Caspase-3 activation as a bifurcation point between plasticity and cell death
Open accessAbstract
Death-mediating proteases such as caspases and caspase-3 in particular, have been implicated in neurodegenerative processes, aging and Alzheimer's disease. However, emerging evidence suggests that in addition to their classical role in cell death, caspases play a key role in modulating synaptic function. It is remarkable that active caspases-3, which can trigger widespread damage and degeneration, aggregates in structures as delicate as synapses and persists in neurons without causing acute cell death. Here, we evaluate this dichotomy, and discuss the hypothesis that caspase-3 may be a bifurcation point in cellular signaling, able to orient the neuronal response to stress down either pathological/apoptotic pathways or towards physiological cellular remodeling. We propose that temporal, spatial and other regulators of caspase activity are key determinants of the ultimate effect of caspase-3 activation in neurons. This concept has implications for differential roles of caspase-3 activation across the lifespan. Specifically, we propose that limited caspase-3 activation is critical for synaptic function in the healthy adult brain while chronic activation is involved in degenerative processes in the aging brain.
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?
In the normal adult brain, activated caspase-3 functions in the remodeling of neuronal processes important for synaptic plasticity and certain forms of memory.
“For example, in the normal adult brain, activated caspase-3 functions in the remodeling of neuronal processes important for synaptic plasticity and certain forms of memory (Snigdha et al., 2012).”
From Programmed cell death in aging (2015) · cites this paper as Snigdha et al., 2012
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
Hengartner, M. O. (2000) · Nature · doi:10.1038/35037710 · Cited by 7,295 · see citing works
Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis
Xia, Z., Dickens, M., Raingeaud, J., Davis, R. J., & Greenberg, M. E. (1995) · Science · doi:10.1126/science.270.5240.1326 · Cited by 5,290 · see citing works
Mammalian MAP kinase signalling cascades
Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,118 · 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
Regulation of Cell Death Protease Caspase-9 by Phosphorylation
Cardone, M. H., Roy, N., Stennicke, H. R., Salvesen, G. S., Franke, T. F., Stanbridge, E. J., Frisch, S. M., & Reed, J. C. (1998) · Science · doi:10.1126/science.282.5392.1318 · Cited by 3,118 · see citing works
Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt
del Peso, L., González‐García, M., Page, C., Herrera, R., & Núñez, G. (1997) · Science · doi:10.1126/science.278.5338.687 · Cited by 2,213 · see citing works
The activation of Akt/PKB signaling pathway and cell survival
Song, G., Ouyang, G., & Bao, S. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00337.x · Cited by 1,891 · see citing works
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592 · see citing works
Caspase structure, proteolytic substrates, and function during apoptotic cell death
Nicholson, D. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400598 · Cited by 1,540 · see citing works
Activation of Mitogen-activated Protein Kinase by H2O2
Guyton, K. Z., Liu, Y., Gorospe, M., Xu, Q., & Holbrook, N. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4138 · Cited by 1,212 · see citing works
Role of Translocation in the Activation and Function of Protein Kinase B
Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J. C., Frech, M., Cron, P., Cohen, P., Lucocq, J. M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31515 · Cited by 1,051 · see citing works
Many cuts to ruin: a comprehensive update of caspase substrates
Fischer, U., Jänicke, R. U., & Schulze‐Osthoff, K. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401160 · Cited by 1,025 · see citing works
Caspase activation: The induced-proximity model
Salvesen, G. S., & Dixit, V. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.10964 · Cited by 932 · see citing works
Caspase function in programmed cell death
Kumar, S. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402060 · Cited by 863 · see citing works
Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works
Too many cooks? Intrinsic and synaptic homeostatic mechanisms in cortical circuit refinement
Turrigiano, G. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-060909-153238 · Cited by 671 · see citing works
Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer's disease
D'Amelio, M., Cavallucci, V., Middei, S., Marchetti, C., Pacioni, S., Ferri, A., Diamantini, A., De Zio, D., Carrara, P., Battistini, L., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2709 · Cited by 572 · see citing works
Akt activation by growth factors is a multiple-step process: the role of the PH domain
Bellacosa, A., Chan, T. O., Ahmed, N. N., Datta, K., Malstrom, S. E., Stokoe, D., McCormick, F. P., Feng, J., & Tsichlis, P. N. (1998) · Oncogene · doi:10.1038/sj.onc.1201947 · Cited by 548 · see citing works
Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420640 · Cited by 543 · see citing works
Self-citationStanciu, M., Wang, Y., Kentor, R., Burke, N., Watkins, S., Kress, G., Reynolds, I., Klann, E., Angiolieri, M. R., Johnson, J. W., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.12200 · Cited by 539 · see citing works
Li, Z., Jo, J., Jia, J., Lo, S., Whitcomb, D. J., Jiao, S., Cho, K., & Sheng, M. (2010) · Cell · doi:10.1016/j.cell.2010.03.053 · Cited by 533 · see citing works
New views of Arc, a master regulator of synaptic plasticity
Shepherd, J. D., & Bear, M. F. (2011) · Nature Neuroscience · doi:10.1038/nn.2708 · Cited by 481 · see citing works
Staurosporine induces apoptosis through both caspase-dependent and caspase-independent mechanisms
Belmokhtar, C. A., Hillion, J., & Ségal-Bendirdjian, E. (2001) · Oncogene · doi:10.1038/sj.onc.1204436 · Cited by 475 · see citing works
Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK
Allan, L. A., MORRICE, N. A., Brady, S. C., Magee, G. J., Pathak, S., & Clarke, P. R. (2003) · Nature Cell Biology · doi:10.1038/ncb1005 · Cited by 474 · see citing works
Local caspase activity directs engulfment of dendrites during pruning
Williams, D. W., Kondo, S., Krzyzanowska, A., Hiromi, Y., & Truman, J. W. (2006) · Nature Neuroscience · doi:10.1038/nn1774 · Cited by 369 · see citing works
Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.06.007 · Cited by 349 · see citing works
NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP
Sun, C. C., Cai, M., Gunasekera, A. H., Meadows, R. P., Wang, H., Chen, J., Zhang, H., Wu, W., Xu, N., Ng, S., et al. (1999) · Nature · doi:10.1038/44617 · Cited by 343 · see citing works
Depletion of GGA3 Stabilizes BACE and Enhances β-Secretase Activity
Tesco, G., Koh, Y. H., Kang, E. L., Cameron, A. N., Das, S., Sena-Esteves, M., Hiltunen, M., Yang, S.-H., Zhong, Z., Shen, Y., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.05.012 · Cited by 337 · see citing works
Aβ1-42 inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3β
Jo, J., Whitcomb, D. J., Olsen, K. M., Kerrigan, T. L., Lo, S.-C., Bru-Mercier, G., Dickinson, B., Scullion, S., Sheng, M., Collingridge, G., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2785 · Cited by 305 · see citing works
The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis
Wilson, R., Goyal, L., Ditzel, M., Zachariou, A., Baker, D. A., Agapite, J., Steller, H., & Meier, P. (2002) · Nature Cell Biology · doi:10.1038/ncb799 · Cited by 296 · see citing works
Du, Y., Bales, K. R., Dodel, R. C., Hamilton‐Byrd, E., Horn, J. W., Czilli, D. L., Simmons, L. K., Ni, B., & Paul, S. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11657 · Cited by 279 · see citing works
Yakovlev, A. G., Ota, K., Wang, G., Movsesyan, V. A., Bao, W., Yoshihara, K., & Faden, A. I. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07439.2001 · Cited by 265 · see citing works
Su, J. H., Zhao, M., Anderson, A. J., Srinivasan, A. N., & Cotman, C. W. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02018-2 · Cited by 260 · see citing works
Self-citationAmyloid β-peptide induces apoptosis-related events in synapses and dendrites
Mattson, M. P., Partin, J. V., & Begley, J. G. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00763-x · Cited by 260 · see citing works
Kuo, C. T., Zhu, S., Younger, S. H., Jan, L. Y., & Jan, Y. N. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.014 · Cited by 257 · see citing works
AMPA receptor downscaling at the onset of Alzheimer's disease pathology in double knockin mice
Chang, E. H., Savage, M. J., Flood, D. G., Thomas, J. M., Levy, R. B., Mahadomrongkul, V., Shirao, T., Aoki, C., & Huerta, P. T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507313103 · Cited by 225 · see citing works
Interleukin-1β impairs brain derived neurotrophic factor-induced signal transduction
Tong, L., Balazs, R., Soiampornkul, R., Thangnipon, W., & Cotman, C. W. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.027 · Cited by 222 · see citing works
Self-citationTong, L., Balazs, R., Thornton, P. L., & Cotman, C. W. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5463-03.2004 · Cited by 221 · see citing works
Self-citationNeural stem cell differentiation is dependent upon endogenous caspase‐3 activity
Fernando, P., Brunette, S., & Megeney, L. A. (2005) · The FASEB Journal · doi:10.1096/fj.04-2981fje · Cited by 210 · see citing works
Caspase-3 Is Enriched in Postsynaptic Densities and Increased in Alzheimer's Disease
Louneva, N., Cohen, J. W., Han, L., Talbot, K., Wilson, R. S., Bennett, D. A., Trojanowski, J. Q., & Arnold, S. E. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080434 · Cited by 207 · see citing works
Bachelder, R. E., Ribick, M. J., Marchetti, A., Falcioni, R., Soddu, S., Davis, K. R., & Mercurio, A. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.1063 · Cited by 180 · see citing works
Role of the Akt/FoxO3a Pathway in TGF-β1–Mediated Mesangial Cell Dysfunction
Kato, M. V., Yuan, H., Xu, Z., Lanting, L. L., Li, S., Wang, M., Hu, M. C. ‐., Reddy, M. A., & Natarajan, R. D. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006070754 · Cited by 174 · see citing works
Ivins, K. J., Bui, E. T. N., & Cotman, C. W. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0228 · Cited by 164 · see citing works
Self-citationCorrelation between Caspase Activation and Neurofibrillary Tangle Formation in Alzheimer’s Disease
Rohn, T. T., Head, E., Su, J. H., Anderson, A. J., Bahr, B. A., Cotman, C. W., & Cribbs, D. H. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63957-0 · Cited by 164 · see citing works
Self-citationMartin, D. S. D., Lonergan, P. E., Boland, B., Fogarty, M. P., Brady, M., Horrobin, D. F., Campbell, V. A., & Lynch, M. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205289200 · Cited by 151 · see citing works
Nonapoptotic Function of BAD and BAX in Long-Term Depression of Synaptic Transmission
Jiao, S., & Li, Z. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.004 · Cited by 143 · see citing works
Glazner, G. W., Chan, S. L., Lu, C., & Mattson, M. P. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-10-03641.2000 · Cited by 134 · see citing works
Inactivation of Effector Caspases through Nondegradative Polyubiquitylation
Ditzel, M., Broemer, M., Tenev, T., Bolduc, C., Lee, T. V., Rigbolt, K. T. G., Elliott, R. J. R., Zvelebil, M., Blagoev, B., Bergmann, A., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.09.025 · Cited by 128 · see citing works
Kritzer, M. F., & Kohama, S. G. (1999) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19990705)409:3 · Cited by 125 · see citing works
Caspase Cleavage Enhances the Apoptosis-Inducing Effects of BAD
Condorelli, F., Salomoni, P., Cotteret, S., Cesi, V., Srinivasula, S. M., Alnemri, E. S., & Calabretta, B. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.9.3025-3036.2001 · Cited by 121 · see citing works
Dynamic Role of Postsynaptic Caspase-3 and BIRC4 in Zebra Finch Song-Response Habituation
Huesmann, G., & Clayton, D. F. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.033 · Cited by 118 · see citing works
Recent advances on neuronal caspases in development and neurodegeneration
Marks, N., & Berg, M. J. (1999) · Neurochemistry International · doi:10.1016/s0197-0186(99)00061-3 · Cited by 109 · see citing works
Changes in Caspase Expression in Alzheimer's Disease: Comparison with Development and Aging
Shimohama, S., Tanino, H., & Fujimoto, S. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0344 · Cited by 107 · see citing works
Lynch, A. M., & Lynch, M. A. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02012.x · Cited by 107 · see citing works
Caspase-mediated Cleavage of DNA Topoisomerase I at Unconventional Sites during Apoptosis
Samejima, K., Svingen, P. A., Basi, G. S., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4335 · Cited by 106 · see citing works
Gillardon, F., Kiprianova, I., Sandkühler, J., Hossmann, K. A., & Spranger, M. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00292-4 · Cited by 105 · see citing works
Zhao, M., Su, J. H., Head, E., & Cotman, C. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.07.006 · Cited by 102 · see citing works
Self-citationThinking Globally, Acting Locally
Turrigiano, G. G., & Nelson, S. B. (1998) · Neuron · doi:10.1016/s0896-6273(00)80607-8 · Cited by 94 · see citing works
Alternative, Nonapoptotic Programmed Cell Death
Castro‐Obregón, S., Rao, R. V., del Rio, G., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312363200 · Cited by 89 · see citing works
Lesuisse, C., & Martin, L. J. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200208000-00005 · Cited by 88 · see citing works
mTOR/S6 Kinase Pathway Contributes to Astrocyte Survival during Ischemia
Pastor, M. D., García‐Yébenes, I., Fradejas‐Villar, N., Pérez‐Ortiz, J. M., Mora-Lee, S., Tranque, P., Moro, M. Á., Pende, M., & Calvo, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.033100 · Cited by 85 · see citing works
Liu, S.-J., Gasperini, R., Foa, L., & Small, D. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-091654 · Cited by 84 · see citing works
Presenilin 1 regulates homeostatic synaptic scaling through Akt signaling
Pratt, K. G., Zimmerman, E. C., Cook, D. G., & Sullivan, J. (2011) · Nature Neuroscience · doi:10.1038/nn.2893 · Cited by 77 · see citing works
Caspase activity plays an essential role in long-term memory
Dash, P. K., Blum, S., & Moore, A. N. (2000) · Neuroreport · doi:10.1097/00001756-200008210-00040 · Cited by 70 · see citing works
Direct Cleavage of AMPA Receptor Subunit GluR1 and Suppression of AMPA Currents by Caspase-3
Mattson, M. P., Lu, C., Fu, W., et al. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:1:1:69 · Cited by 69 · see citing works
Fasulo, L., Ugolini, G., & Cattaneo, A. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-7102 · Cited by 66 · see citing works
Rohn, T. T., Cusack, S. M., Kessinger, S. R., & Oxford, J. T. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.12.029 · Cited by 62 · see citing works
Jackson, T. C., Rani, A., Kumar, A., & Foster, T. C. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.171 · Cited by 58 · see citing works
Central administration of a caspase inhibitor impairs shuttle-box performance in rats
Stepanichev, M. Y., Kudryashova, I. V., Yakovlev, A. A., Onufriev, M. V., Хаспеков, Л. Г., Лыжин, А. А., Лазарева, Н. А., & Gulyaeva, N. V. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.08.010 · Cited by 49 · see citing works
Yang, J.-Y., Michod, D., Walicki, J., & Widmann, C. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.03.043 · Cited by 47 · see citing works
Age-related decrease in constructive activation of Akt/PKB in SAMP10 hippocampus
Nie, K., Yu, J., Fu, Y., Cheng, H., Chen, F.-Y., You, Q., & Han, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.010 · Cited by 36 · see citing works
Caspase activation without apoptosis: insight into Aβ initiation of neurodegeneration
Hyman, B. T. (2010) · Nature Neuroscience · doi:10.1038/nn0111-5 · Cited by 34 · see citing works
Snigdha, S., Berchtold, N. C., Astarita, G., Saing, T., Piomelli, D., & Cotman, C. W. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024652 · Cited by 13 · see citing works
Self-citationde Calignon, A., Spires‐Jones, T. L., & Hyman, B. T. (2010) · médecine/sciences · doi:10.1051/medsci/20102610787 · Cited by 6 · see citing works
Mattson, M. (1999) · doi:10.1002/(sici)1097-4547(19991001)58:1
Flagged first, then by citations
Research works printed but not linked: 2
- [50]Fasulo L Ugolini G Cattaneo A Apoptotic effect of caspase-3 cleaved tau in hippocampal neurons and its potentiation by tau FTDP-mutation N279K J Alzheimers Dis 2005 7 1 3 13 15750210
- [73]Lu C Fu W Salvesen GS Mattson MP Direct cleavage of AMPA receptor subunit GluR1 and suppression of AMPA currents by caspase-3: implications for synaptic plasticity and excitotoxic neuronal death Neuromolecular Med 2002 1 1 69 79 12025817
Cited by
Sorted by citations
Programmed cell death in aging
Tower, J. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.04.002 · Cited by 426 · see citing works
Bioelectric signaling regulates head and organ size during planarian regeneration
Beane, W. S., Morokuma, J., Lemire, J. M., & Levin, M. (2013) · Development · doi:10.1242/dev.086900 · Cited by 155 · see citing works
Kim, W., Ma, L., Lomoio, S., Willen, R., Lombardo, S., Dong, J., Haydon, P. G., & Tesco, G. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0239-7 · Cited by 32 · see citing works
Sinha, S., Patro, N., Tiwari, P. K., & Patro, I. K. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104877 · Cited by 28 · see citing works
Mechanisms of Neuron Loss in Alzheimer’s Disease
Mukhin, V. N., Pavlov, K. I., & Klimenko, V. M. (2017) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-017-0427-x · Cited by 27 · see citing works
- Authors
- Snigdha, S., Smith, E. D., Prieto, G. A., & Cotman, C. W.
- Affiliations
- University of California, Irvine (US)
- Corresponding author
- Snigdha, Shikha
- Venue
- Neuroscience Bulletin
- Published
- 2012-01-25
- Volume
- 28
- Issue
- 1
- Pages
- 14-24
- ISSN
- 1995-8218 (ISSN-L)
- 1673-7067
- PMC
- PMC3838299
- OpenAlex
- W1977709892
- Cited by
- 227
- References
- 75
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 9 · 2023: 9 · 2022: 13 · 2021: 15 · 2020: 11 · 2019: 15 · 2018: 27 · 2017: 21 · 2016: 16 · 2015: 29 · 2014: 22 · 2013: 15 · 2012: 5
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Neuroscience Bulletin (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG012694-16, R01AG012694, R37AG012694)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Keywords
- caspase-3, apoptosis, synaptic plasticity, neurodegeneration, Alzheimer's disease, brain aging, neuronal stress response, caspase regulation, synaptic function, neuronal remodeling
- MeSH terms
- Alzheimer Disease, Animals, Brain, Humans, Neuronal Plasticity, Neurons, Synapses, Signal Transduction, Cell Death, Apoptosis, Mice, Caspase 3
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
