Targeting Fyn Kinase in Alzheimer’s Disease

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

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Long‐lasting potentiation of synaptic transmission in the dentate area of the unanaesthetized rabbit following stimulation of the perforant path

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2016 Alzheimer's disease facts and figures

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Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

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Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

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Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

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Diffusible, nonfibrillar ligands derived from Aβ _1–42 are potent central nervous system neurotoxins

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The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease

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Long-Term Potentiation--A Decade of Progress?

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Cellular functions regulated by Src family kinases.

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Two Phase 3 Trials of Bapineuzumab in Mild-to-Moderate Alzheimer's Disease

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Discovery of a Novel, Potent, and Src Family-selective Tyrosine Kinase Inhibitor

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Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · see citing works

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works

Phase 3 Trials of Solanezumab for Mild-to-Moderate Alzheimer's Disease

Doody, R. S., Thomas, R. G., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., Raman, R., Sun, X., Aisen, P. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1312889 · Cited by 1,668 · see citing works

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 · see citing works

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560 · see citing works

AP24534, a Pan-BCR-ABL Inhibitor for Chronic Myeloid Leukemia, Potently Inhibits the T315I Mutant and Overcomes Mutation-Based Resistance

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Aβ Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease

Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188 · see citing works

Impaired Long-Term Potentiation, Spatial Learning, and Hippocampal Development in fyn Mutant Mice

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Incidence of dementia over three decades in the Framingham heart study

Satizabal, C. L., Beiser, A. S., Chouraki, V., Chêne, G., Dufouil, C., & Seshadri, S. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1504327 · Cited by 1,051 · see citing works

Structure and regulation of Src family kinases

Boggon, T. J., & Eck, M. J. (2004) · Oncogene · doi:10.1038/sj.onc.1208081 · Cited by 712 · see citing works

Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons

Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A. O., Wısnıewskı, T., Gunther, E. C., & Strittmatter, S. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3178 · Cited by 654 · see citing works

Amyloid-β/Fyn–Induced Synaptic, Network, and Cognitive Impairments Depend on Tau Levels in Multiple Mouse Models of Alzheimer's Disease

Roberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4152-10.2011 · Cited by 654 · see citing works

NMDA Channel Regulation by Channel-Associated Protein Tyrosine Kinase Src

Yu, X., Askalan, R., Keil, G. J., & Salter, M. W. (1997) · Science · doi:10.1126/science.275.5300.674 · Cited by 608 · see citing works

The hunting of the Src

Martin, G. S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35073094 · Cited by 599 · see citing works

Metabotropic Glutamate Receptor 5 Is a Coreceptor for Alzheimer Aβ Oligomer Bound to Cellular Prion Protein

Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572 · see citing works

Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitors

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Elongation Factor 2 and Fragile X Mental Retardation Protein Control the Dynamic Translation of Arc/Arg3.1 Essential for mGluR-LTD

Park, S., Park, J. M., Kim, S., Kim, J.-A., Shepherd, J. D., Smith-Hicks, C. L., Chowdhury, S., Kaufmann, W., Kuhl, D., Ryazanov, A. G., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.05.023 · Cited by 516 · see citing works

Defective T cell receptor signaling in mice lacking the thymic isoform of p59fyn

Appleby, M. W., Gross, J. A., Cooke, M. P., et al. (1992) · Cell · doi:10.1016/0092-8674(92)90309-z · Cited by 512 · see citing works

A Cell Surface Receptor Complex for Fibrillar β-Amyloid Mediates Microglial Activation

Bamberger, M. E., Harris, M. E., McDonald, D. R., Husemann, J., & Landreth, G. E. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02665.2003 · Cited by 501 · see citing works

Characterization of Fyn-mediated Tyrosine Phosphorylation Sites on GluRε2 (NR2B) Subunit of the N-Methyl-d-aspartate Receptor

Nakazawa, T., Komai, S., Tezuka, T., Hisatsune, C., Umemori, H., Semba, K., Mishina, M., Manabe, T., & Yamamoto, T. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008085200 · Cited by 466 · see citing works

Stimulation of Protein Tyrosine Phosphorylation by NMDA Receptor Activation

Bading, H., & Greenberg, M. E. (1991) · Science · doi:10.1126/science.1715095 · Cited by 463 · see citing works

Tau interacts with src-family non-receptor tyrosine kinases

Lee, G. S., Newman, S. T., Gard, D. L., Band, H., & Panchamoorthy, G. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3167 · Cited by 445 · see citing works

Masitinib (AB1010), a potent and selective tyrosine kinase inhibitor targeting KIT

Dubreuil, P., Letard, S., Ciufolini, M., Gros, L., Humbert, M., Castéran, N., Borge, L., Hajem, B., Lermet, A., Sippl, W., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007258 · Cited by 421 · see citing works

Memory Impairment in Transgenic Alzheimer Mice Requires Cellular Prion Protein

Gimbel, D. A., Nygaard, H. B., Coffey, E. E., Gunther, E. C., Laurén, J., Gimbel, Z. A., & Strittmatter, S. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.0395-10.2010 · Cited by 418 · see citing works

Phosphorylation of Tau by Fyn: Implications for Alzheimer's Disease

Lee, G. S., Thangavel, R., Sharma, V. M., Litersky, J. M., Bhaskar, K., Fang, S. M., Lana, H., Andreadis, A., Hoesen, G. W. V., & Ksiȩżak-Reding, H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4162-03.2004 · Cited by 414 · see citing works

2-Aminothiazole as a Novel Kinase Inhibitor Template. Structure−Activity Relationship Studies toward the Discovery of N -(2-Chloro-6-methylphenyl)-2-[[6-[4-(2-hydroxyethyl)-1- piperazinyl)]-2-methyl-4-pyrimidinyl]amino)]-1,3-thiazole-5-carboxamide (Dasatinib, BMS-354825) as a Potent pan -Src Kinase Inhibitor

Das, J., Chen, P., Norris, D. J., Padmanabha, R., Lin, J., Moquin, R. V., Shen, Z., Cook, L. S., Doweyko, A. M., Pitt, S., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060727j · Cited by 399 · see citing works

Initial events of myelination involve Fyn tyrosine kinase signalling

Umemori, H., Satot, S., Yagi, T., Aizawal, S., & Yamamoto, T. S. (1994) · Nature · doi:10.1038/367572a0 · Cited by 387 · see citing works

PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N -methyl- d -aspartate receptor subunit NR2A

Tezuka, T., Umemori, H., Akiyama, T., Nakanishi, S., & Yamamoto, T. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.435 · Cited by 377 · see citing works

N-(5-Chloro-1,3-benzodioxol-4-yl)-7-[2-(4-methylpiperazin-1-yl)ethoxy]-5- (tetrahydro-2H-pyran-4-yloxy)quinazolin-4-amine, a Novel, Highly Selective, Orally Available, Dual-Specific c-Src/Abl Kinase Inhibitor

Hennequin, L. F., Allen, J. M., Breed, J., Curwen, J., Fennell, M., Green, T. P., der Brempt, C. L., Morgentin, R., Norman, R. A., Olivier, A., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060434q · Cited by 365 · see citing works

Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress

Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., et al. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1080 · Cited by 352 · see citing works

<scp>F</scp>yn inhibition rescues established memory and synapse loss in <scp>A</scp>lzheimer mice

Kaufman, A. C., Salazar, S. V., Haas, L. T., Yang, J., Kostylev, M. A., Jeng, A. T., Robinson, S. A., Gunther, E. C., van Dyck, C. H., Nygaard, H. B., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24394 · Cited by 314 · see citing works

Fyn kinase induces synaptic and cognitive impairments in a transgenic mouse model of Alzheimer’s disease

Chin, J., Palop, J. J., Puoliväli, J., Massaro, C., Bien-Ly, N., Gerstein, H., Scearce-Levie, K., Masliah, E., & Mucke, L. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2980-05.2005 · Cited by 312 · see citing works

CAKβ/Pyk2 Kinase Is a Signaling Link for Induction of Long-Term Potentiation in CA1 Hippocampus

Huang, Y.-Q., Lu, W.-Y., Ali, D. W., Pelkey, K. A., Pitcher, G. M., Lu, Y. M., Aoto, H., Roder, J. C., Sasaki, T., Salter, M. W., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00220-3 · Cited by 274 · see citing works

Site-specific phosphorylation of tau inhibits amyloid-β toxicity in Alzheimer’s mice

Ittner, A., Chua, S. W., Bertz, J., Volkerling, A., van der Hoven, J., Gladbach, A., Przybyla, M., Bi, M., van Hummel, A., Stevens, C. H., et al. (2016) · Science · doi:10.1126/science.aah6205 · Cited by 263 · see citing works

Amyloid-β Receptors: The Good, the Bad, and the Prion Protein

Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256 · see citing works

Preclinical anticancer activity of the potent, oral Src inhibitor AZD0530

Green, T. P., Fennell, M., Whittaker, R., Curwen, J., Jacobs, V., Allen, J., Logie, A., Hargreaves, J., Hickinson, D. M., Wilkinson, R. W., et al. (2009) · Molecular Oncology · doi:10.1016/j.molonc.2009.01.002 · Cited by 238 · see citing works

Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP<i>In Vivo</i>Is Prevented by Immunotargeting Cellular Prion Protein

Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237 · see citing works

Disease-related Modifications in Tau Affect the Interaction between Fyn and Tau

Bhaskar, K., Yen, S.-H. C., & Lee, G. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505895200 · Cited by 219 · see citing works

Optimization of 4-Phenylamino-3-quinolinecarbonitriles as Potent Inhibitors of Src Kinase Activity

Boschelli, D. H., Ye, F., Wang, Y. D., Dutia, M. D., Johnson, S. L., Wu, B., Miller, K., Powell, D. W., Yaczko, D., Young, M., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm0102250 · Cited by 218 · see citing works

Fyn kinase inhibition as a novel therapy for Alzheimer’s disease

Nygaard, H. B., van Dyck, C. H., & Strittmatter, S. M. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt238 · Cited by 201 · see citing works

Regulation of NMDA receptors by the tyrosine kinase Fyn

Trepanier, C. H., Jackson, M. F., & MacDonald, J. F. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08391.x · Cited by 195 · see citing works

Inhibition of AMP-activated protein kinase signaling alleviates impairments in hippocampal synaptic plasticity induced by amyloid β

Ma, T., Chen, Y., Vingtdeux, V., Zhao, H., Viollet, B., Marambaud, P., & Klann, E. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1694-14.2014 · Cited by 191 · see citing works

Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420

Nguyen, T.-H., Liu, J., & Lombroso, P. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111683200 · Cited by 185 · see citing works

Expression of a novel form of the fyn proto-oncogene in hematopoietic cells.

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Masitinib as an adjunct therapy for mild-to-moderate Alzheimer's disease: a randomised, placebo-controlled phase 2 trial

Piette, F., Belmin, J., Vincent, H., Schmidt, N., Pariel, S., Verny, M., Marquis, C., Mely, J., Hugonot-Diener, L., Kinet, J., et al. (2011) · Alzheimer s Research & Therapy · doi:10.1186/alzrt75 · Cited by 176 · see citing works

A phase Ib multiple ascending dose study of the safety, tolerability, and central nervous system availability of AZD0530 (saracatinib) in Alzheimer’s disease

Nygaard, H. B., Wagner, A. F., Bowen, G. S., Good, S. P., MacAvoy, M. G., Strittmatter, K. A., Kaufman, A. C., Rosenberg, B. J., Sekine-Konno, T., Varma, P., et al. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0119-0 · Cited by 164 · see citing works

NMDA Receptor Subunits ϵ1 (NR2A) and ϵ2 (NR2B) Are Substrates for Fyn in the Postsynaptic Density Fraction Isolated from the Rat Brain

Suzuki, T., & Okamuranoji, K. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2662 · Cited by 163 · see citing works

Tyrosine Phosphorylation of Pyk2 Is Selectively Regulated by Fyn During TCR Signaling

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Fyn Kinase Modulates Synaptotoxicity, But Not Aberrant Sprouting, in Human Amyloid Precursor Protein Transgenic Mice

Chin, J., Palop, J. J., Yu, G.-Q., Kojima, N., Masliah, E., & Mucke, L. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0277-04.2004 · Cited by 161 · see citing works

Post-paralysis tyrosine kinase inhibition with masitinib abrogates neuroinflammation and slows disease progression in inherited amyotrophic lateral sclerosis

Trías, E., Ibarburu, S., Barreto‐Núñez, R., Babdor, J., Maciel, T. T., Guillo, M., Gros, L., Dubreuil, P. C., Díaz‐Amarilla, P., Cassina, P., et al. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0620-9 · Cited by 155 · see citing works

Metabotropic glutamate receptor 5 couples cellular prion protein to intracellular signalling in Alzheimer’s disease

Haas, L. T., Salazar, S. V., Kostylev, M. A., Um, J. W., Kaufman, A. C., & Strittmatter, S. M. (2015) · Brain · doi:10.1093/brain/awv356 · Cited by 140 · see citing works

The protein tyrosine kinase, fyn, in Alzheimerʼs disease pathology

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Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models

Kostylev, M. A., Kaufman, A. C., Nygaard, H. B., Patel, P., Haas, L. T., Gunther, E. C., Vortmeyer, A., & Strittmatter, S. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.643577 · Cited by 133 · see citing works

An Integrin–Contactin Complex Regulates CNS Myelination by Differential Fyn Phosphorylation

Laursen, L. S., Chan, C. W., & ffrench‐Constant, C. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5942-08.2009 · Cited by 133 · see citing works

Inhibition of Src kinase activity attenuates amyloid associated microgliosis in a murine model of Alzheimer’s disease

Manocha, G. D., & Combs, C. K. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-117 · Cited by 119 · see citing works

Aberrant Activation of Focal Adhesion Proteins Mediates Fibrillar Amyloid β-Induced Neuronal Dystrophy

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Effects of the Src kinase inhibitor saracatinib (AZD0530) on bone turnover in healthy men: A randomized, double-blind, placebo-controlled, multiple-ascending-dose phase I trial

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Phase I Safety, Pharmacokinetics, and Inhibition of Src Activity Study of Saracatinib in Patients with Solid Tumors

Baselga, J. M., Cervantes, A. M. R., Martinelli, E., Chirivella, I., Hoekman, K., Hurwitz, H. I., Jodrell, D. I., Hamberg, P., Casado, E., Elvin, P., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0748 · Cited by 109 · see citing works

Src family kinases: modulators of neurotransmitter receptor function and behavior

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Expansion of highly differentiated CD8+ T-cells or NK-cells in patients treated with dasatinib is associated with cytomegalovirus reactivation

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αvβ6-Fyn Signaling Promotes Oral Cancer Progression

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Src Family Kinases Are Required for Prolactin Induction of Cell Proliferation

Vara, J. Á. F., Cáceres, M. A. D., Silva, A., & Martı́n-Pérez, J. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.7.2171 · Cited by 91 · see citing works

Localization of the mRNA for a chicken prion protein by in situ hybridization.

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Critical residues involved in tau binding to fyn: implications for tau phosphorylation in Alzheimer’s disease

Lau, D. H. W., Hogseth, M., Phillips, E. C., O’Neill, M. J., Pooler, A. M., Noble, W. J., & Hanger, D. P. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0317-4 · Cited by 89 · see citing works

Metabolic distinction between vesicular and cytosolic GABA in cultured GABAergic neurons using13C magnetic resonance spectroscopy

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Masitinib for the treatment of mild to moderate Alzheimer’s disease

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