Cited by 150Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.

Enhanced Amyloidogenic Processing of the β-Amyloid Precursor Protein in Gene-targeted Mice Bearing the Swedish Familial Alzheimer's Disease Mutations and a “Humanized” Aβ Sequence

Open access

Reaume, Andrew G., Howland, David S., Trusko, Stephen P., Savage, Mary J., Lang, Diane M., Greenberg, Barry D., Siman, Robert, Scott, Richard W.·1996·Journal of Biological Chemistry

DOI 10.1074/jbc.271.38.23380

Open this paper in CoChat — free account

Abstract

The processing of the beta-amyloid precursor protein (APP) in vivo has been characterized in a novel animal model that recapitulates, in part, the APP genotype of a familial form of Alzheimer's disease (AD). A gene-targeting strategy was used to introduce the Swedish familial AD mutations and convert mouse Abeta to the human sequence. The mutant APP is expressed at normal levels in brain, and cleavage at the mutant beta-secretase site is both accurate and enhanced. Furthermore, human Abeta production is significantly increased to levels 9-fold greater than those in normal human brain while nonamyloidogenic processing is depressed. The results on Abeta production extend similar findings obtained in cell culture to the brain of an animal and substantiate Abeta as a etiological factor in Swedish familial AD. These animals provide several distinguishing features over others created by conventional transgenic methodologies. The spatial and temporal expression patterns of human Abeta are expected to be faithfully reproduced because the gene encoding the mutant APP remains in its normal chromosomal context. Thus, the neuropathological consequences of human Abeta overproduction can be evaluated longitudinally in the absence of potential mitigating effects of APP overexpression or presence of the mouse Abeta peptide.

Integrity signals

Registry

Crossref · 10.1074/jbc.271.38.23380

Cites

69 of 69 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.
Schägger, H., & von Jagow, G. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90587-2 · Cited by 11,420
Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Manipulating the mouse embryo: A laboratory manual
Hogan, B. L. M., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,460
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
The molecular pathology of Alzheimer's disease
Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516

Show all 69 references

Research works printed but not linked: 2

Sauer, 1990, New Biol., 2, 441
Kim, 1990, Neurosci. Res. Commun., 7, 113

Sorted by citations

Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: evidence for augmentation of a 42-specific γ secretase
Jankowsky, J. L., Fadale, D. J., Anderson, J., Xu, G. M., Gonzales, V., Jenkins, N. A., Copeland, N. G., Lee, M. K., Younkin, L. H., Wagner, S. L., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh019 · Cited by 1,575
APP mouse models for Alzheimer’s disease preclinical studies.
Sasaguri, H., Nilsson, P., Hashimoto, S., Nagata, K., Saito, T., De Strooper, B., Hardy, J., Vassar, R., Winblad, B., & Saido, T. C. (2017) · The EMBO Journal · doi:10.15252/embj.201797397 · Cited by 793
Practical considerations for choosing a mouse model of Alzheimer’s disease
Jankowsky, J. L., & Zheng, H. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0231-7 · Cited by 449
Rodent models for Alzheimer disease
Götz, J., Bodea, L., & Goedert, M. (2018) · Nature reviews. Neuroscience · doi:10.1038/s41583-018-0054-8 · Cited by 419
Ts1Cje, a partial trisomy 16 mouse model for Down syndrome, exhibits learning and behavioral abnormalities
Sago, H., Carlson, E. J., Smith, D. J., Kilbridge, J., Rubin, E. M., Mobley, W. C., Epstein, C. J., & Huang, T.-T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6256 · Cited by 382
Transgenic mouse models of Alzheimer’s disease.
Elder, G. A., Gama Sosa, M. A., & De Gasperi, R. (2010) · Mount Sinai Journal of Medicine A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20159 · Cited by 336
Mouse models of Alzheimer's disease
Hall, A. M., & Roberson, E. D. (2012) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.11.017 · Cited by 317
Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice
Larson, J., LYNCH, G. S., Games, D., & Seubert, P. A. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01698-4 · Cited by 291
Long-Term Accumulation of Amyloid-β, β-Secretase, Presenilin-1, and Caspase-3 in Damaged Axons Following Brain Trauma
Chen, X.-H., Siman, R., Iwata, A., Meaney, D. F., Trojanowski, J. Q., & Smith, D. H. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63303-2 · Cited by 271
Self-citation
Modulation of Secreted β-Amyloid Precursor Protein and Amyloid β-Peptide in Brain by Cholesterol
Howland, D., Trusko, S. P., Savage, M. J., Reaume, A. G., Lang, D. M., Hirsch, J. D., Maeda, N., Siman, R., Greenberg, B., Scott, R. W., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16576 · Cited by 256
Self-citation
Decreased Brain-Derived Neurotrophic Factor Depends on Amyloid Aggregation State in Transgenic Mouse Models of Alzheimer's Disease
Peng, S., Garzon, D. J., Marchese, M., Klein, W. L., Ginsberg, S. D., Francis, B. M., Mount, H. T. J., Mufson, E. J., Salehi, A., & Fahnestock, M. L. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4736-08.2009 · Cited by 224
Long-lasting impairment in hippocampal neurogenesis associated with amyloid deposition in a knock-in mouse model of familial Alzheimer's disease
Zhang, C., McNeil, E. M., Dressler, L., & Siman, R. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.09.018 · Cited by 217
Self-citation
Turnover of Amyloid β-Protein in Mouse Brain and Acute Reduction of Its Level by Phorbol Ester
Savage, M. J., Trusko, S. P., Howland, D. S., Pinsker, L. R., Mistretta, S., Reaume, A. G., Greenberg, B. D., Siman, R., & Scott, R. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-05-01743.1998 · Cited by 213
Self-citation
Alzheimer’s Disease in the Retina: Imaging Retinal Aβ Plaques for Early Diagnosis and Therapy Assessment
Koronyo, Y., Salumbides, B. C., Black, K. L., & Koronyo‐Hamaoui, M. (2012) · Neurodegenerative Diseases · doi:10.1159/000335154 · Cited by 202
Animal models of Alzheimer's disease and evaluation of anti-dementia drugs
Yamada, K., & Nabeshima, T. (2000) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(00)00081-4 · Cited by 192
Synaptic plasticity and cell cycle activation in neurons are alternative effector pathways: the 'Dr. Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity
Arendt, T. (2003) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2003.09.007 · Cited by 189
Using Knockout and Transgenic Mice to Study Neurophysiology and Behavior
Picciotto, M. R., & Wickman, K. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.4.1131 · Cited by 189
Unusual phenotypic alteration of β amyloid precursor protein (βAPP) maturation by a new Val-715 → Met βAPP-770 mutation responsible for probable early-onset Alzheimer’s disease
Ancolio, K., Dumanchin‐Njock, C., Barelli, H., Warter, J., Brice, A., Campion, D., Frébourg, T., & Checler, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.4119 · Cited by 183
Sleep and circadian abnormalities in a transgenic mouse model of Alzheimer’s disease: A role for cholinergic transmission
Wisor, J. P., Edgar, D. M., Yesavage, J. A., Ryan, H. S., McCormick, C. M., Lapustea, N., & Murphy, G. M. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.11.018 · Cited by 169
Caveolae, Plasma Membrane Microdomains for α-Secretase-mediated Processing of the Amyloid Precursor Protein
Ikezu, T., Trapp, B. D., Song, K. S., Schlegel, A., Lisanti, M. P., & Okamoto, T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10485 · Cited by 157
β-Amyloid Mediated Nitration of Manganese Superoxide Dismutase
Muthuswamy, A., Tangpong, J., Keller, J. N., Murphy, M. P., Markesbery, W. R., Kiningham, K. K., & Clair, D. K. S. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051223 · Cited by 144
An App knock-in rat model for Alzheimer’s disease exhibiting Aβ and tau pathologies, neuronal death and cognitive impairments
Pang, K., Jiang, R., Zhang, W., Yang, Z., Li, L., Shimozawa, M., Tambaro, S., Mayer, J., Zhang, B., Li, M., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00582-x · Cited by 144
Comprehensive behavioral characterization of an APP/PS-1 double knock-in mouse model of Alzheimer's disease
Webster, S. J., Bachstetter, A. D., & Eldik, L. J. V. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt182 · Cited by 153
Atherosclerosis and Alzheimer - diseases with a common cause? Inflammation, oxysterols, vasculature
Lathe, R., Tsitrina, A. A., & Kotelevtsev, Y. V. (2014) · BMC Geriatrics · doi:10.1186/1471-2318-14-36 · Cited by 141
A neuronal model of Alzheimer's disease: An insight into the mechanisms of oxidative stress–mediated mitochondrial injury
Sompol, P. M., Ittarat, W., Tangpong, J., Chen, Y., Doubinskaia, I. E., Batinic-Haberle, I., Abdul, H. M., Butterfield, D. A., & Clair, D. K. S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.044 · Cited by 137
Presenilin-1 P264L Knock-In Mutation: Differential Effects on Aβ Production, Amyloid Deposition, and Neuronal Vulnerability
Siman, R., Reaume, A. G., Savage, M. J., Trusko, S., Lin, Y.-G., Scott, R. W., & Flood, D. G. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-23-08717.2000 · Cited by 133
Self-citation
FAD mutant PS-1 gene-targeted mice: increased Aβ42 and Aβ deposition without APP overproduction
Flood, D. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00330-x · Cited by 131
Glycogen synthase kinase 3β links neuroprotection by 17β-estradiol to key Alzheimer processes
Goodenough, S., Schleusner, D., Pietrzik, C. U., Skutella, T., & Behl, C. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.12.029 · Cited by 124
Leveraging preclinical models for the development of Alzheimer disease therapeutics
Scearce-Levie, K. A., Sanchez, P. E., & Lewcock, J. W. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0065-9 · Cited by 121
Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau
Rayaprolu, S., Higginbotham, L., Bagchi, P., Watson, C. M., Zhang, T., Levey, A. I., Rangaraju, S., & Seyfried, N. T. (2021) · Neuropsychopharmacology · doi:10.1038/s41386-020-00840-3 · Cited by 118
Cystatin C Protects Neuronal Cells from Amyloid-β-induced Toxicity
Tizón, B., Ribé, E. M., Mi, W., Troy, C. M., & Levy, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1291 · Cited by 115
Humanising the mouse genome piece by piece
Zhu, F., Nair, R., Fisher, E., & Cunningham, T. J. (2019) · Nature Communications · doi:10.1038/s41467-019-09716-7 · Cited by 113
Mutations in amyloid precursor protein and presenilin‐1 genes increase the basal oxidative stress in murine neuronal cells and lead to increased sensitivity to oxidative stress mediated by amyloid β‐peptide (1–42), H2O2 and kainic acid: implications for Alzheimer's disease
Abdul, H. M., Rukhsana Sultana, A., Keller, J. N., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03647.x · Cited by 114
Modeling human neurodegenerative diseases in transgenic systems
Sosa, M. A. G., Gasperi, R. D., & Elder, G. A. (2011) · Human Genetics · doi:10.1007/s00439-011-1119-1 · Cited by 114
Early Stage Drug Treatment That Normalizes Proinflammatory Cytokine Production Attenuates Synaptic Dysfunction in a Mouse Model That Exhibits Age-Dependent Progression of Alzheimer's Disease-Related Pathology
Bachstetter, A. D., Norris, C. M., Sompol, P. M., Wilcock, D. M., Goulding, D. S., Neltner, J. H., Clair, D. K. S., Watterson, D. M., & Eldik, L. J. V. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1496-12.2012 · Cited by 106
APP transgenic modeling of Alzheimer’s disease: mechanisms of neurodegeneration and aberrant neurogenesis
Crews, L. A., Rockenstein, E. M., & Masliah, E. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0232-6 · Cited by 110
APP physiological and pathophysiological functions: insights from animal models
Guo, Q., Wang, Z., Li, H., Wiese, M., & Zheng, H. (2011) · Cell Research · doi:10.1038/cr.2011.116 · Cited by 101
Animal models of amyloid‐β‐related pathologies in Alzheimer’s disease
Philipson, O., Lord, A., Gumucio, A., O'Callaghan, P. W., Lannfelt, L., & Nilsson, L. N. G. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07564.x · Cited by 101
Cognitive impairment in humanized APP×PS1 mice is linked to Aβ1–42 and NOX activation
Bruce-Keller, A. J., Gupta, S., Knight, A. G., Beckett, T. L., McMullen, J. M., Davis, P. R., Murphy, M. P., Van Eldik, L. J., St Clair, D., & Keller, J. N. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.012 · Cited by 96
Changes in Expression of Amyloid Precursor Protein and Interleukin-1β after Experimental Traumatic Brain Injury in Rats
Ciallella, J. R., Ikonomovic, M. D., Paljug, W. R., Wilbur, Y. I., Dixon, C. E., Kochanek, P. M., Marion, D. W., & DeKosky, S. T. (2002) · Journal of Neurotrauma · doi:10.1089/089771502762300229 · Cited by 94
A ketogenic diet improves motor performance but does not affect β-amyloid levels in a mouse model of Alzheimer's Disease
Beckett, T. L., Studzinski, C. M., Keller, J. N., Murphy, M. P., & Niedowicz, D. M. (2013) · Brain Research · doi:10.1016/j.brainres.2013.01.046 · Cited by 94
Brain Trauma in Aged Transgenic Mice Induces Regression of Established Aβ Deposits
Nakagawa, Y., Reed, L., Nakamura, M., McIntosh, T. K., Smith, D. H., Saatman, K. E., Raghupathi, R., Clemens, J., Saido, T. C., Lee, V. M.-Y., et al. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7375 · Cited by 91
Caspase inhibition therapy abolishes brain trauma-induced increases in Aβ peptide: Implications for clinical outcome
Abrahamson, E. E., Ikonomovic, M. D., Ciallella, J. R., Hope, C. E., Paljug, W. R., Isanski, B. A., Flood, D. G., Clark, R. S. B., & DeKosky, S. T. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2005.10.011 · Cited by 90
Cognitive and emotional alterations in App knock-in mouse models of Aβ amyloidosis
Sakakibara, Y., Sekiya, M., Saito, T., Saido, T. C., & Iijima, K. M. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0446-8 · Cited by 90
Brain protein phosphatase 2A: Developmental regulation and distinct cellular and subcellular localization by B subunits
Strack, S., Zaucha, J. A., Ebner, F. F., Colbran, R. J., & Wadzinski, B. E. (1998) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19980323)392:4 · Cited by 181
Reduction in open field activity in the absence of memory deficits in the AppNL−G−F knock-in mouse model of Alzheimer’s disease
Whyte, L. S., Hemsley, K. M., Lau, A. A., Hassiotis, S., Saito, T., Saido, T. C., Hopwood, J. J., & Sargeant, T. J. (2018) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.09.006 · Cited by 88
Simvastatin therapy prevents brain trauma‐induced increases in β‐amyloid peptide levels
Abrahamson, E. E., Ikonomović, M. D., Dixon, C. E., & DeKosky, S. T. (2009) · Annals of Neurology · doi:10.1002/ana.21731 · Cited by 89
Potential in vivo amelioration by N‐acetyl‐L‐cysteine of oxidative stress in brain in human double mutant APP/PS‐1 knock‐in mice: Toward therapeutic modulation of mild cognitive impairment
Huang, Q., Aluise, C. D., Gururaj Joshi, A., Rukhsana Sultana, A., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22422 · Cited by 89
Aβ solubility and deposition during AD progression and in APP × PS-1 knock-in mice
Murphy, M. P., Beckett, T. L., Ding, Q., Patel, E., Markesbery, W. R., Clair, D. K. S., LeVine, H., & Keller, J. N. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.06.002 · Cited by 87
Transgenic mouse models of Alzheimer's disease
Hock, B. J., & Lamb, B. T. (2001) · Trends in Genetics · doi:10.1016/s0168-9525(01)02449-0 · Cited by 85
Obesity and diabetes cause cognitive dysfunction in the absence of accelerated β-amyloid deposition in a novel murine model of mixed or vascular dementia
Niedowicz, D. M., Reeves, V. L., Platt, T. L., Köhler, K., Beckett, T. L., Powell, D. K., Lee, T., Sexton, T. R., Song, E. S., Brewer, L. D., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-64 · Cited by 85
Comparative analysis of cortical gene expression in mouse models of Alzheimer's disease
Wu, Z., Ciallella, J. R., Flood, D. G., O’Kane, T. M., Bozyczko‐Coyne, D., & Savage, M. J. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.02.010 · Cited by 84
Self-citation
Oxidative damage in brain from human mutant APP/PS-1 double knock-in mice as a function of age
Abdul, H. M., Rukhsana Sultana, A., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.012 · Cited by 81
Protein Kinase C ϵ Suppresses Aβ Production and Promotes Activation of α-Secretase
Zhu, G., Wang, D., Lin, Y., McMahon, T., Koo, E. H., & Messing, R. O. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5273 · Cited by 82
Modeling the β-secretase cleavage site and humanizing amyloid-beta precursor protein in rat and mouse to study Alzheimer’s disease
Serneels, L., T’Syen, D., Pérez‐Benito, L., Theys, T., Holt, M. G., & Strooper, B. D. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00399-z · Cited by 78
APP transgenic mice: their use and limitations
Balducci, C., & Forloni, G. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8141-7 · Cited by 79
Closed head injury in an age-related Alzheimer mouse model leads to an altered neuroinflammatory response and persistent cognitive impairment
Webster, S. J., Van Eldik, L. J., Watterson, D. M., & Bachstetter, A. D. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.0291-15.2015 · Cited by 80
Insulin resistance, neuroinflammation, and Alzheimer’s disease
Najem, D., Bamji‐Mirza, M., Chang, N., Liu, Q. Y., & Zhang, W. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2013-0050 · Cited by 76
A Review of the Current Mammalian Models of Alzheimer’s Disease and Challenges That Need to Be Overcome
Mckean, N. E., Handley, R. R., & Snell, R. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313168 · Cited by 81
Animal models in the study of the biological function of genes on human chromosome 21 and their role in the pathophysiology of Down syndrome
Kola, I. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.10.1713 · Cited by 71
Targeted introduction of V642I mutation in amyloid precursor protein gene causes functional abnormality resembling early stage of Alzheimer's disease in aged mice
Kawasumi, M., Chiba, T., Yamada, M., Miyamae‐Kaneko, M., Matsuoka, M., Nakahara, J., Tomita, T., Iwatsubo, T., Kato, S., Aiso, S., et al. (2004) · European Journal of Neuroscience · doi:10.1111/j.0953-816x.2004.03397.x · Cited by 68
Humanized SFTPA1 and SFTPA2 Transgenic Mice Reveal Functional Divergence of SP-A1 and SP-A2
Wang, G., Guo, X., DiAngelo, S. L., Thomas, N. J., & Floros, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.046243 · Cited by 68
Progress toward valid transgenic mouse models for Alzheimer’s disease
Guénette, S. Y., & Tanzi, R. E. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00042-1 · Cited by 67
Amyloid-β plaque formation and reactive gliosis are required for induction of cognitive deficits in App knock-in mouse models of Alzheimer’s disease
Sakakibara, Y., Sekiya, M., Saito, T., Saido, T. C., & Iijima, K. M. (2019) · BMC Neuroscience · doi:10.1186/s12868-019-0496-6 · Cited by 65
Transgenic animals relevant to Alzheimer’s disease
Seabrook, G. R., & Rosahl, T. W. (1999) · Neuropharmacology · doi:10.1016/s0028-3908(98)00170-1 · Cited by 63
Implanted cannula-mediated repetitive administration of Aβ25–35 into the mouse cerebral ventricle effectively impairs spatial working memory
Yamada, M., Chiba, T., Sasabe, J., Nawa, M., Tajima, H., Niikura, T., Terashita, K., Aiso, S., Kita, Y. A., Matsuoka, M., et al. (2005) · Behavioural Brain Research · doi:10.1016/j.bbr.2005.03.026 · Cited by 69
Danish dementia mice suggest that loss of function and not the amyloid cascade causes synaptic plasticity and memory deficits
Tamayev, R., Matsuda, S., Fà, M., Arancio, O., & D'adamio, L. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011689107 · Cited by 61
Sex and gonadal hormones in mouse models of Alzheimer’s disease: what is relevant to the human condition?
Dubal, D. B., Broestl, L., & Worden, K. (2012) · Biology of Sex Differences · doi:10.1186/2042-6410-3-24 · Cited by 58
Enhanced -secretase processing alters APP axonal transport and leads to axonal defects
Rodrigues, E. M., Weissmiller, A. M., & Goldstein, L. S. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds297 · Cited by 55
Time sequence of oxidative stress in the brain from transgenic mouse models of Alzheimer's disease related to the amyloid-β cascade
Belkacemi, A., & Ramassamy, C. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.020 · Cited by 51
Guinea Pigs as a Nontransgenic Model for APP Processing in Vitro and in Vivo
Beck, M., Bigl, V., & Roßner, S. (2003) · Neurochemical Research · doi:10.1023/a:1022850113083 · Cited by 45
Proteomic analysis of brain proteins in APP/PS‐1 human double mutant knock‐in mice with increasing amyloid β‐peptide deposition: Insights into the effects of in vivo treatment with N‐acetylcysteine as a potential therapeutic intervention in mild cognitive impairment and Alzheimer's disease
Robinson, R. A. S., Gururaj Joshi, A., Huang, Q., Rukhsana Sultana, A., Baker, A. S., Cai, J., Pierce, W. M. J., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2011) · PROTEOMICS · doi:10.1002/pmic.201000523 · Cited by 45
Transgenic models of Alzheimer's disease: Better utilization of existing models through viral transgenesis
Platt, T. L., Reeves, V. L., & Murphy, M. P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.017 · Cited by 48
Gene-Environment Interaction Research and Transgenic Mouse Models of Alzheimer's Disease (Erratum)
Chouliaras, L., Sierksma, A. S. R., Kenis, G., Prickaerts, J., Lemmens, M. A. M., Brasnjevic, I., van Donkelaar, E. L., Martínez‐Martínez, P., Losen, M. H., Baets, M. H. D., et al. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/356862 · Cited by 44
Short-term treatment with tolfenamic acid improves cognitive functions in Alzheimer's disease mice
Subaiea, G. M., Adwan, L. I., Ahmed, A. H., Stevens, K. E., & Zawia, N. H. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.04.002 · Cited by 45
Rank-Order of Potencies for Inhibition of the Secretion of Aβ40 and Aβ42 Suggests That Both Are Generated by a Single γ-Secretase
Durkin, J. T., Murthy, S., Husten, E. J., Trusko, S. P., Savage, M. J., Rotella, D. P., Greenberg, B., & Siman, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20499 · Cited by 43
Self-citation
Age-related loss of phospholipid asymmetry in APP /APP x PS-1 /PS-1 human double mutant knock-in mice: Relevance to Alzheimer disease
Lange, M. L. B., Clair, D. K. S., Markesbery, W. R., Studzinski, C. M., Murphy, M. P., & Butterfield, D. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.01.004 · Cited by 41
Proteomic identification of specifically carbonylated brain proteins in APPNLh/APPNLh×PS-1P264L/PS-1P264L human double mutant knock-in mice model of Alzheimer disease as a function of age
Sultana, R., Robinson, R. A. S., Di Domenico, F., Abdul, H. M., Clair, D. K. S., Markesbery, W. R., Cai, J., Pierce, W. M., & Butterfield, D. A. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.015 · Cited by 41
Modeling Alzheimer’s Disease in Mouse without Mutant Protein Overexpression: Cooperative and Independent Effects of Aβ and Tau
Guo, Q., Li, H., Cole, A. L., Hur, J., Li, Y., & Zheng, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080706 · Cited by 41
Alzheimer's disease-like neuropathology of gene-targeted APP-SLxPS1mut mice expressing the amyloid precursor protein at endogenous levels
Köhler, C., Ebert, U., Baumann, K., & Schröder, H. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.04.009 · Cited by 37
Gavage of D-Ribose induces Aβ-like deposits, Tau hyperphosphorylation as well as memory loss and anxiety-like behavior in mice
Wu, B., Yan, W., Wang, Y., Su, T., Zhou, L., Liu, Y., & He, R. (2015) · Oncotarget · doi:10.18632/oncotarget.6021 · Cited by 36
Gamma-secretase subunit composition and distribution in the presenilin wild-type and mutant mouse brain
Siman, R., & Salidas, S. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.08.028 · Cited by 34
Self-citation
PS Dependent APP Cleavage Regulates Glucosylceramide Synthase and is Affected in Alzheimer's Disease
Grimm, M. O. W., Hundsdörfer, B., Grösgen, S., Mett, J., Zimmer, V. C., Stahlmann, C. P., Haupenthal, V. J., Rothhaar, T. L., Lehmann, J., Pätzold, A. J., et al. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000362987 · Cited by 31
Expression of endogenous mouse APP modulates β-amyloid deposition in hAPP-transgenic mice
Steffen, J., Krohn, M., Schwitlick, C., Brüning, T., Paarmann, K., Pietrzik, C. U., Biverstål, H., Jansone, B., Langer, O., & Pahnke, J. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0448-2 · Cited by 31
Drebrin in Alzheimer’s Disease
Ishizuka, Y., & Hanamura, K. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-4-431-56550-5_12 · Cited by 31
Gene-Environment Interaction Research and Transgenic Mouse Models of Alzheimer's Disease
Chouliaras, L., Sierksma, A. S. R., Kenis, G., Prickaerts, J., Lemmens, M. A. M., Brasnjevic, I., van Donkelaar, E. L., Martínez‐Martínez, P., Losen, M. H., Baets, M. H. D., et al. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/859101 · Cited by 30
Thiorphan-induced neprilysin inhibition raises amyloid β levels in rabbit cortex and cerebrospinal fluid
Newell, A., Sue, L. I., Scott, S., Rauschkolb, P. K., Walker, D. G., Potter, P. E., & Beach, T. G. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00902-9 · Cited by 29
Transgenic Animals in Alzheimer's Disease Research
Sturchler, C., & Sommer, B. (1999) · Reviews in the Neurosciences · doi:10.1515/revneuro.1999.10.1.15 · Cited by 29
Retinal Manifestations of Alzheimer’s Disease
Dehabadi, M. H., Davis, B. M., Wong, T. K. Y., & Cordeiro, M. F. (2014) · Neurodegenerative Disease Management · doi:10.2217/nmt.14.19 · Cited by 28
Of mice and men: more neurobiology in dementia
Codita, A., Winblad, B. G., & Mohammed, A. H. (2006) · Current Opinion in Psychiatry · doi:10.1097/01.yco.0000245757.06374.6a · Cited by 29
Differential transgene expression patterns in Alzheimer mouse models revealed by novel human amyloid precursor protein‐specific antibodies
Höfling, C., Morawski, M., Zeitschel, U., Zanier, E. R., Moschke, K., Serdaroglu, A., Canneva, F., von Hörsten, S., Simoni, M. G. D., Forloni, G., et al. (2016) · Aging Cell · doi:10.1111/acel.12508 · Cited by 28
Generation of mice expressing the human glucagon receptor with a direct replacement vector
Shiao, L., Cascieri, M. A., Trumbauer, M. E., Chen, H., & Sullivan, K. A. (1999) · Transgenic Research · doi:10.1023/a:1008922521461 · Cited by 26
Complexity of Sex Differences and Their Impact on Alzheimer’s Disease
Kadlecová, M., Freude, K., & Haukedal, H. (2023) · Biomedicines · doi:10.3390/biomedicines11051261 · Cited by 27
Animal Models of Alzheimer’s Disease
Newman, M., Kretzschmar, D., Khan, I., Chen, M., Verdile, G., & Lardelli, M. T. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809468-6.00040-1 · Cited by 25
Stability of the distribution of spines containing drebrin A in the sensory cortex layer I of mice expressing mutated APP and PS1 genes
Mahadomrongkul, V., Huerta, P. T., Shirao, T., & Aoki, C. J. (2005) · Brain Research · doi:10.1016/j.brainres.2005.10.012 · Cited by 24
Cerebral Blood Flow Changes after Brain Injury in Human Amyloid-Beta Knock-in Mice
Abrahamson, E., Foley, L., DeKosky, S., Hitchens, T., Ho, C., Kochanek, P., & Ikonomovic, M. (2013) · Journal of Cerebral Blood Flow and Metabolism · doi:10.1038/jcbfm.2013.24 · Cited by 20
Guinea-pig primary cell cultures provide a model to study expression and amyloidogenic processing of endogenous amyloid precursor protein
Beck, M., Brückner, M. K., Holzer, M., Kaap, S., Pannicke, T., Arendt, T., & Bigl, V. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00390-5 · Cited by 21
Context dependent function of APPb enhancer identified using enhancer trap-containing BACs as transgenes in zebrafish
Shakes, L. A., Malcolm, T. L., Allen, K. L., De, S., Harewood, K. R., & Chatterjee, P. K. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn628 · Cited by 20
Beta Amyloid Differently Modulate Nicotinic and Muscarinic Receptor Subtypes which Stimulate in vitro and in vivo the Release of Glycine in the Rat Hippocampus
Zappettini, S., Grilli, M., Olivero, G., Mura, E., Preda, S., Govoni, S. M., Salamone, A., & Marchi, M. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00146 · Cited by 20
Mouse models of neurological disorders—A comparison of heritable and acquired traits
Harper, A. J. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.05.009 · Cited by 21

Authors: Reaume, A. G., Howland, D. S., Trusko, S. P., Savage, M. J., Lang, D. M., Greenberg, B. D., Siman, R., & Scott, R. W.
Corresponding author: Scott, Richard W.
ORCID: Reaume, Andrew G.
Howland, David S.
Greenberg, Barry D.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1996-09
Volume: 271
Issue: 38
Pages: 23380-23388
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.271.38.23380
OpenAlex: W2001834310
Cited by: 150
References: 69
Citations by year: 2026: 2 · 2025: 6 · 2024: 4 · 2023: 2 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 6 · 2016: 2 · 2015: 3 · 2014: 7 · 2013: 7 · 2012: 8
FWCI: 5.27
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8809 d)
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: amyloid precursor protein, amyloidogenic processing, gene-targeted mice, animal models of Alzheimer's disease
MeSH terms: Alzheimer Disease, Animals, Base Sequence, Brain Chemistry, Chimera, Disease Models, Animal, Genotype, Humans, Molecular Sequence Data, Mutation, Peptide Fragments, Endopeptidases, Protein Processing, Post-Translational, Sweden, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Gene Targeting, Mice, Amyloid Precursor Protein Secretases

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

Enhanced Amyloidogenic Processing of the β-Amyloid Precursor Protein in Gene-targeted Mice Bearing the Swedish Familial Alzheimer's Disease Mutations and a “Humanized” Aβ Sequence

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks