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Alzheimer's Disease: From Pathology to Therapeutic Approaches
Abstract
Mind how you go: The current strategies for the development of therapies for Alzheimer's disease are very diverse. Particular attention is given to the search for inhibitors (see picture for two examples) of the proteolytic enzyme beta- and gamma-secretase, which inhibits the cleavage of the amyloid precursor proteins into amyloid beta peptides, from which the disease-defining deposits of plaque in the brains of Alzheimer's patients originates.Research on senile dementia and Alzheimer's disease covers an extremely broad range of scientific activities. At the recent international meeting of the Alzheimer's Association (ICAD 2008, Chicago) more than 2200 individual scientific contributions were presented. The aim of this Review is to give an overview of the field and to outline its main areas, starting from behavioral abnormalities and visible pathological findings and then focusing on the molecular details of the pathology. The "amyloid hypothesis" of Alzheimer's disease is given particular attention, since the majority of the ongoing therapeutic approaches are based on its theoretical framework.
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“However, use of non-specific chelators (i.e., CQ) that do not interact selectively with the Aβ–metal species exhibit adverse side effects that will likely limit their long term clinical use.3,28,29,31,44,46–48”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [3]
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“as well as lead to formation of reactive oxygen species (ROS) and oxidative stress.3,26–31,33–36”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [3]
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Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedNeuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
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
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B
Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Gauthier, S. G., Reisberg, ., Zaudig, M., Petersen, R. C., Ritchie, K. A., Broich, K., Belleville, S., Brodaty, H., Bennett, D. A., Chertkow, H. M., et al. (2006) · The Lancet · doi:10.1016/s0140-6736(06)68542-5 · Cited by 4,094
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
Research works printed but not linked: 11
- Stokin G. B., 2006, J. Physiol., 99, 193
- Younkin S. G., 1986, Fed. Proc., 45, 2982
- Cras P., 1990, Am. J. Pathol., 137, 241
- Yamaguchi H., 1992, Am. J. Pathol., 141, 249
- Tanzi R. E., 2004, Neuron, 43, 605
- Gandy S., 2005, J. Clin. Invest., 115, 1121
- Higgins G. A., 2003, Behav. Pharmacol., 14, 419
- 10.1124/jpet.105.100271 · DOI
- Pissarnitski D., 2007, Curr. Opin. Drug Discovery Dev., 10, 392
- Hills I. D., 2007, Curr. Opin. Drug Discovery Dev., 10, 383
- Durham T. B., 2006, Curr. Opin. Drug Discovery Dev., 9, 776
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Yang, A., Yi, X., Zhang, H., Shen, R., & Kou, X. (2024) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14529 · 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
Xu, C., Zou, H., Yu, X., Xie, Y., Cai, J., Shang, Q., Ouyang, N., Wang, Y., Xu, P., He, Z., et al. (2020) · ChemistryOpen · doi:10.1002/open.202000235 · Cited by 7
Hiremathad, A., Chaves, S., & Keri, R. S. (2021) · Chemistry & Biodiversity · doi:10.1002/cbdv.202000083 · Cited by 7
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Soares, J. Z., Valeur, J., Benth, J. Š., Knapskog, A., Selbæk, G., Bogdanović, N., & Pettersen, R. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220407 · Cited by 8
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Pan, X., Coban‐Akdemir, Z., Gao, R., Jiang, X., Sheynkman, G., Wu, E., Huang, J. H., Sahni, N., & Yi, S. S. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad030 · Cited by 6
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Xiaoyan, D., Du, W., & Liu, F. (2012) · Acta Physico-Chimica Sinica · doi:10.3866/pku.whxb201207162 · Cited by 6
Borioni, J. L., Cavallaro, V., Pierini, A. B., Murray, A. P., Peñéñory, A. B., Puiatti, M., & García, M. E. (2020) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-020-00324-y · Cited by 6
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Sylla, T., Pouységu, L., Costa, G. D., Deffieux, D., Monti, J., & Quideau, S. (2015) · Angewandte Chemie · doi:10.1002/ange.201411606 · Cited by 6
COB231 targets amyloid plaques in post‐mortem human brain tissue and in an Alzheimer mouse model
Garin, D., Virgone‐Carlotta, A., Gözel, B., Oukhatar, F., Perret, P., Batlle, D. M., Touret, M., Millet, P., Dubois‐Dauphin, M., Meyronet, D., et al. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12951 · Cited by 6
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Shabestari, M. H., Plug, T., Motazacker, M. M., Meeuwenoord, N. J., Filippov, D. V., Meijers, J. C. M., & Huber, M. (2013) · Applied Magnetic Resonance · doi:10.1007/s00723-013-0469-3 · Cited by 5
Chen, Z., Yu, X., Chen, L., Xu, L., Cai, Y., Hou, S., Zheng, M., & Liu, F. (2022) · Annals of Translational Medicine · doi:10.21037/atm-22-730 · Cited by 5
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Zhang, J.-A., Zhang, L., Zou, X.-Z., Liu, Y., Gao, W., & Li, Y. (2015) · Inorganic Chemistry Communications · doi:10.1016/j.inoche.2015.11.017 · Cited by 5
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Dhala, I., Khan, T. A., & Prabhu, A. (2020) · Exon Publications eBooks · doi:10.36255/exonpublications.alzheimersdisease.2020.ch10 · Cited by 5
Yuan, N., Ye, L., Sun, Y. P., Wu, H., Xiao, Z., Fu, W., Chen, Z., Pei, Y., Min, Y., & Wang, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087673 · Cited by 5
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Santis, S. D., Chiaraluce, R., Consalvi, V., Novelli, F., Petrosino, M., Punzi, P., Sciubba, F., Giordano, C., Masci, G., & Scipioni, A. (2016) · ChemPlusChem · doi:10.1002/cplu.201600550 · Cited by 5
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Henriksen, G., & Drzezga, A. E. (2010) · Springer eBooks · doi:10.1007/978-3-642-12945-2_33 · Cited by 5
Wu, C., Chen, S., Huang, W., Zhao, K., Fang, C., Liu, F., Zhang, Y., & Li, H. (2025) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2025.126200 · Cited by 4
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Nakazono, M., Obayashi, K., Oshikawa, Y., Tani, K., Suenaga, G., Ando, Y., Nanbu, S., & Kuwano, R. (2014) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2014.04.027 · Cited by 4
Chromosomal DNA damage in APOE ɛ4 carriers and noncarriers does not appear to be different
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Porter, M. R., & Zaleski, J. M. (2015) · Polyhedron · doi:10.1016/j.poly.2015.10.041 · Cited by 4
Liu, L., & Xia, N. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.074 · Cited by 4
RetractedBrain neurotrophic supply in ontogenesis and during development of neurodegenerative diseases
Rudnitskaya, E. A., Kolosova, N. G., & Stefanova, N. A. (2016) · Moscow University Biological Sciences Bulletin · doi:10.3103/s009639251604009x · Cited by 4
Kim, D., Bang, J. K., & Kim, S. H. (2014) · Angewandte Chemie · doi:10.1002/ange.201410389 · Cited by 4
Kim, D., Kim, N. H., & Kim, S. H. (2012) · Angewandte Chemie · doi:10.1002/ange.201208108 · Cited by 4
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Kumar, D. R. P., Reja, R. M., Senapati, D. K., Singh, M., Nalawade, S. A., George, G., Kaul, G., Akhir, A., Chopra, S., Raghothama, S., et al. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00414c · Cited by 4
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Konno, H., & Teruya, K. (2023) · Heterocycles · doi:10.3987/rev-22-999 · 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
Fayed, E. A., Najm, M. A. A., Oudah, K. H., Ebrahim, M. A., Gohar, N. A., Abu‐Elfotuh, K., Mohamed, E. K., Hamdan, A. M. E., Albalawi, N. A., Alzahrani, S. F., et al. (2026) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2598741 · Cited by 3
Ligand steric effects of nano-inhibitors on Aβ fibrillation at the nano-bio interfaces
Zhang, B., Gao, G., Zhang, Z., Cao, B., & Sun, T. (2023) · Applied Surface Science · doi:10.1016/j.apsusc.2023.158427 · Cited by 3
Ghamsary, M. S., Ghiasi, M., & Naghavi, S. S. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp05687b · Cited by 3
Apply the Feature of Entropy Convergence of ACO to Short the Runtime of Gene Order
Hu, B.-Q., Wang, S., Jiang, G., & Pang, C.-Y. (2010) · International Conference on Genetic and Evolutionary Computing · doi:10.1109/icgec.2010.77 · Cited by 3
Protein interaction in the mechanism of platinum anticancer drugs
Zhao, L., Fang, T., Liu, Y., Cao, K., & Cheng, L. (2017) · Scientia Sinica Chimica · doi:10.1360/n032016-00167 · Cited by 3
Wang, D., Wang, G., Wang, X., Ren, Z., & Jia, C. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00075 · Cited by 3
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Sandgren, V., Belda, O., Kvarnström, I., Lindberg, J., Samuelsson, B., & Dahlgren, A. (2015) · The Open Medicinal Chemistry Journal · doi:10.2174/1874104501509010013 · Cited by 3
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Sandhya, A., & Gomathi, K. (2018) · Asian Journal of Pharmaceutical and Clinical Research · doi:10.22159/ajpcr.2018.v11i7.25104 · Cited by 3
Ahmadi, A., Roghani, M., Noori, S. K., & Nahri-Niknafs, B. (2018) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557518666180716122608 · Cited by 3
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Dhavale, D. D. (2009) · Louisiana State University · doi:10.31390/gradschool_theses.3810 · Cited by 3
Desai, A., Shah, P., & Jain, S. (2025) · Polymer Bulletin · doi:10.1007/s00289-025-05881-6 · Cited by 2
Tarasov, A. S., Зуфарович, Р. И., Blokhin, D. S., Klochkov, A. V., Il'yasov, K. A., & Klochkov, V. V. (2023) · Results in Chemistry · doi:10.1016/j.rechem.2023.100762 · Cited by 2
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Dewangan, B., Kumar, K., Kumar, A., Bodhe, P. R., Beni, S., & Sahu, B. (2023) · Springer eBooks · doi:10.1007/978-981-99-6038-5_13 · Cited by 2
Chen, Y., Huang, X., Chen, H., & Yi, C. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e33077 · Cited by 2
Kwon, Y. R., Kim, J.-H., Lee, S., Kim, H. Y., & Cho, E. J. (2022) · Nutrition Research and Practice · doi:10.4162/nrp.2022.16.2.173 · Cited by 2
Arce, F. T., Jang, H., Connelly, L. S., Ramachandran, S., Kagan, B. L., Nussinov, R., & Lal, R. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00036-5 · Cited by 3
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Wang, J.-S., Yu, Z., Yu, Q., Kong, Q., Zhang, N., He, L., & Yi, Y. (2014) · Journal of Food and Nutrition Research · doi:10.12691/jfnr-2-12-4 · Cited by 2
López, N. (2009) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t3m61kdj · Cited by 2
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Stillman, N. H., Dohoney, R. A., Baysah, C. Z., & Kumar, S. (2025) · Wiley eBooks · doi:10.1002/9783527845828.ch8 · Cited by 2
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Kumar, A., Lakhawat, S. S., Malik, N. K., Sharma, V., Singh, Y., Jain, A., Sharma, V., Singh, S. K., & Sharma, P. K. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110500 · Cited by 1
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Talele, C., Aundhia, C. J., Talele, D. R., Shah, N., Kumari, M., & Sadhu, P. (2025) · Micro and Nanosystems · doi:10.2174/0118764029366173250706232958 · Cited by 1
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Ali, N., Alotaibi, F. T., Babu, M. A., Singh, T., Tyagi, Y., Alotaibi, A. N., Bansal, N., & Puri, S. (2026) · Archiv der Pharmazie · doi:10.1002/ardp.70220 · Cited by 1
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Gillman, A. L., Lee, J., Ramachandran, S., Capone, R. F., Gonzalez, T., Wrasidlo, W., Masliah, E., & Lal, R. (2016) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2016.06.001 · Cited by 1
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Sun, Y., Sun, J. W., Feng, Y., Zhang, Y., Li, J., Wang, F., Loznik, M., Tian, Y., Zhang, H., Herrmann, A. P., et al. (2024) · Fundamental Research · doi:10.1016/j.fmre.2024.03.017 · Cited by 1
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Mishra, S., Senthilkumar, D., & Yadav, V. K. (2024) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815256505124010010 · Cited by 1
Structure-Based Ligand Design I
Sun, H. (2015) · Elsevier eBooks · doi:10.1016/b978-0-08-100098-4.00002-8 · Cited by 1
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Fatima, A., Alam, A., & Singh, R. (2018) · Springer eBooks · doi:10.1007/978-981-13-1123-9_15 · Cited by 1
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Dhavale, D. D. (2012) · Louisiana State University · doi:10.31390/gradschool_dissertations.2446 · Cited by 1
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Vilaprinyó-Pascual, S. (2015) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)
Schieb, H. (2011) · DuEPublico (University of Duisburg-Essen)
Marques, E. L. (2014) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2014.tde-24102014-104455
Vidal, B. (2014) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Murtishaw, A. S. (2020) · Digital Scholarship - UNLV (University of Nevada Reno) · doi:10.34917/6456429
León, N., & Medicina, F. D. (2014)
Aβ Fibril Polymorphism and Alzheimer’s Disease
Bereza, M., & Fändrich, M. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00017-1
Stability and folding of G-protein coupled receptors associated to degenerative diseases
Dong, X. (2016) · UPCommons institutional repository (Universitat Politècnica de Catalunya) · doi:10.5821/dissertation-2117-96351
ChemInform Abstract: Alzheimer′s Disease: From Pathology to Therapeutic Approaches
Jakob‐Roetne, R., & Jacobsen, H. (2009) · ChemInform · doi:10.1002/chin.200925262
Self-citationEngineering Sciences (Mechanical Engineering)
Conroy, D. T., Kastner, M., Lasheras, J. C., Reeburgh, W. S., Rottman, J. W., & Tartakovsky, D. M. (2008)
GM1 mediates the formation and maintenance of cytotoxic Aβ oligomersPreprint
Zhang, D. Y., Wang, J., Fleeman, R. M., Kuhn, M. K., Swulius, M. T., Proctor, E. A., & Dokholyan, N. V. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.22.453392
Tùng, T. T., Quang, T. V., Phuong, P. V. N., Hoang, D. V., & Hien, D. T. T. (2021) · Tạp chí Nghiên cứu Y học · doi:10.52852/tcncyh.v148i12.772
Yang, J., Yin, W. H., Van, R. S., Yin, K., Wang, P., Zheng, C., Zhu, B., Ran, K. R., Zhang, C. M., Shao, Y., et al. (2020) · ChemRxiv · doi:10.26434/chemrxiv.12142578
Kitaoka, Y. (2014) · Springer eBooks · doi:10.1007/978-4-431-54965-9_9
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Mellacheruvu, A., Bondoc, M., & Torraca, E. (2022) · Journal of Student Research · doi:10.47611/jsrhs.v11i3.3301
Lifestyle modifications and nutrition in Alzheimer's disease
Bhatti, G. K., Mishra, J., Sehrawat, A., Sharma, E., Kanozia, R., Navik, U., Reddy, P. H., & Bhatti, J. S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-89834-8.00049-0
Na, C., Kim, G., Bal, W., Nam, E., & Lim, M. H. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-061jk
Role of Enzymes in Alzheimer’s Disease
Patel, S., Shrivastava, S., Marar, P. V., Swami, R., & Jeengar, M. K. (2024) · Springer eBooks · doi:10.1007/978-981-97-6822-6_2
Saporito-Magriñá, C., Lopez-Montañana, L., Facio, M. L., Pagano, G., Topp, N., Danzi, A., Bellida, J. I., Silva, A., Albizzati, M., & Repetto, M. G. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112905
Dementia Seen from The Lens of An Educational Therapist
Wong, C. L. (2024) · The Asian Educational Therapist · doi:10.64663/aet.34
Ryu, W., Lee, D., Hong, S., Kim, J., Lee, J., Bang, J. K., Jung, Y., Kim, H.-J., & Kim, S. H. (2025) · Inorganic Chemistry Frontiers · doi:10.1039/d5qi02016f
Cantador, C. G. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Substitution of disulphide bonds to hydrophobic amino acids in BACE1
Halvarsson, C. (2009) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Metadata
- Authors
- Jakob‐Roetne, R., & Jacobsen, H.
- Affiliations
- F. Hoffmann-La Roche AG (CH)
- Corresponding author
- Jakob‐Roetne, Roland
- Jacobsen, Helmut
- ORCID
- Jacobsen, Helmut
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2009-04-07
- Volume
- 48
- Issue
- 17
- Pages
- 3030-3059
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2065100984
- Cited by
- 626
- References
- 314
- Citations by year
- 2026: 21 · 2025: 19 · 2024: 27 · 2023: 26 · 2022: 39 · 2021: 27 · 2020: 38 · 2019: 37 · 2018: 39 · 2017: 49 · 2016: 40 · 2015: 52 · 2014: 45 · 2013: 45 · 2012: 43
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Angewandte Chemie International Edition (publishedVersion)
- PubMed (publishedVersion)
- 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
- Alzheimer's disease, amyloid hypothesis, beta-secretase inhibitors, gamma-secretase inhibitors, amyloid precursor protein, amyloid-beta, amyloid plaques, behavioral abnormalities, Alzheimer's disease pathology, Alzheimer's disease therapeutics
- MeSH terms
- Alzheimer Disease, Amyloid, Humans, Protease Inhibitors, Amyloid Precursor Protein Secretases, Drug Discovery
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