Cited by 158Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.

Nonfibrillar diffuse amyloid deposition due to a gamma42-secretase site mutation points to an essential role for N-truncated Abeta42 in Alzheimer's disease

Kumar-Singh, S.·2000·Human Molecular Genetics

DOI 10.1093/hmg/9.18.2589

Open this paper in CoChat — free account

Abstract

Amyloidogenic processing of the amyloid precursor protein (APP) with deposition in brain of the 42 amino acid long amyloid beta-peptide (A beta(42)) is considered central to Alzheimer's disease (AD) pathology. However, it is generally believed that nonfibrillar pre-amyloid A beta(42) deposits have to mature in the presence of A beta(40) into fibrillar amyloid plaques to cause neurodegeneration. Here, we describe an aggressive form of AD caused by a novel missense mutation in APP (T714I) directly involving gamma-secretase cleavages of APP. The mutation had the most drastic effect on A beta(42)/A beta(40) ratio in vitro of approximately 11-fold, simultaneously increasing A beta(42) and decreasing A beta(40) secretion, as measured by matrix-assisted laser disorption ionization time-of-flight mass spectrometry. This coincided in brain with deposition of abundant and predominant nonfibrillar pre-amyloid plaques composed primarily of N-truncated A beta(42) in complete absence of A beta(40). These data indicate that N-truncated A beta(42) as diffuse nonfibrillar plaques has an essential but undermined role in AD pathology. Importantly, inhibiting secretion of full-length A beta(42 )by therapeutic targeting of APP processing should not result in secretion of an equally toxic N-truncated A beta(42).

Integrity signals

Registry

Crossref · 10.1093/hmg/9.18.2589

Cites

51 of 51 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
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
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
β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE
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
The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., & Selkoe, D. J. (1999) · Nature · doi:10.1038/19077 · Cited by 1,959
Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
De Strooper, B., Saftig, P., Craessaerts, K., Vanderstichele, H., Guhde, G., Annaert, W., Von Figura, K., & Van Leuven, F. (1998) · Nature · doi:10.1038/34910 · Cited by 1,818
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
A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid
Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513
An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp 717 ) Mutants
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471

Flagged first, then by citations

Show all 51 references

Sorted by citations

Items 101–158 of 158

Aquaporin 4 modulation drives amyloid burden and cognitive abilities in an APPPS1 mouse model of Alzheimer's disease
Mănescu, M. D., Cătălin, B., Bâldea, I., Mateescu, V. O., Roşu, G. C., Boboc, I. K. Ş., Istrate-Ofiţeru, A.-M., Liliac, I. M., Streba, C. T., Kumar‐Singh, S., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70164 · Cited by 17
Self-citation
APP substrate ectodomain defines amyloid‐β peptide length by restraining γ‐secretase processivity and facilitating product release
Koch, M. K., Enzlein, T., Chen, S., Petit, D., Lismont, S., Zacharias, M., Hopf, C., & Chávez‐Gutiérrez, L. (2023) · The EMBO Journal · doi:10.15252/embj.2023114372 · Cited by 17
Modeling Alzheimer’s Disease: A Review of Gene-Modified and Induced Animal Models, Complex Cell Culture Models, and Computational Modeling
Timofeeva, A. M., Aulova, K. S., & Nevinsky, G. A. (2025) · Brain Sciences · doi:10.3390/brainsci15050486 · Cited by 17
Genetic Complexity of Early-Onset Alzheimer’s Disease
Ghani, M., Reitz, C., George‐Hyslop, P. S., & Rogaeva, E. A. (2018) · Springer eBooks · doi:10.1007/978-3-319-72938-1_3 · Cited by 15
Specific Mutations near the Amyloid Precursor Protein Cleavage Site Increase γ-Secretase Sensitivity and Modulate Amyloid-β Production
Suzuki, R., Takahashi, H., Yoshida, C., Hidaka, M., Ogawa, T., & Futai, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043970 · Cited by 14
Anti-11[E]-pyroglutamate-modified amyloid β antibodies cross-react with other pathological Aβ species: Relevance for immunotherapy
Pérez-Garmendia, R., Ibarra-Bracamontes, V., Vasilevko, V., Luna‐Muñoz, J., Mena, R., Govezensky, T., Acero, G., Manoutcharian, K., Cribbs, D. H., & Gevorkian, G. (2010) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2010.08.020 · Cited by 14
Impact of Amyloid Precursor Protein Hydrophilic Transmembrane Residues on Amyloid-Beta Generation
Oestereich, F., Bittner, H. J., Weise, C., Grohmann, L., Janke, L.-K., Hildebrand, P. W., Multhaup, G., & Munter, L. M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00217 · Cited by 13
The Impact of the ‘Austrian’ Mutation of the Amyloid Precursor Protein Transmembrane Helix is Communicated to the Hinge Region
Stelzer, W., Scharnagl, C., Leurs, U., Rand, K. D., & Langosch, D. (2016) · ChemistrySelect · doi:10.1002/slct.201601090 · Cited by 13
Comparable dimerization found in wildtype and familial Alzheimer's disease amyloid precursor protein mutants.
So, P. P., Khodr, C. E., Chen, C.-D., & Abraham, C. R. (2013) · Europe PMC (PubMed Central) · Cited by 13
Peptides based on the presenilin‐APP binding domain inhibit APP processing and Aβ production through interfering with the APP transmembrane domain
Esselens, C. W., Sannerud, R., Gallardo, R. U., Baert, V., Kaden, D., Serneels, L., Strooper, B. D., Rousseau, F., Multhaup, G., Schymkowitz, J. W. H., et al. (2012) · The FASEB Journal · doi:10.1096/fj.11-201368 · Cited by 12
Vascular models of Alzheimer's disease: An overview of recent in vitro models of the blood-brain barrier
Takeuchi, L. E., Kalia, L. V., & Simmons, C. A. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106864 · Cited by 11
Clinical characterization of a presenilin 1 mutation (F177S) in a family with very early‐onset Alzheimer's disease in the third decade of life
Hausner, L., Tschäpe, J. A., Schmitt, H. P., Hentschel, F., Hartmann, T., & Frölich, L. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.02.006 · Cited by 11
Amyloid precursor protein induces reactive astrogliosis
Jáuregui, G. V., Vukić, D., Onyango, I. G., Arias, C., Novotný, J., Texlova, K., Wang, S., Kovačovicova, K. L., Polakova, N., Zelinková, J., et al. (2024) · Acta Physiologica · doi:10.1111/apha.14142 · Cited by 10
A role for β2* nicotinic receptors in a model of local amyloid pathology induced in dentate gyrus
Lombardo, S., Catteau, J., Besson, M., & Maskos, U. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.06.005 · Cited by 10
Autosomal Dominant Alzheimer’s Disease: Underlying Causes
Ghani, M., & Rogaeva, E. A. (2014) · Springer eBooks · doi:10.1007/978-1-4471-6380-0_3 · Cited by 8
Novel Vaccine against Pathological Pyroglutamate-Modified Amyloid Beta for Prevention of Alzheimer’s Disease
Zagorski, K., King, O., Hovakimyan, A., Petrushina, I., Antonyan, T., Chailyan, G., Ghazaryan, M., Hyrc, K. L., Chadarevian, J. P., Davtyan, H., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129797 · Cited by 8
Amyloid pathology and cognitive impairment in hAβ-KI and APPSAA-KI mouse models of Alzheimer's disease
Lü, W., Shue, F., Kurti, A., Jeevaratnam, S., Macyczko, J. R., Roy, B., Izhar, T., Wang, N., Bu, G., Kanekiyo, T., et al. (2024) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2024.10.005 · Cited by 9
The Formation Mechanism of Segmented Ring-Shaped Aβ Oligomers and Protofibrils
Choi, H., Lee, W., Lee, G., Yoon, D. S., & Na, S. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00324 · Cited by 8
Genetics and pathology of alpha-secretase site AβPP mutations in the understanding of Alzheimer's disease
Broeckhoven, C. V., & Kumar‐Singh, S. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s344 · Cited by 8
Self-citation
Alzheimer's Disease; Mechanism, Mutations, and Applications of Nano-Medicine
Maisam, M., Khan, M. T., Lodhi, M. S., Mou, K., Liu, Z., & Wei, D. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2810258 · Cited by 7
Importance of GWAS in finding un-targeted genetic association of sporadic Alzheimer’s disease
Bagaria, J., Nho, K. T., & An, S. S. A. (2021) · Molecular & Cellular Toxicology · doi:10.1007/s13273-021-00130-z · Cited by 8
Clinical characteristics and genotype-phenotype correlation analysis of familial Alzheimer’s disease patients with pathogenic/likely pathogenic amyloid protein precursor mutations
Liu, Y., Xiao, X., Liu, H., Liao, X., Zhou, Y., Weng, L., Zhou, L., Liu, X., Bi, X., Xu, T., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1013295 · Cited by 8
Influence of the familial Alzheimer's disease–associated T43I mutation on the transmembrane structure and γ-secretase processing of the C99 peptide
Tang, T.-C., Kienlen‐Campard, P., Hu, Y., Perrin, F., Opsomer, R., Octave, J., Constantinescu, S. N., & Smith, S. O. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006061 · Cited by 7
An insight into Alzheimer’s disease and its on-setting novel genes
Vigneswaran, J., Muthukumar, S. A., Shafras, M., & Pant, G. (2021) · The Egyptian Journal of Neurology Psychiatry and Neurosurgery · doi:10.1186/s41983-021-00420-2 · Cited by 7
The Role of Genetics in Alzheimer's Disease and Parkinson's Disease
Porter, T., Gozt, A., Mastaglia, F. L., & Laws, S. M. (2019) · Wiley eBooks · doi:10.1002/9781119356752.ch15 · Cited by 6
Key questions for the future of amyloid research in dementia: a framework for integrating complex datasets
Hunter, S., Walsh, S., & Brayne, C. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-03156-0 · Cited by 7
Alzheimer’s Disease: Significant Benefit from the Yeast-Based Models
Epremyan, K. K., Mamaev, D. V., & Zvyagilskaya, R. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129791 · Cited by 7
A closer look at pathogenic amyloid-β in Alzheimer’s disease using cryo-electron microscopy: a narrative review
Gao, Y., Schedin‐Weiss, S., & Tjernberg, L. O. (2024) · Advanced technology in neuroscience . · doi:10.4103/atn.atn-d-24-00014 · Cited by 5
γ-Secretase Inhibitors – from Molecular Probes to New Therapeutics?
Harrison, T., & Beher, D. (2003) · Progress in medicinal chemistry · doi:10.1016/s0079-6468(02)41003-x · Cited by 5
The contribution of N-terminally modified amyloid beta to the etiology of Alzheimer's disease
Wittnam, J. L. (2012) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3182 · Cited by 5
Preclinical MRI and NMR Biomarkers of Alzheimer's Disease: Concepts and Applications
Dhénain, M. (2008) · Magnetic Resonance Insights · doi:10.4137/mri.s971 · Cited by 4
Generation of Amyloid‐β Peptides by γ‐Secretase
Aguayo‐Ortiz, R., & Domı́nguez, L. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600073 · Cited by 4
The Role of HSP70 in the Protection of: (A) The Brain in Alzheimer’s Disease and (B) The Heart in Cardiac Surgery
Malyshev, I. Y. (2013) · SpringerBriefs in biochemistry and molecular biology · doi:10.1007/978-94-007-5943-5_8 · Cited by 4
Reduced brain volumes in mice expressing APP-Austrian mutation but not in mice expressing APP-Swedish–Austrian mutations
Broeck, B. V., Vanhoutte, G., Cuijt, I., Pereson, S., Joris, G., Timmermans, J., der Linden, A. V., Broeckhoven, C. V., & Kumar‐Singh, S. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.09.073 · Cited by 4
Self-citation
Early-Onset Alzheimer’s disease and amyloid precursor protein gene mutations
Varte, V., Ralte, L., & Kumar, N. S. (2025) · Discover Neuroscience · doi:10.1186/s13064-025-00203-y · Cited by 7
Early Intraneuronal β-Amyloid Pathology: Do Transgenic Mice Represent Valid Model Systems?
Wirths, O., & Bayer, T. A. (2008) · Open Longevity Science · doi:10.2174/1874369200802010007 · Cited by 2
Models of Alzheimer’s Disease
Chen, M., Kretzschmar, D., Verdile, G., & Lardelli, M. T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415894-8.00025-7 · Cited by 2
The Molecular Basis of Alzheimer's Disease
Ingelsson, M., & Hyman, B. T. (2007) · Elsevier eBooks · doi:10.1016/b978-012369509-3.50018-4 · Cited by 1
Pathological Validation of Animal Models of Dementia
Pirici, D. N., Broeckhoven, C. V., & Kumar‐Singh, S. (2010) · Neuromethods · doi:10.1007/978-1-60761-898-0_7 · Cited by 1
Self-citation
BACE, APP Processing, and Signal Transduction in Alzheimer's Disease
Bredesen, D. E., & Koo, E. H. (2010) · Wiley eBooks · doi:10.1002/9780470594087.ch1 · Cited by 1
SERF deletion modifies amyloid aggregation in a mouse model of Alzheimer’s diseasePreprint
Stroo, E., Janssen, L., Sin, O., Hogewerf, W., Koster, M. H., Harkema, L., Youssef, S. A., Beschörner, N., Wolters, A. H. G., Bakker, B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.05.423442 · Cited by 1
Early Onset Familial Alzheimer's Disease: Is a Mutation Predictive of Pathology?
Galasko, D. R. (2005) · Research and perspectives in Alzheimer's disease · doi:10.1007/3-540-26522-8_5 · Cited by 1
Die Amyloidablagerung in einem Mausmodell der Alzheimer Demenz und die Modulation der β-Amyloid-Peptidentstehung durch membranverankerte Inhibitoren
Schieb, H. (2011) · DuEPublico (University of Duisburg-Essen)
Caenorhabditis elegans model for admixed proteinopathy of Huntington’s and Alzheimer-typePreprint
Kapulkin, W. J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/648923
Cortical Activity and Rhythmic Patterns in Mouse Models of Aging and Alzheimer’s Disease
Ruiz-Mejías, M., Castano-Prat, P., Donegan, T., & Sanchez-Vives, M. V. (2020) · OBM Geriatrics · doi:10.21926/obm.geriatr.2001105
Genomics of Alzheimer’s disease
Rosenberg, R. N., Lambracht‐Washington, D., Yu, G., & Xia, W. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813866-3.00001-1
Genomics of Alzheimer’s disease
Rosenberg, R. N., Lambracht‐Washington, D., Yu, G., & Xia, W. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19176-3.00035-2
Familial Alzheimer’s disease and Down syndrome
Castellani, R. J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-99651-8.00022-3
The amyloid cascade hypothesis
Castellani, R. J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-99651-8.00003-x
Additional file 17 of Novel App knock-in mouse model shows key features of amyloid pathology and reveals profound metabolic dysregulation of microglia
Xia, D., Lianoglou, S., Sandmann, T., Calvert, M., Suh, J. H., Thomsen, E. R., Dugas, J. C., Pizzo, M. E., DeVos, S. L., Earr, T., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20056383
Additional file 10 of Novel App knock-in mouse model shows key features of amyloid pathology and reveals profound metabolic dysregulation of microglia
Xia, D., Lianoglou, S., Sandmann, T., Calvert, M., Suh, J. H., Thomsen, E. R., Dugas, J. C., Pizzo, M. E., DeVos, S. L., Earr, T., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20056359
Additional file 9 of Novel App knock-in mouse model shows key features of amyloid pathology and reveals profound metabolic dysregulation of microglia
Xia, D., Lianoglou, S., Sandmann, T., Calvert, M., Suh, J. H., Thomsen, E. R., Dugas, J. C., Pizzo, M. E., DeVos, S. L., Earr, T., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20056422
Insights into Missense SNPs on Amyloidogenic Proteins
Galanis, F. P., Apostolakou, A. E., Nasi, G. I., Litou, Z. I., & Iconomidou, V. A. (2025) · Proteomes · doi:10.3390/proteomes13040064
The role of the α7 nicotinic acetylcholine receptor in a model of amyloid pathology
Santos, D. G. (2024) · theses.fr (ABES) · doi:10.70675/b3ed4de5zcd9ez4421za129z0a05130d86b9
BindingDB Entry 50008429: Discovery of Conformationally Restricted Human Glutaminyl Cyclase Inhibitors as Potent Anti-Alzheimer's Agents by Structure-Based Design.
BindingDB (2021) · UC San Diego · doi:10.7270/q2w0999v
BindingDB Entry 50049250: Discovery of Potent Human Glutaminyl Cyclase Inhibitors as Anti-Alzheimer's Agents Based on Rational Design.
BindingDB (2019) · UC San Diego · doi:10.7270/q23x88x9
BindingDB Entry 50002182: Potent human glutaminyl cyclase inhibitors as potential anti-Alzheimer's agents: Structure-activity relationship study of Arg-mimetic region.
BindingDB (2020) · UC San Diego · doi:10.7270/q2sn0ckg
Die Alzheimer-Krankheit: Molekulare Grundlagen und Therapieansätze
Finckh, U., Höck, C., & Nitsch, R. M. (2004) · Springer eBooks · doi:10.1007/978-3-642-18741-4_6

Authors: Kumar-Singh, S.
Venue: Human Molecular Genetics
Publisher: Oxford University Press (OUP)
Published: 2000-11-01
Volume: 9
Issue: 18
Pages: 2589-2598
ISSN: 0964-6906 (ISSN-L)
1460-2083
DOI: 10.1093/hmg/9.18.2589
OpenAlex: W2126690234
Cited by: 158
References: 51
Citations by year: 2025: 8 · 2024: 7 · 2023: 8 · 2022: 6 · 2021: 7 · 2020: 8 · 2019: 9 · 2018: 3 · 2017: 4 · 2016: 10 · 2015: 4 · 2014: 5 · 2013: 9 · 2012: 5
FWCI: 3.30
Type: journal article
Language: en
Open access: closed
Locations: Human Molecular Genetics (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
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 42, gamma-secretase, APP processing, amyloid precursor protein, Aβ40
MeSH terms: Alzheimer Disease, Cell Line, Enzyme-Linked Immunosorbent Assay, Female, Humans, Immunohistochemistry, Male, Pedigree, Peptide Fragments, Endopeptidases, Protein Processing, Post-Translational, Solubility, Transfection, Amyloid beta-Peptides, Aspartic Acid Endopeptidases, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Amino Acid Substitution, Mutation, Missense, Amyloid Precursor Protein Secretases, Plaque, Amyloid

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

Nonfibrillar diffuse amyloid deposition due to a gamma42-secretase site mutation points to an essential role for N-truncated Abeta42 in Alzheimer's disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks