The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer’s disease
Open accessAbstract
A proposed key event in the pathogenesis of Alzheimer's disease (AD) is the formation of neurotoxic amyloid beta (Abeta) oligomers and amyloid plaques in specific brain regions that are affected by the disease. The main plaque component is the 42 amino acid isoform of Alphabeta (Abeta1-42), which is thought to initiate plaque formation and AD pathogenesis. Numerous isoforms of Abeta, e.g., Abeta1-42, Abeta1-40 and the 3-pyroglutamate derivate of Abeta3-42 (pGluAbeta3-42), have been detected in the brains of sporadic AD (SAD) and familial AD (FAD) subjects. However, the relative importance of these isoforms in the pathogenesis of AD is not fully understood. Here, we report a detailed study using immunoprecipitation in combination with mass spectrometric analysis to determine the Abeta isoform pattern in the cerebellum, cortex and hippocampus in AD, including subjects with a mutation in the presenilin (M146V) or amyloid precursor protein (KM670/671NL) genes, SAD subjects and non-demented controls. We show that the dominating Abeta isoforms in the three different brain regions analyzed from control, SAD, and FAD are Abeta1-42, pGluAbeta3-42, Abeta4-42 and Abeta1-40 of which Abeta1-42 and Abeta4-42 are the dominant isoforms in the hippocampus and the cortex in all groups analyzed, controls included. No prominent differences in Abeta isoform patterns between FAD and SAD patients were seen, underscoring the similarity in the amyloid pathology of these two disease entities.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The cited source says what the claim attributes to it.
In the citing paper
“Among the different Aβ variants, the N-terminally truncated peptide Aβ4–42 is among the most abundant.”
From Characterization of a Mouse Model of Alzheimer’s Disease Expressing Aβ4-42 and Human Mutant Tau (2021) · cites this paper as [22]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
McKhann, 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
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
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
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · cited 1×
“b-Secretase is an aspartyl protease encoded by the b-site APP-cleaving enzyme 1 (BACE1) gene [18, 34, 37, 39] while c-secretase is a protease complex consisting of at least four essential components of which the homologous presenilin 1 and 2 proteins (PSEN1 and PSEN2, respectively) constitute the active site [5].”
BackgroundPhases of Aβ-deposition in the human brain and its relevance for the development of AD
Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490
Consortium to Establish a Registry for Alzheimer's Disease (CERAD)
Fillenbaum, G., & Heyman, A. (2002) · doi:10.1002/0470846410.ch42(iii · Cited by 2,859
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
Purification and cloning of amyloid precursor protein β-secretase from human brain
Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612
Cited by
Sorted by citations
Masters, C. L., Bateman, R., Blennow, K., Rowe, C. C., Sperling, R. A., & Cummings, J. L. (2015) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2015.56 · Cited by 1,853
Self-citationAmyloid biomarkers in Alzheimer's disease
Blennow, K., Mattsson, N., Schöll, M., Hansson, O., & Zetterberg, H. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.03.002 · Cited by 470
Self-citationKvartsberg, H., Duits, F. H., Ingelsson, M., Andreasen, N., Öhrfelt, A., Andersson, K., Brinkmalm, G., Lannfelt, L., Minthon, L., Hansson, O., et al. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2014.10.009 · Cited by 349
Self-citationγ-Secretase in Alzheimer’s disease
Hur, J. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00754-8 · Cited by 339
The role of metallobiology and amyloid-β peptides in Alzheimer's disease
Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07500.x · Cited by 266
Immunotherapy for Alzheimer’s disease: targeting β-amyloid and beyond
Song, C., Shi, J., Zhang, P., Zhang, Y., Xu, J., Zhao, L., Zhang, R., Wang, H., & Chen, H. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00292-3 · Cited by 266
Garza-Lombó, C., Posadas, Y., Quintanar, L., Gonsebatt, M. E., & Franco, R. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7272 · Cited by 263
McColl, G., Roberts, B. R., Pukala, T. L., Kenche, V. B., Roberts, C. M., Link, C. D., Ryan, T. M., Masters, C. L., Barnham, K. J., Bush, A. I., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-57 · Cited by 257
Halim, A., Brinkmalm, G., Rüetschi, U., Brinkmalm, A., Portelius, E., Zetterberg, H., Blennow, K., Larson, G., & Nilsson, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102664108 · Cited by 250
Self-citationZetterberg, H. (2012) · Archives of Neurology · doi:10.1001/archneurol.2012.90 · Cited by 234
Self-citationRasmussen, J., Mahler, J., Beschörner, N., Kaeser, S. A., Häsler, L. M., Baumann, F., Nyström, S., Portelius, E., Blennow, K., Lashley, T., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713215114 · Cited by 232
Self-citationPyroglutamate Amyloid-β (Aβ): A Hatchet Man in Alzheimer Disease
Jawhar, S., Wirths, O., & Bayer, T. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.288308 · Cited by 220
Distinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice
Stöhr, J., Condello, C., Watts, J. C., Bloch, L., Oehler, A., Nick, M., DeArmond, S. J., Giles, K., DeGrado, W. F., & Prusiner, S. B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408968111 · Cited by 175
Pathways to Alzheimer's disease
Hardy, J., Bogdanović, N., Winblad, B. G., Portelius, E., Andreasen, N. C., Cedazo-Mínguez, Á., & Zetterberg, H. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12192 · Cited by 180
Self-citationBouter, Y., Dietrich, K., Wittnam, J. L., Rezaei-Ghaleh, N., Pillot, T., Papot-Couturier, S., Lefebvre, T., Sprenger, F., Wirths, O., Zweckstetter, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1129-2 · Cited by 175
Diversity of Amyloid-beta Proteoforms in the Alzheimer’s Disease Brain
Wildburger, N. C., Esparza, T. J., LeDuc, R. D., Fellers, R. T., Thomas, P. M., Cairns, N. J., Kelleher, N. L., Bateman, R. J., & Brody, D. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-10422-x · Cited by 164
Bayer, T. A., & Wirths, O. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1287-x · Cited by 170
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
Proteinopathies, a core concept for understanding and ultimately treating degenerative disorders?
Bayer, T. A. (2013) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2013.03.007 · Cited by 149
Hansson, O., Batrla, R., Brix, B., Carrillo, M. C., Corradini, V., Edelmayer, R. M., Esquivel, R. N., Hall, C., Lawson, J., Bastard, N. L., et al. (2021) · Alzheimer's & Dementia · doi:10.1002/alz.12316 · Cited by 136
Self-citationA Functional Role for Aβ in Metal Homeostasis? N‐Truncation and High‐Affinity Copper Binding
Mital, M., Wezynfeld, N. E., Frączyk, T., Wiloch, M. Z., Wawrzyniak, U. E., Bonna, A., Tumpach, C., Barnham, K. J., Haigh, C. L., Bal, W., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502644 · Cited by 135
Kakuda, N., Miyasaka, T., Iwasaki, N., Nirasawa, T., Wada‐Kakuda, S., Takahashi‐Fujigasaki, J., Murayama, S., Ihara, Y., & Ikegawa, M. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0477-x · Cited by 131
Tan, J. Z. A., & Gleeson, P. A. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.11.013 · Cited by 137
Neuroinflammatory Signals in Alzheimer Disease and APP/PS1 Transgenic Mice
López‐González, I., Schlüter, A., Aso, E., Garcia‐Esparcia, P., Ansoleaga, B., Llorens, F., Carmona, M., Moreno, J. R., Fuso, A., Portero‐Otín, M., et al. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000176 · Cited by 128
Hansson, O., Mikulskis, A., Fagan, A. M., Teunissen, C. E., Zetterberg, H., Vanderstichele, H., Molinuevo, J. L., Shaw, L. M. J., Vandijck, M. L. J., Verbeek, M. M., et al. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.05.008 · Cited by 123
Self-citationDistinct patterns of APP processing in the CNS in autosomal-dominant and sporadic Alzheimer disease.
Pera, M., Alcolea, D., Sánchez-Valle, R., Guardia-Laguarta, C., Colom-Cadena, M., Badiola, N., Suárez-Calvet, M., Lladó, A., Barrera-Ocampo, A. A., Sepulveda-Falla, D., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-012-1062-9 · Cited by 115
APP/Aβ structural diversity and Alzheimer's disease pathogenesis
Roher, A. E., Kokjohn, T. A., Clarke, S. G., Sierks, M. R., Maarouf, C. L., Serrano, G. E., Sabbagh, M., & Beach, T. G. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.007 · Cited by 126
Are N- and C-terminally truncated Aβ species key pathological triggers in Alzheimer's disease?
Dunys, J., Valverde, A., & Checler, F. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.r118.003999 · Cited by 120
Identification of neurotoxic cross-linked amyloid-β dimers in the Alzheimer’s brain
Brinkmalm, G., Hong, W., Wang, Z., Liu, W., O’Malley, T. T., Sun, X., Frosch, M. P., Selkoe, D. J., Portelius, E., Zetterberg, H., et al. (2019) · Brain · doi:10.1093/brain/awz066 · Cited by 114
Self-citationMorawski, M., Schilling, S., Kreuzberger, M., Waniek, A., Jäger, C., Koch, B. M., Cynis, H., Kehlen, A., Arendt, T., Hartlage‐Rübsamen, M., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131535 · Cited by 114
Biomarkers in Sporadic and Familial Alzheimer’s Disease
Lista, S., O’Bryant, S. E., Blennow, K., Dubois, B., Hugon, J., Zetterberg, H., & Hampel, H. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-143006 · Cited by 106
Self-citationAβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease
Gao, C. M., Yam, A. Y., Wang, X., Magdangal, E., Salisbury, C., Peretz, D., Zuckermann, R. N., Connolly, M. D., Hansson, O., Minthon, L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015725 · Cited by 105
“also been found in AD cortical brain tissue [34].”
BackgroundSelf-citationMammalian Metallothionein-3: New Functional and Structural Insights
Vašák, M., & Meloni, G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061117 · Cited by 105
Jawhar, S., Wirths, O., Schilling, S., Graubner, S., Demuth, H., & Bayer, T. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185819 · Cited by 105
The binding of resveratrol to monomer and fibril amyloid beta
Ge, J., Qiao, J., Qi, C., Wang, C.-W., & Zhou, J. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.08.012 · Cited by 109
Santos, A. N., Ewers, M., Minthon, L., Simm, A., Silber, R., Blennow, K., Prvulovic, D., Hansson, O., & Hampel, H. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111361 · Cited by 101
Self-citationAlzheimer’s disease Aβ assemblies mediating rapid disruption of synaptic plasticity and memory
Klyubin, I. V., Cullen, W. K., Hu, N., & Rowan, M. J. (2012) · Molecular Brain · doi:10.1186/1756-6606-5-25 · Cited by 105
Davis, R. C., Marsden, I. T., Maloney, M. T., Minamide, L. S., Podlisny, M. B., Selkoe, D. J., & Bamburg, J. R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-10 · Cited by 102
Pyroglutamate Aβ cascade as drug target in Alzheimer’s disease
Bayer, T. A. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01409-2 · Cited by 102
Extracellular Vesicles in Alzheimer’s Disease: Friends or Foes? Focus on Aβ-Vesicle Interaction
Joshi, P., Benussi, L., Furlan, R., Ghidoni, R., & Verderio, C. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16034800 · Cited by 99
Hook, G., Reinheckel, T., Ni, J., Wu, Z., Kindy, M. S., Peters, C., & HOOK, V. Y. H. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000527 · Cited by 98
The Case for Abandoning Therapeutic Chelation of Copper Ions in Alzheimer's Disease
Drew, S. C. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00317 · Cited by 93
Advancements in Top-Down Proteomics
Zhou, H., Ning, Z., Starr, A. E., Abu‐Farha, M., & Figeys, D. (2011) · Analytical Chemistry · doi:10.1021/ac202882y · Cited by 96
Bouter, Y., Kacprowski, T., Weissmann, R., Dietrich, K., Borgers, H., Brauß, A., Sperling, C., Wirths, O., Albrecht, M., Jensen, L. R., et al. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00075 · Cited by 76
Akhtar, A., Dhaliwal, J., & Sah, S. P. (2021) · Psychopharmacology · doi:10.1007/s00213-021-05826-7 · Cited by 89
Brody, D. L., Jiang, H., Wildburger, N. C., & Esparza, T. J. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0293-3 · Cited by 86
The missing link in the amyloid cascade of Alzheimer’s disease – Metal ions
Tiiman, A., Palumaa, P., & Tõugu, V. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.023 · Cited by 92
Oligomers, fact or artefact? SDS-PAGE induces dimerization of β-amyloid in human brain samples
Watt, A. D., Perez, K. A., Rembach, A., Sherratt, N. A., Hung, L. W., Johanssen, T., McLean, C., Kok, W. M., Hutton, C. A., Fodero‐Tavoletti, M. T., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1083-z · Cited by 88
Kaya, I., Zetterberg, H., Blennow, K., & Hanrieder, J. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00121 · Cited by 87
Self-citationMolecular subtypes of Alzheimer’s disease
Fede, G. D., Catania, M., Maderna, E., Ghidoni, R., Benussi, L., Tonoli, E., Giaccone, G., Moda, F., Paterlini, A., Campagnani, I., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-21641-1 · Cited by 86
Walker, L. C. (2020) · Free Neuropathology · doi:10.17879/freeneuropathology-2020-3025 · Cited by 113
Muratore, C., Zhou, C. Q., Liao, M., Fernandez, M. A., Taylor, W. M., Lagomarsino, V. N., Pearse, R. V., Rice, H. C., Negri, J. M., He, A., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.10.015 · Cited by 82
Capping of Aβ42 Oligomers by Small Molecule Inhibitors
Fu, Z., Aucoin, D., Ahmed, M., Ziliox, M., Nostrand, W. E. V., & Smith, S. O. (2014) · Biochemistry · doi:10.1021/bi500910b · Cited by 87
Gunn, A. P., Wong, B. X. W., Johanssen, T., Griffith, J. C., Masters, C. L., Bush, A. I., Barnham, K. J., Duce, J. A., & Cherny, R. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.655183 · Cited by 86
Hook, G., Yu, J., Toneff, T., Kindy, M. S., & HOOK, V. Y. H. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131370 · Cited by 87
Mechanism of Nucleated Conformational Conversion of Aβ42
Fu, Z., Aucoin, D., Davis, J., Nostrand, W. E. V., & Smith, S. O. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00467 · Cited by 83
Cummings, D. M., Liu, W., Portelius, E., Bayram, S., Yasvoina, M. V., Ho, H., Smits, H., Ali, S. S., Steinberg, R., Pegasiou, C.-M., et al. (2015) · Brain · doi:10.1093/brain/awv127 · Cited by 84
Self-citationPyroglutamate-Aβ: Role in the natural history of Alzheimer's disease
Gunn, A. P., Masters, C. L., & Cherny, R. A. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.08.015 · Cited by 79
Hüttenrauch, M., Brauß, A., Kurdakova, A., Borgers, H., Klinker, F., Liebetanz, D., Salinas-Riester, G., Wiltfang, J., Klafki, H. W., & Wirths, O. (2016) · Translational Psychiatry · doi:10.1038/tp.2016.65 · Cited by 78
Hoffmann, T., Meyer, A., Heiser, U. F., Kurat, S., Böhme, L., Kleinschmidt, M., Bühring, K. U., Hutter‐Paier, B., Farcher, M., Demuth, H., et al. (2017) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.117.240614 · Cited by 77
Fruhwürth, S., Zetterberg, H., & Paludan, S. R. (2024) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2024.578342 · Cited by 77
Self-citationWittnam, J. L., Portelius, E., Zetterberg, H., Gustavsson, M. K., Schilling, S., Koch, B. C. P., Demuth, H., Blennow, K., Wirths, O., & Bayer, T. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308601 · Cited by 77
Self-citationHighly potent soluble amyloid-β seeds in human Alzheimer brain but not cerebrospinal fluid
Fritschi, S. K., Langer, F., Kaeser, S. A., Maia, L. F., Portelius, E., Pinotsi, D., Kaminski, C. F., Winkler, D. T., Maetzler, W., Keyvani, K., et al. (2014) · Brain · doi:10.1093/brain/awu255 · Cited by 83
Self-citationNeuron Loss in Alzheimer’s Disease: Translation in Transgenic Mouse Models
Wirths, O., & Zampar, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218144 · Cited by 75
“Aβ42 peptides starting with phenylalanine (F) at position 4 (Aβ4–42) are among the first Aβ peptides that have been isolated from amyloid plaque cores in the human AD brain [101] and represent a highly abundant species in brains from both sporadic and familial AD cases [102].”
Background18F-FDG-PET Detects Drastic Changes in Brain Metabolism in the Tg4–42 Model of Alzheimer’s Disease
Bouter, C., Henniges, P., Franke, T. N., Irwin, C., Sahlmann, C. O., Sichler, M. E., Beindorff, N., Bayer, T. A., & Bouter, Y. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00425 · Cited by 77
Michno, W., Nyström, S., Wehrli, P. M., Lashley, T., Brinkmalm, G., Guérard, L., Syvänen, S., Sehlin, D., Kaya, I., Brinet, D., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006604 · Cited by 75
Self-citationA comparative analysis of the aggregation behavior of amyloid‐β peptide variants
Vandersteen, A., Hubin, E., Sarroukh, R., Baets, G. D., Schymkowitz, J. W. H., Rousseau, F., Subramaniam, V., Raussens, V., Wenschuh, H., Wildemann, D., et al. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.10.022 · Cited by 76
Analysis of Motor Function in the Tg4-42 Mouse Model of Alzheimer’s Disease
Wagner, J. M., Sichler, M., Schleicher, E. M., Franke, T., Irwin, C., Löw, M. J., Beindorff, N., Bouter, C., Bayer, T., & Bouter, Y. (2019) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2019.00107 · Cited by 62
Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies
Martinelli, A. H. S., Lopes, F. C., John, E. B. D. O., Carlini, C. R., & Ligabue‐Braun, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061322 · Cited by 99
Parodi‐Rullán, R. M., Ghiso, J. A., Cabrera, E., Rostagno, A. A., & Fossati, S. (2020) · Aging Cell · doi:10.1111/acel.13258 · Cited by 71
Mattsson, N., Rajendran, L., Zetterberg, H., Gustavsson, M. K., Andréasson, U., Olsson, M., Brinkmalm, G., Lundkvist, J., Jacobson, L. H., Perrot, L., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031084 · Cited by 71
Self-citationChang, Y., & Chen, Y. (2014) · FEBS Journal · doi:10.1111/febs.12813 · Cited by 68
Gkanatsiou, E., Portelius, E., Toomey, C. E., Blennow, K., Zetterberg, H., Lashley, T., & Brinkmalm, G. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.02.033 · Cited by 68
Self-citationd’Abramo, C., D'adamio, L., & Giliberto, L. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030116 · Cited by 71
Cerebral white matter lesions – associations with Aβ isoforms and amyloid PET
van Westen, D., Lindqvist, D., Blennow, K., Minthon, L., Nägga, K., Stomrud, E., Zetterberg, H., & Hansson, O. (2016) · Scientific Reports · doi:10.1038/srep20709 · Cited by 66
Self-citationWalter, S., Jumpertz, T., Hüttenrauch, M., Ogorek, I., Gerber, H., Storck, S. E., Zampar, S., Dimitrov, M., Lehmann, S., Lepka, K., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1929-5 · Cited by 65
Hartlage‐Rübsamen, M., Morawski, M., Waniek, A., Jäger, C., Zeitschel, U., Koch, B. C. P., Cynis, H., Schilling, S., Schliebs, R., Demuth, H., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0806-2 · Cited by 66
Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer´s Disease Immunotherapy
Pérez-Garmendia, R., & Gevorkian, G. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311050004 · Cited by 65
Wirths, O., Walter, S., Kraus, I., Klafki, H., Stazi, M., Oberstein, T. J., Ghiso, J. A., Wiltfang, J., Bayer, T. A., & Weggen, S. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0309-z · Cited by 66
Cai, Y., Xiong, K., Zhang, X., Cai, H., Luo, X., Feng, J., Clough, R. W., Struble, R. G., Patrylo, P. R., Chu, Y., et al. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07376.x · Cited by 62
Proteopathic Strains and the Heterogeneity of Neurodegenerative Diseases
Walker, L. C. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-120215-034943 · Cited by 60
Isoglutaminyl cyclase contributes to CCL2-driven neuroinflammation in Alzheimer’s disease
Hartlage‐Rübsamen, M., Waniek, A., Meißner, J., Morawski, M., Schilling, S., Jäger, C., Kleinschmidt, M., Cynis, H., Kehlen, A., Arendt, T., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1395-2 · Cited by 62
Maiti, B. K., Govil, N., Kundu, T., & Moura, J. J. G. (2020) · iScience · doi:10.1016/j.isci.2020.101792 · Cited by 64
Protective properties of lysozyme on β-amyloid pathology: implications for Alzheimer disease
Helmfors, L., Boman, A., Civitelli, L., Nath, S., Sandin, L., Janefjord, C., McCann, H., Zetterberg, H., Blennow, K., Halliday, G. M., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.08.024 · Cited by 62
Self-citationAlzheimer therapy with an antibody against N-terminal Abeta 4-X and pyroglutamate Abeta 3-X
Antonios, G., Borgers, H., Richard, B. C., Brauß, A., Meißner, J., Weggen, S., Pena, V., Pillot, T., Davies, S. L., Bakrania, P., et al. (2015) · Scientific Reports · doi:10.1038/srep17338 · Cited by 61
Wezynfeld, N. E., Stefaniak, E., Stachucy, K., Drozd, A., Płonka, D., Drew, S. C., Krężel, A., & Bal, W. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201511968 · Cited by 60
Michno, W., Wehrli, P. M., Zetterberg, H., Blennow, K., & Hanrieder, J. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.09.010 · Cited by 60
Self-citationCurdt, N., Schmitt, F. W., Bouter, C., Iseni, T., Weile, H. C., Altunok, B., Beindorff, N., Bayer, T. A., Cooke, M. B., & Bouter, Y. (2022) · Scientific Reports · doi:10.1038/s41598-022-09270-1 · Cited by 63
Antonios, G., Saiepour, N., Bouter, Y., Richard, B. C., Paetau, A., Verkkoniemi-Ahola, A., Lannfelt, L., Ingelsson, M., Kovacs, G. G., Pillot, T., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-56 · Cited by 53
Michno, W., Kaya, I., Nyström, S., Guérard, L., Nilsson, K. P. R., Hammarström, P., Blennow, K., Zetterberg, H., & Hanrieder, J. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b01361 · Cited by 54
Self-citationCuII Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function
Stefaniak, E., & Bal, W. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01399 · Cited by 56
Portelius, E., Olsson, M., Brinkmalm, G., Rüetschi, U., Mattsson, N., Andréasson, U., Gobom, J., Brinkmalm, A., Hölttä, M., Blennow, K., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120994 · Cited by 51
Self-citationPortelius, E., Lashley, T., Westerlund, A., Persson, R., Fox, N. C., Blennow, K., Révész, T., & Zetterberg, H. (2015) · Neurodegenerative Diseases · doi:10.1159/000369465 · Cited by 51
Self-citationCu II Binding to Various Forms of Amyloid‐β Peptides: Are They Friends or Foes?
Borghesani, V., Aliès, B., & Hureau, C. (2017) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201700776 · Cited by 50
Morel, B., Carrasco, M. P., Jurado, S., Marco, C., & Conejero‐Lara, F. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp02685h · Cited by 50
Carlred, L., Michno, W., Kaya, I., Sjövall, P., Syvänen, S., & Hanrieder, J. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13645 · Cited by 48
Giesers, N. K., & Wirths, O. (2020) · ASN Neuro · doi:10.1177/1759091420925356 · Cited by 47
Statistically quantified measurement of an Alzheimer's marker by surface‐enhanced Raman scattering
Buividas, R., Dzingelevičius, N., Kubiliūtė, R., Stoddart, P. R., Truong, V. K., Ivanova, E. P., & Juodkazis, S. (2014) · Journal of Biophotonics · doi:10.1002/jbio.201400017 · Cited by 47
Schwab, S. K., Shearer, J., Conklin, S. E., Aliès, B., & Haas, K. L. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.12.021 · Cited by 47
Blennow, K., & Zetterberg, H. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.07.006 · Cited by 46
Self-citation
Metadata
- Authors
- Portelius, E., Bogdanovic, N., Gustavsson, M. K., Volkmann, I., Brinkmalm, G., Zetterberg, H., Winblad, B., & Blennow, K.
- Affiliations
- University of Gothenburg (SE)
- Karolinska Institutet (SE)
- Corresponding author
- Portelius, Erik
- Venue
- Acta Neuropathologica
- Published
- 2010-04-24
- Volume
- 120
- Issue
- 2
- Pages
- 185-193
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC3568930
- OpenAlex
- W2045197448
- Cited by
- 348
- References
- 41
- Citations by year
- 2026: 13 · 2025: 19 · 2024: 27 · 2023: 22 · 2022: 21 · 2021: 25 · 2020: 26 · 2019: 28 · 2018: 26 · 2017: 20 · 2016: 22 · 2015: 31 · 2014: 23 · 2013: 10 · 2012: 16
- FWCI
- 9.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Acta Neuropathologica (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- National Institute on Aging (K08 AG-22228, AG023185, K08AG022228, U01AG016976, P50AG005131, AG-O5131, R01AG023185)
- 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
- Alzheimer's disease, amyloid-beta isoforms, amyloid-beta 42, Aβ40, amyloid-beta oligomers, amyloid plaques, familial Alzheimer's disease, sporadic Alzheimer's disease, amyloid precursor protein mutations, hippocampus, cerebral cortex, cerebellum
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Brain, Female, Humans, Male, Middle Aged, Peptide Fragments, Mass Spectrometry, Statistics as Topic, Amyloid beta-Peptides, Protein Isoforms, Immunoprecipitation
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
