The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Partial Reduction of BACE1 Has Dramatic Effects on Alzheimer Plaque and Synaptic Pathology in APP Transgenic Mice
Open accessAbstract
The aspartyl protease beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) initiates processing of amyloid precursor protein (APP) into amyloid beta (Abeta) peptide, the major component of Alzheimer disease (AD) plaques. To determine the role that BACE1 plays in the development of Abeta-driven AD-like pathology, we have crossed PDAPP mice, a transgenic mouse model of AD overexpressing human mutated APP, onto mice with either a homozygous or heterozygous BACE1 gene knockout. Analysis of PDAPP/BACE(-/-) mice demonstrated that BACE1 is absolutely required for both Abeta generation and the development of age-associated plaque pathology. Furthermore, synaptic deficits, a neurodegenerative pathology characteristic of AD, were also reversed in the bigenic mice. To determine the extent of BACE1 reduction required to significantly inhibit pathology, PDAPP mice having a heterozygous BACE1 gene knock-out were evaluated for Abeta generation and for the development of pathology. Although the 50% reduction in BACE1 enzyme levels caused only a 12% decrease in Abeta levels in young mice, it nonetheless resulted in a dramatic reduction in Abeta plaques, neuritic burden, and synaptic deficits in older mice. Quantitative analyses indicate that brain Abeta levels in young APP transgenic mice are not the sole determinant for the changes in plaque pathology mediated by reduced BACE1. These observations demonstrate that partial reductions of BACE1 enzyme activity and concomitant Abeta leve…
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“In fact, several studies unequivocally demonstrated that inhibition of BACE1 by RNAi-mediated knock-down or genetic deletion ameliorates Aβ-associated pathologies and cognitive deficits in mouse models of Aβ-amyloidosis (Laird et al. 2005, Luo et al. 2001, McConlogue et al. 2007, Ohno et al. 2004, Singer et al. 2005).”
From miR‐186 is decreased in aged brain and suppresses BACE 1 expression (2016) · cites this paper as McConlogue et al. 2007
In the citing paper
“In in vivo model systems, similar magnitudes of Aβ reductions are sufficient to prevent or halt Aβ plaque accumulation (53, 54).”
From Serotonin signaling is associated with lower amyloid-β levels and plaques in transgenic mice and humans (2011) · cites this paper as [53]
In the citing paper
“In studies using BACE knock-out mice, a 12% decrease in Aβ concentrations, assessed in total brain tissue, resulted in a marked blocking of plaque formation (33).”
From An Antidepressant Decreases CSF Aβ Production in Healthy Individuals and in Transgenic AD Mice (2014) · cites this paper as [33]
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Cited by
Sorted by citations
Items 201–269 of 269
The BACE1 inhibitor LY2886721 improves diabetic phenotypes of BACE1 knock-in mice.
Dekeryte, R., Franklin, Z., Hull, C., Croce, L., Kamli-Salino, S., Helk, O., Hoffmann, P. A., Yang, Z.-X., Riedel, G., Delibegović, M., et al. (2021) · Biochimica et Biophysica Acta - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166149 · Cited by 17
“23 inhibition would lead to ~20% decrease in brain Aβ [28,29].”
BackgroundCoimbra, J. R. M., Baptista, S. J., Dinis, T., Silva, M. C., Moreira, P., Santos, A., & Salvador, J. A. R. (2020) · Biomolecules · doi:10.3390/biom10040535 · Cited by 17
“Fortunately, studies suggest that partial inhibition of BACE1 activity might be enough to prevent amyloid pathology and reduce the risk of developing AD [19].”
BackgroundImpact of the Cannabinoid System in Alzheimer's Disease
Li, S., Huang, Y., Yu, L., Ji, X., & Wu, J. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220201091006 · Cited by 28
“Then insoluble Aβ fibrils form oligomers, diffuse into the synaptic cleft, and interfere with synaptic signaling [6-8].”
Identification of ovalbumin-derived peptides as multi-target inhibitors of AChE, BChE and BACE1.
Yu, Z.-P., Dong, W., Wu, S.-J., Shen, J., Zhao, W.-Z., Ding, L., Liu, J.-B., & Zheng, F.-P. (2020) · The Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.10295 · Cited by 16
Electroacupuncture Reduces Aβ Production and BACE1 Expression in SAMP8 Mice
Dong, W., Wang, F., Chen, Y., Zheng, X.-H., Xie, Y.-C., Guo, W., & Shi, H. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00148 · Cited by 16
“Lowering BACE1 expression reduced the formation of Aβ, thereby preventing its subsequent aggregation into toxic aggregates (Citron, 2002; McConlogue et al., 2007).”
BackgroundResultQuartino, A. L., Huledal, G., Sparve, E., Lüttgen, M., Bueters, T., Karlsson, P., Olsson, T., Paraskos, J., Maltby, J., Claeson‐Bohnstedt, K., et al. (2014) · Clinical Pharmacology in Drug Development · doi:10.1002/cpdd.130 · Cited by 17
“In BACE1 heterozygous knockout mice, a 12% decrease in soluble Ab levels at early age resulted in a dramatic reduction of Ab plaques, neuritic burden, and synaptic deficits at an older age.(33) Also, an average 20–25% lowering of central Ab levels with a g-secretase inhibitor attenuated progression of amyloid plaque i…”
BackgroundDorresteijn, B., Rotman, M., Faber, D., Schravesande, R., Suidgeest, E., van der Weerd, L., van der Maarel, S. M., Verrips, C. T., & Khattabi, M. E. (2015) · FEBS Journal · doi:10.1111/febs.13367 · Cited by 15
Yi, L., Luo, M., Wang, M., Dong, Z., & Du, Y. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1288506 · Cited by 15
Mycroft-West, C. J., Cooper, L. C., Devlin, A., Procter, P., Guimond, S., Guerrini, M., Fernig, D., Lima, M., Yates, E., & Skidmore, M. (2019) · bioRxiv · doi:10.3390/md17050293 · Cited by 14
BACE1-cleavage of Sez6 and Sez6L is elevated in Niemann-Pick type C disease mouse brains
Čaušević, M., Dominko, K., Malnar, M., Vidatic, L., Čermak, S., Pigoni, M., Kuhn, P., Colombo, A. V., Havas, D., Flunkert, S., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0200344 · Cited by 20
“cleaved by BACE1 [32], together with studies on AD-transgenic mice crossed with genetically deleted BACE1 mice, showing a decrease in Aβ levels and protection against AD and cognitive decline [33, 34, 35, 36, 37], strongly suggest that BACE1-inhibition should prove effective for AD treatment.”
BackgroundSynthesis and SAR of hydroxyethylamine based phenylcarboxyamides as inhibitors of BACE.
Wu, Y.-J., Zhang, Y.-H., Good, A., Burton, C., Toyn, J., Albright, C., Macor, J., & Thompson, L. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.03.144 · Cited by 14
Putative pathological mechanisms of late-life depression and Alzheimer’s disease
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Membrane Anchored and Lipid Raft Targeted β-Secretase Inhibitors for Alzheimer's Disease Therapy
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“Endogenous Abeta levels were unchanged in BACE1(+/−) mice compared to BACE1(+/+) mice [13] and Abeta reduction was minimal (∼12%) and not statistically significant reduced in BACE(+/−)/APP mice at 3 months of age [ 12 ].”
Resende, R., Ferreira‐Marques, M., Moreira, P., Coimbra, J. R. M., Baptista, S. J., Isidoro, C., Salvador, J. A. R., Dinis, T. C. P., Pereira, C., & Santos, A. E. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200381 · Cited by 17
“Of note, our aim was to inhibit only a small percentage of A (cid:2) production since it is known from the literature that this translates into a considerably greater effect on insoluble A (cid:2) levels upon chronic administration [15].”
InfluentialBACE1 Levels by APOE Genotype in Non-Demented and Alzheimer’s Post-Mortem Brains
Decourt, B., Gonzales, A., Beach, T. G., Malek‐Ahmadi, M. H., Walker, A. W., Sue, L. I., Walker, D. G., & Sabbagh, M. N. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310030010 · Cited by 11
“Recent evidence from transgenic animal and in vitro studies suggests that beta-site APP-cleaving enzyme 1 (BACE1) is the major β-secretase in the brain [4, 5] and the rate-limiting enzyme in amyloidogenesis [6, 7].”
BackgroundExpression analysis of human β-secretase in transgenic tomato fruits.
Kim, H. S., Youm, J., Moon, K.-B., Jang, H.-H., Kim, Y. H., Joung, H., & Jeon, J. (2012) · Protein Expression and Purification · doi:10.1016/j.pep.2011.11.012 · Cited by 12
“These highly insoluble, plastic-like deposits are composed of a 4-kDa b-amyloid protein (Ab) derived from the amyloid precursor protein (APP) by sequential proteolysis of b-secretase and c-secretase [1,2].”
BackgroundWang, S., & Jia, J. (2009) · American Journal of Medical Genetics Part B: Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30968 · Cited by 12
“BACE1 knockout mice, without developmental deficits, have abolished Ab generation [McConlogue et al., 2007].”
BackgroundLee, W. J., Ham, S. A., Lee, G. H., Choi, M., Yoo, H., Paek, K. S., Lim, D., Hong, K., Hwang, J. S., & Seo, H. G. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14715 · Cited by 13
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“Previous in vivo studies have shown that a 50% reduction in BACE1 levels causes only a 12% decrease in Ab levels in heterozygous BACE1 gene knock-out mice [77].”
BackgroundThe amyloid-β peptide: Guilty as charged?
Murphy, M. P., Buzinova, V. A., & Johnson, C. E. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166945 · Cited by 12
Huang, P., He, X.-Y., & Xu, M. (2021) · Revista da Associação Médica Brasileira · doi:10.1590/1806-9282.67.02.20200378 · Cited by 10
Yang, S.-G., Wang, S.-W., Zhao, M., Zhang, R., Zhou, W.-W., Li, Y.-N., Su, Y.-J., Zhang, H., Yu, X.-L., & Liu, R.-T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048540 · Cited by 10
[3H]BMS-599240--a novel tritiated ligand for the characterization of BACE1 inhibitors.
Iben, L., Kopcho, L., Marcinkeviciene, J., Zheng, C.-S., Thompson, L., Albright, C., & Toyn, J. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.06.112 · Cited by 9
Biofluid biomarkers for Alzheimer’s disease
Wang, S., Xie, S., Zheng, Q., Zhang, Z., Wang, T., & Zhang, G. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1380237 · Cited by 9
Sulfonamido-derivatives of unsubstituted carbazoles as BACE1 inhibitors.
Bertini, S., Ghilardi, E., Asso, V., Minutolo, F., Rapposelli, S., Digiacomo, M., Saccomanni, G., Salmaso, V., Sturlese, M., Moro, S., et al. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.09.058 · Cited by 8
Alzheimer’s Disease and Animal Models in Retrospect
Fajemiroye, J. O. (2014) · Medicinal Chemistry · doi:10.4172/2161-0444.1000215 · Cited by 6
Silencing of Amyloid Precursor Protein Expression Using a New Engineered Delta Ribozyme
Aissa, M. B., April, M.-C., Bergeron, L. J., Perreault, J., & Lévesque, G. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/947147 · Cited by 5
“Because only a 12% decrease in Aβ levels in mice resulted in a dramatic reduction in Aβ build-up and synaptic deficits [49], we are optimistic that the results obtained in our cellular model will allow for the development of an efficacious form of SOFA-HDV ribozyme-based therapy.”
O’Day, D. H. (2023) · Biomolecules · doi:10.3390/biom13040678 · Cited by 8
“As a result, due to these many roles the complete removal of the enzyme using gene knockouts or the complete inhibition of enzyme activity has led to neurological and other defects [48,49].”
BackgroundTian, S., Huang, R., Guo, D., Lin, H., Wang, J., An, K., & Wang, S. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200522210957 · Cited by 7
Kawai, T., Kawashima, H., Kuge, Y., & Saji, H. (2013) · Nuclear Medicine and Biology · doi:10.1016/j.nucmedbio.2013.03.008 · Cited by 7
“Because Aβ constitute senile plaque, which is one of the major pathological changes in Alzheimer's disease (AD) brain, it is considered that BACE1 plays an important role in the development of AD [1–3].”
BackgroundPotential Therapeutic Strategies to Prevent the Progression of Alzheimer to Disease States
Aso, E., & Ferrer, I. (2013) · InTech eBooks · doi:10.5772/54783 · Cited by 5
“The research of drugs inhibiting BACE1 activity was encouraged by studies revealing that the expression of mutated BACE1 reduces amyloidogenesis and cognitive impairment in APP transgenic mice [9, 10].”
Nuclear factor kappa B (NF-κB) participates in the aluminum-induced down-regulation of miR29a/b1
Wang, L., Zhang, J., Zhao, Y., Li, J., Lu, X., Song, J., Zhang, L., & Niu, Q. L. (2023) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2023.127309 · Cited by 6
Fluid Biomarkers in Clinical Trials for Alzheimer’s Disease: Current and Future Application
Yang, J., Jia, L., Li, Y., Qiu, Q., Quan, M., & Jia, J. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201068 · Cited by 4
“Work in animal models indicates that even partial reduction of A (cid:2) 42 concentration in CSF is associated with a substantial lowering of amyloid plaque formation and growth [78, 79].”
AAV mediated delivery of a novel anti-BACE1 VHH reduces Abeta in an Alzheimer’s disease mouse modelPreprint
Rincón, M. Y., Zhou, L., Marneffe, C., Voytyuk, I., Wouters, Y., Dewilde, M., Duqué, S. I., Vincke, C., Levites, Y., Golde, T. E., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/698506 · Cited by 7
“…a reduction of 50% in the levels of BACE1 activity is sufficient to significantly reduce Aβ plaques, neuritic burden, and synaptic deficits in mouse models of AD (McConlogue et al, 2007), similar to the effects seen with a reduction of 30% in the levels of gamma secretase activity (Li et al, 2007).”
BackgroundDevelopment of a Novel β-Secretase Binding Assay Using the AlphaScreen Platform
Ren, Z., Tam, D., Xu, Y., Wone, D. W. G., Yuan, S., Sham, H. L., Cheung, H., Regnström, K. J., Chen, X., Rudolph, D., et al. (2013) · SLAS DISCOVERY · doi:10.1177/1087057113482138 · Cited by 7
TNIP2 inhibits amyloidogenesis by regulating the 3′UTR of BACE1: An in vitro study
Chen, L., Wang, L., Zhou, G., Liu, Y., Chen, X., Xie, X., Wen, Q., Li, C., Yang, J., & Chen, G. (2023) · Neuroscience Letters · doi:10.1016/j.neulet.2023.137265 · Cited by 6
Campagna, J. J., Vadivel, K., Jagodzinska, B., Jun, M., Bilousova, T. V., Spilman, P., & John, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.04.002 · Cited by 5
Shin, Y., Hamm, L., Murakami, S., Buirst, K., Buonarati, M., Cox, A. A., Regal, K., Hunt, K. W., Scearce-Levie, K., Watts, R., et al. (2013) · Archives of pharmacal research · doi:10.1007/s12272-013-0215-2 · Cited by 5
“Importantly, hAPP transgenic mice that are heterozygous for BACE1 knockout show a dramatic reduction in amyloid plaques and protection against synaptic and cognitive deficits (Laird et al. 2005; McConlogue et al. 2007; Ohno et al. 2004).”
BackgroundMethodological Issues : Do Membrane Rafts Exist ?
Gulati, V., & Wallace, R. (2012) · doi:10.4324/9780203104507-16 · Cited by 5
“Investigators suggest that partial inhibition of BACE1 may be required, a strategy perhaps sufficient, to prevent Aβ synthesis [114].”
Emerging Novel Therapeutic Approaches for the Treatment of Alzheimer’s Disease
Panwar, A., Khan, M. I. K., Kumar, R., Kumar, R., Kumar, S., & Kumar, A. (2024) · Advances in Alzheimer s Disease · doi:10.4236/aad.2024.133006 · Cited by 5
Vassar, R. J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00003-4 · Cited by 3
Dysregulation of Long Non-coding RNAs in Human Disease
Lin, N., & Rana, T. M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8621-3_5 · Cited by 5
Carney, R. S. E. (2018) · eNeuro · doi:10.1523/eneuro.0384-18.2018 · Cited by 3
“Supporting this approach is the observation that transgenic models of AD do not exhibit amyloid pathology when crossed with mice deficient in BACE1 (Luo et al., 2003; Laird et al., 2005; McConlogue et al., 2007; Ohno et al., 2007).”
BackgroundPark, S., Huh, J., Eom, T., Na, N., Lee, Y., Kim, J.-S., Kim, S.-U., Shim, I., Lee, S.-R., & Kim, E. (2017) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1707.07003 · Cited by 3
“Moreover, AD does not develop from a single gene abnormality, but from double gene modification due to co-factors such as BACE, apolipoprotein E, and presenilin [22-26].”
BackgroundEmerging role of G-quadruplexes in alternative splicing regulation
Peynet, A., Sénéchal, R. L., Keruzoré, M., Lejault, P., Quillévéré, A., Loaëc, N., Martin, N. G., Lepan, T., Teulade‐Fichou, M., Corcos, L., et al. (2026) · Trends in Genetics · doi:10.1016/j.tig.2026.05.001 · Cited by 2
Effect of Functional Inhibition of BACE1 on Sensitization to γ-Irradiation in Cancer Cells
Nakamoto, K., Kikuhara, S., Fujimori, H., Saraswat, B., Gao, Z., Velu, A. V., Zhang, Z., Tong, Y., Imamichi, S., Nozaki, T., et al. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46010028 · Cited by 2
“BACE1 knockout mice have been produced but showed no apparent phenotypes, suggesting that BACE1 inhibition will not cause severe side effects [13–15].”
BackgroundFrontiers in Clinical Drug Research - Alzheimer Disorders
Atta-ur-rahman, Mavoungou, C., Zimmerman, K. S., Wright, J., Harding, J., Cavallaro, R., Fuso, A., Yoshiyama, Y., Asija, Z., Clifford, A., et al. (2015) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/97816810806801150301 · Cited by 1
BACE: A (Almost) Perfect Target for Staving off Alzheimer's Disease
Sinha, S. (2010) · Methods and principles in medicinal chemistry · doi:10.1002/9783527630943.ch14 · Cited by 1
Self-citationOrganofluorine Compounds in Neurological Disorders
Reddy, V. (2015) · Elsevier eBooks · doi:10.1016/b978-0-444-53748-5.00008-3 · Cited by 2
Lee, H. J., Jung, Y. H., Choi, G. E., Kim, J. S., Chae, C. W., Lim, J. R., Kim, S. Y., Yoon, J. H., Cho, J. H., Lee, S., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0593-1 · Cited by 180
Wendt, G. (2014) · doi:10.22028/d291-23005 · Cited by 1
“&0%'&%' various APP-overexpressing mouse models (Laird et al., 2005, McConlogue et al., 2007, Kobayashi et al., 2008).”
BackgroundAlzheimer’s Disease and Frontotemporal Lobar Degeneration: Mouse Models
van Eersel, J., Delerue, F., Ittner, L. M., & Ke, Y. D. (2014) · Springer eBooks · doi:10.1007/978-1-4471-6380-0_8
Vasconcelos, B., Bird, M., Stancu, I., Terwel, D., & Dewachter, I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805120-7.00006-3 · Cited by 2
Role of BACE1 in Cognitive Function, from Alzheimer’s Disease to Traumatic Brain Injury
Lombardo, S., & Tesco, G. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802851-3.00008-5 · Cited by 2
Aspartic Proteases of Alzheimer’s Disease: β- and γ-Secretases
Wolfe, M. S. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10077-x · Cited by 2
Modulation of BACE1 Activity as a Potential Therapeutic Strategy for Treating Alzheimer’s Disease
Klaver, D. W., & Tesco, G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50009-x · Cited by 1
Ly, P. (2012) · cIRcle (University of British Columbia) · doi:10.14288/1.0072944 · Cited by 1
“In fact, even a partial reduction of BACE1 can have dramatically beneficial effects on AD pathology (McConlogue et al., 2007), suggesting that inhibition of BACE1 is a valid therapeutic target for AD treatment.”
Noroozzadeh, M., Changaei, M., Farhadi-Azar, M., Mousavi, M., Mousapour, P., Amiri, M., Jorjani, M., & Tehrani, F. R. (2026) · International Journal of Endocrinology and Metabolism · doi:10.5812/ijem-167083
Discovery of an APP-selective BACE1 inhibitor for Alzheimer's disease
Campagna, J. J., Jagodzinska, B. M., Wi, D., Zhu, C., Lee, J. L., Cohn, W., Jun, M., Elias, C. J., Padder, S., Descamps, O., et al. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00610 · Cited by 10
“Such a partial BACE1 inhibition therapeutic approach is supported by the previous fi nding of McConlogue et al. [38] that indicated, at least in a mouse model of AD, that only a 12 % decrease in A β levels in brain results in dramatic reduction in plaque pathology.”
Synthesis of a carbon-11 radiolabeled BACE1 inhibitor
Zhu, Y., Fiedler, S. A., Hibert, M., & Wang, C. (2019) · Medicinal Chemistry Research · doi:10.1007/s00044-019-02480-9
Lotz, G. P., & Muchowski, P. J. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch44
Implications of alpha- and beta-secretase expression and function in Alzheimer's disease
Reinhardt, S., & Endres, K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815868-5.00016-5
“Various in vivo studies have shown that full or partial genetic ablation of BACE1 in APP transgenic mouse models can reduce Aβ burden and rescue Aβ-induced memory deficits (Laird et al., 2005; McConlogue et al., 2007; Ohno et al., 2004), further cementing the importance of BACE1 in AD pathogenesis.”
BackgroundDie Rolle der neuronalen p38α Mitogen-aktivierten Proteinkinase in der Alzheimer-Krankheit
Schnöder, L. (2017) · doi:10.22028/d291-27214
“Studien an BACE knock-out (ko) Mäusen (Luo, 2003; Ohno et al., 2004; Laird et al., 2005; Ohno et al., 2006; Mcconlogue et al., 2007; Ohno et al., 2007; May et al., 2011) oder Applikation von BACE Inhibitoren (Filser et al., 2015) verringern den zerebralen Aβ-Gehalt und beheben Defizite in…”
BackgroundInfluentialStamford, 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
BACE1 Inhibitors: Attractive Therapeutics for Alzheimer’s Disease
Decourt, B., Macias, M. P., Sabbagh, M. N., & Adem, A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50010-6
The effect of high glucose on APP metabolism and Abeta production
Yang, Y. (2013) · Joint Conference of the Information Retrieval Communities in Europe · doi:10.14288/1.0073763
“In addition, 50% reduction in BACE1 activity resulted in a remarkable reduction in Aβ plaques and synaptic deficits (McConlogue et al., 2007).”
Metadata
- Authors
- McConlogue, L., Buttini, M., Anderson, J. P., Brigham, E. F., Chen, K. S., Freedman, S. B., Games, D., Johnson-Wood, K., Lee, M., Zeller, M., Liu, W., Motter, R., & Sinha, S.
- Affiliations
- Elan Pharmaceuticals, Inc. (Ireland) (IE)
- Corresponding author
- McConlogue, Lisa
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-09
- Volume
- 282
- Issue
- 36
- Pages
- 26326-26334
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2000536660
- Cited by
- 300
- References
- 56
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 9 · 2023: 8 · 2022: 7 · 2021: 8 · 2020: 18 · 2019: 16 · 2018: 13 · 2017: 17 · 2016: 18 · 2015: 24 · 2014: 24 · 2013: 17 · 2012: 23
- FWCI
- 14.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- 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
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- BACE1, Alzheimer's disease, amyloid-beta, amyloid plaques, APP transgenic mice, PDAPP mice, synaptic deficits, neuritic plaques, therapeutic target
- MeSH terms
- Aging, Alzheimer Disease, Animals, Disease Models, Animal, Enzyme Activation, Humans, Synaptic Membranes, Aspartic Acid Endopeptidases, Neurites, Amyloid beta-Protein Precursor, Mice, Knockout, Mice, Amyloid Precursor Protein Secretases
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