Cited by 113Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

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Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models

Levites, Yona, Smithson, Lisa A., Price, Robert W., Dakin, Rachel S., Yuan, Bin, Sierks, Michael R., Kim, Jungsu, McGowan, Eileen, Kim Reed, Dana, Rosenberry, Terrone L., Das, Pritam, Golde, Todd E., Levites, Yona, Smithson, Lisa A., Price, Robert W., Dakin, Rachel S., Yuan, Bin, Sierks, Michael R., Kim, Jungsu, McGowan, Eileen, Kim Reed, Dana, Rosenberry, Terrone L., Das, Pritam, Golde, Todd E.·2006·The FASEB Journal

DOI 10.1096/fj.06-6463fje

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Abstract

A number of hypotheses regarding how anti‐Aβ antibodies alter amyloid deposition have been postulated, yet there is no consensus as to how Aβ immunotherapy works. We have examined the in vivo binding properties, pharmacokinetics, brain penetrance, and alterations in Aβ levels after a single peripheral dose of anti‐Aβ antibodies to both wild‐type (WT) and young non‐Aβ depositing APP and BRI‐Aβ42 mice. The rapid rise in plasma Aβ observed after antibody (Ab) administration is attributable to prolongation of the half‐life of Aβ bound to the Ab. Only a miniscule fraction of Ab enters the brain, and despite dramatic increases in plasma Aβ, we find no evidence that total brain Aβ levels are significantly altered. Surprisingly, cerebral spinal fluid Aβ levels transiently rise, and when Ab:Aβ complex is directly injected into the lateral ventricles of mice, it is rapidly cleared from the brain into the plasma where it remains stable. When viewed in context of daily turnover of Aβ, these data provide a framework to evaluate proposed mechanisms of Aβ attenuation mediated by peripheral administration of an anti‐Aβ monoclonal antibody (mAb) effective in passive immunization paradigm. Such quantitative data suggest that the mAbs are either indirectly enhancing clearance of Aβ or targeting a low abundance aggregation intermediate.—Levites, Y., Smithson, L. A., Price, R. W., Dakin. R. S., Yuan, B., Sierks, M. R., Kim, J., McGowan, E., Reed, D. K., Rosenberry, T. L., Das, P., Golde, T. E. Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models. FASEB J. 20, E2002–E2014 (2006)

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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
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
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
Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431
Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report
Nicoll, J. A. R., Wilkinson, D., Holmes, C., Steart, P., Markham, H., & Weller, R. O. (2003) · Nature Medicine · doi:10.1038/nm840 · Cited by 1,397
Subacute meningoencephalitis in a subset of patients with AD after Aβ42 immunization
Orgogozo, J.-M., Gilman, S., Dartigues, J.-F., Laurent, B., Puel, M., Kirby, L. C., Jouanny, P., Dubois, B., Eisner, L., Flitman, S., et al. (2003) · Neurology · doi:10.1212/01.wnl.0000073623.84147.a8 · Cited by 1,356
Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial
Gilman, S., Koller, M., Black, R. S., Jenkins, L., Griffith, S. G., Fox, N. C., Eisner, L., Kirby, L., Rovira, M. B., Forette, F., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000159740.16984.3c · Cited by 1,329
Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease
DeMattos, R. B., Bales, K. R., Cummins, D. J., Dodart, J.-C., Paul, S. M., & Holtzman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261398 · Cited by 1,298
The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory
Sweatt, J. D. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00054.x · Cited by 1,131
Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease
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×
“brain is 10 nmol (equivalent to the A turned over in the brain in 40 d) (58).”
Background
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
Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model
Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858
Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer’s disease
Georganopoulou, D. G., Chang, L., Nam, J.-M., Thaxton, C. S., Mufson, E. J., Klein, W. L., & Mirkin, C. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409336102 · Cited by 835
Antibodies against β-Amyloid Slow Cognitive Decline in Alzheimer's Disease
Höck, C., Konietzko, U., Streffer, J. R., Tracy, J., Signorell, A., Müller-Tillmanns, B., Lemke, U., Henke, K., Moritz, E., Garcia, E., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00294-0 · Cited by 786
Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo
Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., & Holtzman, D. M. (2006) · Nature Medicine · doi:10.1038/nm1438 · Cited by 599
Brain to Plasma Amyloid-β Efflux: a Measure of Brain Amyloid Burden in a Mouse Model of Alzheimer's Disease
DeMattos, R. B., Bales, K. R., Cummins, D. J., Paul, S. M., & Holtzman, D. M. (2002) · Science · doi:10.1126/science.1067568 · Cited by 563
Effects of Aβ immunization (AN1792) on MRI measures of cerebral volume in Alzheimer disease
Fox, N. C., Black, R. S., Gilman, S., Rossor, M. N., Griffith, S. G., Jenkins, L., & Koller, M. (2005) · Neurology · doi:10.1212/01.wnl.0000159743.08996.99 · Cited by 550 · cited 1×
“Reports of individuals enrolled in the now discontinued phase II trial suggest that those subjects who developed robust anti-A amyloid Ab titers did show some clinical benefit relative to subjects that did not develop robust titers (4, 8, 9).”
Background
Amyloid-β oligomers: their production, toxicity and therapeutic inhibition
Walsh, D. M., Klyubin, I. V., Fadeeva, J. V., Rowan, M. J., & Selkoe, D. J. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300552 · Cited by 507
Amyloid-β immunotherapy for Alzheimer's disease: the end of the beginning
Schenk, D. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn938 · Cited by 436
Epitope and isotype specificities of antibodies to β-amyloid peptide for protection against Alzheimer's disease-like neuropathology
Bard, F., Barbour, R., Cannon, C., Carretto, R., Fox, M., Games, D., Guido, T., Hoenow, K., Hu, K., Johnson-Wood, K., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0436286100 · Cited by 411
In Vivo Assessment of Brain Interstitial Fluid with Microdialysis Reveals Plaque-Associated Changes in Amyloid-β Metabolism and Half-Life
Cirrito, J. R., May, P. C., O'Dell, M. A., Taylor, J. W., Parsadanian, M., Cramer, J. W., Audia, J. E., Nissen, J. S., Bales, K. R., Paul, S. M., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08844.2003 · Cited by 394
Aβ vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
Masliah, E., Hansen, L., Adame, A., Crews, L. A., Bard, F., Lee, C., Seubert, P. A., Games, D., Kirby, L., & Schenk, D. (2005) · Neurology · doi:10.1212/01.wnl.0000148590.39911.df · Cited by 355
Amyloid β-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma
Biere, A. L., Ostaszewski, B., Stimson, E. R., Hyman, B. T., Maggio, J. E., & Selkoe, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32916 · Cited by 331
Novel Therapeutic Approach for the Treatment of Alzheimer's Disease by Peripheral Administration of Agents with an Affinity to β-Amyloid
Matsuoka, Y., Saito, M., LaFrancois, J. J., Saito, M., Gaynor, K., Olm, V., Wang, L., Casey, E., Lu, Y., Shiratori, C., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-01-00029.2003 · Cited by 324
Non-Fc-Mediated Mechanisms Are Involved in Clearance of Amyloid-β In Vivo by Immunotherapy
Bacskai, B. J., Kajdasz, S. T., McLellan, M. E., Games, D., Seubert, P., Schenk, D., & Hyman, B. T. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-18-07873.2002 · Cited by 323
Intravenous immunoglobulins containing antibodies against -amyloid for the treatment of Alzheimer's disease
Dodel, R. C. (2004) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2003.033399 · Cited by 319
Passive Amyloid Immunotherapy Clears Amyloid and Transiently Activates Microglia in a Transgenic Mouse Model of Amyloid Deposition
Wilcock, D. M., Rojiani, A. M., Rosenthal, A., Levkowitz, G., Subbarao, S., Alamed, J., Wilson, D. H., Wilson, N., Freeman, M. J., Gordon, M. N., et al. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1090-04.2004 · Cited by 302
Generation of antibodies specific for β-amyloid by vaccination of patients with Alzheimer disease
Höck, C., Konietzko, U., Papassotiropoulos, A., Wollmer, A., Streffer, J. R., von Rotz, R. C., Davey, G. E., Moritz, E., & Nitsch, R. M. (2002) · Nature Medicine · doi:10.1038/nm783 · Cited by 284
Immunization with a Nontoxic/Nonfibrillar Amyloid-β Homologous Peptide Reduces Alzheimer's Disease-Associated Pathology in Transgenic Mice
Sigurdsson, E. M., Scholtzova, H., Mehta, P. D., Frangione, B., & Wısnıewskı, T. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61715-4 · Cited by 260
Targeting Amyloid-β Peptide (Aβ) Oligomers by Passive Immunization with a Conformation-selective Monoclonal Antibody Improves Learning and Memory in Aβ Precursor Protein (APP) Transgenic Mice
Lee, E. B., Leng, L. Z., Zhang, B., Kwong, L. K., Trojanowski, J. Q., Abel, T. G., & Lee, V. M. ‐. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511018200 · Cited by 254
IgG-Assisted Age-Dependent Clearance of Alzheimer's Amyloid β Peptide by the Blood–Brain Barrier Neonatal Fc Receptor
Deane, R., Sagare, A. P., Hamm, K., Parisi, M., LaRue, B., Guo, H., Wu, Z., Holtzman, D. M., & Zloković, B. V. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3697-05.2005 · Cited by 238
Intracranially Administered Anti-Αβ Antibodies Reduce β-Amyloid Deposition by Mechanisms Both Independent of and Associated with Microglial Activation
Wilcock, D. M., DiCarlo, G., Henderson, D., Jackson, J., Clarke, K., Ugen, K. E., Gordon, M. N., & Morgan, D. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-09-03745.2003 · Cited by 232
Amyloid-β Peptides Interact with Plasma Proteins and Erythrocytes: Implications for Their Quantitation in Plasma
Kuo, Y.-M., Kokjohn, T. A., Kalback, W., Luehrs, D., Galasko, D. R., Chevallier, N., Koo, E. H., Emmerling, M. R., & Roher, A. E. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2222 · Cited by 230
Safety, Tolerability, and Changes in Amyloid β Concentrations After Administration of a γ-Secretase Inhibitor in Volunteers
Siemers, E., Skinner, M., Dean, R. A., Gonzales, C., Satterwhite, J. H., Farlow, M. R., NESS, D. K., & May, P. C. (2005) · Clinical Neuropharmacology · doi:10.1097/01.wnf.0000167360.27670.29 · Cited by 215
Amyloid-β Immunization Effectively Reduces Amyloid Deposition in FcRγ-/-Knock-Out Mice
Das, P., HOWARD, V. G., Loosbrock, N., Dickson, D. W., Murphy, M. P., & Golde, T. E. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-24-08532.2003 · Cited by 213
Self-citation
Systemic Catabolism of Alzheimer's Aβ40 and Aβ42
Ghiso, J., Shayo, M., Calero, M., Ng, D., Tomidokoro, Y., Gandy, S., Rostagno, A., & Frangione, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407668200 · Cited by 209
Anti-A 42- and anti-A 40-specific mAbs attenuate amyloid deposition in an Alzheimer disease mouse model
Levites, Y. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25410 · Cited by 209
Self-citation
Reversible in vitro growth of Alzheimer disease beta-amyloid plaques by deposition of labeled amyloid peptide.
Maggio, J. E., Stimson, E. R., Ghilardi, J. R., Allen, C. J., Dahl, C. E., Whitcomb, D. C., Vigna, S. R., Vinters, H. V., Labenski, M. E., & Mantyh, P. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5462 · Cited by 195
Anti-Aβ antibody treatment promotes the rapid recovery of amyloid-associated neuritic dystrophy in PDAPP transgenic mice
Brendza, R. P., Bacskai, B. J., Cirrito, J. R., Simmons, K. A., Skoch, J. M., Klunk, W. E., Mathis, C. A., Bales, K. R., Paul, S. M., Hyman, B. T., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23269 · Cited by 190
Morphological Characterization of Thioflavin-S-Positive Amyloid Plaques in Transgenic Alzheimer Mice and Effect of Passive Aβ Immunotherapy on Their Clearance
Bussière, T., Bard, F., Barbour, R., Grajeda, H., Guido, T., Khan, K., Schenk, D., Games, D., Seubert, P. A., & Buttini, M. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63360-3 · Cited by 170
Alzheimer disease therapy: Can the amyloid cascade be halted?
Golde, T. E. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17527 · Cited by 164
Self-citation
Reduced effectiveness of Aβ1-42 immunization in APP transgenic mice with significant amyloid deposition
Das, P., Murphy, M. P., Younkin, L. H., Younkin, S. G., & Golde, T. E. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00245-7 · Cited by 150
Self-citation
Alzheimer disease therapy: Can the amyloid cascade be halted?
Golde, T. E. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200317527 · Cited by 139
Self-citation
Aβ42 immunization in Alzheimer's disease generates Aβ N-terminal antibodies
Lee, M., Bard, F., Johnson‐Wood, K., Lee, C., Hu, K., Griffith, S. G., Black, R. S., Schenk, D., & Seubert, P. A. (2005) · Annals of Neurology · doi:10.1002/ana.20592 · Cited by 129
Binding of Gelsolin, a Secretory Protein, to Amyloid β-Protein
Chauhan, V. P. S., Ray, I., Chauhan, A., & Wı́sniewski, H. M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0623 · Cited by 98
Number of A β Inoculations in APP+PS1 Transgenic Mice Influences Antibody Titers, Microglial Activation, and Congophilic Plaque Levels
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
Apolipoprotein E influences amyloid-beta clearance from the murine periphery
Hone, E., Martins, I., Fonte, J., & Martins, R. N. (2003) · Journal of Alzheimer's Disease · doi:10.3233/jad-2003-5101 · Cited by 78
Intravascular infusions of soluble β-amyloid compromise the blood–brain barrier, activate CNS glial cells and induce peripheral hemorrhage
Su, G. C., Arendash, G. W., Kalaria, R. N., Bjugstad, K. B., & MULLAN, M. J. (1999) · Brain Research · doi:10.1016/s0006-8993(98)01143-3 · Cited by 70
Lack of Specific Amyloid-β(1-42) Suppression by Nonsteroidal Anti-Inflammatory Drugs in Young, Plaque-Free Tg2576 Mice and in Guinea Pig Neuronal Cultures
Lanz, T. A., Fici, G. J., & Merchant, K. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.073965 · Cited by 66
Spontaneous Aggregation and Cytotoxicity of the β-Amyloid Aβ1–40: A Kinetic Model
Taylor, B. M., Sarver, R. W., Fici, G. J., Poorman, R. A., Lutzke, B. S., Molinari, A., Kawabe, T. T., Kappenman, K., Buhl, A. E., & Epps, D. E. V. (2003) · Journal of Protein Chemistry · doi:10.1023/a:1023063626770 · Cited by 47
The F(ab′)2 fragment of an Aβ-specific monoclonal antibody reduces Aβ deposits in the brain
Tamura, Y., Hamajima, K., Matsui, K., Yanoma, S., Narita, M., Tajima, N., Xin, K.-Q., Klinman, D. M., & Okuda, K. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.04.007 · Cited by 38
The bulk of endogenously produced IgG2a is eliminated from the serum of adult C57BL/6 mice with a half‐life of 6–8 days
Vieira, P., & Rajewsky, K. (1986) · European Journal of Immunology · doi:10.1002/eji.1830160727 · Cited by 33
Risk Factors Associated With β-Amyloid(1-42) Immunotherapy in Preimmunization Gene Expression Patterns of Blood Cells
O’Toole, M. (2005) · Archives of Neurology · doi:10.1001/archneur.62.10.1531 · Cited by 29
Effects of a behaviorally active antibody on the brain uptake and clearance of amyloid beta proteins
Banks, W. A., Pagliari, P., Nakaoke, R., & Morley, J. E. (2004) · Peptides · doi:10.1016/j.peptides.2004.09.016 · Cited by 26
β‐Amyloid Vasoactivity and Proinflammation in Microglia Can Be Blocked by cGMP‐Elevating Agents
Paris, D., Town, T., Parker, T. A., Humphrey, J., & MULLAN, M. J. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06397.x · Cited by 22
A technique for the collection of cerebrospinal fluid from mice.
Vogelweid, C. M., & Kier, A. B. (1988) · PubMed · 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-citation

Research works printed but not linked: 3

Levites Y., 2005, Anti‐Abeta42 and Anti‐Abeta40 specific monoclonal antibodies attenuate amyloid deposition in an Alzheimer's disease mouse model, J. Clin. Invest, 116, 193, 10.1172/jci25410 · DOI
Lee E. B., 2005, Targeting Abeta oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in APP transgenic mice, J. Biol. Chem, 281, 4292, 10.1074/jbc.m511018200 · DOI
Gravina S. A., 1995, Amyloid beta protein (A beta) in Alzheimer's disease brain, Biochemical and immunocytochemical analysis with antibodies specific for forms ending at A beta 40 or A beta 42(43). J. Biol. Chem, 270, 7013

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Authors: 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., Das, P., Golde, T. E., 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., Das, P., & Golde, T. E.
Venue: The FASEB Journal
Publisher: Wiley
Published: 2006-10-26
Volume: 20
Issue: 14
Pages: 2576-2578
ISSN: 0892-6638 (ISSN-L)
1530-6860
DOI: 10.1096/fj.06-6463fje
OpenAlex: W2091723502
Semantic Scholar: 97676444e5cdee032b67a599961944ce98e967f9
Cited by: 113
References: 60
Citations by year: 2025: 1 · 2024: 3 · 2023: 3 · 2022: 6 · 2021: 3 · 2020: 7 · 2019: 3 · 2018: 8 · 2017: 8 · 2016: 4 · 2015: 8 · 2014: 10 · 2013: 8 · 2012: 7
FWCI: 4.11
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The FASEB Journal (publishedVersion)
PubMed (publishedVersion)
ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
Funders: Mayo Foundation for Medical Education and Research
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: anti-amyloid beta antibodies, Alzheimer's disease, amyloid-beta immunotherapy, passive immunization, amyloid-beta clearance, pharmacokinetics, brain penetration, APP transgenic mice
MeSH terms: Alzheimer Disease, Animals, Antibodies, Monoclonal, Brain, Disease Models, Animal, Female, Immunization, Passive, Mice, Transgenic, Amyloid beta-Peptides, Mice

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Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models

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