The DOI matches its Crossref record; 53 of the 54 references it cites were found in a registry or an index.
Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity
Open accessAbstract
The accumulation of metal ions and amyloid-β (Aβ) aggregates found in the brain of patients with Alzheimer's disease (AD) has been suggested to be involved in AD pathogenesis. To investigate metal-Aβ-associated pathways in AD, development of chemical tools to target metal-Aβ species is desired. Only a few efforts, however, have been reported. Here, we report bifunctional small molecules, N-(pyridin-2-ylmethyl)aniline (L2-a) and N(1),N(1)-dimethyl-N(4)-(pyridin-2-ylmethyl)benzene-1,4-diamine (L2-b) that can interact with both metal ions and Aβ species, as determined by spectroscopic methods including high-resolution NMR spectroscopy. Using the bifunctional compound L2-b, metal-induced Aβ aggregation and neurotoxicity were modulated in vitro as well as in human neuroblastoma cells. Furthermore, treatment of human AD brain tissue homogenates containing metal ions and Aβ species with L2-b showed disassembly of Aβ aggregates. Therefore, our studies presented herein demonstrate the value of bifunctional compounds as chemical tools for investigating metal-Aβ-associated events and their mechanisms in the development and pathogenesis of AD and as potential therapeutics.
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
“In this context, two approaches have been pursued in BFC design. 31,49–58 One strategy is based on the direct incorporation of metal-binding atom donors into the structural framework of an Aβ-interacting compoud (Scheme 1, approach A), and the other involves linking the metal-chelating and Aβ-binding molecular fragments (Scheme 1, approach B).”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [52]
In the citing paper
“Based on previously reported acidity constants for phenols, amines,76 and pyridines,52 we assigned the two lower pKa values to the deprotonation of the two pyridinium groups, and the third pKa value to the ammonium group. The highest pKa value is likely due to phenol deprotonation in L1.”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [52]
In the citing paper
“By comparison, the clinically tested compound CQ shows <30% cell survival at concentrations >2 μM, while EDTA shows 90–95% cell survival up to 20 μM concentration (Figure S26).51,52”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [52]
In the citing paper
“Thus, the use of both these methods provides a more complete picture of the extent and pathways of Aβ aggregation under various conditions.51,52”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [52]
In the citing paper
“Except for one recent report,99 compounds that inhibit metal-mediated Aβ40 aggregation or promote disaggregation of amyloid fibrils were shown to lead to increased cell viability.49,51,52”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [52]
In the citing paper
“However, the majority of these BFCs have been studied for their effect on aggregation of the Aβ40 peptide,25,31 and fewer studies have focused on their interaction with the more neurotoxic Aβ42 peptide.20,21”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [25]
In the citing paper
“Compounds that inhibit metal-mediated Aβ40 aggregation or promote disaggregation of amyloid fibrils were shown to lead to increased cell viability.25,31,32”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [25]
In the citing paper
“metal chelators have been shown to reduce metal-mediated Aβ aggregation, ROS formation, and neurotoxicity in vitro.23−26”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [25]
In the citing paper
“The first and second pKa values can be assigned to deprotonation of the nitrogen atoms of the benzothiazole and diethylamino groups, while the largest pKa value is likely due to phenol deprotonation.25,42”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [25]
In the citing paper
“Recent efforts to control abnormal Aβ–metal interactions have focused on small molecules, bifunctional chelators (BFCs), that have binding affinity for both metal ions and Aβ aggregates.20,25,27−30”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [25]
In the citing paper
“the clinically tested compound CQ was quite toxic to cells even at 2 μM concentration, while EDTA does not show any toxicity up to 20 μM.25,31”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [25]
Citations
Cites
AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., & Olson, A. J. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21256 · Cited by 26,294
Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (2001) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(00)00129-0 · Cited by 18,139
Martell, A. E., & Smith, R. M. (1982) · Springer eBooks · doi:10.1007/978-1-4615-6761-5 · Cited by 6,025
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Baes, C. F., & Mesmer, R. E. (1976) · Medical Entomology and Zoology · Cited by 4,657
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Smith, R. M., & Martell, A. E. (1975) · Springer eBooks · doi:10.1007/978-1-4613-4452-0 · Cited by 2,281
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
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
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365
Cited by
Sorted by citations
Items 201–279 of 279
Miotto, M., Pavese, M. D., Quintanar, L., Zweckstetter, M., Griesinger, C., & Fernández, C. O. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b01292 · Cited by 14
Branch, T., Girvan, P., Barahona, M., & Ying, L. (2014) · Angewandte Chemie · doi:10.1002/ange.201408810 · Cited by 14
Cary, B. P., Brooks, A. F., Fawaz, M. V., Shao, X., Desmond, T. J., Carpenter, G. M., Sherman, P. S., Quesada, C., Albin, R. L., & Scott, P. J. H. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml500413d · Cited by 14
A label-free fluorescent probe for dynamic in situ visualization of amyloid-β peptides aggregation
Ding, C., Li, C., Meng, Q. Y., Qian, C., Zhang, C., Liu, Y., Wang, X., & Wang, Y. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.130607 · Cited by 13
A Unified View of Assessing the Pro‐oxidant versus Antioxidant Nature of Amyloid Beta Conformers
Mitra, S., Prasad, P., & Chakraborty, S. (2018) · ChemBioChem · doi:10.1002/cbic.201800446 · Cited by 13
Baul, T. S. B., Kundu, S., Singh, P., Shaveta, S., & da Silva, M. F. C. G. (2014) · Dalton Transactions · doi:10.1039/c4dt03151b · Cited by 13
Copper stabilizes antiparallel β-sheet fibrils of the amyloid β40 (Aβ40)-Iowa variant
Crooks, E. J., Irizarry, B. A., Ziliox, M., Kawakami, T., Victor, T. W., Xu, F., Hojo, H., Chiu, K., Simmerling, C. L., Nostrand, W. E. V., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011955 · Cited by 12
Zhang, Q., Liu, J., Hu, X., Wang, W., & Yuan, Z. (2015) · ACS Macro Letters · doi:10.1021/acsmacrolett.5b00033 · Cited by 12
Xu, L., Gao, K., Bao, C., & Wang, X. (2012) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-012-9588-4 · Cited by 11
Sarkar, D., & Bhunia, A. (2023) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.3c00055 · Cited by 11
Zhou, B., Sheng, X., Xie, H., Zhou, S., Zhong, M., & Liu, A. (2022) · Chemistry & Biodiversity · doi:10.1002/cbdv.202200342 · Cited by 11
Wang, L., Li, Y., Lu, T., & Li, F. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.09.002 · Cited by 11
Hong, S., Go, Y. K., Derrick, J. S., Han, S., Kim, J., Lim, M. H., & Kim, S. H. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b01824 · Cited by 10
Self-citationLiu, C., Wu, J., Hu, C., Yang, A., Shen, R., & Kou, X. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.112086 · Cited by 10
Jureschi, M., Lupăescu, A.-V., Ion, L., Petre, B. A., & Drochioiu, G. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-15950-4_23 · Cited by 10
Peng, Q., Shi, X., Yan, X., Ji, L., Hu, Y., Shi, G., & Yu, Y. (2020) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.0c13759 · Cited by 10
Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein
Uber, D., Wyrzykowski, D., Tiberi, C., Sabatino, G., Żmudzińska, W., Chmurzyński, L., Papini, A. M., & Makowska, J. (2016) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-016-5387-9 · Cited by 9
Osman, W., Mohamed, T., Sit, V. M.-S., Vasefi, M., Beazely, M. A., & Rao, P. P. N. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12800 · Cited by 9
Guo, L., & Sun, B. (2020) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b20-00574 · Cited by 9
Multifunctional metallochaperone modifications for targeting subsite cavities in mutant p53-Y220C
Miller, J. J., Kwan, K., Blanchet, A., Orvain, C., Mellitzer, G., Smith, J. R., Lento, C., Nouchikian, L., Omoregbee‐Leichnitz, S., Sabatou, M., et al. (2023) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2023.112164 · Cited by 9
Rana, M., Terpstra, K., GUTIERREZ, C. G., Xu, K., Arya, H., Bhatt, T. K., Mirica, L. M., & Sharma, A. K. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202402748 · Cited by 8
Kumar, R., Pavlov, P. F., & Winblad, B. G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190695 · Cited by 8
Ligand Design to Target and Modulate Metal–Protein Interactions in Neurodegenerative Diseases
Beck, M. W., Pithadia, A. S., DeToma, A. S., Korshavn, K. J., & Lim, M. H. (2014) · Wiley eBooks · doi:10.1002/9781118697191.ch10 · Cited by 8
Self-citationZhao, J., Lai, S., Ruan, L.-L., Cheng, J., Tan, C., & Zhu, G. (2013) · Pest Management Science · doi:10.1002/ps.3536 · Cited by 7
Wang, L., Zhang, Y., Yu, X., He, H., & Zhang, J. (2012) · Synthetic Metals · doi:10.1016/j.synthmet.2012.09.012 · Cited by 7
Meena, P., Manral, A., Nemaysh, V., Saini, V., Siraj, F., Luthra, P. M., & Tiwari, M. (2016) · RSC Advances · doi:10.1039/c6ra24017h · Cited by 7
Klenner, M. A., Fraser, B. H., Moon, V., Evans, B. J., Massi, M., & Pascali, G. (2020) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202000433 · Cited by 8
Impact of Cu( ii ) and Al( iii ) on the conformational landscape of amyloidβ 1-42
Roldán-Martín, L., Peccati, F., Sciortino, G., Sodupe, M., & Maréchal, J. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp01561c · Cited by 7
Toxic mechanisms of amyloid oligomers and therapeutic strategies
Ivanova, M. I., Rosa, C. L., & Ramamoorthy, A. (2026) · Protein Science · doi:10.1002/pro.70519 · Cited by 6
Self-citationClinical Biomarkers and Novel Drug Targets to Cut Gordian Knots of Alzheimer's Disease
Mir, R. H., Masoodi, M. H., Shah, A. J., Mohi-ud-din, R., Sabreen, S., Wani, T. U., Jan, R., Javed, M. N., & Mir, P. A. (2022) · Current Molecular Pharmacology · doi:10.2174/1874467215666220903095837 · Cited by 6
Warerkar, O. D., Mudliar, N. H., Momin, M. M., & Singh, P. K. (2023) · Critical Reviews in Therapeutic Drug Carrier Systems · doi:10.1615/critrevtherdrugcarriersyst.2023046209 · Cited by 7
The Therapeutic Potential of Melatonin in Alzheimer's Disease: A Comprehensive Review
Zhang, J., Feng, M., & Kong, L. (2024) · Current Medicinal Chemistry · doi:10.2174/0109298673286807240326085736 · Cited by 6
Ghosh, P., Mukhopadhyay, S., Singh, M., Ghosh, S. S., & Iyer, P. K. (2025) · Small · doi:10.1002/smll.202506572 · Cited by 5
Dong, X., Zhang, Z., Zhao, D. Y., Liu, Y., Meng, Y., Zhang, Y., Zhang, D., & Liu, C. (2015) · Scientific Reports · doi:10.1038/srep13897 · Cited by 5
Drug repurposing: small molecules against Cu(II)–amyloid-β and free radicals
Nam, G., Suh, J., Yi, Y., & Lim, M. H. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111592 · Cited by 5
Self-citationWang, Y., Wang, X., Xu, K., Chen, Z., Pan, B., Peng, L., Zhou, Y., & Liu, X. (2023) · Organic Chemistry Frontiers · doi:10.1039/d3qo01144e · Cited by 5
Kwan, K., Castro-Sandoval, O., Ma, B. N., Martelino, D., Saffari, A., Liu, X. L., Orvain, C., Mellitzer, G., Gaiddon, C., & Storr, T. (2023) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2023.112433 · Cited by 5
Synthesis and Evaluation of New Cyclodextrin Derivatives as Amyloid‐β Aggregation Inhibitors
Oliveri, V., & Vecchio, G. (2019) · ChemistrySelect · doi:10.1002/slct.201902402 · Cited by 5
Lefèvre, M., Lantigner, L., Andolfo, L., Vanucci‐Bacqué, C., Benoist, É., Esmieu, C., Bedos‐Belval, F., & Hureau, C. (2023) · Comptes Rendus Chimie · doi:10.5802/crchim.255 · Cited by 4
Metabolism of copper and possibilities for its regulation
Palumaa, P. (2023) · Proceedings of the Estonian Academy of Sciences · doi:10.3176/proc.2023.4.03 · Cited by 4
Nakano, H., Hikishima, S., Mori, M., Minamikawa, J., Muramatsu, D., Sakashita, Y., Ikeda, T., Noguchi‐Shinohara, M., Teplow, D. B., & Ono, K. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106775 · Cited by 4
Ahn, S. H., & Lee, H. (2015) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.10616 · Cited by 4
Lung nodules after whole lung radiation.
Cohen, M. D., Mirkin, D. L., Provisor, A. J., Hornback, N. B., Smith, J. A., & Slabaugh, R. D. (1983) · PubMed · Cited by 4
Metal Ions and Complexes in A lzheimer's Disease: From Fundamental to Therapeutic Perspectives
Hureau, C. (2018) · Wiley eBooks · doi:10.1002/9781119951438.eibc2635 · Cited by 4
Advancing Antiamyloidogenic Activity by Fine-Tuning Macromolecular Topology
Firdaus, S., Boye, S., Janke, A., Friedel, P., Janaszewska, A., Appelhans, D., Müller, M., Klajnert‐Maculewicz, B., Voit, B. I., & Lederer, A. (2023) · Biomacromolecules · doi:10.1021/acs.biomac.3c00817 · Cited by 3
Alzheimer Hastalığı Tedavisindeki Güncel Yaklaşımlar
ODABAŞI, M. D., & KÜÇÜKKILINÇ, Z. T. T. (2021) · Hacettepe University Journal of the Faculty of Pharmacy · doi:10.52794/hujpharm.955421 · Cited by 6
A Comparative Study on the Self-Assembly of Peptide TGV-9 by In Situ Atomic Force Microscopy
Li, Y., Li, N., Wang, L., Lu, Q., Ji, X., & Zhang, F. (2020) · Microscopy and Microanalysis · doi:10.1017/s1431927620000082 · Cited by 3
Zhang, G., Huo, Z., Zhou, Y., Zhu, X., Wang, H., Liang, Y. L., & Xu, M. (2012) · International Journal of Electrochemical Science · doi:10.1016/s1452-3981(23)16255-9 · Cited by 3
The Design of Metal Complexes to Target the Amyloid‐β Peptide in Alzheimer's Disease
Webb, M. I. (2023) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2846 · Cited by 3
Bhatt, S., Malpani, P., Pati, S. S., Kumar, N., Bhuvanesh, N. S. P., Joshi, H., & Sharma, A. K. (2024) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202400623 · Cited by 2
Sarangi, N. K., Mondal, S., & Keyes, T. E. (2025) · Biophysical Chemistry · doi:10.1016/j.bpc.2025.107441 · Cited by 2
Molecular Imaging of In Vivo Zinc Distribution Using Nuclear and Magnetic Resonance Imaging
Mu, C., Liu, X., Ali, U., Larson, P. E. Z., Ho, S. P., & Flavell, R. R. (2026) · Chemical & Biomedical Imaging · doi:10.1021/cbmi.5c00264 · Cited by 2
Li, X., Dong, X., Liu, Y., Meng, Y., Zhang, Y., Zhang, D., & Liu, C. (2016) · New Journal of Chemistry · doi:10.1039/c6nj02004f · Cited by 2
Pyridine derivatives as anti-Alzheimer agents
Veer, B., & Singh, R. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91221-1.00017-8 · Cited by 2
Ghosh, P., Mukhopadhyay, S., Sarkar, A., Ghosh, S. S., & Iyer, P. K. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.71341 · Cited by 1
Brain PET Poster Sessions PP01-M01 to PP02-N07
Lange, D., Tejada, I. M., xiong, M., Hillebrand, B., Noergaard, M., Baerentzen, S., Shalgunov, V., Herth, M. M., Svarer, C., & Palner, M. (2019) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x19851018 · Cited by 1
Liu, C., Wu, J., Hu, C., Yang, A., Shen, R., & Kou, X. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4199898
Keyes, T. E., Sarangi, N. K., & Mondal, S. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5123588
C3N Nanosheets Inhibit Aβ Dimerization in a Size-Dependent Manner
Man, J., Chen, J., & Gu, Z. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c05718
Alzheimer Hastalığı Tedavisindeki Güncel Yaklaşımlar
ODABAŞI, M. D., & KÜÇÜKKILINÇ, Z. T. T. (2021) · DergiPark (Istanbul University)
Molecular insights into suppression of amyloid-β dimerization by all-metal fullerenes
Zeng, R., Gu, Z., & Liu, X. (2026) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2026.140383
Lelong, E. (2021) · theses.fr (ABES) · doi:10.70675/7cda5a3ez022cz475az9b2bz977814a60663
Milardi, D., Han, J., Lee, H. J., Ding, F., Miller, Y., Faller, P., Bush, A. I., Crouch, P. J., Finkelstein, D. I., Double, K. L., et al. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00420
Self-citationBindingDB (2022) · UC San Diego · doi:10.7270/q21j9fgh
Metadata
- Authors
- Choi, J.-S., Braymer, J. J., Nanga, R. P. R., Ramamoorthy, A., & Lim, M. H.
- Affiliations
- University of Michigan (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-12-03
- Volume
- 107
- Issue
- 51
- Pages
- 21990-21995
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3009803
- OpenAlex
- W2080100823
- Cited by
- 264
- References
- 54
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 7 · 2023: 16 · 2022: 7 · 2021: 10 · 2020: 15 · 2019: 16 · 2018: 21 · 2017: 28 · 2016: 28 · 2015: 22 · 2014: 25 · 2013: 21 · 2012: 23
- FWCI
- 13.22
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
- Funders
- National Institute on Aging (P50AG008671, P50 AG08671)
- National Institute of Diabetes and Digestive and Kidney Diseases (R21DK078885, DK078885)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta, metal ions, Alzheimer's disease, bifunctional small molecules, neurotoxicity, chemical probes, pyridine derivatives, neuroblastoma cells
- MeSH terms
- Alzheimer Disease, Copper, Humans, Phenylenediamines, Pyridines, Zinc, Amyloid beta-Peptides, Cell Line, Tumor
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