The DOI matches its Crossref record; 40 of the 44 references it cites were found in a registry or an index.
Dynamics of β-Amyloid Reductions in Brain, Cerebrospinal Fluid, and Plasma of β-Amyloid Precursor Protein Transgenic Mice Treated with a γ-Secretase Inhibitor
Abstract
gamma-Secretase inhibitors are one promising approach to the development of a therapeutic for Alzheimer's disease (AD). gamma-Secretase inhibitors reduce brain beta-amyloid peptide (Abeta), which is believed to be a major contributor in the etiology of AD. Transgenic mice overexpressing the human beta-amyloid precursor protein (APP) are valuable models to examine the dynamics of Abeta changes with gamma-secretase inhibitors in plaque-free and plaque-bearing animals. BMS-299897 2-[(1R)-1-[[(4-chlorophenyl)sulfony](2,5-difluorophenyl)amino]ethyl]-5-fluorobenzenepropanoic acid, a gamma-secretase inhibitor, showed dose- and time dependent reductions of Abeta in brain, cerebrospinal fluid (CSF), and plasma in young transgenic mice, with a significant correlation between brain and CSF Abeta levels. Because CSF and brain interstitial fluid are distinct compartments in composition and location, this correlation could not be assumed. In contrast, aged transgenic mice with large accumulations of Abeta in plaques showed reductions in CSF Abeta in the absence of measurable changes in plaque Abeta in the brain after up to 2 weeks of treatment. Hence, CSF Abeta levels were a valuable measure of gamma-secretase activity in the central nervous system in either the presence or absence of plaques. Transgenic mice were also used to examine potential side effects due to Notch inhibition. BMS-299897 was 15-fold more effective at preventing the cleavage of APP than of Notch in vitro. No changes in…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“The half-life of Aβ clearance in these studies ranged from 30 min to 2 h.”
From Measurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling (2012) · cites this paper as [50]
In the citing paper
“Previous studies have measured Aβ clearance from the brain either using 35 S]methionine labeling [48], or by measuring the disappearance of Aβ following the pharmacological inhibition of Aβ production [49-51].”
From Measurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling (2012) · cites this paper as [50]
In the citing paper
“The rapid degradation of Aβ in the periphery (t1/2 = 2–3 min) precludes a direct and sensitive measurement of the rate of Aβ appearance from brain into blood (27, 28).”
From Low-density lipoprotein receptor overexpression enhances the rate of brain-to-blood Aβ clearance in a mouse model of β-amyloidosis (2012) · cites this paper as [28]
In the citing paper
“The rapid degradation of Aβ once it enters the blood from brain precludes direct and reliable measurement of its influx rate by conventional means (27, 28).”
From Low-density lipoprotein receptor overexpression enhances the rate of brain-to-blood Aβ clearance in a mouse model of β-amyloidosis (2012) · cites this paper as [28]
Citations
Cites
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
BACE1 is the major β-secretase for generation of Aβ peptides by neurons
Cai, H., Wang, Y., McCarthy, D. B., Wen, H., Borchelt, D., Price, D. L., & Wong, P. C. (2001) · Nature Neuroscience · doi:10.1038/85064 · Cited by 1,087
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 1×
“The mice have high levels of human A in brain, plasma, and CSF, and low levels in peripheral tissues where there is some limited transgene expression (Kawarabayashi et al., 2001).”
BackgroundIbuprofen Suppresses Plaque Pathology and Inflammation in a Mouse Model for Alzheimer's Disease
Lim, G. P., Yang, F., Chu, T., Chen, P., Beech, W. K., Teter, B., Tran, T., Ubeda, O. J., Ashe, K. H., Frautschy, S. A., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-15-05709.2000 · Cited by 876
Functional gamma‐secretase inhibitors reduce beta‐amyloid peptide levels in brain
Dovey, H. F., John, V., Anderson, J. P., Chen, L. Z., Andrieu, P. D. S. I., Fang, L. Y., Freedman, S. B., Folmer, B., Goldbach, E. G., Holsztynska, E. J., et al. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00012.x · Cited by 870
Self-citationT-cell development and the CD4–CD8 lineage decision
Germain, R. N. (2002) · Nature reviews. Immunology · doi:10.1038/nri798 · Cited by 813
Flagged first, then by citations
4 of the 44 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Ghersi-Egea JF and Strazielle N (2001) Brain drug delivery, drug metabolism and multidrug resistance at the choroid plexus. Microsc Res Tech 52: 83-88. · DOI
Cited by
Sorted by citations
Items 101–176 of 176
Shapiro, J. S., Stiteler, M., Wu, G., Price, E. A., Simon, A. J., & Sankaranarayanan, S. (2011) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2011.12.010 · Cited by 18
Effect of mouse strain as a background for Alzheimer’s disease models on the clearance of amyloid-β
Qosa, H., & Kaddoumi, A. (2016) · Journal of Systems and Integrative Neuroscience · doi:10.15761/jsin.1000123 · Cited by 20
Dosing, collection, and quality control issues in cerebrospinal fluid research using animal models
Barten, D. M., Cadelina, G. W., & Weed, M. R. (2017) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804279-3.00004-6 · Cited by 17
Self-citationCurrent Experimental Therapy for Alzheimers Disease
Chen, S., Zhang, X.-J., Li, L., & Le, W.-D. (2007) · Current Neuropharmacology · doi:10.2174/157015907780866901 · Cited by 17
Park, H., Yoo, J.-S., Kim, J., Hwang, B. Y., Han, J., Yeon, S.-W., & Kang, J. (2014) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2014.01.008 · Cited by 17
At the frontline of Alzheimer’s disease treatment: γ-secretase inhibitor/modulator mechanism
Tomita, T. (2007) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-007-0206-2 · Cited by 17
Pharmacotherapy of Alzheimer’s Disease: Current State and Future Perspectives
Korábečný, J., Zemek, F., Soukup, O., Špilovská, K., Musílek, K., Jun, D., Nepovimová, E., & Kuča, K. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50001-5 · Cited by 18
Unlocking Truths of γ-Secretase In Alzheimer'S Disease: What Is the Translational Potential?
Wolfe, M. S. (2014) · Future Neurology · doi:10.2217/fnl.14.35 · Cited by 17
Chapter 3 Secretase Inhibitors and Modulators for the Treatment of Alzheimer's Disease
Olson, R. E., & Marcin, L. R. (2007) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(07)42003-6 · Cited by 16
Is abeta a sufficient biomarker for monitoring anti-abeta clinical studies? A critical review
Moreth, J., Mavoungou, C., & Schindowski, K. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00025 · Cited by 15
Brodney, M. A., Auperin, D. D., Becker, S. L., Bronk, B. S., Brown, T. M., Coffman, K. J., Finley, J. E., Hicks, C. D., Karmilowicz, M. J., Lanz, T. A., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.12.117 · Cited by 15
Identification and Preclinical Pharmacology of the γ -Secretase Modulator BMS-869780
Toyn, J. H., Thompson, L. A., Lentz, K. A., Meredith, J. E., Burton, C. R., Sankaranararyanan, S., Guss, V. L., Hall, T., Iben, L. G., Krause, C., et al. (2014) · International Journal of Alzheimer s Disease · doi:10.1155/2014/431858 · Cited by 13
Self-citationPu, J., Kreft, A. F., Aschmies, S., Atchison, K. P., Berkowitz, J. D., Caggiano, T. J., Chlenov, M., Diamantidis, G., Harrison, B. L., Hu, Y., et al. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.04.052 · Cited by 13
Amino-caprolactam derivatives as γ-secretase inhibitors
Parker, M. F., Bronson, J. J., Barten, D. M., Corsa, J. A., Du, W., Felsenstein, K. M., Guss, V. L., Izzarelli, D. G., Loo, A. T., McElhone, K. E., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.08.047 · Cited by 13
Self-citationNitrogen-appended N-alkylsulfonamides as inhibitors of γ-secretase
Bergstrom, C. P., Sloan, C. P., Wang, H. H., Parker, M. F., Smith, D. W., Zheng, M., Hansel, S. B., Polson, C. T., Barber, L. E., Bursuker, I., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.10.105 · Cited by 12
Self-citationGoldstein, M. E., Cao, Y., Fiedler, T., Toyn, J. H., Iben, L. G., Barten, D. M., Pierdomenico, M., Corsa, J. A., Prasad, C. V. C., Olson, R. E., et al. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.125492 · Cited by 11
Self-citationCarbamate-appended N-alkylsulfonamides as inhibitors of γ-secretase
Bergstrom, C. P., Sloan, C. P., Lau, W.-Y., Smith, D. W., Zheng, M., Hansel, S. B., Polson, C. T., Corsa, J. A., Barten, D. M., Felsenstein, K. M., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.11.102 · Cited by 11
Self-citationGregory, J. L., Prada, C. M., Fine, S., Garcı́a-Alloza, M., Betensky, R. A., Arbel‐Ornath, M., Greenberg, S. M., Bacskai, B. J., & Frosch, M. P. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182729845 · Cited by 11
Kojima, K., Kitaoka, Y., Munemasa, Y., & Ueno, S. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-10271 · Cited by 10
N-(5-Chloro-2-(hydroxymethyl)-N-alkyl-arylsulfonamides as γ-secretase inhibitors
Parker, M. F., Barten, D. M., Bergstrom, C. P., Bronson, J. J., Corsa, J. A., Deshpande, M., Felsenstein, K. M., Guss, V. L., Hansel, S. B., Johnson, G., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.06.022 · Cited by 10
Self-citationModeling of age-related neurological disease: utility of zebrafish
Kanoh, T., Mizoguchi, T., Tonoki, A., & Itoh, M. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1399098 · Cited by 9
Tai, L. M., Jacobsen, H., Ozmen, L., Flohr, A., Jakob‐Roetne, R., Caruso, A., & Grimm, H. P. (2012) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-012-9246-4 · Cited by 9
PARKINSON, J. R., Ploeger, B. A., Appelkvist, P., Bogstedt, A., Bergstedt, K. D., Eketjäll, S., & Visser, S. A. G. (2013) · Pharmacology Research & Perspectives · doi:10.1002/prp2.12 · Cited by 9
Treatment of dementia: anything new?
Machado, J. C., & Caramelli, P. (2006) · Current Opinion in Psychiatry · doi:10.1097/01.yco.0000245756.29244.b9 · Cited by 9
Lipid metabolism and Alzheimer's disease: pathways and possibilities
Saxena, U. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220902738720 · Cited by 9
Development of a disease‐modifying treatment for Alzheimer's disease: Alzhemed
Aisen, P. S. S. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.03.009 · Cited by 8
Aging of the Brain and Alzheimer’s Disease
Price, D. L., Savonenko, A. V., Albert, M., Troncoso, J. C., & Wong, P. C. (2009) · Elsevier eBooks · doi:10.1016/b978-008045046-9.00539-8 · Cited by 8
Kurosumi, M., Nishio, Y., Osawa, S., Kobayashi, H., Iwatsubo, T., Tomita, T., & Miyachi, H. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.06.131 · Cited by 7
Targeting γ-secretase for familial Alzheimer’s disease
Wolfe, M. S. (2021) · Medicinal Chemistry Research · doi:10.1007/s00044-021-02744-3 · Cited by 8
Drug Development for Alzheimer's Disease: Recent Progress
Ji, W., & Ha, I. (2010) · Experimental Neurobiology · doi:10.5607/en.2010.19.3.120 · Cited by 7
In vitro characterization of a γ‐secretase radiotracer in mammalian brain
Patel, S., O'Malley, S. S., Connolly, B., Liu, W., Hargreaves, R. J., Sur, C., & Gibson, R. E. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03525.x · Cited by 7
β‐Amyloid Therapeutic Strategies for Alzheimer's Disease
Imbimbo, B. P., & Speroni, F. (2005) · Wiley eBooks · doi:10.1002/0471266949.bmc112 · Cited by 6
Hyde, L. A., Zhang, Q., Vecchio, R. A. D., Leach, P. T., Cohen-Williams, M. E., Chen, L., Wong, G. T., McHugh, N. A., Chen, J., Higgins, G. A., et al. (2013) · International Journal of Alzheimer s Disease · doi:10.1155/2013/823528 · Cited by 6
Targeting Amyloid with Tramiprosate in Patients with Mild-to-Moderate Alzheimer Disease
Aisen, P. S. S., Briand, R., Saumier, D., Laurin, J., Duong, A., & Garceau, D. (2007) · Progress in Neurotherapeutics and Neuropsychopharmacology · doi:10.1017/s1748232107000171 · Cited by 6
Cerebrospinal Fluid Analysis in Toxicological Neuropathology
Vernau, W., Vernau, K. M., & Bolon, B. N. (2011) · doi:10.1002/9780470939956.ch19 · Cited by 6
Nonpeptide BACE1 Inhibitors: Design and Synthesis
Cole, D. C., & Bursavich, M. G. (2010) · Methods and principles in medicinal chemistry · doi:10.1002/9783527630943.ch17 · Cited by 6
Gamma secretase activity modulates BMP-7-induced dendritic growth in primary rat sympathetic neurons
Karunungan, K. L., Garza, R. H., Grodzki, A. C., Holt, M., Lein, P. J., & Chandrasekaran, V. (2023) · Autonomic Neuroscience · doi:10.1016/j.autneu.2023.103085 · Cited by 5
Zheng, M., Wang, J., Lubinski, J. M., Flint, O. P., Krishna, R., Yao, M., Pursley, J. M., Thakur, A., Boulton, D., Santone, K. S., et al. (2009) · Xenobiotica · doi:10.1080/00498250902928555 · Cited by 5
Self-citationYu, P., Wang, H., Mu, L., Ding, X., & Ding, W. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3814 · Cited by 4
Synergistic inhibition of Aβ production by combinations of γ-secretase modulators
Robertson, A. S., Iben, L. G., Wei, C., Meredith, J. E., Drexler, D. M., Banks, M. N., Vite, G. D., Olson, R. E., Thompson, L. A., Albright, C. F., et al. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.07.019 · Cited by 4
Utilization of fluorinated α-amino acids in small molecule drug design
Richardson, P. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2577996 · Cited by 3
Computational Modeling of Gamma-Secretase Inhibitors as Anti-Alzheimer Agents
Manoharan, P., & Ghoshal, N. (2017) · Neuromethods · doi:10.1007/978-1-4939-7404-7_12 · Cited by 3
Secretase Processing of Amyloid Precursor Protein (APP) and Neurodegeneration
Marks, N., & Berg, M. J. (2007) · Springer eBooks · doi:10.1007/978-0-387-30379-6_16 · Cited by 2
Translational Research in Alzheimer’s Disease for Development of Antibody-Based Therapeutics
Yuen, E., Liu, E., & Kinney, G. G. (2012) · Springer eBooks · doi:10.1007/978-1-4419-5955-3_14 · Cited by 1
Stamford, A. W., Cumming, J. N., Scott, J. D., & Strickland, C. O. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12453-9 · Cited by 1
Physiologic and Neurotoxic Properties of Aβ Peptides
Gregory, G. C., Shepherd, C. E., & Halliday, G. M. (2006) · Springer eBooks · doi:10.1007/978-1-84628-440-3_11 · Cited by 1
Alzheimer Disease: Protein Misfolding, Model Systems, and Experimental Therapeutics
Price, D. L., Savonenko, A. V., Li, T., Lee, M. K., & Wong, P. C. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch12 · Cited by 1
Hamblett, C. L., Shah, S., Heidebrecht, R. W., & Muñoz, B. (2010) · Methods and principles in medicinal chemistry · doi:10.1002/9783527630943.ch13 · Cited by 1
The Role of Apolipoprotein E Concentration and Isoform in Amyloid-beta Metabolism In Vivo
Castellano, J. M. (2011) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7416v3s
Approaches to Amyloid Therapies for the Treatment of Alzheimer's Disease
Robichaud, A. J., Kim, J., & Jacobsen, J. S. (2010) · Wiley eBooks · doi:10.1002/0471266949.bmc249
Modulating Amyloid Beta Clearance by Altering Cellular and Whole Brain Apolipoprotein E Metabolism
Basak, J. M. (2014) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7dz06bk
Cerebrospinal fluid markers for the early and differential diagnosis of Alzheimer's disease
Schoonenboom, S. N. M. (2006) · Digital Academic REpository of VU University Amsterdam (Vrije Universiteit Amsterdam)
Pharmacodynamics and Pharmacokinetics of the -Secretase Inhibitor PF-3084014 □ S
Lanz, T. A., Wood, K. M., Richter, K. E. G., Nolan, C. E., Becker, S. L., Pozdnyakov, N., Martin, B., Du, P., Oborski, C., Wood, D. E., et al. (2010)
with oral administration of a BACE1 inhibitor in nonhuman primates
Sankaranarayanan, S., Holahan, M. A., Colussi, D. J., Crouthamel, M., Devanarayan, V., Ellis, J. D., Espeseth, A. S., Gates, A. T., Hazuda, D. J., Hochman, J. H., et al. (2008)
Inhibitor and regulator of presenilin for Alzheimer’s disease
Chen, T., Huang, X., Cui, L., & Zhang, Y. (2009) · Shengming kexue
Price, D. L., Savonenko, A. V., Li, T., & Wong, P. C. (2012) · Cambridge University Press eBooks · doi:10.1017/cbo9780511980053.009
Chio, S. N. (2010) · TSpace (University of Toronto)
Molecular Basis of Role of Insulin Resistance in Pathophysiology of Alzheimer’s Disease
Gupta, A. (2022) · International Journal of Health Sciences and Pharmacy · doi:10.47992/ijhsp.2581.6411.0094
BindingDB (2020) · UC San Diego · doi:10.7270/q2gb26td
BindingDB Entry 50003950: Nitrogen-appended N-alkylsulfonamides as inhibitors of gamma-secretase.
BindingDB (2020) · UC San Diego · doi:10.7270/q2k0772b
BindingDB (2020) · UC San Diego · doi:10.7270/q2708465
BindingDB (2020) · UC San Diego · doi:10.7270/q2xd14gf
BindingDB Entry 3175: Carbamate-appended N-alkylsulfonamides as inhibitors of gamma-secretase.
BindingDB (2009) · UC San Diego · doi:10.7270/q2z60md6
BindingDB Entry 3172: Discovery of a novel series of Notch-sparing gamma-secretase inhibitors.
BindingDB (2009) · UC San Diego · doi:10.7270/q26q1vjm
BindingDB Entry 50003931: Amino-caprolactam derivatives as gamma-secretase inhibitors.
BindingDB (2020) · UC San Diego · doi:10.7270/q2wd43b2
Metadata
- Authors
- Barten, D. M., Guss, V. L., Corsa, J. A., Loo, A., Hansel, S. B., Zheng, M., Munoz, B., Srinivasan, K., Wang, B., Robertson, B. J., Polson, C. T., Wang, J., Roberts, S. B., Hendrick, J. P., Anderson, J. J., Loy, J. K., Denton, R., Verdoorn, T. A., Smith, D. W., & Felsenstein, K. M.
- Affiliations
- Merck & Co., Inc., Rahway, NJ, USA (United States) (US)
- Venue
- The Journal of Pharmacology and Experimental Therapeutics
- Publisher
- Elsevier BV
- Published
- 2005-02
- Volume
- 312
- Issue
- 2
- Pages
- 635-643
- ISSN
- 0022-3565 (ISSN-L)
- OpenAlex
- W2167864502
- Cited by
- 159
- References
- 44
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 1 · 2018: 1 · 2017: 6 · 2016: 3 · 2015: 3 · 2014: 8 · 2013: 5 · 2012: 13
- FWCI
- 12.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Pharmacology and Experimental Therapeutics (publishedVersion)
- PubMed (publishedVersion)
- 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
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Keywords
- amyloid-beta, gamma-secretase inhibitors, Alzheimer's disease, APP transgenic mice, cerebrospinal fluid, amyloid plaques, Notch signaling, CD8+ thymocytes, intestinal goblet cells, amyloid precursor protein
- MeSH terms
- Aging, Animals, Brain Chemistry, Cell Separation, Dose-Response Relationship, Drug, Enzyme-Linked Immunosorbent Assay, Flow Cytometry, Humans, Membrane Proteins, Mice, Inbred C57BL, Mice, Transgenic, Endopeptidases, Protease Inhibitors, T-Lymphocytes, Blotting, Western, Amyloid beta-Peptides, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Immunoprecipitation, Mice, Receptors, Notch, 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
