The DOI matches its Crossref record; 797 of the 797 references it cites were found in a registry or an index.
Neuronal Cell Death
Open accessAbstract
Neuronal cell death occurs extensively during development and pathology, where it is especially important because of the limited capacity of adult neurons to proliferate or be replaced. The concept of cell death used to be simple as there were just two or three types, so we just had to work out which type was involved in our particular pathology and then block it. However, we now know that there are at least a dozen ways for neurons to die, that blocking a particular mechanism of cell death may not prevent the cell from dying, and that non-neuronal cells also contribute to neuronal death. We review here the mechanisms of neuronal death by intrinsic and extrinsic apoptosis, oncosis, necroptosis, parthanatos, ferroptosis, sarmoptosis, autophagic cell death, autosis, autolysis, paraptosis, pyroptosis, phagoptosis, and mitochondrial permeability transition. We next explore the mechanisms of neuronal death during development, and those induced by axotomy, aberrant cell-cycle reentry, glutamate (excitoxicity and oxytosis), loss of connected neurons, aggregated proteins and the unfolded protein response, oxidants, inflammation, and microglia. We then reassess which forms of cell death occur in stroke and Alzheimer’s disease, two of the most important pathologies involving neuronal cell death. We also discuss why it has been so difficult to pinpoint the type of neuronal death involved, if and why the mechanism of neuronal death matters, the molecular overlap and interplay between death subroutines, and the therapeutic implications of these multiple overlapping forms of neuronal death.
Overview
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
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
2 retracted
RETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009) · Nature · doi:10.1038/nature07767 · Cited by 992
RetractedValencia, A., Sapp, E., Kimm, J. S., McClory, H., Reeves, P., Alexander, J., Ansong, K. A., Masso, N., Frosch, M., Kegel, K., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/dds516 · Cited by 98
RetractedFerroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y.-J., Jiang, Q., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,304
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,725
Down-Regulation of Na+/K+ATPase Activity by Human Parvovirus B19 Capsid Protein VP1
Almilaji, A., Szteyn, K., Fein, E., Pakladok, T., Munoz, C., Elvira, B., Towhid, S. T., Alesutan, I., Shumilina, E., Bock, C.-T., et al. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350083 · Cited by 8,675
Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, K., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,203
The BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,679
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · cited 1×
“A surrogate marker often used to demonstrate autophagic flux in tissue extracts is the disappearance of the autophagic substrate p62/SQTM1 (51, 532).”
Microglia-mediated neurotoxicity: uncovering the molecular mechanisms
Block, M. L., Zecca, L., & Hong, J.-S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2038 · Cited by 4,110
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988
Pathobiology of ischaemic stroke: an integrated view
Dirnagl, U., Iadecola, C., & Moskowitz, M. A. (1999) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01401-0 · Cited by 3,943
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686
Mechanisms underlying inflammation in neurodegeneration
Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., & Gage, F. H. (2010) · Cell · doi:10.1016/j.cell.2010.02.016 · Cited by 3,580
Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy
Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., Packer, M., Schneider, M. D., & Levine, B. (2005) · Cell · doi:10.1016/j.cell.2005.07.002 · Cited by 3,536
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530
AGEING AND PARKINSON'S DISEASE: SUBSTANTIA NIGRA REGIONAL SELECTIVITY
FEARNLEY, J. M., & LEES, A. J. (1991) · Brain · doi:10.1093/brain/114.5.2283 · Cited by 3,529
Post-embryonic cell lineages of the nematode, Caenorhabditis elegans
Sulston, J. E., & Horvitz, H. R. (1977) · Developmental Biology · doi:10.1016/0012-1606(77)90158-0 · Cited by 3,475
Complement and microglia mediate early synapse loss in Alzheimer mouse models
Hong, S., Beja-Glasser, V. F., Nfonoyim, B. M., Frouin, A., Li, S., Ramakrishnan, S., Merry, K. M., Shi, Q., Rosenthal, A., Barres, B. A., et al. (2016) · Science · doi:10.1126/science.aad8373 · Cited by 3,343
Apoptosis, oncosis, and necrosis. An overview of cell death.
Majno, G., & Joris, I. (1995) · PubMed · Cited by 3,306
Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
Liu, X., Zhang, Z., Ruan, J., Pan, Y., Magupalli, V. G., Wu, H., & Lieberman, J. (2016) · Nature · doi:10.1038/nature18629 · Cited by 3,202
The Nerve Growth Factor 35 Years Later
Levi-Montalcini, R. (1987) · Science · doi:10.1126/science.3306916 · Cited by 3,125
Pyroptosis: Gasdermin-Mediated Programmed Necrotic Cell Death
Shi, J., Gao, W., & Shao, F. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.10.004 · Cited by 3,088
Ferroptosis: Death by Lipid Peroxidation
Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088
Cell death during development of the nervous system
Oppenheim, R. W. (1991) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.14.030191.002321 · Cited by 3,084
Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
Degterev, A., Huang, Z., Boyce, M., Li, Y., Jagtap, P., Mizushima, N., Cuny, G. D., Mitchison, T. J., Moskowitz, M. A., & Yuan, J. (2005) · Nature Chemical Biology · doi:10.1038/nchembio711 · Cited by 3,068
Ischemic Cell Death in Brain Neurons
Lipton, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1431 · Cited by 3,043
Regulation of cell death: the calcium–apoptosis link
Orrenius, S., Zhivotovsky, B., & Nicotera, P. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1150 · Cited by 3,012
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738
Gasdermin D is an executor of pyroptosis and required for interleukin-1β secretion
He, W.-T., Wan, H., Hu, L., Chen, P., Wang, X., Huang, Z., Yang, Z.-H., Zhong, C.-Q., & Han, J. (2015) · Cell Research · doi:10.1038/cr.2015.139 · Cited by 2,517
Ballard, C., Gauthier, S., Corbett, A., Brayne, C., Aarsland, D., & Jones, E. (2011) · The Lancet · doi:10.1016/s0140-6736(10)61349-9 · Cited by 2,336
Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis
Yang, W. S., Kim, K. J., Gaschler, M. M., Patel, M., Shchepinov, M. S., & Stockwell, B. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603244113 · Cited by 2,329
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310
Bloom (2014) · doi:10.1001/jamaneurol.2013.5847 · Cited by 2,194
Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,108 · cited 1×
“Although this study highlights the relative importance of this subset of BH3-only proteins in causing apoptosis in a variety of cell types, the lack of complete phenocopy of the Bax/Bak double knockout argues against the absolute requirement for direct activation for Bax activation or indicate that other direct activa…”
Dixon, S. J., Patel, D. N., Welsch, M., Skouta, R., Lee, E. D., Hayano, M., Thomas, A. G., Gleason, C. E., Tatonetti, N. P., Slusher, B. S., et al. (2014) · eLife · doi:10.7554/elife.02523 · Cited by 2,088
Bonfoco, E., Krainc, D., Ankarcrona, M., Nicotera, P., & Lipton, S. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.16.7162 · Cited by 1,958
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,921
Mitochondria as the central control point of apoptosis
Desagher, S., & Martinou, J.-C. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01803-1 · Cited by 1,913
Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
Kuida, K., Zheng, T. S., Na, S., Kuan, C.-Y., Yang, D., Karasuyama, H., Rakic, P., & Flavell, R. A. (1996) · Nature · doi:10.1038/384368a0 · Cited by 1,882
Yang, W. S., & Stockwell, B. R. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.02.010 · Cited by 1,876
MacDermott, A. B., Mayer, M. L., Westbrook, G. L., Smith, S. J., & Barker, J. L. (1986) · Nature · doi:10.1038/321519a0 · Cited by 1,835
Lipid peroxidation in cell death
Gaschler, M. M., & Stockwell, B. R. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.086 · Cited by 1,828
Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor
Yu, S.-W., Wang, H., Poitras, M. F., Coombs, C., Bowers, W. J., Federoff, H. J., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2002) · Science · doi:10.1126/science.1072221 · Cited by 1,826
Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., & Huang, D. C. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.030 · Cited by 1,816
Ionic dependence of glutamate neurotoxicity
Choi, D. (1987) · The Journal of Neuroscience · doi:10.1523/jneurosci.07-02-00369.1987 · Cited by 1,802
A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738
Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735
Cheng, E. H.-Y. A., Wei, M. C., Weiler, S., Flavell, R. A., Mak, T. W., Lindsten, T., & Korsmeyer, S. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00320-3 · Cited by 1,707
Developmental cell death: morphological diversity and multiple mechanisms
Clarke, P. H. (1990) · Anatomy and Embryology · doi:10.1007/bf00174615 · Cited by 1,695
Blockade of N -Methyl-D-Aspartate Receptors May Protect Against Ischemic Damage in the Brain
Simon, R. P., Swan, J. H., Griffiths, T., & Meldrum, B. S. (1984) · Science · doi:10.1126/science.6093256 · Cited by 1,682
Letai, A., Bassik, M. C., Walensky, L. D., Sorcinelli, M. D., Weiler, S., & Korsmeyer, S. J. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00127-7 · Cited by 1,677
Autophagy in cell death: an innocent convict?
Levine, B. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26390 · Cited by 1,676
Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9
Kuida, K., Haydar, T. F., Kuan, C.-Y., Gu, Y., Taya, C., Karasuyama, H., Su, M. S.-S., Rakic, P., & Flavell, R. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81476-2 · Cited by 1,643
Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635 · cited 1×
“In general, opening of mPTP results in necrotic/oncotic cell death due to energy depletion (39, 489).”
RAS–RAF–MEK-dependent oxidative cell death involving voltage-dependent anion channels
Yagoda, N., von Rechenberg, M., Zaganjor, E., Bauer, A. J., Yang, W. S., Fridman, D. J., Wolpaw, A. J., Smukste, I., Peltier, J. M., Boniface, J. J., et al. (2007) · Nature · doi:10.1038/nature05859 · Cited by 1,631
Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study
Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588
Rogers, C., Fernandes-Alnemri, T., Mayes, L., Alnemri, D., Cingolani, G., & Alnemri, E. S. (2017) · Nature Communications · doi:10.1038/ncomms14128 · Cited by 1,510 · cited 1×
“More recently it was found that DFNA5, a gasdermin D-related protein, can form necrosis-inducing pores at the plasma membrane following caspase-3-dependent cleavage, in a manner analogous to the cleavage and activation of gasdermin D by caspase-1/11 during pyroptosis (577).”
Gardai, S. J., McPhillips, K. A., Frasch, S. C., Janssen, W. J., Starefeldt, A., Murphy-Ullrich, J. E., Bratton, D. L., Oldenborg, P.-A., Michalak, M., & Henson, P. M. (2005) · Cell · doi:10.1016/j.cell.2005.08.032 · Cited by 1,473
Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470
Functions of the neurotrophins during nervous system development: What the knockouts are teaching us
Snider, W. D. (1994) · Cell · doi:10.1016/0092-8674(94)90048-5 · Cited by 1,428
Crosstalk between apoptosis.; necrosis and autophagy
Nikoletopoulou, V., Markaki, M., Palikaras, K., & Tavernarakis, N. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.001 · Cited by 1,366 · cited 1×
“Ischemia initiates apoptosis in the penumbra; however, if apoptotic signaling is compromised, affected cells may still die by necro(pto)sis (409, 506).”
Seglen, P. O., & Gordon, P. B. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.6.1889 · Cited by 1,360
Bredt, D. S., Glatt, C. E., Hwang, P. M., Fotuhi, M., Dawson, T. M., & Snyder, S. H. (1991) · Neuron · doi:10.1016/0896-6273(91)90374-9 · Cited by 1,359
Differential Requirement for Caspase 9 in Apoptotic Pathways In Vivo
Hakem, R., Hakem, A., Duncan, G. S., Henderson, J. T., Woo, M., Soengas, M. S., Elia, A., de la Pompa, J. L., Kagi, D., Khoo, W., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81477-4 · Cited by 1,292
Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278
Cell death by mitotic catastrophe: a molecular definition
Castedo, M., Perfettini, J.-L., Roumier, T., Andreau, K., Medema, R., & Kroemer, G. (2004) · Oncogene · doi:10.1038/sj.onc.1207528 · Cited by 1,269
Apoptotic Mechanisms After Cerebral Ischemia
Broughton, B. R. S., Reutens, D. C., & Sobey, C. G. (2009) · Stroke · doi:10.1161/strokeaha.108.531632 · Cited by 1,266
Varfolomeev, E. E., Schuchmann, M., Luria, V., Chiannilkulchai, N., Beckmann, J. S., Mett, I. L., Rebrikov, D., Brodianski, V. M., Kemper, O. C., Kollet, O., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80609-3 · Cited by 1,234
The Pseudokinase MLKL Mediates Necroptosis via a Molecular Switch Mechanism
Murphy, J. M., Czabotar, P. E., Hildebrand, J. M., Lucet, I. S., Zhang, J.-G., Alvarez-Diaz, S., Lewis, R., Lalaoui, N., Metcalf, D., Webb, A. I., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.06.018 · Cited by 1,220
PET Imaging of Tau Deposition in the Aging Human Brain
Schöll, M., Lockhart, S. N., Schonhaut, D. R., O’Neil, J. P., Janabi, M., Ossenkoppele, R., Baker, S. L., Vogel, J. W., Faria, J., Schwimmer, H. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.028 · Cited by 1,214
Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212
CELL DEATHS IN NORMAL VERTEBRATE ONTOGENY
GLÜCKSMANN, A. (1951) · Biological Reviews · doi:10.1111/j.1469-185x.1951.tb00774.x · Cited by 1,205
Kuwana, T., Bouchier-Hayes, L., Chipuk, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., & Newmeyer, D. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.003 · Cited by 1,185
Tau PET patterns mirror clinical and neuroanatomical variability in Alzheimer’s disease
Ossenkoppele, R., Schonhaut, D. R., Schöll, M., Lockhart, S. N., Ayakta, N., Baker, S. L., O’Neil, J. P., Janabi, M., Lazaris, A., Cantwell, A., et al. (2016) · Brain · doi:10.1093/brain/aww027 · Cited by 1,185
Ferrostatins Inhibit Oxidative Lipid Damage and Cell Death in Diverse Disease Models
Skouta, R., Dixon, S. J., Wang, J., Dunn, D. E., Orman, M., Shimada, K., Rosenberg, P. A., Lo, D. C., Weinberg, J. M., Linkermann, A., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja411006a · Cited by 1,146 · cited 1×
“Overexpression of huntingtin exon-1 fragment with an expanded pathogenic polyglutamine repeat (Q73) in corticostriatal brain slices resulted in death of medium spiny neurons by ferroptosis (634).”
Apaf1 Is Required for Mitochondrial Pathways of Apoptosis and Brain Development
Yoshida, H., Kong, Y.-Y., Yoshida, R., Elia, A. J., Hakem, A., Hakem, R., Penninger, J. M., & Mak, T. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81733-x · Cited by 1,138
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134
Tau pathology and neurodegeneration
Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133
Protection against Fatal Sindbis Virus Encephalitis by Beclin, a Novel Bcl-2-Interacting Protein
Liang, X. H., Kleeman, L. K., Jiang, H. H., Gordon, G., Goldman, J. E., Berry, G., Herman, B., & Levine, B. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.8586-8596.1998 · Cited by 1,132
Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak
Willis, S. N., Fletcher, J. I., Kaufmann, T., van Delft, M. F., Chen, L., Czabotar, P. E., Ierino, H., Lee, E. F., Fairlie, W. D., Bouillet, P., et al. (2007) · Science · doi:10.1126/science.1133289 · Cited by 1,125
Nitric Oxide Activation of Poly(ADP-Ribose) Synthetase in Neurotoxicity
Zhang, J., Dawson, V. L., Dawson, T. M., & Snyder, S. H. (1994) · Science · doi:10.1126/science.8080500 · Cited by 1,118
Excitotoxicity and stroke: Identifying novel targets for neuroprotection
Lai, T. W., Zhang, S., & Wang, Y. T. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.11.006 · Cited by 1,106
Linkermann, A., & Green, D. R. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1310050 · Cited by 1,103
Historical landmarks of autophagy research
Ohsumi, Y. (2014) · Cell Research · doi:10.1038/cr.2013.169 · Cited by 1,089
Martinou, J.-C., Dubois-Dauphin, M., Staple, J. K., Rodriguez, I., Frankowski, H., Missotten, M., Albertini, P., Talabot, D., Catsicas, S., & Pietra, C. (1994) · Neuron · doi:10.1016/0896-6273(94)90266-6 · Cited by 1,087
Chapter 12 Monitoring Autophagic Degradation of p62/SQSTM1
Bjørkøy, G., Lamark, T., Pankiv, S., Øvervatn, A., Brech, A., & Johansen, T. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(08)03612-4 · Cited by 1,069
Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration
Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060
RIP3 mediates the embryonic lethality of caspase-8-deficient mice
Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., & Mocarski, E. S. (2011) · Nature · doi:10.1038/nature09857 · Cited by 1,057
Brown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055
Self-citationPoly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia
Eliasson, M. J. L., Sampei, K., Mandir, A. S., Hurn, P. D., Traystman, R. J., Bao, J., Pieper, A., Wang, Z.-Q., Dawson, T. M., Snyder, S. H., et al. (1997) · Nature Medicine · doi:10.1038/nm1097-1089 · Cited by 1,018
An alternative, nonapoptotic form of programmed cell death
Sperandio, S., de Belle, I., & Bredesen, D. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.26.14376 · Cited by 1,006
Essential versus accessory aspects of cell death: recommendations of the NCCD 2015
Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002
Calcium-dependent phospholipid scrambling by TMEM16F
Suzuki, J., Umeda, M., Sims, P. J., & Nagata, S. (2010) · Nature · doi:10.1038/nature09583 · Cited by 979
Microglia Regulate the Number of Neural Precursor Cells in the Developing Cerebral Cortex
Cunningham, C. L., Martínez-Cerdeño, V., & Noctor, S. C. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.3441-12.2013 · Cited by 976
Novelli, A., Reilly, J. A., Lysko, P. G., & Henneberry, R. C. (1988) · Brain Research · doi:10.1016/0006-8993(88)90765-2 · Cited by 971
Du, H., Guo, L., Fang, F., Chen, D., A Sosunov, A., M McKhann, G., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 932
Dimers of mitochondrial ATP synthase form the permeability transition pore
Giorgio, V., von Stockum, S., Antoniel, M., Fabbro, A., Fogolari, F., Forte, M., Glick, G. D., Petronilli, V., Zoratti, M., Szabó, I., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217823110 · Cited by 922
Calpain and caspase: can you tell the difference?
Wang, K. K. W. (2000) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01479-4 · Cited by 912
Apaf1 (CED-4 Homolog) Regulates Programmed Cell Death in Mammalian Development
Cecconi, F., Alvarez-Bolado, G., Meyer, B. I., Roth, K. A., & Gruss, P. (1998) · Cell · doi:10.1016/s0092-8674(00)81732-8 · Cited by 896
Activation and Cleavage of Caspase-3 in Apoptosis Induced by Experimental Cerebral Ischemia
Namura, S., Zhu, J., Fink, K., Endres, M., Srinivasan, A., Tomaselli, K. J., Yuan, J., & Moskowitz, M. A. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-10-03659.1998 · Cited by 893
The LIR motif – crucial for selective autophagy
Birgisdottir, Å. B., Lamark, T., & Johansen, T. (2013) · Journal of Cell Science · doi:10.1242/jcs.126128 · Cited by 885
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882
Microglial Phagocytosis of Live Neurons
Brown, G. C., & Neher, J. J. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3710 · Cited by 853
Self-citationHambright, W. S., Fonseca, R. S., Chen, L., Na, R., & Ran, Q. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.021 · Cited by 851
Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration
Mandelkow, E.-M., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 847
McCoy, M. K., & Tansey, M. G. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-45 · Cited by 847
Chaperone-mediated autophagy: roles in disease and aging
Cuervo, A. M., & Wong, E. (2014) · Cell Research · doi:10.1038/cr.2013.153 · Cited by 846
Herrero-Mendez, A., Almeida, A., Fernández, E., Maestre, C., Moncada, S., & Bolaños, J. P. (2009) · Nature Cell Biology · doi:10.1038/ncb1881 · Cited by 844
Crompton, M., Ellinger, H., & COSTI, A. (1988) · PubMed Central · Cited by 841
Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
Woo, M., Hakem, R., Soengas, M. S., Duncan, G. S., Shahinian, A., Kagi, D., Hakem, A., McCurrach, M., Khoo, W., Kaufman, S. A., et al. (1998) · Genes & Development · doi:10.1101/gad.12.6.806 · Cited by 840
Mitotic catastrophe: a mechanism for avoiding genomic instability
Vitale, I., Galluzzi, L., Castedo, M., & Kroemer, G. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3115 · Cited by 834
Hara, H., Friedlander, R. M., Gagliardini, V., Ayata, C., Fink, K., Huang, Z., Shimizu-Sasamata, M., Yuan, J., & Moskowitz, M. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.2007 · Cited by 834
Molecular Pathophysiology of Cerebral Hemorrhage: Secondary Brain Injury
Aronowski, J., & Zhao, X. (2011) · Stroke · doi:10.1161/strokeaha.110.596718 · Cited by 832
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
Chen, X., He, W.-T., Hu, L., Li, J., Fang, Y., Wang, X., Xu, X., Wang, Z., Huang, K., & Han, J. (2016) · Cell Research · doi:10.1038/cr.2016.100 · Cited by 831
Pathogenic Lysosomal Depletion in Parkinson's Disease
Dehay, B., Bové, J., Rodríguez-Muela, N., Perier, C., Recasens, A., Boya, P., & Vila, M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1920-10.2010 · Cited by 825
Schinzel, A. C., Takeuchi, O., Huang, Z., Fisher, J. K., Zhou, Z., Rubens, J., Hetz, C., Danial, N. N., Moskowitz, M. A., & Korsmeyer, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505294102 · Cited by 820
MLKL Compromises Plasma Membrane Integrity by Binding to Phosphatidylinositol Phosphates
Dondelinger, Y., Declercq, W., Montessuit, S., Roelandt, R., Goncalves, A., Bruggeman, I., Hulpiau, P., Weber, K., Sehon, C. A., Marquis, R. W., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.026 · Cited by 815
Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D
Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808 · cited 1×
“In general, opening of mPTP results in necrotic/oncotic cell death due to energy depletion (39, 489).”
Zong, W.-X., Lindsten, T., Ross, A. J., MacGregor, G. R., & Thompson, C. B. (2001) · Genes & Development · doi:10.1101/gad.897601 · Cited by 808
Lashuel, H. A., Petre, B. M., Wall, J., Simon, M., Nowak, R. J., Walz, T., & Lansbury, P. T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00735-0 · Cited by 805
Endogenous nitric oxide synthesis: Biological functions and pathophysiology
Bredt, D. S. (1999) · Free Radical Research · doi:10.1080/10715769900301161 · Cited by 796
The Ca2+-induced membrane transition in mitochondria
Haworth, R. A., & Hunter, D. R. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90372-2 · Cited by 793
Mitochondrial Dysfunction Is a Primary Event in Glutamate Neurotoxicity
Schinder, A. F., Olson, E. C., Spitzer, N. C., & Montal, M. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-19-06125.1996 · Cited by 769
Brain homogenates from human tauopathies induce tau inclusions in mouse brain
Clavaguera, F., Akatsu, H., Fraser, G., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 760
Allen, B., Ingram, E., Takao, M., Smith, M. J., Jakes, R., Virdee, K., Yoshida, H., Holzer, M., Craxton, M., Emson, P. C., et al. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-21-09340.2002 · Cited by 751
BAX Is Required for Neuronal Death after Trophic Factor Deprivation and during Development
Deckwerth, T. L., Elliott, J. L., Knudson, C. M., Johnson, E. M., Snider, W. D., & Korsmeyer, S. J. (1996) · Neuron · doi:10.1016/s0896-6273(00)80173-7 · Cited by 749
A Nonapoptotic Cell Death Process, Entosis, that Occurs by Cell-in-Cell Invasion
Overholtzer, M., Mailleux, A. A., Mouneimne, G., Normand, G., Schnitt, S. J., King, R. W., Cibas, E. S., & Brugge, J. S. (2007) · Cell · doi:10.1016/j.cell.2007.10.040 · Cited by 748
Halestrap, A. P., & Davidson, A. M. (1990) · Biochemical Journal · doi:10.1042/bj2680153 · Cited by 747
Autosis and autophagic cell death: the dark side of autophagy
Liu, Y., & Levine, B. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.143 · Cited by 742
p53 Opens the Mitochondrial Permeability Transition Pore to Trigger Necrosis
Vaseva, A. V., Marchenko, N. D., Ji, K., Tsirka, S. E., Holzmann, S., & Moll, U. M. (2012) · Cell · doi:10.1016/j.cell.2012.05.014 · Cited by 740
The neurotrophic factor concept: a reexamination
Korsching, S. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-07-02739.1993 · Cited by 739
The morphology of various types of cell death in prenatal tissues
Schweichel, J. ‐., & Merker, H. ‐. (1973) · Teratology · doi:10.1002/tera.1420070306 · Cited by 738
The acetylation of tau inhibits its function and promotes pathological tau aggregation
Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724
BAX activation is initiated at a novel interaction site
Gavathiotis, E., Suzuki, M., Davis, M. L., Pitter, K., Bird, G. H., Katz, S. G., Tu, H.-C., Kim, H., Cheng, E. H.-Y., Tjandra, N., et al. (2008) · Nature · doi:10.1038/nature07396 · Cited by 700
Death through a tragedy: mitotic catastrophe
Vakifahmetoglu, H., Olsson, M., & Zhivotovsky, B. (2008) · Cell Death & Differentiation · doi:10.1038/cdd.2008.47 · Cited by 700
Spangenberg, E. E., Lee, R. J., Najafi, A. R., Rice, R. A., Elmore, M. R. P., Blurton-Jones, M., West, B. L., & Green, K. N. (2016) · Brain · doi:10.1093/brain/aww016 · Cited by 695
Do Van, B., Gouel, F., Jonneaux, A., Timmerman, K., Gelé, P., Pétrault, M., Bastide, M., Laloux, C., Moreau, C., Bordet, R., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.011 · Cited by 689
dSarm/Sarm1 Is Required for Activation of an Injury-Induced Axon Death Pathway
Osterloh, J. M., Yang, J., Rooney, T. M., Fox, A. N., Adalbert, R., Powell, E. H., Sheehan, A. E., Avery, M. A., Hackett, R., Logan, M. A., et al. (2012) · Science · doi:10.1126/science.1223899 · Cited by 687
Self-citationBal-Price, A., & Brown, G. C. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-17-06480.2001 · Cited by 686
Self-citationLipinski, M. M., Zheng, B., Lu, T., Yan, Z., Py, B. F., Ng, A., Xavier, R. J., Li, C., Yankner, B. A., Scherzer, C. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009485107 · Cited by 680
Heterogeneity of CNS myeloid cells and their roles in neurodegeneration
Prinz, M., Priller, J., Sisodia, S. S., & Ransohoff, R. M. (2011) · Nature Neuroscience · doi:10.1038/nn.2923 · Cited by 674
Salmonella induces macrophage death by caspase‐1‐dependent necrosis
Brennan, M. A., & Cookson, B. T. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02103.x · Cited by 674
Li, S., Jin, M., Koeglsperger, T., Shepardson, N. E., Shankar, G. M., & Selkoe, D. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0203-11.2011 · Cited by 671
Autophagic programmed cell death by selective catalase degradation
Yu, L., Wan, F., Dutta, S., Welsh, S., Liu, Z., Freundt, E., Baehrecke, E. H., & Lenardo, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511288103 · Cited by 667
Lysosomal cell death at a glance
Aits, S., & Jäättelä, M. (2013) · Journal of Cell Science · doi:10.1242/jcs.091181 · Cited by 667
Autophagy Gene-Dependent Clearance of Apoptotic Cells during Embryonic Development
Qu, X., Zou, Z., Sun, Q., Luby-Phelps, K., Cheng, P., Hogan, R. N., Gilpin, C., & Levine, B. (2007) · Cell · doi:10.1016/j.cell.2006.12.044 · Cited by 653
Absence of Wallerian Degeneration does not Hinder Regeneration in Peripheral Nerve
Lunn, E. R., Perry, V. H., Brown, M. C., Rosen, H., & Gordon, S. (1989) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1989.tb00771.x · Cited by 646
Poly(ADP-ribose) (PAR) polymer is a death signal
Andrabi, S. A., Kim, N. S., Yu, S.-W., Wang, H., Koh, D. W., Sasaki, M., Klaus, J. A., Otsuka, T., Zhang, Z., Koehler, R. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606526103 · Cited by 643
Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features
Berghe, T. V., Vanlangenakker, N., Parthoens, E., Deckers, W., Devos, M., Festjens, N., Guerin, C. J., Brunk, U. T., Declercq, W., & Vandenabeele, P. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.184 · Cited by 639
Conradt, B., & Horvitz, H. R. (1998) · Cell · doi:10.1016/s0092-8674(00)81182-4 · Cited by 639
Regulated necrosis: disease relevance and therapeutic opportunities
Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630
Ischemic Brain Injury is Mediated by the Activation of Poly(ADP-Ribose)Polymerase
Endres, M., Wang, Z.-Q., Namura, S., Waeber, C., & Moskowitz, M. A. (1997) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199711000-00002 · Cited by 622
Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo
Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620
RIP3 Induces Apoptosis Independent of Pronecrotic Kinase Activity
Mandal, P., Berger, S. B., Pillay, S., Moriwaki, K., Huang, C., Guo, H., Lich, J. D., Finger, J., Kasparcova, V., Votta, B., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.021 · Cited by 618
Molecular genetics of early-onset Alzheimer’s disease revisited
Cacace, R., Sleegers, K., & Van Broeckhoven, C. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.01.012 · Cited by 617
Humanin peptide suppresses apoptosis by interfering with Bax activation
Guo, B., Zhai, D., Cabezas, E., Welsh, K., Nouraini, S., Satterthwait, A. C., & Reed, J. C. (2003) · Nature · doi:10.1038/nature01627 · Cited by 617
Prevention of Vertebrate Neuronal Death by the crmA Gene
Gagliardini, V., Fernandez, P.-A., Lee, R. K. K., Drexler, H. C. A., Rotello, R. J., Fishman, M. C., & Yuan, J. (1994) · Science · doi:10.1126/science.8303301 · Cited by 612
Wallerian degeneration: an emerging axon death pathway linking injury and disease
Conforti, L., Gilley, J., & Coleman, M. P. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3680 · Cited by 611
Self-citationWallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene
Mack, T. G. A., Reiner, M., Beirowski, B., Mi, W., Emanuelli, M., Wagner, D., Thomson, D., Gillingwater, T., Court, F., Conforti, L., et al. (2001) · Nature Neuroscience · doi:10.1038/nn770 · Cited by 611
Self-citationLiu, Y., Shoji-Kawata, S., Sumpter, R. M., Wei, Y., Ginet, V., Zhang, L., Posner, B., Tran, K. A., Green, D. R., Xavier, R. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1319661110 · Cited by 607
RIPK1 mediates axonal degeneration by promoting inflammation and necroptosis in ALS
Ito, Y., Ofengeim, D., Najafov, A., Das, S., Saberi, S., Li, Y., Hitomi, J., Zhu, H., Chen, H., Mayo, L., et al. (2016) · Science · doi:10.1126/science.aaf6803 · Cited by 606
Preclinical and clinical research on inflammation after intracerebral hemorrhage
Wang, J. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.08.001 · Cited by 602
TAM receptors regulate multiple features of microglial physiology
Fourgeaud, L., Través, P. G., Tufail, Y., Leal-Bailey, H., Lew, E. D., Burrola, P. G., Callaway, P., Zagórska, A., Rothlin, C. V., Nimmerjahn, A., et al. (2016) · Nature · doi:10.1038/nature17630 · Cited by 600
Stepwise Activation of BAX and BAK by tBID, BIM, and PUMA Initiates Mitochondrial Apoptosis
Kim, H., Tu, H.-C., Ren, D., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.030 · Cited by 600
Hildebrand, J. M., Tanzer, M. C., Lucet, I. S., Young, S. N., Spall, S. K., Sharma, P., Pierotti, C., Garnier, J.-M., Dobson, R. C. J., Webb, A. I., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408987111 · Cited by 598
Parthanatos: mitochondrial‐linked mechanisms and therapeutic opportunities
Fatokun, A. A., Dawson, V. L., & Dawson, T. M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12416 · Cited by 594
SARM1 activation triggers axon degeneration locally via NAD + destruction
Gerdts, J., Brace, E. J., Sasaki, Y., DiAntonio, A., & Milbrandt, J. (2015) · Science · doi:10.1126/science.1258366 · Cited by 593
Caspase signalling controls microglia activation and neurotoxicity
Burguillos, M. A., Deierborg, T., Kavanagh, E., Persson, A., Hajji, N., Garcia-Quintanilla, A., Cano, J., Brundin, P., Englund, E., Venero, J. L., et al. (2011) · Nature · doi:10.1038/nature09788 · Cited by 585
Baird, A. E., Benfield, A., Schlaug, G., Siewert, B., Lövblad, K., Edelman, R. R., & Warach, S. (1997) · Annals of Neurology · doi:10.1002/ana.410410506 · Cited by 581
An Autophagic Flux Probe that Releases an Internal Control
Kaizuka, T., Morishita, H., Hama, Y., Tsukamoto, S., Matsui, T., Toyota, Y., Kodama, A., Ishihara, T., Mizushima, T., & Mizushima, N. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.037 · Cited by 575
Czabotar, P. E., Westphal, D., Dewson, G., Ma, S., Hockings, C., Fairlie, W. D., Lee, E. F., Yao, S., Robin, A. Y., Smith, B. J., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.031 · Cited by 573
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
PUMA mediates the apoptotic response to p53 in colorectal cancer cells
Yu, J., Wang, Z., Kinzler, K. W., Vogelstein, B., & Zhang, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2627984100 · Cited by 563
Lovell, J. F., Billen, L. P., Bindner, S., Shamas-Din, A., Fradin, C., Leber, B., & Andrews, D. W. (2008) · Cell · doi:10.1016/j.cell.2008.11.010 · Cited by 563
Microglial Cx3cr1 knockout prevents neuron loss in a mouse model of Alzheimer's disease
Fuhrmann, M., Bittner, T., Jung, C. K. E., Burgold, S., Page, R. M., Mitteregger, G., Haass, C., LaFerla, F. M., Kretzschmar, H., & Herms, J. (2010) · Nature Neuroscience · doi:10.1038/nn.2511 · Cited by 562
Canonical and non-canonical autophagy: variations on a common theme of self-eating?
Codogno, P., Mehrpour, M., & Proikas-Cezanne, T. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3249 · Cited by 549
Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548
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
The preclinical phase of the pathological process underlying sporadic Alzheimer’s disease
Braak, H., & Del Tredici, K. (2015) · Brain · doi:10.1093/brain/awv236 · Cited by 540
NADPH oxidase is the primary source of superoxide induced by NMDA receptor activation
Brennan, A. M., Won Suh, S., Joon Won, S., Narasimhan, P., Kauppinen, T. M., Lee, H., Edling, Y., Chan, P. H., & Swanson, R. A. (2009) · Nature Neuroscience · doi:10.1038/nn.2334 · Cited by 539
Deter, R. L., & de Duve, C. (1967) · The Journal of Cell Biology · doi:10.1083/jcb.33.2.437 · Cited by 538
Cleavage of the Plasma Membrane Na+/Ca2+ Exchanger in Excitotoxicity
Bano, D., Young, K. W., Guerin, C. J., LeFeuvre, R., Rothwell, N. J., Naldini, L., Rizzuto, R., Carafoli, E., & Nicotera, P. (2005) · Cell · doi:10.1016/j.cell.2004.11.049 · Cited by 533
Wang, J.-Z., Xia, Y.-Y., Grundke-Iqbal, I., & Iqbal, K. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-129031 · Cited by 532
Yuan, J., & Horvitz, H. R. (1990) · Developmental Biology · doi:10.1016/0012-1606(90)90174-h · Cited by 529
Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure
Segawa, K., Kurata, S., Yanagihashi, Y., Brummelkamp, T. R., Matsuda, F., & Nagata, S. (2014) · Science · doi:10.1126/science.1252809 · Cited by 525
Oxytosis: a novel form of programmed cell death
Shirlee Tan, B. S. P., David Schubert, B. S. P., & Pamela Maher, B. S. P. (2001) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026013394741 · Cited by 522
Hamelin, L., Lagarde, J., Dorothée, G., Leroy, C., Labit, M., Comley, R. A., de Souza, L. C., Corne, H., Dauphinot, L., Bertoux, M., et al. (2016) · Brain · doi:10.1093/brain/aww017 · Cited by 519
Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits
Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516
The HOPS complex mediates autophagosome–lysosome fusion through interaction with syntaxin 17
Jiang, P., Nishimura, T., Sakamaki, Y., Itakura, E., Hatta, T., Natsume, T., & Mizushima, N. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-08-0447 · Cited by 501
Kamat, P. K., Kalani, A., Rai, S., Swarnkar, S., Tota, S., Nath, C., & Tyagi, N. (2016) · Molecular Neurobiology · doi:10.1007/s12035-014-9053-6 · Cited by 500
Chen, L., Hambright, W. S., Na, R., & Ran, Q. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.680090 · Cited by 498
Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494
Inhibition of Autophagy Prevents Hippocampal Pyramidal Neuron Death after Hypoxic-Ischemic Injury
Koike, M., Shibata, M., Tadakoshi, M., Gotoh, K., Komatsu, M., Waguri, S., Kawahara, N., Kuida, K., Nagata, S., Kominami, E., et al. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070876 · Cited by 486
Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy
Berger, Z., Roder, H., Hanna, A., Carlson, A., Rangachari, V., Yue, M., Wszolek, Z., Ashe, K., Knight, J., Dickson, D., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0587-07.2007 · Cited by 485
Cited by
Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789
Signaling pathways involved in ischemic stroke: molecular mechanisms and therapeutic interventions
Qin, C., Yang, S., Chu, Y.-H., Zhang, H., Pang, X.-W., Chen, L., Zhou, L.-Q., Chen, M., Tian, D.-S., & Wang, W. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01064-1 · Cited by 939
Lee, J.-H., Yang, D.-S., Goulbourne, C. N., Im, E., Stavrides, P., Pensalfini, A., Chan, H., Bouchet-Marquis, C., Bleiwas, C., Berg, M. J., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01084-8 · Cited by 638
Wang, Y., & Kanneganti, T.-D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.038 · Cited by 545
The endotoxin hypothesis of neurodegeneration
Brown, G. C. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1564-7 · Cited by 457
Self-citation
Metadata
- Authors
- Fricker, M., Tolkovsky, A. M., Borutaite, V., Coleman, M., & Brown, G. C.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2018-04-01
- Volume
- 98
- Issue
- 2
- Pages
- 813-880
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2789018622
- Cited by
- 1,108
- References
- 797
- FWCI
- 6.95
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
