Gain-of-function mutations in protein kinase Cα (PKCα) may promote synaptic defects in Alzheimer’s disease
Open accessAbstract
PKCα variants in some patients with Alzheimer’s disease may mediate the pathological effects of amyloid-β.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The PRKCA gene encodes protein kinase Cα (PKCα), which participates in synaptic loss resulting from the accumulation of amyloid-β in AD neuropathology.
“The PRKCA gene encodes protein kinase Cα (PKCα), which participates in synaptic loss resulting from the accumulation of amyloid-β (Aβ) in AD neuropathology [73, 74].”
From Sex-specific DNA methylation differences in Alzheimer’s disease pathology (2021) · cites this paper as [73]
The Abstract identifies PRKCA as the gene encoding PKCα, and the Results (‘PKCα is necessary for the synaptic effects of Aβ’) show that PKCα is required for Aβ-related synaptic depression in mouse hippocampal slices. The Discussion links Aβ accumulation with synaptic loss in AD, but the study does not directly show that PKCα causes synaptic loss in human AD. (LLM, conf=0.82)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The Genome Analysis Toolkit: A MapReduce framework for analyzing next-generation DNA sequencing data
McKenna, A., Hanna, M., Banks, E., Sivachenko, A., Cibulskis, K., Kernytsky, A., Garimella, K., Altshuler, D., Gabriel, S., Daly, M., et al. (2010) · Genome Research · doi:10.1101/gr.107524.110 · Cited by 27,895 · see citing works
Bootstrap methods: another look at the jackknife
Efron, B. (1979) · The Annals of Statistics · doi:10.1214/aos/1176344552 · Cited by 17,602 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429 · see citing works
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · see citing works
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397 · see citing works
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · see citing works
A simple method for organotypic cultures of nervous tissue
Stoppini, L., Buchs, P., & Muller, D. (1991) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(91)90128-m · Cited by 3,097 · see citing works
<i>TREM2</i> Variants in Alzheimer's Disease
Guerreiro, R., Wojtas, A., Bras, J., Carrasquillo, M., Rogaeva, E., Majounie, E., Cruchaga, C., Sassi, C., Kauwe, J. S. K., Younkin, S., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1211851 · Cited by 3,020 · see citing works
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856 · see citing works
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644 · see citing works
Self-citationPlaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works
Trafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works
AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042 · see citing works
Self-citationNeurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000 · see citing works
Protein kinase C, an elusive therapeutic target?
Mochly‐Rosen, D., Das, K., & Grimes, K. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3871 · Cited by 565 · see citing works
A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
Violin, J. D., Zhang, J., Tsien, R. Y., & Newton, A. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302125 · Cited by 552 · see citing works
Self-citationProtein kinase C: poised to signal
Newton, A. C. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00477.2009 · Cited by 520 · see citing works
Self-citationProtein kinase C is regulated in vivo by three functionally distinct phosphorylations
Keranen, L. M., Sonnenburg, E. D., & Newton, A. C. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00277-6 · Cited by 470 · see citing works
Self-citationRare coding variants in the phospholipase D3 gene confer risk for Alzheimer’s disease
Cruchaga, C., Karch, C. M., Jin, S. C., Benitez, B. A., Cai, Y., Guerreiro, R., Harari, O., Norton, J., Budde, J., Bertelsen, S., et al. (2014) · Nature · doi:10.1038/nature12825 · Cited by 461 · see citing works
Inverse association between cancer and Alzheimer's disease: results from the Framingham Heart Study
Driver, J. A., Beiser, A., Au, R., Kreger, B. E., Splansky, G. L., Kurth, T., Kiel, D. P., Lu, K. P., Seshadri, S., & Wolf, P. A. (2012) · BMJ · doi:10.1136/bmj.e1442 · Cited by 425 · see citing works
GEMINI: Integrative Exploration of Genetic Variation and Genome Annotations
Paila, U., Chapman, B., Kirchner, R., & Quinlan, A. R. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003153 · Cited by 423 · see citing works
Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
Sonnenburg, E. D., Toker, A., & Newton, A. C. (1998) · Current Biology · doi:10.1016/s0960-9822(98)00017-7 · Cited by 381 · see citing works
Self-citationAmyloid beta from axons and dendrites reduces local spine number and plasticity
Wei, W., Nguyen, L. N., Kessels, H. W., Hagiwara, H., Sisodia, S., & Malinow, R. (2010) · Nature Neuroscience · doi:10.1038/nn.2476 · Cited by 357 · see citing works
Self-citationResults of a high-resolution genome screen of 437 Alzheimer's Disease families
Blacker, D. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg007 · Cited by 344 · see citing works
Cancer-Associated Protein Kinase C Mutations Reveal Kinase’s Role as Tumor Suppressor
Antal, C. E., Hudson, A., Kang, E., Zanca, C., Wirth, C., Stephenson, N. L., Trotter, E. W., Gallegos, L. L., Miller, C. J., Furnari, F. B., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.001 · Cited by 331 · see citing works
Self-citationAmyloid-Independent Mechanisms in Alzheimer's Disease Pathogenesis
Pimplikar, S. W., Nixon, R. A., Robakis, N. K. R. K., Shen, J., & Tsai, L. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4305-10.2010 · Cited by 281 · see citing works
Specific Interaction of the PDZ Domain Protein PICK1 with the COOH Terminus of Protein Kinase C-α
Staudinger, J. L., Lu, J., & Olson, E. N. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32019 · Cited by 254 · see citing works
Roe, C. M., Behrens, M. I., Xiong, C., Miller, J. P., & Morris, J. C. (2005) · Neurology · doi:10.1212/01.wnl.0000152889.94785.51 · Cited by 225 · see citing works
Metabotropic NMDA receptor function is required for β-amyloid–induced synaptic depression
Kessels, H. W. H. G., Nabavi, S., & Malinow, R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219605110 · Cited by 196 · see citing works
Self-citationGallegos, L. L., Kunkel, M. T., & Newton, A. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603741200 · Cited by 186 · see citing works
Self-citationKinome-wide Decoding of Network-Attacking Mutations Rewiring Cancer Signaling
Creixell, P., Schoof, E. M., Simpson, C. D., Longden, J., Miller, C. J., Lou, H. J., Perryman, L., Cox, T. R., Zivanovic, N., Palmeri, A., et al. (2015) · Cell · doi:10.1016/j.cell.2015.08.056 · Cited by 175 · see citing works
In vivo regulation of protein kinase C by trans-phosphorylation followed by autophosphorylation.
Sonnenburg, E. D., Keranen, L. M., DePaoli-Roach, A. A., & Newton, A. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43883-5 · Cited by 160 · see citing works
Self-citationKnockout of PKCα Enhances Insulin Signaling Through PI3K
Letiges, M., Plomann, M., Standaert, M. L., Bandyopadhyay, G. K., Sajan, M. P., Kanoh, Y., & Farese, R. V. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.4.0809 · Cited by 158 · see citing works
Aβ Oligomer-Induced Synapse Degeneration in Alzheimer’s Disease
Wilcox, K. C., Lacor, P. N., Pitt, J. E., & Klein, W. L. (2011) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-011-9691-4 · Cited by 156 · see citing works
Alzheimer Disease in 2020Preprint
Holtzman, D. M., Mandelkow, E., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011585 · Cited by 151 · see citing works
Wagner, J., von Matt, P., Sedrani, R. C., Albert, R., Cooke, N. G., Ehrhardt, C., Geiser, M., Rummel, G., Stark, W., Strauss, A., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901108b · Cited by 132 · see citing works
A Unique PDZ Ligand in PKCα Confers Induction of Cerebellar Long-Term Synaptic Depression
Leitges, M., Kovac, J., Plomann, M., & Linden, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.10.024 · Cited by 123 · see citing works
Self-citationInteraction with AKAP79 Modifies the Cellular Pharmacology of PKC
Hoshi, N., Langeberg, L. K., Gould, C. M., Newton, A. C., & Scott, J. D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.014 · Cited by 110 · see citing works
Self-citationIdentification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity
Chen, C., Ha, B. H., Thévenin, A. F., Lou, H. J., Zhang, R., Yip, K. Y.-L., Peterson, J. R., Gerstein, M., Kim, P. M., Filippakopoulos, P., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.11.013 · Cited by 102 · see citing works
Verbeek, D. S., Goedhart, J., Bruinsma, L., Sinke, R. J., & Reits, E. A. (2008) · Journal of Cell Science · doi:10.1242/jcs.027698 · Cited by 87 · see citing works
Tagawa, K., Homma, H., Saito, A., Fujita, K., Chen, X., Imoto, S., Oka, T., Ito, H., Motoki, K., Yoshida, C., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddu475 · Cited by 86 · see citing works
Alzheimer disease and cancer risk: a meta-analysis
Shi, H., Tang, B., Liu, Y.-W., Wang, X., & Chen, G. (2014) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-014-1773-5 · Cited by 74 · see citing works
Kinouchi, T., Sorimachi, H., Maruyama, K., Mizuno, K., Ohno, S., Ishiura, S., & Suzuki, K. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00392-m · Cited by 69 · see citing works
O’Neill, A., Gallegos, L. L., Justilien, V., Garcia, E. L., Leitges, M., Fields, A. P., Hall, R. A., & Newton, A. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.294603 · Cited by 64 · see citing works
Self-citationIntramolecular Conformational Changes Optimize Protein Kinase C Signaling
Antal, C. E., Violin, J. D., Kunkel, M. T., Skovsø, S., & Newton, A. C. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.02.008 · Cited by 64 · see citing works
Self-citationSynapto‐depressive effects of amyloid beta require PICK 1
Alfonso, S., Kessels, H. W. H. G., Banos, C. C., Chan, T. R., Lin, E. Y.-S., Kumaravel, G., Scannevin, R. H., Rhodes, K. J., Huganir, R. L., Guckian, K. M., et al. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12499 · Cited by 62 · see citing works
Self-citationIntramolecular C2 Domain-Mediated Autoinhibition of Protein Kinase C βII
Antal, C. E., Callender, J. A., Kornev, A. P., Taylor, S. S., & Newton, A. C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.039 · Cited by 61 · see citing works
Self-citationDetecting Aβ*56 Oligomers in Brain Tissues
Sherman, M. A., & Lesné, S. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-744-0_4 · Cited by 35 · see citing works
Self-citationFunction and Dysfunction of Presenilin
Shen, J. (2013) · Neurodegenerative Diseases · doi:10.1159/000354971 · Cited by 32 · see citing works
Silva, O. A. B. D. C. E., Rebelo, S., Vieira, S. I., Gandy, S., Silva, E. F. D. C. E., & Greengard, P. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05770.x · Cited by 32 · see citing works
Protein Kinase C‐Regulated Aβ Production and Clearance
Kim, T. H., Hinton, D. J., & Choi, D. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/857368 · Cited by 26 · see citing works
Lane, R. F., Small, S. A., Gatson, J. W., Ehrlich, M. E., & Gandy, S. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-62 · Cited by 21 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [14]Alfonso S Kessels HW Banos CC Chan TR Lin ET Kumaravel G Scannevin RH Rhodes KJ Huganir R Guckian KM Dunah AW Malinow R Synapto-depressive effects of amyloid beta require PICK1 Eur J Neurosci 39 1225 1233 2014 24713001 PMC3983572
Cited by
Sorted by citations
López, J. A., González, H. M., & Léger, G. C. (2019) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804766-8.00013-3 · Cited by 834 · see citing works
Synaptic Impairment in Alzheimer’s Disease: A Dysregulated Symphony
Forner, S., Baglietto-Vargas, D., Martini, A. C., Trujillo-Estrada, L., & LaFerla, F. M. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.04.002 · Cited by 430 · see citing works
Protein kinase C: perfectly balanced
Newton, A. C. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1442408 · Cited by 338 · see citing works
Self-citationGAP-43 and BASP1 in Axon Regeneration: Implications for the Treatment of Neurodegenerative Diseases
Chung, D., Shum, A. K., & Caraveo, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.567537 · Cited by 203 · see citing works
AGC kinases, mechanisms of regulation and innovative drug development
Leroux, A. E., Schulze, J. O., & Biondi, R. M. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.05.011 · Cited by 155 · see citing works
Amyloid-β effects on synapses and memory require AMPA receptor subunit GluA3
Reinders, N. R., Pao, Y., Renner, M., Matos, C. D. S., Lodder, T. R., Malinow, R., & Kessels, H. W. H. G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614249113 · Cited by 126 · see citing works
Self-citationDistinct Signaling Pathways Regulate TREM2 Phagocytic and NFκB Antagonistic Activities
Yao, H., Coppola, K., Schweig, J. E., Crawford, F., Mullan, M., & Paris, D. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00457 · Cited by 110 · see citing works
Scalable synthesis of bryostatin 1 and analogs, adjuvant leads against latent HIV
Wender, P. A., Hardman, C., Ho, S., Jeffreys, M. S., Maclaren, J. K., Quiroz, R. V., Ryckbosch, S. M., Shimizu, A., Sloane, J. L., & Stevens, M. C. (2017) · Science · doi:10.1126/science.aan7969 · Cited by 108 · see citing works
Protein kinase C as a tumor suppressor
Newton, A. C. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.04.017 · Cited by 106 · see citing works
Self-citationProkopenko, D., Morgan, S. L., Mullin, K., Hofmann, O., Chapman, B., Kirchner, R., (ADNI), A. D. N. I., Amberkar, S., Wohlers, I., Lange, C., et al. (2021) · Alzheimer's & Dementia · doi:10.1002/alz.12319 · Cited by 107 · see citing works
Self-citationConventional protein kinase C in the brain: 40 years later
Callender, J. A., & Newton, A. C. (2017) · Neuronal Signaling · doi:10.1042/ns20160005 · Cited by 103 · see citing works
Self-citationReversing the Paradigm: Protein Kinase C as a Tumor Suppressor
Newton, A. C., & Brognard, J. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.02.002 · Cited by 100 · see citing works
Self-citationPellegrini, C., Pirazzini, C., Sala, C., Sambati, L., Yusipov, I., Kalyakulina, A., Ravaioli, F., Kwiatkowska, K. M., Durso, D. F., Ivanchenko, M., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.639428 · Cited by 88 · see citing works
Xu, J., Zhang, P., Huang, Y., Zhou, Y., Hou, Y., Bekris, L. M., Lathia, J. D., Chiang, C., Li, L., Pieper, A. A., et al. (2021) · Genome Research · doi:10.1101/gr.272484.120 · Cited by 82 · see citing works
PTEN: Local and Global Modulation of Neuronal Function in Health and Disease
Knafo, S., & Esteban, J. A. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2016.11.008 · Cited by 79 · see citing works
Diacylglycerol kinase control of protein kinase C
Mérida, I., Arranz‐Nicolás, J., Rodríguez‐Rodríguez, C., & Ávila‐Flores, A. (2019) · Biochemical Journal · doi:10.1042/bcj20180620 · Cited by 61 · see citing works
Sex-specific DNA methylation differences in Alzheimer’s disease pathology
Zhang, L., Young, J. I., Gomez, L., Silva, T. C., Schmidt, M. A., Cai, J., Chen, X., Martin, E. R., & Wang, L. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01177-8 · Cited by 58 · see citing works
Quantitative phosphoproteomics uncovers dysregulated kinase networks in Alzheimer’s disease
Morshed, N., Lee, M. J., Rodriguez, F. H., Lauffenburger, D. A., Mastroeni, D., & White, F. M. (2021) · Nature Aging · doi:10.1038/s43587-021-00071-1 · Cited by 58 · see citing works
Protein kinase C mechanisms that contribute to cardiac remodelling
Newton, A. C., Antal, C. E., & Steinberg, S. F. (2016) · Clinical Science · doi:10.1042/cs20160036 · Cited by 58 · see citing works
Self-citationOrtiz-Sanz, C., Balantzategi, U., Quintela‐López, T., Ruiz, A., Luchena, C., Zuazo-Ibarra, J., Capetillo‐Zarate, E., Matute, C., Zugaza, J. L., & Alberdi, E. M. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04687-y · Cited by 55 · see citing works
Drange, O. K., Smeland, O. B., Shadrin, A. A., Finseth, P. I., Witoelar, A., & Frei, O. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00220 · Cited by 53 · see citing works
Tomassoni‐Ardori, F., Fulgenzi, G., Becker, J., Barrick, C. A., Palko, M. E., Kuhn, S. A., Kopardé, V. N., Cam, M. C., Yanpallewar, S. U., Oberdoerffer, S., et al. (2019) · eLife · doi:10.7554/elife.49673 · Cited by 53 · see citing works
Altered translation elongation contributes to key hallmarks of aging in the killifish brain
Fraia, D. D., Marino, A., Lee, J. H., Sacramento, E. K., Baumgart, M., Bagnoli, S., Balla, T., Schalk, F., Kamrad, S., Guan, R., et al. (2025) · Science · doi:10.1126/science.adk3079 · Cited by 55 · see citing works
Synthesis and evaluation of designed PKC modulators for enhanced cancer immunotherapy
Hardman, C., Ho, S., Shimizu, A., Luu-Nguyen, Q. H., Sloane, J. L., Soliman, M. S. A., Marsden, M. D., Zack, J. A., & Wender, P. A. (2020) · Nature Communications · doi:10.1038/s41467-020-15742-7 · Cited by 49 · see citing works
Phosphoproteomics identifies microglial Siglec‐F inflammatory response during neurodegeneration
Morshed, N., Ralvenius, W. T., Nott, A., Watson, L. A., Rodriguez, F. H., Akay, L. A., Joughin, B. A., Pao, P., Penney, J., LaRocque, L. M., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20209819 · Cited by 46 · see citing works
Russo, R., Cattaneo, F., Lippiello, P., Cristiano, C., Zurlo, F., Castaldo, M., Irace, C., Borsello, T., Santamaria, R., Ammendola, R., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.02.025 · Cited by 47 · see citing works
Callender, J. A., Yang, Y., Lordén, G., Stephenson, N. L., Jones, A. C., Brognard, J., & Newton, A. C. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805046115 · Cited by 44 · see citing works
Self-citationLordén, G., Wozniak, J. M., Doré, K., Dozier, L. E., Cates‐Gatto, C., Patrick, G. N., Gonzalez, D. J., Roberts, A. J., Tanzi, R. E., & Newton, A. C. (2022) · Nature Communications · doi:10.1038/s41467-022-34679-7 · Cited by 41 · see citing works
Self-citationSex-specific DNA methylation: impact on human health and development
Govender, P., Ghai, M., & Okpeku, M. (2022) · Molecular Genetics and Genomics · doi:10.1007/s00438-022-01935-w · Cited by 42 · see citing works
REDOR NMR Reveals Multiple Conformers for a Protein Kinase C Ligand in a Membrane Environment
Yang, H., Staveness, D., Ryckbosch, S. M., Axtman, A. D., Loy, B. A., Barnes, A. B., Pande, V. S., Schaefer, J., Wender, P. A., & Cegelski, L. (2018) · ACS Central Science · doi:10.1021/acscentsci.7b00475 · Cited by 37 · see citing works
Protein Kinase C: Targets to Regenerate Brain Injuries?
Geribaldi‐Doldán, N., Gómez‐Oliva, R., Domínguez‐García, S., Nunez‐Abades, P., & Castro, C. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00039 · Cited by 37 · see citing works
Chowdhury, U. N., Ahmad, S., Islam, M. B., Huq, F., Quinn, J. M. W., & Moni, M. A. (2020) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2020.100309 · Cited by 34 · see citing works
Protein Kinase C as a Therapeutic Target in Non-Small Cell Lung Cancer
Sadeghi, M. M., Salama, M. F., & Hannun, Y. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115527 · Cited by 31 · see citing works
Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology
Fujita, K., Chen, X., Homma, H., Tagawa, K., Amano, M., Saito, A., Imoto, S., Akatsu, H., Hashizume, Y., Kaibuchi, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-02821-z · Cited by 31 · see citing works
Petrov, A. M., Mast, N., Li, Y., & Pikuleva, I. A. (2019) · The FASEB Journal · doi:10.1096/fj.201900092r · Cited by 31 · see citing works
HMGB1 signaling phosphorylates Ku70 and impairs DNA damage repair in Alzheimer’s disease pathology
Tanaka, H., Kondo, K., Fujita, K., Homma, H., Tagawa, K., Jin, X., Jin, M., Yoshioka, Y., Takayama, S., Masuda, H., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02671-4 · Cited by 31 · see citing works
PKCα and PKCδ: Friends and Rivals
Black, J. D., Affandi, T., Black, A. R., & Reyland, M. E. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102194 · Cited by 30 · see citing works
Cooke, M., Casado‐Medrano, V., Ann, J., Lee, J., Blumberg, P. M., Abba, M. C., & Kazanietz, M. G. (2019) · Scientific Reports · doi:10.1038/s41598-019-42581-4 · Cited by 28 · see citing works
Lordén, G., & Newton, A. C. (2021) · Neuronal Signaling · doi:10.1042/ns20210036 · Cited by 27 · see citing works
Self-citationCarpenter, C., Zestos, A. G., Altshuler, R. D., Sorenson, R. J., Guptaroy, B., Showalter, H. D., Kennedy, R. T., Jutkiewicz, E. M., & Gnegy, M. E. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2017.95 · Cited by 27 · see citing works
Land, M., & Rubin, C. S. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00192-17 · Cited by 24 · see citing works
The role of PKC/PKR in aging, Alzheimer's disease, and perioperative neurocognitive disorders
Lü, W., Tang, S., Li, A., Huang, Q., Dou, M., Zhang, Y., Hu, X., Chang, R. C., Wong, G. T. C., & Huang, C. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.973068 · Cited by 23 · see citing works
Profiling of Alzheimer’s disease related genes in mild to moderate vitamin D hypovitaminosis
Grimm, M. O. W., Lauer, A. A., Grösgen, S., Thiel, A., Lehmann, J., Winkler, J., Janitschke, D., Herr, C., Beißwenger, C., Bals, R., et al. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.01.015 · Cited by 22 · see citing works
Shim, K.-H., Kim, S.-H., Hur, J., Kim, D., Demirev, A. V., & Yoon, S. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104519 · Cited by 22 · see citing works
Pilo, C. A., Baffi, T. R., Kornev, A. P., Kunkel, M. T., Malfavon, M., Chen, D.-H., Rossitto, L.-A. M., Chen, D. X., Huang, L., Longman, C., et al. (2022) · Science Signaling · doi:10.1126/scisignal.abk1147 · Cited by 21 · see citing works
Self-citationRegulation of spermatid polarity by the actin- and microtubule (MT)-based cytoskeletons
Li, L., Mao, B., Wu, S., Lian, Q., Ge, R., Silvestrini, B., & Cheng, C. Y. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.01.013 · Cited by 20 · see citing works
TASK channels: channelopathies, trafficking, and receptor-mediated inhibition
Inoue, M., Matsuoka, H., Harada, K., Mugishima, G., & Kameyama, M. (2020) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-020-02403-3 · Cited by 20 · see citing works
Zhang, S., An, X., Huang, S., Zeng, L., Xu, Y., Su, D., Qu, Y., Tang, X., Ma, J., Yang, J., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.02.015 · Cited by 20 · see citing works
Muraleedharan, A., Rotem‐Dai, N., Strominger, I., Anto, N. P., Isakov, N., Monsonego, A., & Livneh, E. (2020) · Glia · doi:10.1002/glia.23921 · Cited by 16 · see citing works
Putative role of natural products as Protein Kinase C modulator in different disease conditions
Singh, R. K., Kumar, S., Tomar, M. S., Verma, P. K., Kumar, A., Kumar, S., Kumar, N., Singh, J. P., & Acharya, A. (2021) · DARU Journal of Pharmaceutical Sciences · doi:10.1007/s40199-021-00401-z · Cited by 17 · see citing works
Wu, J., Yarmey, V. R., Yang, O. J., Soderblom, E. J., San‐Miguel, A., & Yan, D. (2025) · Nature Neuroscience · doi:10.1038/s41593-025-01989-0 · Cited by 16 · see citing works
Mechanistic insight of the potential of geraniol against Alzheimer’s disease
Liu, Y., Zhou, S., Huang, X., & Rehman, H. M. (2022) · European journal of medical research · doi:10.1186/s40001-022-00699-8 · Cited by 14 · see citing works
Liu, D., Zinski, A. L., Mishra, A., Noh, H., Park, G.-H., Qin, Y., Olorife, O., Park, J. M., Abani, C. P., Park, J. S., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01654-z · Cited by 14 · see citing works
Impaired biogenesis of basic proteins impacts multiple hallmarks of the aging brainPreprint
Fraia, D. D., Marino, A., Lee, J. H., Sacramento, E. K., Baumgart, M., Bagnoli, S., da Silva, P. T., Sahu, A. K., Siano, G., Tiessen, M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.20.549210 · Cited by 13 · see citing works
Saleh, B., Srikanth, K. D., Sneh, T., Yue, L., Pelech, S., Elliott, E., & Gil-Henn, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169055 · Cited by 10 · see citing works
PKCα Isoform Inhibits Insulin Signaling and Aggravates Neuronal Insulin Resistance
Mishra, D., Reddy, I., & Dey, C. S. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03486-6 · Cited by 10 · see citing works
Cancer-associated mutations in protein kinase C theta are loss-of-function
Hodapp, S. J., Gravel, N., Kannan, N., & Newton, A. C. (2024) · Biochemical Journal · doi:10.1042/bcj20240148 · Cited by 10 · see citing works
Self-citationReinders, N. R., van der Spek, S. J. F., Klaassen, R. V., Koymans, K. J., MacGillavry, H. D., Smit, A. B., & Kessels, H. W. H. G. (2025) · Journal of Neuroscience · doi:10.1523/jneurosci.0393-24.2024 · Cited by 9 · see citing works
Wu, M., Li, Y., Miao, Y., Qiao, H., & Wang, Y. (2023) · Journal of drug targeting · doi:10.1080/1061186x.2023.2245582 · Cited by 9 · see citing works
Fujita, S., Yoshida, S., Matsuki, T., Jaiswal, M. K., & Seki, K. (2020) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000605 · Cited by 9 · see citing works
Capuano, A., Sarsani, V., Tasaki, S., Mehta, R. I., Li, J., Ahima, R., Arnold, S., Bennett, D. A., Petyuk, V., Liang, L.-M., et al. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.14460 · Cited by 9 · see citing works
Balantzategi, U., Gaminde‐Blasco, A., Kearns, C. A., Bayón‐Cordero, L., Sánchez‐Gómez, M. V., Zugaza, J. L., Appel, B., & Alberdi, E. M. (2025) · Glia · doi:10.1002/glia.70015 · Cited by 8 · see citing works
PKCα: Prospects in Regulating Insulin Resistance and AD
Mishra, D., & Dey, C. S. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.03.006 · Cited by 9 · see citing works
PKC in Regenerative Therapy: New Insights for Old Targets
Rui, M., Nasti, R., Bignardi, E., Volpe, S. D., Rossino, G., Rossi, D., & Collina, S. (2017) · Pharmaceuticals · doi:10.3390/ph10020046 · Cited by 8 · see citing works
Wei, J., Wang, Y., Wang, X., Zhang, Y., Zheng, Y., Shao, J., Cheng, W., & Li, Y. (2023) · Fitoterapia · doi:10.1016/j.fitote.2023.105613 · Cited by 7 · see citing works
The KLDpT activation loop motif is critical for MARK kinase activity
Sonntag, T., Moresco, J. J., Yates, J. R., & Montminy, M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0225727 · Cited by 7 · see citing works
Mosna, S., & Dormann, D. (2025) · BioEssays · doi:10.1002/bies.70084 · Cited by 6 · see citing works
Single-residue mutation in protein kinase C toggles between cancer and neurodegeneration
Jones, A. C., Kornev, A. P., Weng, J., Manning, G., Taylor, S. S., & Newton, A. C. (2023) · Biochemical Journal · doi:10.1042/bcj20220397 · Cited by 6 · see citing works
Self-citationGuo, P., Meng, C., Zhang, S., Cai, Y., Huang, J., Shu, J., Wang, J., & Cai, C. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109802 · Cited by 6 · see citing works
Gene co-expression changes underlying the functional connectomic alterations in Alzheimer’s disease
He, B., Gorijala, P., Xie, L., Cao, S., & Yan, J. (2022) · BMC Medical Genomics · doi:10.1186/s12920-022-01244-6 · Cited by 6 · see citing works
Yang, J., Yang, N., Zhao, H., Qiao, Y., Li, Y., Wang, C., Lim, K., Zhang, C., Yang, W., & Lu, L. (2023) · Stem Cell Research & Therapy · doi:10.1186/s13287-023-03463-9 · Cited by 6 · see citing works
Jin, M., Jin, X., Homma, H., Fujita, K., Tanaka, H., Murayama, S., Akatsu, H., Tagawa, K., & Okazawa, H. (2021) · Communications Biology · doi:10.1038/s42003-021-02475-6 · Cited by 5 · see citing works
Ma, X., Zhiming, H., Mingwen, S., Hong, W., Tao, Y., Jun, X., & Gong, N. (2025) · Scientific Reports · doi:10.1038/s41598-025-94861-x · Cited by 5 · see citing works
Gaurón, M. C., Prokopenko, D., Lee, S., Wolfe, S. A., Hecker, J., Willett, J., Waqas, M., Lordén, G., Yang, Y., Mayfield, J. E., et al. (2025) · Science Signaling · doi:10.1126/scisignal.adv0970 · Cited by 7 · see citing works
Self-citationChen, X., Dixit, K., Yang, Y., McDermott, M. I., Imam, H. T., Bankaitis, V. A., & Igumenova, T. I. (2024) · eLife · doi:10.7554/elife.92884 · Cited by 4 · see citing works
Do, A. N., Song, S., Ali, M., Timsina, J., Wang, L., Western, D., Liu, M., Sanford, J., Rosende-Roca, M., Boada, M., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71063 · Cited by 4 · see citing works
Azargoonjahromi, A., Eivazi, M., Nasiri, H., Tarhriz, V., Payandeh, Z., & Initiative, A. D. N. (2025) · Journal of Molecular Neuroscience · doi:10.1007/s12031-025-02333-8 · Cited by 2 · see citing works
Hodapp, S. J., Kao, T. H., Wu, J., Balasuriya, N., Antal, C. E., Taylor, S. S., & Newton, A. C. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110921 · Cited by 2 · see citing works
Self-citationHoffmann, D. B., Ahola, V., Huber, N., Natunen, T., Leskelä, S., Takalo, M., Martiskainen, H., Ballweg, S., Vorontsov, E. A., Selzer, S., et al. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2026.119347 · Cited by 1 · see citing works
Synapse engineering: A new level of brain modulation
Chen, Y., & Geng, Y. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.10.003 · Cited by 1 · see citing works
How can cancer research be illuminated by brain research (and vice versa)?
Mentis, A. A., Papavassiliou, K. A., Piperi, C., & Papavassiliou, A. G. (2023) · International Journal of Cancer · doi:10.1002/ijc.34682 · Cited by 1 · see citing works
Paul Greengard, Ph.D. (1925‐2019)
Gandy, S., & Suzuki, T. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.08.001 · Cited by 1 · see citing works
Farese, R. V., Kindy, M. S., & Sajan, M. P. (2020) · Exon Publications eBooks · doi:10.36255/exonpublications.alzheimersdisease.2020.ch6 · Cited by 1 · see citing works
Science Signaling Podcast for 10 May 2016: PKCα in Alzheimer’s disease
Newton, A. C., Tanzi, R. E., & VanHook, A. M. (2016) · Science Signaling · doi:10.1126/scisignal.aaf9436
Self-citationFRETting over postsynaptic PKC signaling
Dell’Acqua, M. L., & Woolfrey, K. M. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0190-5
Protein Kinase Cγ Mutations Drive Spinocerebellar Ataxia Type 14 by Impairing AutoinhibitionPreprint
Pilo, C. A., Baffi, T. R., Kornev, A. P., Kunkel, M. T., Malfavon, M., Chen, D., Huang, L., Longman, C., Kannan, N., Raskind, W. H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.24.449810
Self-citationNewton, A. C. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101822
Self-citationMira, H., Díez del Corral, R., & Morales, A. V. (2020) · Frontiers research topics · doi:10.3389/978-2-88963-988-5
Newton, A. C. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101822-1
Self-citationEditorial expression of concern
Foley, J. F. (2022) · Science Signaling · doi:10.1126/scisignal.add4323
Rodríguez, D., Montes, L. U., Quiñones, B. J., Zamora, S., Moreno, L., Villamil, W., González‐Giraldo, Y., Báez, S., Forero, D. A., & Trujillo‐Güiza, M. L. (2023) · The Open Psychology Journal · doi:10.2174/0118743501266432231122062610 · Cited by 1 · see citing works
Additional file 1 of Mechanistic insight of the potential of geraniol against Alzheimer’s disease
Liu, Y., Zhou, S., Huang, X., & Rehman, H. M. (2022) · Figshare · doi:10.6084/m9.figshare.20070019
Additional file 2 of Sex-specific DNA methylation differences in Alzheimer’s disease pathology
Zhang, L., Young, J. I., Gomez, L., Silva, T. C., Schmidt, M. A., Cai, J., Chen, X., Martin, E. R., & Wang, L. (2021) · Figshare · doi:10.6084/m9.figshare.14490464
Balantzategi, U., Gaminde‐Blasco, A., Bayón‐Cordero, L., Sánchez‐Gómez, M. V., Zugaza, J. L., Appel, B., & Alberdi, E. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.10.598246
Jiang, M., Shi, T., Miryala, R., Rodriguez, M., Wang, R. S., Sultania, R., Guttman, L. C., Johnston, J., Mulligan, L., Li, Y., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.18.677178
Gene-Exercise Interactions in Amyloid Metabolism and Clearance: Implications for Alzheimer’s Disease
Astorino, M. F., Cipriano, G. L., Anchesi, I., Lui, M., Raffaele, I., Calabrò, M., & Crisafulli, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26199816
Additional file 1 of Sex-specific DNA methylation differences in Alzheimer’s disease pathology
Zhang, L., Young, J. I., Gomez, L., Silva, T. C., Schmidt, M. A., Cai, J., Chen, X., Martin, E. R., & Wang, L. (2021) · Figshare · doi:10.6084/m9.figshare.14490461
Yang, J., Yang, N., Zhao, H., Qiao, Y., Li, Y., Wang, C., Lim, K., Zhang, C., Yang, W., & Lu, L. (2023) · Figshare · doi:10.6084/m9.figshare.24098424
Yang, J., Yang, N., Zhao, H., Qiao, Y., Li, Y., Wang, C., Lim, K., Zhang, C., Yang, W., & Lu, L. (2023) · Figshare · doi:10.6084/m9.figshare.24098421
Yang, J., Yang, N., Zhao, H., Qiao, Y., Li, Y., Wang, C., Lim, K., Zhang, C., Yang, W., & Lu, L. (2023) · Figshare · doi:10.6084/m9.figshare.24098427
- Authors
- Alfonso, S. I., Callender, J. A., Hooli, B., Antal, C. E., Mullin, K., Sherman, M. A., Lesné, S. E., Leitges, M., Newton, A. C., Tanzi, R. E., & Malinow, R.
- Affiliations
- University of California San Diego (US)
- Harvard University (US)
- University of Minnesota (US)
- University of Oslo (NO)
- Corresponding author
- Alfonso, Stephanie I.
- Callender, Julia A.
- Hooli, Basavaraj
- Antal, Corina E.
- Newton, Alexandra C.
- Tanzi, Rudolph E.
- Malinow, Roberto
- ORCID
- Venue
- Science Signaling
- Published
- 2016-05-10
- Volume
- 9
- Issue
- 427
- Pages
- ra47-ra47
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- PMC
- PMC5154619
- OpenAlex
- W2359021079
- Cited by
- 103
- References
- 54
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 4 · 2023: 12 · 2022: 11 · 2021: 14 · 2020: 9 · 2019: 12 · 2018: 7 · 2017: 11 · 2016: 5
- FWCI
- 9.39
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- NIH (GM43154, MH060009, AG032132, GM007752, DGE1144086)
- Cure Alzheimer's Fund
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, protein kinase C alpha, gain-of-function mutations, amyloid-beta, synaptic dysfunction, late-onset Alzheimer's disease, familial Alzheimer's disease, synaptic depression, hippocampus
- MeSH terms
- Protein Domains, Alzheimer Disease, Animals, Chlorocebus aethiops, Family Health, Hippocampus, Humans, Mutation, Neoplasms, Synapses, Genome, Human, Genome, COS Cells, Neurodegenerative Diseases, Mice, Protein Kinase C-alpha
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