The DOI matches its Crossref record; 248 of the 250 references it cites were found in a registry or an index.
Disease modifying therapy for AD?1
Open accessAbstract
Alzheimer's disease (AD) is the most common form of dementia in industrialized nations. If more effective therapies are not developed that either prevent AD or block progression of the disease in its very early stages, the economic and societal cost of caring for AD patients will be devastating. Only two types of drugs are currently approved for the treatment of AD: inhibitors of acetyl cholinesterase, which symptomatically enhance cognitive state to some degree but are not disease modifying; and the adamantane derivative, memantine. Memantine preferentially blocks excessive NMDA receptor activity without disrupting normal receptor activity and is thought to be a neuroprotective agent that blocks excitotoxicty. Memantine therefore may have a potentially disease modifying effect in multiple neurodegenerative conditions. An improved understanding of the pathogeneses of AD has now led to the identification of numerous therapeutic targets designed to alter amyloid beta protein (Abeta) or tau accumulation. Therapies that alter Abeta and tau through these various targets are likely to have significant disease modifying effects. Many of these targets have been validated in proof of concept studies in preclinical animal models, and some potentially disease modifying therapies targeting Abeta or tau are being tested in the clinic. This review will highlight both the promise of and the obstacles to developing such disease modifying AD therapies.
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“AD disease-modifying strategies are designed to target abnormal Aβ aggregates, clear, and delay or prevent the formation of aggregates [33].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [33]
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Items 201–248 of 248
Choi, D., Wang, D., Yu, G.-Q., Zhu, G., Kharazia, V., Paredes, J. P., Chang, W. S., Deitchman, J. K., Mucke, L., & Messing, R. O. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509725103 · Cited by 119
Modeling Tau Polymerization in Vitro: A Review and Synthesis
Gamblin, T. C., Berry, R. W., & Binder, L. I. (2003) · Biochemistry · doi:10.1021/bi035722s · Cited by 114
Tissue Plasminogen Activator Requires Plasminogen to Modulate Amyloid‐β Neurotoxicity and Deposition
Tucker, H. M., Kihiko‐Ehmann, M., Wright, S., Rydel, R. E., & Estus, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752172.x · Cited by 113
Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models
Levites, Y., Smithson, L. A., Price, R. W., Dakin, R. S., Yuan, B., Sierks, M. R., Kim, J., McGowan, E., Kim Reed, D., Rosenberry, T. L., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-6463fje · Cited by 113
Self-citationChackerian, B., Rangel, M., Hunter, Z. N., & Peabody, D. S. (2006) · Vaccine · doi:10.1016/j.vaccine.2006.05.059 · Cited by 110
Stabilization of the Tau Exon 10 Stem Loop Alters Pre-mRNA Splicing
Donahue, C. P., Muratore, C., Wu, J. Y., Kosik, K. S., & Wolfe, M. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600143200 · Cited by 110
Neurovascular Pathways and Alzheimer Amyloid β-peptide
Zlokovic, B. V., Deane, R., Sallstrom, J., Chow, N., & Miano, J. M. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00103.x · Cited by 104
Takaki, Y., Iwata, N., Tsubuki, S., Taniguchi, S., Toyoshima, S., Lu, B., Gerard, N. P., Gerard, C. J., Lee, H., Shirotani, K., et al. (2000) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022839 · Cited by 101
Fraering, P. C., Ye, W., LaVoie, M. J., Ostaszewski, B. L., Selkoe, D. J., & Wolfe, M. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501368200 · Cited by 100
Golde, T. E. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00104.x · Cited by 99
Self-citationMolecular Genetics of Chromosome 17 Tauopathies
HUTTON, M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06906.x · Cited by 92
Wilcock, D. M., Gordon, M. N., Ugen, K. E., Gottschall, P. E., DiCarlo, G., Dickey, C. A., Boyett, K. W., Jantzen, P. T., Connor, K. E., Melachrino, J., et al. (2001) · DNA and Cell Biology · doi:10.1089/10445490152717596 · Cited by 87
Potter, H. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00308-6 · Cited by 87
Rockenstein, E. M., Adame, A., Mante, M., Moessler, H., Windisch, M., & Masliah, E. (2003) · Journal of Neural Transmission · doi:10.1007/s00702-003-0025-7 · Cited by 83
In Vivo Reversal of Amyloid-β Lesions in Rat Brain
Sigurdsson, E. M., Permanne, B., Soto, C. A., Wısnıewskı, T., & Frangione, B. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.1.11 · Cited by 83
Splicing of juvenile and adult tau mRNA variants is regulated by thyroid hormone.
Aniello, F., Couchie, D., Bridoux, A.-M., Gripois, D., & Nunez, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.4035 · Cited by 82
Inhibition of amyloid precursor protein processing by β-secretase through site-directed antibodies
Arbel, M., Yacoby, I., & Solomon, B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502427102 · Cited by 76
α‐Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure
Fahrenholz, F., GILBERT, S., Kojro, E., Lammich, S., & Postina, R. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06925.x · Cited by 75
Alternate Aggregation Pathways of the Alzheimer β-Amyloid Peptide
Huang, T. H. J., Yang, D., Fraser, P. E., & Chakrabartty, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005698200 · Cited by 74
From Acetylcholine to Amyloid: Neurotransmitters and the Pathology of Alzheimer's Disease
Nitsch, R. M. (1996) · Neurodegeneration · doi:10.1006/neur.1996.0066 · Cited by 71
Sparks, D. L., Sabbagh, M., Connor, D. J., Lopez, J., Launer, L. J., Petanceska, S. S., Browne, P. J., Wassar, D., Johnson‐Traver, S., & Lochhead, J. J. (2005) · Current Alzheimer Research · doi:10.2174/1567205054367900 · Cited by 71
Inhibitors of TACE and Caspase-1 As Anti-inflammatory Drugs
Le, G. T., & Abbenante, G. (2005) · Current Medicinal Chemistry · doi:10.2174/092986705774462851 · Cited by 66
Ertekin‐Taner, N., Ronald, J., Feuk, L., Prince, J. A., Tucker, M., Younkin, L. H., Hella, M., Jain, S., Hackett, A. M., Scanlin, L., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi041 · Cited by 66
Newman, J., Rissman, R. A., Sarsoza, F. M., Kim, R. C., Dick, M. B., Bennett, D. A., Cotman, C. W., Rohn, T. T., & Head, E. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1027-3 · Cited by 55
Immunological and Anti-Chaperone Therapeutic Approaches for Alzheimer Disease
Wısnıewskı, T., & Frangione, B. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00102.x · Cited by 54
The molecular genetics of the tauopathies
vanSlegtenhorst, M., LEWIS, J., & Hutton, M. L. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00114-5 · Cited by 51
Translational Research on the Way to Effective Therapy for Alzheimer Disease
Rosenberg, R. N. (2005) · Archives of General Psychiatry · doi:10.1001/archpsyc.62.11.1186 · Cited by 51
Amyloid Inhibitors and β-Sheet Breakers
Soto, C. A., & Estrada, L. D. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_18 · Cited by 47
Feyt, C., Kienlen‐Campard, P., Leroy, K., N’Kuli, F., Courtoy, P. J., Brion, J., & Octave, J. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501610200 · Cited by 46
Cuadrado, A., García‐Fernández, L., Imai, T., Okano, H., & Múñoz, A. (2002) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2002.1131 · Cited by 43
Maier, M., Seabrook, T. J., & Lemere, C. A. (2005) · Vaccine · doi:10.1016/j.vaccine.2005.06.018 · Cited by 42
Anti‐amyloid activity of neprilysin in plaque‐bearing mouse models of Alzheimer's disease
Mohajeri, M. H., Kuehnle, K., Li, H., Poirier, R., Tracy, J., & Nitsch, R. M. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00169-3 · Cited by 42
Roßner, S., Beck, M., Stahl, T., Mendla, K. D., Schliebs, R., & Bigl, V. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00211.x · Cited by 41
Plasmin deficiency does not alter endogenous murine amyloid beta levels in mice.
Tucker, H., Simpson, J., Kihiko‐Ehmann, M., Younkin, L., Mcgillis, J. P., Younkin, S., Degen, J., & Estus, S. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.07.011 · Cited by 40
Utsuki, T., Yu, Q.-S., Davidson, D., Chen, D., Holloway, H. W., Brossi, A. R., Sambamurti, K., Lahiri, D. K., Greig, N. H., & Giordano, T. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.103309 · Cited by 39
Physiologic and Pathologic Events Mediated by Intramembranous and Juxtamembranous Proteolysis
Golde, T. E., & Eckman, C. B. (2003) · Science Signaling · doi:10.1126/stke.2003.172.re4 · Cited by 36
Self-citationLeenders, K. L., & Oertel, W. H. (2001) · Neural Plasticity · doi:10.1155/np.2001.99 · Cited by 34
Regulated cleavage of the Alzheimer amyloid precursor protein: Molecular and cellular basis
Gandy, S., & Greengard, P. (1994) · Biochimie · doi:10.1016/0300-9084(94)90162-7 · Cited by 30
Kang, H. J., Yoon, W. J., Moon, G. J., Kim, D. Y., Sohn, S., Kwon, H. J., & Gwag, B. J. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.12.004 · Cited by 27
Zurbriggen, R., Amacker, M., Kammer, A. R., Westerfeld, N., Borghgraef, P., LEUVEN, F. V., der Auwera, I. V., & Wera, S. (2005) · Journal of Molecular Neuroscience · doi:10.1385/jmn:27:2:157 · Cited by 25
Apolipoprotein E4 as a Target for Developing New Therapeutics for Alzheimer's Disease
Refolo, L. M., & Fillit, H. M. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:3:151 · Cited by 20
Koo, E. H. (1997) · PubMed · Cited by 19
Koo, E. H., & Greengard, P. (1997) · Molecular Medicine · doi:10.1007/bf03401673 · Cited by 16
Cellular Models for Tau Filament Assembly
Ko, L., Deture, M. A., Sahara, N., Chihab, R., & Yen, S.-H. C. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:19:3:309 · Cited by 14
Open peer commentary regarding Aβ immunization and CNS inflammation by Pasinetti et al.
DAS, P., & Golde, T. E. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00031-3 · Cited by 10
Self-citationAlpha 1-antichymotrypsin in brain aging and disease.
Abraham, C. R., & Potter, H. (1989) · PubMed · Cited by 9
Aisen, P. S., Schafer, K. A., Grundman, M., Pfeiffer, E., Sano, M., Davis, K. L., Farlow, M. R., Jin, S., Thomas, R. G., Thal, L. J., et al. (2003) · JAMA · doi:10.1001/jama.289.21.2819 · Cited by 5
Pgp deficiency increases amyloid concetrations in the brain
Thomas, L. L. (2005) · The Lancet Neurology · doi:10.1016/s1474-4422(05)70238-6 · Cited by 2
Flagged first, then by citations
2 of the 250 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Black S., 2006, Efficacy and safety ofMPC‐7869 (R.‐flurbiprofen), a selective Abeta42 loering agent in mild Alzheimer's disease: results of a 12‐month phase 2 trial and 1‐year follow on study, Neurology, 66, A347
- Seabrook T. J., 2006, Dendrimeric Abeta1–15 is an effective immunogen in wildtype and APP‐tg mice, Neurobiol. Aging.
Cited by
Sorted by citations
Parsons, C. G., Stöffler, A., & Danysz, W. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.07.013 · Cited by 724
Gong, C., & Iqbal, K. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708785909111 · Cited by 672
Leon, R. M., García, A. G., & Marco, J. L. (2011) · Medicinal Research Reviews · doi:10.1002/med.20248 · Cited by 447
Common pathological processes in Alzheimer disease and type 2 diabetes: A review
Li, L., & Hölscher, C. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2007.09.001 · Cited by 367
Kim, J., Castellano, J. M., Jiang, H., Basak, J. M., Parsadanian, M., Pham, V., Mason, S. M., Paul, S. M., & Holtzman, D. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.11.013 · Cited by 274
Metadata
- Authors
- Golde, T. E.
- Affiliations
- Mayo Clinic (US)
- Corresponding author
- Golde, Todd E.
- ORCID
- Golde, Todd E.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2006-10-02
- Volume
- 99
- Issue
- 3
- Pages
- 689-707
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2056442085
- Cited by
- 117
- References
- 250
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 3 · 2016: 5 · 2015: 3 · 2014: 3 · 2013: 5 · 2012: 6
- FWCI
- 2.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- National Institutes of Health
- National Institute on Aging
- 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
- Alzheimer's disease, disease-modifying therapy, amyloid-beta, tau protein, acetylcholinesterase inhibitors, memantine, NMDA receptor, neuroprotection, excitotoxicity, therapeutic target, clinical trials, dementia
- MeSH terms
- Alzheimer Disease, Animals, Humans, Immunotherapy, Peptide Hydrolases, Phosphorylation, Protease Inhibitors, Amyloid beta-Peptides, Neurofibrillary Tangles, tau Proteins, Protein Folding, Molecular Chaperones, Alzheimer Vaccines
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