, S., Le Bastard, N., Lewczuk, P., Molinuevo, J. L., Parnetti, L., Perret‐Liaudet, A., Shaw, L. M., Teunissen, C., et al. (2012) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.07.004 · Cited by 358 · see citing works
Neurochemical Aftermath of Amateur Boxing
Zetterberg, H., Hietala, M. A., Jonsson, M. A. G., Andreasen, N., Styrud, E., Karlsson, I., Edman, Å., Popa, C., Rasulzada, A., Wahlund, L., et al. (2006) · Archives of Neurology · doi:10.1001/archneur.63.9.1277 · Cited by 355 · see citing works
Slunt, H. H., Thinakaran, G., von Koch, C., Lo, A., Tanzi, R. E., & Sisodia, S. S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41992-2 · Cited by 346 · see citing works
Elevated levels of tau-protein in cerebrospinal fluid of patients with Creutzfeldt–Jakob disease
Otto, M., Wiltfang, J., Tumani, H., Zerr, I., Lantsch, M., Kornhuber, J., Weber, T., Kretzschmar, H. A., & Poser, S. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00215-2 · Cited by 339 · see citing works
Correlation between rates of brain atrophy and cognitive decline in AD
Fox, N. C., Scahill, R. I., Crum, W. R., & Rossor, M. N. (1999) · Neurology · doi:10.1212/wnl.52.8.1687 · Cited by 338 · see citing works
Delacourte, A., & Défossez, A. (1986) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(86)90167-x · Cited by 325 · see citing works
Initial CSF total tau correlates with 1-year outcome in patients with traumatic brain injury
Öst, M., Nylén, K., Csajbok, L., Öhrfelt, A. O., Tullberg, M., Wikkelsö, C., Nellgård, P., Rosengren, L., Blennow, K., & Nellgård, B. (2006) · Neurology · doi:10.1212/01.wnl.0000242732.06714.0f · Cited by 321 · see citing works
Homo‐ and heterodimerization of APP family members promotes intercellular adhesion
Soba, P., Eggert, S., Wagner, K., Zentgraf, H., Siehl, K., Kreger, S., Loewer, A., Langer, A., Merdes, G., Paro, R., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600824 · Cited by 317 · see citing works
The future of blood‐based biomarkers for Alzheimer's disease
Henriksen, K., O’Bryant, S. E., Hampel, H. J., Trojanowski, J. Q., Montine, T. J., Jeromin, A., Blennow, K., Lönneborg, A., Wyss‐Coray, T., Soares, H. D., et al. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.01.013 · Cited by 312 · 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
The cerebrospinal fluid “Alzheimer profile”: Easily said, but what does it mean?
Duits, F. H., Teunissen, C. E., Bouwman, F. H., Visser, P. J., Mattsson, N., Zetterberg, H., Blennow, K., Hansson, O., Minthon, L., Andreasen, N., et al. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.12.023 · Cited by 300 · see citing works
Grimmer, T., Riemenschneider, M., Förstl, H., Henriksen, G., Klunk, W. E., Mathis, C. A., Shiga, T., Wester, H.-J., Kurz, A., & Drzezga, A. (2009) · Biological Psychiatry · doi:10.1016/j.biopsych.2009.01.027 · Cited by 278 · see citing works
Prevalence of dementia disorders in the oldest-old: an autopsy study
Jellinger, K. A., & Attems, J. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0654-5 · Cited by 276 · see citing works
Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., Lanté, F., & Buisson, A. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4261-13.2014 · Cited by 272 · see citing works
Kaether, C., Skehel, P., & Dotti, C. G. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.4.1213 · Cited by 270 · see citing works
Duits, F. H., Martínez‐Lage, P., Paquet, C., Engelborghs, S., Lleó, A., Hausner, L., Molinuevo, J. L., Stomrud, E., Farotti, L., Ramakers, I. H. G. B., et al. (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.08.003 · Cited by 260 · see citing works
Violet, M., Delattre, L., Tardivel, M., Sultan, A., Chauderlier, A., Caillierez, R., Talahari, S., Nesslany, F., Lefebvre, B., Bonnefoy, E., et al. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00084 · Cited by 251 · see citing works
Downregulation of amyloid precursor protein inhibits neurite outgrowth in vitro.
Allinquant, B., Hantraye, P., Mailleux, P., Moya, K. L., Bouillot, C., & Prochiantz, A. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.128.5.919 · Cited by 251 · see citing works
Amyloidosis: a convoluted story
Kyle, R. (2001) · British Journal of Haematology · doi:10.1046/j.1365-2141.2001.02999.x · Cited by 239 · see citing works
Snider, B. J., Fagan, A. M., Roe, C. M., Shah, A. R., Grant, E., Xiong, C., Morris, J. C., & Holtzman, D. M. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.55 · Cited by 227 · see citing works
Identification of nuclear tau isoforms in human neuroblastoma cells.
Loomis, P. A., Howard, T. H., Castleberry, R. P., & Binder, L. I. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8422 · Cited by 217 · see citing works
Cerebrospinal Fluid Markers for Alzheimer's Disease Evaluated after Acute Ischemic Stroke
Hesse, C., Rosengren, L., Vanmechelen, E., Vanderstichele, H., Jensen, C., Davidsson, P., & Blennow, K. (2000) · Journal of Alzheimer s Disease · doi:10.3233/jad-2000-23-402 · Cited by 215 · see citing works
Sensitivity, specificity, and stability of CSF-tau in AD in a community-based patient sample
Andreasen, N. C., Minthon, L., Clarberg, A., Davidsson, P., Gottfries, J., Vanmechelen, E., Vanderstichele, H., Winblad, B. G., & Blennow, K. (1999) · Neurology · doi:10.1212/wnl.53.7.1488 · Cited by 210 · see citing works
Young-Pearse, T. L., Chen, A. C., Chang, R., Marquez, C., & Selkoe, D. J. (2008) · Neural Development · doi:10.1186/1749-8104-3-15 · Cited by 210 · see citing works
Fluid Biomarkers in Alzheimer Disease
Blennow, K., Zetterberg, H., & Fagan, A. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006221 · Cited by 208 · see citing works
Yamazaki, T., Selkoe, D. J., & Koo, E. H. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.2.431 · Cited by 207 · see citing works
Nostrand, W. E. V., Wagner, S. L., Shankle, W. R., Farrow, J. S., Dick, M. B., Rozemüller, A. J. M., Kuiper, M. A., Wolters, E. C., Zimmerman, J. B., & Cotman, C. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.2551 · Cited by 205 · see citing works
Prion-like Properties of Tau Protein: The Importance of Extracellular Tau as a Therapeutic Target
Holmes, B. B., & Diamond, M. I. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.549295 · Cited by 202 · see citing works
Molinuevo, J. L., Blennow, K., Dubois, B., Engelborghs, S., Lewczuk, P., Perret‐Liaudet, A., Teunissen, C. E., & Parnetti, L. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2014.03.003 · Cited by 198 · see citing works
Fetal‐Type Phosphorylation of the τ in Paired Helical Filaments
Kanemaru, K., Takio, K., Miura, R., Titani, K., & Ihara, Y. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10039.x · Cited by 197 · see citing works
The purification of tau protein and the occurrence of two phosphorylation states of tau in brain.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)71345-1 · Cited by 191 · see citing works
Meier, S., Bell, M., Lyons, D. N., Rodriguez-Rivera, J., Ingram, A., Fontaine, S. N., Mechas, E., Chen, J., Wolozin, B., LeVine, H., et al. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.3029-15.2016 · Cited by 190 · see citing works
beta-Amyloid precursor protein binds to the neurite-promoting IKVAV site of laminin.
Kibbey, M. C., Jucker, M., Weeks, B. S., Neve, R. L., Nostrand, W. E. V., & Kleinman, H. K. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.21.10150 · Cited by 183 · see citing works
Alzheimer‐related neuronal protein A68: Specificity and distribution
Wolozin, B. L., & Davies, P. (1987) · Annals of Neurology · doi:10.1002/ana.410220412 · Cited by 178 · see citing works
Virchow, R. (1854) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf01930815 · Cited by 178 · see citing works
Characterization of the Amyloid Fibril as a Cross- Protein
Bonar, L. C., Cohen, A. S., & Skinner, M. M. (1969) · Experimental Biology and Medicine · doi:10.3181/00379727-131-34110 · Cited by 177 · see citing works
Alz‐50 Antibody recognizes alzheimer‐related neuronal changes
Hyman, B. T., Hoesen, G. W. V., Wolozin, B. L., Davies, P., Vogt, L. J., & Damasio, A. R. (1988) · Annals of Neurology · doi:10.1002/ana.410230410 · Cited by 176 · see citing works
Beher, D., Hesse, L., Masters, C. L., & Multhaup, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1613 · Cited by 170 · see citing works
Ashley, J., Packard, M. C., Ataman, B., & Budnik, V. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1144-05.2005 · Cited by 164 · see citing works
Brain atrophy associated with baseline and longitudinal measures of cognition
Cardenas, V. A., Chao, L. L., Studholme, C., Yaffe, K. S., Miller, B. L., Madison, C. A., Buckley, S. T., Mungas, D., Schuff, N. W., & Weiner, M. W. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.04.011 · Cited by 161 · see citing works
Relationship of Cerebrospinal Fluid Markers to11C-PiB and18F-FDDNP Binding
Tolboom, N., van der Flier, W. M., Yaqub, M. M., Boellaard, R., Verwey, N. A., Blankenstein, M. A., Windhorst, A. D., Scheltens, P., Lammertsma, A. A., & van Berckel, B. N. M. (2009) · Journal of Nuclear Medicine · doi:10.2967/jnumed.109.064360 · Cited by 160 · see citing works
Clinical features and APOE genotype of pathologically proven early-onset Alzheimer disease
Balasa, M., Gelpí, E., Antonell, A., Rey, M. J., Sánchez‐Valle, R., Molinuevo, J. L., & Lladó, A. (2011) · Neurology · doi:10.1212/wnl.0b013e31821a44dd · Cited by 154 · see citing works
Hornsten, A., Lieberthal, J. G., Fadia, S., Malins, R., Ha, L., Xu, X., Daigle, I., Markowitz, M. K., O'Connor, G., Plasterk, R. H. A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603997104 · Cited by 146 · see citing works
Vandermeeren, M., Mercken, M., Vanmechelen, E., Six, J., Voorde, A., Martin, J.-J., & Cras, P. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09823.x · Cited by 145 · see citing works
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 144 · see citing works
Tai, H., Wang, B. Y., Serrano‐Pozo, A., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0146-2 · Cited by 142 · see citing works
Blom, E. S., Giedraitis, V., Zetterberg, H., Fukumoto, H., Blennow, K., Hyman, B. T., Irizarry, M. C., Wahlund, L., Lannfelt, L., & Ingelsson, M. (2009) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000216841 · Cited by 141 · see citing works
Volumetric MRI and cognitive measures in Alzheimer disease
Ridha, B. H., Anderson, V. M., Barnes, J., Boyes, R. G., Price, S. L., Rossor, M. N., Whitwell, J. L., Jenkins, L., Black, R. S., Grundman, M., et al. (2008) · Journal of Neurology · doi:10.1007/s00415-008-0750-9 · Cited by 139 · see citing works
Cerebrospinal fluid total tau as a marker of Alzheimer's disease intensity
Sämgård, K., Zetterberg, H., Blennow, K., Hansson, O., Minthon, L., & Londos, E. (2009) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.2353 · Cited by 133 · see citing works
Treatment Strategies Targeting Amyloid -ProteinPreprint
Schenk, D., Basi, G. S., & Pangalos, M. N. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006387 · Cited by 128 · see citing works
Delacourte, A., Flament, S., Dibe, E. M., Hublau, P., Sablnni�re, P., H�mon, B., Sh�rrer, V., & D�fossez, A. (1990) · Acta Neuropathologica · doi:10.1007/bf00308912 · Cited by 127 · see citing works
Soluble Amyloid β-Protein Is a Marker of Alzheimer Amyloid in Brain But Not in Cerebrospinal Fluid
Tabaton, M., Nunzi, M. G., Xue, R., Usiak, M., AUTILIO‐GAMBETTI, L., & Gambetti, P. L. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1634 · Cited by 126 · see citing works
Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets
Lee, V. M.-Y., Brunden, K. R., Hutton, M., & Trojanowski, J. Q. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006437 · Cited by 122 · see citing works
Upcoming Candidate Cerebrospinal Fluid Biomarkers of Alzheimer’s Disease
Fagan, A. M., & Perrin, R. J. (2012) · Biomarkers in Medicine · doi:10.2217/bmm.12.42 · Cited by 115 · see citing works
de Garcini, E. M., Serrano, L. G., & Ávila, J. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80242-x · Cited by 110 · see citing works
Southwick, P. C., Yamagata, S. K., Echols, C. L., Higson, G. J., Neynaber, S. A., Parson, R. E., & Munroe, W. A. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66010259.x · Cited by 89 · see citing works
Clarris, H. J., Cappai, R., Heffernan, D., Beyreuther, K. T., Masters, C. L., & Small, D. H. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68031164.x · Cited by 85 · see citing works
Concentrations of amyloid β protein in cerebrospinal fluid of patients with alzheimer's disease
van Gool, W. A., Walstra, G. J. M., Bolhuis, P. A., Kuiper, M. A., & Wolters, E. C. (1995) · Annals of Neurology · doi:10.1002/ana.410370221 · Cited by 82 · see citing works
Biomarkers in Alzheimer's disease with a special emphasis on event-related oscillatory responses
Yener, G., & Başar, E. (2013) · Supplements to Clinical neurophysiology · doi:10.1016/b978-0-7020-5307-8.00020-x · Cited by 82 · see citing works
Characterization of Tau in Cerebrospinal Fluid Using Mass Spectrometry
Portelius, E., Hansson, S., Tran, A. J., Zetterberg, H., Grognet, P., Vanmechelen, E., Höglund, K., Brinkmalm, G., Brinkmalm, A., Nordhoff, E., et al. (2008) · Journal of Proteome Research · doi:10.1021/pr7008669 · Cited by 79 · see citing works
Pro-aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation
Decker, J., Krüger, L., Sydow, A., Zhao, S., Frotscher, M., Mandelkow, E., & Mandelkow, E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0193-3 · Cited by 77 · see citing works
Measurement of distinct immunochemical presentations of tau protein in Alzheimer disease.
Harrington, C. R., Mukaetova‐Ladinska, E. B., Hills, R., et al. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5842 · Cited by 73 · see citing works
ALZHEIMER'S DISEASE AND TAU PROTEINS
Brion, J., Flament-Durand, J., & Dustin, P. (1986) · The Lancet · doi:10.1016/s0140-6736(86)90495-2 · Cited by 72 · see citing works
THE ISOLATION OF AMYLOID FIBRILS AND A STUDY OF THE EFFECT OF COLLAGENASE AND HYALURONIDASE
Cohen, A. S., & Calkins, E. (1964) · The Journal of Cell Biology · doi:10.1083/jcb.21.3.481 · Cited by 68 · see citing works
Ueber den Gang der amyloiden Degeneration
Virchow, R. (1855) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf01935311 · Cited by 61 · see citing works
siRNA targeted against amyloid precursor protein impairs synaptic activity in vivo
Hérard, A., Besret, L., Dubois, A., Dauguet, J., Delzescaux, T., Hantraye, P., Bonvento, G., & Moya, K. L. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.10.020 · Cited by 57 · see citing works
Farlow, M. R. (1992) · The Lancet · doi:10.1016/0140-6736(92)91771-y · Cited by 55 · see citing works
Alzheimer's disease: paired helical filament immunoreactivity in cerebrospinal fluid
Wang, G. P., Iqbal, K., Bucht, G., Winblad, B. G., Wisniewski, H. M., & Grundke, I. (1991) · Acta Neuropathologica · doi:10.1007/bf00310917 · Cited by 47 · see citing works
Amyloid β-peptide is produced by cultured cells during normal metabolism: A reprise
Selkoe, D. J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s319 · Cited by 39 · see citing works
Purification and Reconstitution of the Periodic Fibril and Unit Structure of Human Amyloid
Glenner, G. G., & Bladen, H. A. (1966) · Science · doi:10.1126/science.154.3746.271 · Cited by 39 · see citing works
Lace, G., Wharton, S. B., & Ince, P. G. (2007) · Clinical Neuropathology · doi:10.5414/npp26043 · Cited by 37 · see citing works
Gu, L., & Zhang, Z. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161286 · Cited by 33 · see citing works
PAIRED HELICAL FILAMENT ANTIGEN IN CSF
Mehta, P. D., Thal, L. J., Wisniewski, H. M., et al. (1985) · The Lancet · doi:10.1016/s0140-6736(85)90074-1 · Cited by 30 · see citing works
“Amyloid” — Historical Aspects
Tanskanen, M. (2013) · InTech eBooks · doi:10.5772/53423 · Cited by 24 · see citing works
How can we recognize “disease modification” effects?
Siemers, E. (2009) · The journal of nutrition health & aging · doi:10.1007/s12603-009-0036-7 · Cited by 24 · see citing works
Frontotemporal dementia—time to target inflammation?
Piguet, O. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.84 · Cited by 11 · see citing works
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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
“An ELISA assay called as INNOTEST has been used for two decades for quantification of t-tau, p-tau and Aβ42 in CSF which gives a unique ‘Alzheimer’s CSF profile’ where an increased level of t-tau and p-tau is observed with decreased Aβ42 level [45, 46].”
MethodKynurenic Acid Levels are Increased in the CSF of Alzheimer’s Disease Patients
González-Sánchez, M., Jiménez, J., Narváez, A., Antequera, D., Llamas-Velasco, S., Martín, A. H.-S., Molina Arjona, J. A., López de Munain, A., Lleó Bisa, A., Marco, M.-P., et al. (2020) · Biomolecules · doi:10.3390/biom10040571 · Cited by 84 · see citing works
- Authors
- Pawlowski, M., Meuth, S., & Duning, T.
- Affiliations
- University Hospital Münster (DE)
- Corresponding author
- Pawlowski, Matthias
- Meuth, Sven
- Duning, Thomas
- Venue
- Diagnostics
- Publisher
- MDPI AG
- Published
- 2017-07-13
- Volume
- 7
- Issue
- 3
- Pages
- 42
- ISSN
- 2075-4418 (ISSN-L)
- PMC
- PMC5617942
- OpenAlex
- W2736051916
- Cited by
- 25
- References
- 175
- Citations by year
- 2026: 3 · 2025: 2 · 2023: 3 · 2022: 4 · 2021: 4 · 2020: 6 · 2019: 2 · 2018: 1
- FWCI
- 0.30
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Diagnostics (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Cerebrospinal fluid and hydrocephalus
- Keywords
- Alzheimer's disease, cerebrospinal fluid biomarkers, amyloid-beta, tau protein, amyloid plaques, tau pathology, dementia diagnosis, disease-modifying therapy, early diagnosis, clinical guidelines, candidate biomarkers
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 ›
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