Cited by 244

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Biochemical detection of Aβ isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer’s disease

Golde, Todd E, Eckman, Christopher B, Younkin, Steven G·2000·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

DOI 10.1016/s0925-4439(00)00043-0

Open this paper in CoChat — free account

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

Crossref · 10.1016/s0925-4439(00)00043-0

Cites

19 of 19 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Self-citation
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
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
Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774
Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757
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
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507

Show all 19 references

Research works printed but not linked: 87

Wong, 1985, Proc. Natl. Acad. Sci. USA, 82, 8729, 10.1073/pnas.82.24.8729 · DOI
Masters, 1985, Proc. Natl. Acad. Sci. USA, 82, 4245, 10.1073/pnas.82.12.4245 · DOI · Paper page
Glenner, 1984, Biochem. Biophys. Res. Commun., 122, 1131, 10.1016/0006-291X(84)91209-9 · DOI · Paper page
Goldgaber, 1987, Science, 235, 877, 10.1126/science.3810169 · DOI
Robakis, 1987, Proc. Natl. Acad. Sci. USA, 84, 4190, 10.1073/pnas.84.12.4190 · DOI
Busciglio, 1993, Proc. Natl. Acad. Sci. USA, 90, 2092, 10.1073/pnas.90.5.2092 · DOI · Paper page
Seubert, 1993, Nature, 361, 260, 10.1038/361260a0 · DOI
Lammich, 1999, Proc. Natl. Acad. Sci. USA, 96, 3922, 10.1073/pnas.96.7.3922 · DOI · Paper page
Buxbaum, 1998, J. Biol. Chem., 273, 27765, 10.1074/jbc.273.43.27765 · DOI
T.E. Golde, S.G. Younkin, in: A. Goate, (Ed.), Pathology of Alzheimer’s Disease, Academic press, New York, 1996, p. 113.
Wang, 1996, J. Biol. Chem., 271, 31894, 10.1074/jbc.271.50.31894 · DOI
Suzuki, 1994, Science, 264, 1336, 10.1126/science.8191290 · DOI · Paper page
Borchelt, 1996, Neuron, 17, 1005, 10.1016/S0896-6273(00)80230-5 · DOI · Paper page
Duff, 1996, Nature, 383, 710, 10.1038/383710a0 · DOI
Tomita, 1997, Proc. Natl. Acad. Sci. USA, 94, 2025, 10.1073/pnas.94.5.2025 · DOI
Roses, 1994, J. Neuropathol. Exp. Neurol., 53, 429, 10.1097/00005072-199409000-00002 · DOI · Paper page
Jarrett, 1993, Ann. New York Acad. Sci., 695, 144, 10.1111/j.1749-6632.1993.tb23043.x · DOI
Jarrett, 1993, Biochemistry, 32, 4693, 10.1021/bi00069a001 · DOI · Paper page
Holcomb, 1998, Nat. Med., 4, 97, 10.1038/nm0198-097 · DOI · Paper page
Hsiao, 1996, Science, 274, 99, 10.1126/science.274.5284.99 · DOI · Paper page
Johnson-Wood, 1997, Proc. Natl. Acad. Sci. USA, 94, 1550, 10.1073/pnas.94.4.1550 · DOI
Yankner, 1996, Neuron, 16, 921, 10.1016/S0896-6273(00)80115-4 · DOI
Ishii, 1997, Brain Res., 748, 250, 10.1016/S0006-8993(96)01363-7 · DOI · Paper page
McNamara, 1998, Arch. Neurol., 55, 1001, 10.1001/archneur.55.7.1001 · DOI
Roher, 1993, Proc. Natl. Acad. Sci. USA, 90, 10836, 10.1073/pnas.90.22.10836 · DOI · Paper page
Levy, 1990, Science, 248, 1124, 10.1126/science.2111584 · DOI
De Jonghe, 1998, Neurobiol. Dis., 5, 281, 10.1006/nbdi.1998.0202 · DOI
Castano, 1995, Biochem. J., 306, 599, 10.1042/bj3060599 · DOI · Paper page
Hendriks, 1992, Nat. Gen., 1, 218, 10.1038/ng0692-218 · DOI
Haass, 1994, J. Biol. Chem., 269, 17741, 10.1016/S0021-9258(17)32503-6 · DOI
Russo, 1997, FEBS Lett., 409, 411, 10.1016/S0014-5793(97)00564-4 · DOI
Saido, 1995, Neuron, 14, 457, 10.1016/0896-6273(95)90301-1 · DOI · Paper page
Tekirian, 1998, J. Neuropathol. Exp. Neurol., 57, 76, 10.1097/00005072-199801000-00009 · DOI
Roher, 1993, J. Biol. Chem., 268, 3072, 10.1016/S0021-9258(18)53661-9 · DOI · Paper page
Fonseca, 1999, Exp. Neurol., 157, 277, 10.1006/exnr.1999.7058 · DOI
Dickson, 1997, J. Neuropathol. Exp. Neurol., 56, 321, 10.1097/00005072-199704000-00001 · DOI · Paper page
Davies, 1993, Am. J. Pathol., 143, 1594
Masliah, 1996, J. Neurosci., 16, 5795, 10.1523/JNEUROSCI.16-18-05795.1996 · DOI
Chen, 1998, Prog. Brain Res., 117, 327, 10.1016/S0079-6123(08)64025-X · DOI
Gowing, 1994, J. Biol. Chem., 269, 10987, 10.1016/S0021-9258(19)78080-6 · DOI · Paper page
Ancolio, 1999, Proc. Natl. Acad. Sci. USA, 96, 4119, 10.1073/pnas.96.7.4119 · DOI
McGeer, 1994, Alzheimer Dis. Assoc. Disord., 8, 149, 10.1097/00002093-199408030-00001 · DOI
Rogers, 1992, Proc. Natl. Acad. Sci. USA, 89, 10016, 10.1073/pnas.89.21.10016 · DOI · Paper page
Velazquez, 1997, Nat. Med., 3, 77, 10.1038/nm0197-77 · DOI
Webster, 1997, Am. J. Pathol., 150, 1531
Giulian, 1998, J. Biol. Chem., 273, 29719, 10.1074/jbc.273.45.29719 · DOI
Wertkin, 1993, Proc. Natl. Acad. Sci. USA, 90, 9513, 10.1073/pnas.90.20.9513 · DOI · Paper page
Wild-Bode, 1997, J. Biol. Chem., 272, 16085, 10.1074/jbc.272.26.16085 · DOI · Paper page
Hartmann, 1998, Nat. Med., 3, 1016, 10.1038/nm0997-1016 · DOI
Cook, 1997, Nat. Med., 3, 1021, 10.1038/nm0997-1021 · DOI
Harder, 1997, Curr. Opin. Cell Biol., 9, 534, 10.1016/S0955-0674(97)80030-0 · DOI
Morishima-Kawashima, 1998, Biochemistry, 37, 15247, 10.1021/bi981843u · DOI
Lee, 1998, Nat. Med., 4, 730, 10.1038/nm0698-730 · DOI
Yanagisawa, 1998, Neurobiol. Aging, 19, S65, 10.1016/S0197-4580(98)00032-3 · DOI
Yanagisawa, 1997, FEBS Lett., 420, 43, 10.1016/S0014-5793(97)01484-1 · DOI
Yanagisawa, 1995, Nat. Med., 1, 1062, 10.1038/nm1095-1062 · DOI
Vey, 1996, Proc. Natl. Acad. Sci. USA, 93, 14945, 10.1073/pnas.93.25.14945 · DOI
Choo-Smith, 1997, FEBS Lett., 402, 95, 10.1016/S0014-5793(96)01504-9 · DOI
Choo-Smith, 1997, J. Biol. Chem., 272, 22987, 10.1074/jbc.272.37.22987 · DOI
Crook, 1998, Nat. Med., 4, 452, 10.1038/nm0498-452 · DOI
Barnes, 1998, J. Neurosci., 18, 5869, 10.1523/JNEUROSCI.18-15-05869.1998 · DOI
Weidemann, 1999, J. Biol. Chem., 274, 5823, 10.1074/jbc.274.9.5823 · DOI
Schagger, 1987, Anal. Biochem., 166, 368, 10.1016/0003-2697(87)90587-2 · DOI
Wiltfang, 1997, Electrophoresis, 18, 527, 10.1002/elps.1150180332 · DOI
Podlisny, 1998, Biochemistry, 37, 3602, 10.1021/bi972029u · DOI
Xia, 1997, J. Biol. Chem., 272, 7977, 10.1074/jbc.272.12.7977 · DOI
Lambert, 1997, Hum. Mol. Genet., 6, 2151, 10.1093/hmg/6.12.2151 · DOI
Barelli, 1997, Mol. Med., 3, 695, 10.1007/BF03401708 · DOI
Kim, 1988, Neurosci. Res. Commun., 2, 121
Murphy, 1999, J. Biol. Chem., 274, 11914, 10.1074/jbc.274.17.11914 · DOI
Walsh, 1997, J. Biol. Chem., 272, 22364, 10.1074/jbc.272.35.22364 · DOI
Harper, 1997, Chem. Biol., 4, 951, 10.1016/S1074-5521(97)90303-3 · DOI
Pitschke, 1998, Nat. Med., 4, 832, 10.1038/nm0798-832 · DOI
Group, 1998, Neurobiol. Aging, 19, 109, 10.1016/S0197-4580(98)00022-0 · DOI
Kosaka, 1997, Neurology, 48, 741, 10.1212/WNL.48.3.741 · DOI
Eckman, 1997, Hum. Mol. Genet., 6, 2087, 10.1093/hmg/6.12.2087 · DOI · Paper page
Matsubara, 1999, Ann. Neurol., 45, 537, 10.1002/1531-8249(199904)45:4<537::AID-ANA20>3.0.CO;2-2 · DOI
Jensen, 1999, Ann. Neurol., 45, 504, 10.1002/1531-8249(199904)45:4<504::AID-ANA12>3.0.CO;2-9 · DOI
Kuo, 1999, Biochem. Biophys. Res. Commun., 257, 787, 10.1006/bbrc.1999.0552 · DOI
Qian, 1998, Neuron, 20, 611, 10.1016/S0896-6273(00)80999-X · DOI
Nakano, 1999, Eur. J. Neurosci., 11, 2577, 10.1046/j.1460-9568.1999.00698.x · DOI
Oyama, 1998, J. Neurochem., 71, 313, 10.1046/j.1471-4159.1998.71010313.x · DOI
Cai, 1997, Am. J. Med. Genet., 74, 202, 10.1002/(SICI)1096-8628(19970418)74:2<202::AID-AJMG18>3.0.CO;2-M · DOI
Murayama, 1997, Neurosci. Lett., 229, 61, 10.1016/S0304-3940(97)00417-5 · DOI
Johnston, 1994, FEBS Lett., 354, 274, 10.1016/0014-5793(94)01137-0 · DOI
Citron, 1994, Proc. Natl. Acad. Sci. USA, 91, 11993, 10.1073/pnas.91.25.11993 · DOI · Paper page
Ghiso, 1997, FEBS Lett., 408, 105, 10.1016/S0014-5793(97)00400-6 · DOI

Sorted by citations

Alzheimer's disease
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
Alzheimer’s Disease: The Challenge of the Second Century
Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424
Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease
DeMattos, R. B., Bales, K. R., Cummins, D. J., Dodart, J.-C., Paul, S. M., & Holtzman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261398 · Cited by 1,298
Green tea Epigallocatechin-3-Gallate (EGCG) Modulates Amyloid Precursor Protein Cleavage and Reduces Cerebral Amyloidosis in Alzheimer Transgenic Mice
Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1521-05.2005 · Cited by 713
NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ42 in vivo
Eriksen, J. L., Sagi, S. A., Smith, T. E., Weggen, S., Das, P., McLendon, D. C., Ozols, V. V., Jessing, K. W., Zavitz, K. H., Koo, E. H., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18162 · Cited by 634
Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo
Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., & Holtzman, D. M. (2006) · Nature Medicine · doi:10.1038/nm1438 · Cited by 599
Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice
McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565
Self-citation
Disruption of the Sleep-Wake Cycle and Diurnal Fluctuation of β-Amyloid in Mice with Alzheimer’s Disease Pathology
Roh, J. H., Huang, Y., Bero, A. W., Kasten, T., Stewart, F. R., Bateman, R. J., & Holtzman, D. M. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004291 · Cited by 563
Green tea epigallocatechin-3-gallate (EGCG) reduces β-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice
Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., & Tan, J. (2008) · Brain Research · doi:10.1016/j.brainres.2008.02.107 · Cited by 459
REVIEW: Curcumin and Alzheimer’s disease
Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450
In Vivo Assessment of Brain Interstitial Fluid with Microdialysis Reveals Plaque-Associated Changes in Amyloid-β Metabolism and Half-Life
Cirrito, J. R., May, P. C., O'Dell, M. A., Taylor, J. W., Parsadanian, M., Cramer, J. W., Audia, J. E., Nissen, J. S., Bales, K. R., Paul, S. M., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08844.2003 · Cited by 394
Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies
Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349
Fluctuations of CSF amyloid-β levels: Implications for a diagnostic and therapeutic biomarker
Bateman, R. J., Wen, G., Morris, J. C., & Holtzman, D. M. (2007) · Neurology · doi:10.1212/01.wnl.0000256043.50901.e3 · Cited by 260
Cystatin C-Cathepsin B Axis Regulates Amyloid Beta Levels and Associated Neuronal Deficits in an Animal Model of Alzheimer's Disease
Sun, B., Zhou, Y., Halabisky, B., Lo, I., Cho, S.-H., Mueller-Steiner, S., Devidze, N., Wang, X., Grubb, A., & Gan, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.001 · Cited by 231
Microglial activation facilitates Aβ plaque removal following intracranial anti-Aβ antibody administration
Wilcock, D. M., Munireddy, S. K., Rosenthal, A., Ugen, K. E., Gordon, M. N., & Morgan, D. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.09.015 · Cited by 202
Purification and characterization of astrocyte-secreted apolipoprotein E and J-containing lipoproteins from wild-type and human apoE transgenic mice
DeMattos, R. B., Brendza, R. P., Heuser, J. E., Kierson, M., Cirrito, J. R., Fryer, J., Sullivan, P. M., Fagan, A. M., Han, X., & Holtzman, D. M. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00049-3 · Cited by 180
Cerebrovascular Dysfunction in Amyloid Precursor Protein Transgenic Mice: Contribution of Soluble and Insoluble Amyloid-β Peptide, Partial Restoration via γ-Secretase Inhibition
Han, B. H., Zhou, M.-L., Abousaleh, F., Brendza, R. P., Dietrich, H. H., Koenigsknecht-Talboo, J., Cirrito, J. R., Milner, E., Holtzman, D. M., & Zipfel, G. J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4686-08.2008 · Cited by 138
Neurotheranostics as Personalized Medicines
Kevadiya, B. D., Ottemann, B. M., Thomas, M. B., Mukadam, I., Nigam, S., McMillan, J., Gorantla, S., Bronich, T. K., Edagwa, B., & Gendelman, H. E. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.10.011 · Cited by 124
Disease modifying therapy for AD?1
Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117
Self-citation
Coenzyme Q10 Attenuates β-Amyloid Pathology in the Aged Transgenic Mice with Alzheimer Presenilin 1 Mutation
Yang, X., Yang, Y., Li, G., Wang, J., & Yang, E. S. (2008) · Journal of Molecular Neuroscience · doi:10.1007/s12031-007-9033-7 · Cited by 111
Proteinopathy-induced neuronal senescence: a hypothesis for brain failure in Alzheimer’s and other neurodegenerative diseases
Golde, T. E., & Miller, V. M. (2009) · Alzheimer's Research & Therapy · doi:10.1186/alzrt5 · Cited by 98
Self-citation
Targeting Aβ and tau in Alzheimer's disease, an early interim report
Golde, T. E., Petrucelli, L., & Lewis, J. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.035 · Cited by 89
Self-citation
Aβ1–42 stimulates adult SVZ neurogenesis through the p75 neurotrophin receptor
Sotthibundhu, A., Li, Q.-X., Thangnipon, W., & Coulson, E. J. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.02.004 · Cited by 81
Inactivation of VCP/ter94 Suppresses Retinal Pathology Caused by Misfolded Rhodopsin in Drosophila
Griciuc, A., Aron, L., Roux, M. J., Klein, R., Giangrande, A., & Ueffing, M. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001075 · Cited by 78
Mutations in APP have independent effects on Aβ and CTFγ generation
Hecimovic, S., Wang, J., Dolios, G., Martinez, M., Wang, R., & Goate, A. M. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.04.018 · Cited by 70
High throughput screens for the identification of compounds that alter the accumulation of the Alzheimer's amyloid β peptide (Aβ)
Haugabook, S. J., Yager, D. M., Eckman, E. A., Golde, T. E., Younkin, S. G., & Eckman, C. B. (2001) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(01)00388-0 · Cited by 39
Self-citation

Authors: Golde, T. E., Eckman, C. B., & Younkin, S. G.
Venue: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Publisher: Elsevier BV
Published: 2000-07
Volume: 1502
Issue: 1
Pages: 172-187
ISSN: 0925-4439
DOI: 10.1016/s0925-4439(00)00043-0
Cited by: 244
References: 19
Language: en
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4765 d)

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

Biochemical detection of Aβ isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer’s disease

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks