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
Items 601–797 of 797
Hippocampal Damage in the Human Brain after Cardiac Arrest
Fujioka, M., Nishio, K., Miyamoto, S., Hiramatsu, K.-I., Sakaki, T., Okuchi, K., Taoka, T., & Fujioka, S. (2000) · Cerebrovascular Diseases · doi:10.1159/000016018 · Cited by 86
Ambacher, K. K., Pitzul, K. B., Karajgikar, M., Hamilton, A., Ferguson, S. S. G., & Cregan, S. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046885 · Cited by 86
Granulovacuolar degeneration: a neurodegenerative change that accompanies tau pathology
Köhler, C. N. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1562-0 · Cited by 86
The proapoptotic proteins Bax and Bak are not involved in Wallerian degeneration
Whitmore, A. V., Lindsten, T., RAFF, M. C., & Thompson, C. B. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401147 · Cited by 85
Scarlett, J. L., Packer, M. A., Porteous, C. M., & Murphy, M. P. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(96)99426-5 · Cited by 85
Burguillos, M. Á., Hajji, N., Englund, E. M., Persson, A., Cenci, M. A., Machado, A., Cano, J., Joseph, B., & Venero, J. L. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.09.005 · Cited by 84
Wilfling, F., Weber, A., Potthoff, S., Vögtle, F. ‐., Meisinger, C., Paschen, S. A., & Häcker, G. A. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.9 · Cited by 84
Phosphoinositide 3-kinase couples NMDA receptors to superoxide release in excitotoxic neuronal death
Brennan, A., Shen, Y., Benna, J. E., & Swanson, R. A. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.111 · Cited by 84
Cystatin C protects neuronal cells against mutant copper-zinc superoxide dismutase-mediated toxicity
Watanabe, S., Hayakawa, T., Wakasugi, K., & Yamanaka, K. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.459 · Cited by 83
Monsell, S. E., Kukull, W. A., Roher, A. E., Maarouf, C. L., Serrano, G., Beach, T. G., Caselli, R. J., Montine, T. J., & Reiman, E. M. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.1721 · Cited by 82
PolyADP-Ribosylation Is Involved in Neurotrophic Activity
Visochek, L., Steingart, R. A., Vulih-Shultzman, I., Klein, R., Priel, E., Gozes, I., & Cohen‐Armon, M. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0333-05.2005 · Cited by 82
Necroptosis contributes to the NMDA-induced excitotoxicity in rat’s cultured cortical neurons
Li, Y., Yang, X., Ma, C., Qiao, J., & Zhang, C. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.08.037 · Cited by 82
Analysis of the PKC-γ-Related Immunocrossreactive Region of a Novel Leukocyte Protein γ-rp
Smallwood, J. I., & Malawista, S. E. (1999) · Inflammation · doi:10.1023/a:1020265701407 · Cited by 81
Shahani, N., Subramaniam, S., Wolf, T., Tackenberg, C., & Brandt, R. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4245-05.2006 · Cited by 81
Wong, H. K., Fricker, M., Wyttenbach, A., Villunger, A., Michalak, E. M., Strasser, A., & Tolkovsky, A. M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8732-8747.2005 · Cited by 81
Self-citationApaf-1 deficiency and neural tube closure defects are found in fog mice
Honarpour, N., Gilbert, S. L., Lahn, B. T., Wang, X., & Herz, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171283198 · Cited by 81
Yaron, A., & Schuldiner, O. (2016) · Current Biology · doi:10.1016/j.cub.2016.05.025 · Cited by 81
Tau Oligomers as Potential Targets for Immunotherapy for Alzheimers Disease and Tauopathies
A. Lasagna-Reeves, C., L. Castillo-Carranza, D., R. Jackson, G., & Kayed, R. (2011) · Current Alzheimer Research · doi:10.2174/156720511796717177 · Cited by 80
Kitay, B. M., McCormack, R., Wang, Y., Tsoulfas, P., & Zhai, R. G. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt009 · Cited by 80
Wang, L., Wang, T., Li, H., Liu, Q. L., Zhang, Z., Xie, W., Feng, Y., Socorburam, T., Wu, G., Xia, Z., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155723 · Cited by 80
Neuronal death after perinatal cerebral hypoxia‐ischemia: Focus on autophagy—mediated cell death
Descloux, C., Ginet, V., Clarke, P. G. H., Puyal, J., & Truttmann, A. C. (2015) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2015.06.008 · Cited by 79
Lam, T. I., Brennan-Minnella, A. M., Won, S. J., Shen, Y., Hefner, C., Shi, Y., Sun, D., & Swanson, R. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313029110 · Cited by 79
Pallast, S., Arai, K., Pekcec, A., Yiğitkanlı, K., Yu, Z., Wang, X., Lo, E. H., & van Leyen, K. (2010) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.281 · Cited by 79
Hetz, C. A., Thielen, P., Fisher, J. K., Pasinelli, P., Brown, R. H., Korsmeyer, S. J., & Glimcher, L. H. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402166 · Cited by 79
Majd, S., Power, J. H. T., & Grantham, H. J. M. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0211-1 · Cited by 79
Liu, T., Zhao, D.-X., Cui, H., Chen, L., Bao, Y., Wang, Y., & Jiang, J. (2016) · Scientific Reports · doi:10.1038/srep24547 · Cited by 79
Cell Death: History and Future
Zakeri, Z. F., & Lockshin, R. A. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-1-4020-6554-5_1 · Cited by 78
The trophic theory of neural concentrations
Purves, D. (1986) · Trends in Neurosciences · doi:10.1016/0166-2236(86)90155-4 · Cited by 78
Golde, S., Chandran, S., Brown, G. C., & Compston, A. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00973.x · Cited by 77
Self-citationDomańska‐Janik, K., Bużańska, L., Dłużniewska, J., Kozłowska, H., Sarnowska, A., & Zabłocka, B. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2003.11.006 · Cited by 77
The role of PARP activation in glutamate-induced necroptosis in HT-22 cells
Xu, X., Chua, C. C., Zhang, M., Geng, D., Liu, C., Hamdy, R. C., & Chua, B. H. L. (2010) · Brain Research · doi:10.1016/j.brainres.2010.04.080 · Cited by 77
Chen, S.-H., Oyarzabal, E. A., & Hong, J.-S. (2016) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2015.10.001 · Cited by 76
Li, P. A., Kristián, T., He, Q. P., & Siesjö, B. K. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7459 · Cited by 76
Role of cyclophilin D in the resistance of brain mitochondria to the permeability transition
Eliseev, R. A., Filippov, G., Velos, J., VanWinkle, B., Goldman, A. J., Rosier, R. N., & Gunter, T. E. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.022 · Cited by 76
Jiang, X., Li, L., Ying, Z., Pan, C., Huang, S., Li, L., Dai, M., Yan, B., Li, M., Jiang, H., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.016 · Cited by 76
Yin, B., Xu, Y., Wei, R., He, F., Luo, B., & Wang, J. (2015) · Brain Research · doi:10.1016/j.brainres.2015.03.024 · Cited by 75
Calpains Are Downstream Effectors ofbax-Dependent Excitotoxic Apoptosis
D’Orsi, B., Bonner, H. P., Tuffy, L. P., Düßmann, H., Woods, I., Courtney, M. J., Ward, M. W., & Prehn, J. H. M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2345-11.2012 · Cited by 75
Phosphorylation of Puma modulates its apoptotic function by regulating protein stability
Fricker, M., O’Prey, J., Tolkovsky, A. M., & Ryan, K. M. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.38 · Cited by 75
Self-citationPhysiological and Pathophysiological Implications of Synaptic Tau
Regan, P. L., Whitcomb, D. J., & Cho, K. (2016) · The Neuroscientist · doi:10.1177/1073858416633439 · Cited by 75
Impaired protein degradation in FTLD and related disorders
Götzl, J. K., Lang, C. M., Haass, C., & Capell, A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.008 · Cited by 75
Rautureau, G. J. P., Yabal, M., Yang, H. J., Huang, D. C. S., Kvansakul, M., & Hinds, M. G. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.178 · Cited by 74
Krajewska, M., You, Z., Rong, J., Kress, C. L., Huang, X., Yang, J., Kyoda, T., Leyva, R., Banares, S., Hu, Y., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024341 · Cited by 74
AMINO ACID CONTROL OF PROTEIN SYNTHESIS AND DEGRADATION IN ISOLATED RAT HEPATOCYTES*
Seglen, P. O., Solheim, A. E., Grinde, B., Gordon, P. B., Schwarze, P. E., Gjessing, R., & Poli, A. (1980) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1980.tb29510.x · Cited by 74
The Progranulin Cleavage Products, Granulins, Exacerbate TDP-43 Toxicity and Increase TDP-43 Levels
Salazar, D. A., Butler, V. J., Argouarch, A. R., Hsu, T.-Y., Mason, A. R., Nakamura, A., McCurdy, H., Cox, D., Ng, R., Pan, G., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.4808-14.2015 · Cited by 73
Rami, A., Sims, J. A., Botez, G., & Winckler, J. (2003) · Neurochemistry International · doi:10.1016/s0197-0186(02)00194-8 · Cited by 73
Redox Stress and the Contributions of BH3-Only Proteins to Infarction
Webster, K. A., Graham, R. M., Thompson, J. W., Spiga, M., Frazier, D. P., Wilson, A., & Bishopric, N. H. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1667 · Cited by 73
Motor neuron trophic factors: Therapeutic use in ALS?
Gould, T. W., & Oppenheim, R. W. (2010) · Brain Research Reviews · doi:10.1016/j.brainresrev.2010.10.003 · Cited by 73
Aparici, C. M., Karabiyikoglu, M., Goris, M. L., Tait, J. F., Yenari, M. A., & Blankenberg, F. G. (2004) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-004-1473-5 · Cited by 73
Brain μ‐Calpain Autolysis During Global Cerebral Ischemia
Neumar, R. W., Hagle, S. M., DeGracia, D. J., Krause, G. S., & White, B. C. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66010421.x · Cited by 73
Togo, T., & Dickson, D. W. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0520-1 · Cited by 72
Chang, P., Dong, W., Zhang, M., Wang, Z., Wang, Y., Wang, T., Gao, Y. Z., Meng, H., Luo, B., Luo, C., et al. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0132-3 · Cited by 72
Cao, G., Xiao, M., Sun, F., Xiao, X., Pei, W., Li, J., Graham, S. H., Simon, R. P., & Chen, J. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1426-04.2004 · Cited by 72
Sakurai, A., Okamoto, K., Fujita, Y., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010000182 · Cited by 71
Yamada, K. H., Kozlowski, D. A., Seidl, S. E., Lance, S., Wieschhaus, A. J., Sundivakkam, P. C., Tiruppathì, C., Chishti, I., Herman, I. M., Kuchay, S., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302612 · Cited by 71
Lysosomal membrane permeabilization in Parkinson disease
Vila, M., Bové, J., Dehay, B., Rodríguez‐Muela, N., & Boya, P. (2010) · Autophagy · doi:10.4161/auto.7.1.13933 · Cited by 71
Prions: Generation and Spread Versus Neurotoxicity
Halliday, M., Radford, H., & Mallucci, G. R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.568477 · Cited by 71
Umeda, T., Ramser, E. M., Yamashita, M., Nakajima, K., Mori, H., Silverman, M. A., & Tomiyama, T. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0230-2 · Cited by 70
Brennan, A., Shen, Y., Benna, J. E., & Swanson, R. A. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.164 · Cited by 69
The UPR and synaptic dysfunction in neurodegeneration
Freeman, O. J., & Mallucci, G. R. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.029 · Cited by 69
Cyclosporine in acute ischemic stroke
Nighoghossian, N., Berthezène, Y., Mechtouff, L., Derex, L., Cho, T., Ritzenthaler, T., Rheims, S., Chauveau, F., Béjot, Y., Jacquin, A., et al. (2015) · Neurology · doi:10.1212/wnl.0000000000001639 · Cited by 68
NADPH Oxidase: A Potential Target for Treatment of Stroke
Zhang, L., Wu, J., Duan, X., Tian, X., Shen, H., Sun, Q., & Chen, G. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/5026984 · Cited by 68
Inhibition of apoptotic Bax translocation to the mitochondria is a central function of parkin
Charan, R. A., Johnson, B. N., Zaganelli, S., Nardozzi, J. D., & LaVoie, M. J. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.278 · Cited by 67
Liu, R. R., & Murphy, T. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.055301 · Cited by 67
Doti, N., Reuther, C., Scognamiglio, P. L., Dolga, A. M., Plesnila, N., Ruvo, M., & Culmsee, C. (2014) · Cell Death and Disease · doi:10.1038/cddis.2013.518 · Cited by 67
Poly(ADP-Ribose) Polymerase-1 Causes Mitochondrial Damage and Neuron Death Mediated by Bnip3
Lü, P., Kamboj, A. K., Gibson, S. B., & Anderson, C. M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2499-14.2014 · Cited by 67
Nitric oxide‐dependent damage to neuronal mitochondria involves the NMDA receptor
Stewart, V. C., Heslegrave, A., Brown, G. C., Clark, J. B., & Heales, S. (2002) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01878.x · Cited by 67
Self-citationHansson, M. J., Månsson, R., Mattiasson, G., Ohlsson, J., Karlsson, J., Keep, M. F., & Elmér, E. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02400.x · Cited by 67
Piao, C.-S., Loane, D. J., Stoica, B. A., Li, S., Hanscom, M., Cabatbat, R. M., Blomgren, K., & Faden, A. I. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.018 · Cited by 66
Li, X., Lei, P., Tuo, Q., Ayton, S., Li, Q., Moon, S., Volitakis, I., Liu, R., Masters, C. L., Finkelstein, D. I., et al. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0378-2 · Cited by 65
Kuzhandaivel, A., Nistri, A., & Mladinić, M. (2010) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-010-9531-y · Cited by 64
Olsen, O., Kallop, D. Y., McLaughlin, T., Huntwork-Rodriguez, S., Wu, Z., Duggan, C. D., Simon, D. J., Lu, Y., Easley-Neal, C., Takeda, K., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3522-13.2014 · Cited by 64
Microglial NADPH oxidase activation mediates rod cell death in the retinal degeneration in rd mice
Zeng, H., Ding, M., Chen, X.-X., & Lu, Q. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.05.065 · Cited by 64
Engel, T., Plesnila, N., Prehn, J. H. M., & Henshall, D. C. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.26 · Cited by 64
SARM1, Not MyD88, Mediates TLR7/TLR9-Induced Apoptosis in Neurons
Mukherjee, P., Winkler, C. W., Taylor, K. G., Woods, T. A., Nair, V., Khan, B. A., & Peterson, K. E. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500953 · Cited by 64
Smith, M. I., & Deshmukh, M. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402089 · Cited by 63
bcl-2 Overexpression Eliminates Deprivation-Induced Cell Death of Brainstem Auditory Neurons
Mostafapour, S. P., del Puerto, N. M., & Rubel, E. W. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-11-04670.2002 · Cited by 63
Can ‘calpain-cathepsin hypothesis’ explain Alzheimer neuronal death?
Yamashima, T. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.008 · Cited by 63
Tehranian, R., Rose, M. E., Vagni, V., Pickrell, A. M., Griffith, R. P., Liu, H., Clark, R. S. B., Dixon, C. E., Kochanek, P. M., & Graham, S. H. (2008) · Journal of Neurotrauma · doi:10.1089/neu.2007.0441 · Cited by 62
Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage
Yokota, M., Tani, E., Tsubuki, S., Yamaura, I., Nakagaki, I., Hori, S., & Saido, T. C. (1999) · Brain Research · doi:10.1016/s0006-8993(98)01334-1 · Cited by 62
The emerging generality of the neurotrophic hypothesis
Davies, A. M. (1988) · Trends in Neurosciences · doi:10.1016/0166-2236(88)90099-9 · Cited by 62
Baburamani, A. A., Hurling, C., Stolp, H. B., Sobotka, K. S., Gressèns, P., Hagberg, H., & Thornton, C. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160922509 · Cited by 62
Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes
Gillies, L. A., Du, H., Peters, B., Knudson, C. M., Newmeyer, D. D., & Kuwana, T. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-11-0638 · Cited by 61
WEI, T., Kang, Q., Ma, B., Gao, S., Li, X., & Liu, Y. (2014) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2014.2084 · Cited by 60
Li, X., Klaus, J. A., Zhang, J., Xu, Z., Kibler, K. K., Andrabi, S. A., Rao, K., Yang, Z., Dawson, T. M., Dawson, V. L., et al. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06667.x · Cited by 60
Bax Regulates Neuronal Ca2+Homeostasis
D’Orsi, B., Kilbride, S. M., Chen, G., Perez‐Alvarez, S., Bonner, H. P., Pfeiffer, S., Plesnila, N., Engel, T., Henshall, D. C., Düßmann, H., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2453-14.2015 · Cited by 59
Necrostatin-1 Reduces Neurovascular Injury after Intracerebral Hemorrhage
King, M. D., Whitaker-Lea, W. A., Campbell, J. M., Alleyne, C. H., & Dhandapani, K. M. (2014) · International Journal of Cell Biology · doi:10.1155/2014/495817 · Cited by 59
The First Molecular Evidence That Autophagy Relates Rimmed Vacuole Formation in Chloroquine Myopathy
Suzuki, T., Nakagawa, M. M., Yoshikawa, A., Sasagawa, N., Yoshimori, T., Ohsumi, Y., Nishino, I., Ishiura, S., & Nonaka, I. (2002) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a003147 · Cited by 59
AIF, reactive oxygen species, and neurodegeneration: A “complex” problem
Polster, B. M. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.12.002 · Cited by 59
AIP-1 ameliorates β-amyloid peptide toxicity in a Caenorhabditis elegans Alzheimer's disease model
Hassan, W. M., Merin, D. A., Fonte, V. G., & Link, C. D. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp209 · Cited by 59
Mouw, G., Zechel, J. L., Zhou, Y., Lust, W. D., Selman, W. R., & Ratcheson, R. A. (2002) · Metabolic Brain Disease · doi:10.1023/a:1019921904378 · Cited by 58
A DR6/p75NTR complex is responsible for β-amyloid-induced cortical neuron death
Hu, Y., Lee, X., Shao, Z., Apicco, D. J., Huang, G., Gong, B., Pepinsky, R. B., & Mi, S. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.110 · Cited by 58
Tomashevski, A., Webster, D. R., Grammas, P., Gorospe, M., & Kruman, I. I. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2009.221 · Cited by 57
Kins, S., Lauther, N., Szodorai, A., & Beyreuther, K. T. (2006) · Neurodegenerative Diseases · doi:10.1159/000095259 · Cited by 57
Yu, W., Mechawar, N., Krantic, S. M., & Quirion, R. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090496 · Cited by 57
Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies
Iyer, S., Anwari, K., Alsop, A. E., Yuen, W. S., Huang, D. C. S., Carroll, J., Smith, N. A., Smith, B. J., Dewson, G., & Kluck, R. M. (2016) · Nature Communications · doi:10.1038/ncomms11734 · Cited by 57
Sadasivan, S., Zhang, Z., Larner, S. F., Liu, M. C., Zheng, W., Kobeissy, F. H., Hayes, R. L., & Wang, K. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-21 · Cited by 56
Caspase‐6 as a novel early target in the treatment of Alzheimer's disease
LeBlanc, A. C. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12250 · Cited by 56
Canudas, A. M., Pezzi, S., Canals, J. M., Pallàs, M., & Alberch, J. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.11.012 · Cited by 56
Carlo, M. D. (2009) · European Biophysics Journal · doi:10.1007/s00249-009-0439-8 · Cited by 56
D’Orsi, B., Engel, T., Pfeiffer, S., Nandi, S., Kaufmann, T., Henshall, D. C., & Prehn, J. H. M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3780-15.2016 · Cited by 56
Proteolytic Cleavage of Polymeric Tau Protein by Caspase-3: Implications for Alzheimer Disease
Jarero-Basulto, J. J., Luna‐Muñoz, J., Mena, R., Krištofíková, Z., Řípová, D., Perry, G. L., Binder, L. I., & García‐Sierra, F. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000013 · Cited by 55
Is Cell Death Primary or Secondary in the Pathophysiology of Idiopathic Parkinson’s Disease?
Schulz‐Schaeffer, W. (2015) · Biomolecules · doi:10.3390/biom5031467 · Cited by 54
Kallop, D. Y., Meilandt, W. J., Gogineni, A., Easley-Neal, C., Wu, T., Jubb, A. M., Yaylaoglu, M., Shamloo, M., Tessier-Lavigne, M., Scearce-Levie, K., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4963-13.2014 · Cited by 54
Hernandes, M. S., Santos, G. D. R., Café-Mendes, C. C., Lima, L. S., Scavone, C., Munhoz, C. D., & Britto, L. R. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075532 · Cited by 54
NADPH Oxidase-2: Linking Glucose, Acidosis, and Excitotoxicity in Stroke
Brennan, A., Won, S. J., & Swanson, R. A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5767 · Cited by 54
Tolnay, M., & Probst, A. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00250-x · Cited by 54
Postnatal neuronal apoptosis in the cerebral cortex: Physiological and pathophysiological mechanisms
Nikolić, M., Gardner, H., & Tucker, K. L. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.09.035 · Cited by 53
Genetic iron chelation protects against proteasome inhibition-induced dopamine neuron degeneration
Zhu, W., Li, X., Xie, W., Luo, F., Kaur, D., Andersen, J. K., Jankovic, J. J., & Le, W. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.09.024 · Cited by 53
Autophagy and checkpoints for intracellular pathogen defense
Paulus, G. L. C., & Xavier, R. J. (2014) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000134 · Cited by 53
Strosznajder, R. P., Gadamski, R., Czapski, G. A., Jęśko, H. M., & Strosznajder, J. B. (2003) · Journal of Molecular Neuroscience · doi:10.1385/jmn:20:1:61 · Cited by 52
Copani, A., Caraci, F., Hoozemans, J. J. M., Calafiore, M., Sortino, M. A., & Nicoletti, F. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.016 · Cited by 51
NADPH Oxidase and the Degeneration of Dopaminergic Neurons in Parkinsonian Mice
Hernandes, M. S., Café-Mendes, C. C., & Britto, L. R. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/157857 · Cited by 51
Zhao, K., Zhou, H., Zhao, X., Wolff, D. W., Tu, Y., Liu, H., Wei, T., & Yang, F. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m027557 · Cited by 51
Bambrick, L. L., Chandrasekaran, K., Mehrabian, Z., Wright, C. L., Krueger, B. K., & Fiskum, G. M. (2006) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9004-7 · Cited by 51
Injury site‐specific targeting of complement inhibitors for treating stroke
Alawieh, A. M., & Tomlinson, S. (2016) · Immunological Reviews · doi:10.1111/imr.12470 · Cited by 51
Li, V., Brustovetsky, T., & Brustovetsky, N. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.02.007 · Cited by 50
Death Commitment Point Is Advanced by Axotomy in Sympathetic Neurons
Fletcher, G. C., Xue, L., Passingham, S. K., & Tolkovsky, A. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.4.741 · Cited by 50
Self-citationBuss, R. R., Gould, T. W., Ma, J., Vinsant, S. L., Prevette, D. M., Winseck, A. K., Toops, K. A., Hammarback, J. A., Smith, T. L., & Oppenheim, R. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3528-06.2006 · Cited by 49
Pathophysiology and Biomarkers in Acute Ischemic Stroke – A Review
Guo, Y. H., Li, P., Guo, Q. J., Shang, K., Yan, D., Du, S., & Lu, Y. (2014) · Tropical Journal of Pharmaceutical Research · doi:10.4314/tjpr.v12i6.35 · Cited by 48
Prions: generation and spread versus neurotoxicity.
Halliday, M., Radford, H. E., & Mallucci, G. R. (2014) · Figshare · doi:10.17863/cam.14500 · Cited by 48
Programmed Cell Death in Neuronal Development
Dekkers, M. P. J., & Barde, Y. (2013) · Science · doi:10.1126/science.1236152 · Cited by 47
Li, T., Lü, C., Xia, Z., Xiao, B., & Luo, Y. (2006) · Brain Research · doi:10.1016/j.brainres.2006.04.131 · Cited by 47
Maor-Nof, M., Romi, E., Shalom, H. S., Ulisse, V., Raanan, C., Nof, A., Leshkowitz, D., Lang, R., & Yaron, A. (2016) · Neuron · doi:10.1016/j.neuron.2016.10.061 · Cited by 47
Wootz, H., Weber, E., Korhonen, L., & Lindholm, D. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.07.048 · Cited by 46
Mechanisms of tau and Aβ-induced excitotoxicity
Pallo, S. P., DiMaio, J., Cook, A., Nilsson, B., & Johnson, G. V. W. (2016) · Brain Research · doi:10.1016/j.brainres.2015.12.048 · Cited by 46
Xue, L., Borutaite, V., & Tolkovsky, A. M. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01181-4 · Cited by 45
Self-citationA Critical role for Bim in retinal ganglion cell death
McKernan, D. P., & Cotter, T. G. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04573.x · Cited by 45
Morkūnienė, R., Čižas, P., Jankevičiūtė, S., Petrolis, R., Arandarčikaitė, O., Kriščiukaitis, A., & Borutaitė, V. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23510 · Cited by 44
Lyons, B., Friedrich, M. G., Raftery, M. J., & Truscott, R. J. W. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b03891 · Cited by 44
Protection Provided by Cyclosporin A against Excitotoxic Neuronal Death Is Genotype Dependent
Santos, J. B., & Schauwecker, P. E. (2003) · Epilepsia · doi:10.1046/j.1528-1157.2003.66302.x · Cited by 42
Caspase substrates and neurodegenerative diseases
Bulat, N., & Widmann, C. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.07.007 · Cited by 42
Nighoghossian, N., Ovize, M., Mewton, N., Ong, E., & Cho, T. (2016) · Cerebrovascular Diseases · doi:10.1159/000446850 · Cited by 42
In vitro glutaminase regulation and mechanisms of glutamate generation in HIV‐1‐infected macrophage
Erdmann, N. B., Tian, C., Huang, Y., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05989.x · Cited by 41
Scott, G. S., Szabó, C., & Hooper, D. C. (2004) · Journal of Neurotrauma · doi:10.1089/neu.2004.21.1255 · Cited by 41
Jekabsone, A., Neher, J. J., Borutaitė, V., & Brown, G. C. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04765.x · Cited by 41
Self-citationContribution of autophagy to antiviral immunity
Rey-Jurado, E., Riedel, C. A., González, P. A., Bueno, S. M., & Kalergis, A. M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.07.047 · Cited by 40
The Effects of Soluble A.β Oligomers on Neurodegeneration in Alzheimer's Disease
Brouillette, J. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113199990498 · Cited by 39
Caspase inhibitors promote the survival of avulsed spinal motoneurons in neonatal rats
Chan, Y.-M., Wu, W., Yip, H. K.-F., So, K., & Oppenheim, R. W. (2001) · Neuroreport · doi:10.1097/00001756-200103050-00022 · Cited by 39
Function of BID – a Molecule of the bcl-2 Family – in Ischemic Cell Death in the Brain
Plesnila, N., Zinkel, S. S., Amin‐Hanjani, S., Qiu, J., Korsmeyer, S. J., & Moskowitz, M. A. (2002) · European Surgical Research · doi:10.1159/000048885 · Cited by 39
Programmed Cell Death and Caspase Functions During Neural Development
Yamaguchi, Y., & Miura, M. (2015) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2015.07.016 · Cited by 39
Novel model for the mechanisms of glutamate-dependent excitotoxicity: Role of neuronal gap junctions
Belousov, A. B. (2012) · Brain Research · doi:10.1016/j.brainres.2012.05.063 · Cited by 38
Gowran, A., & Campbell, V. A. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05278.x · Cited by 38
A BAX/BAK and Cyclophilin D-Independent Intrinsic Apoptosis Pathway
Zamorano, S., Rojas‐Rivera, D., Lisbona, F., Parra, V., Court, F. A., Villegas, R., Cheng, E. H. Y., Korsmeyer, S. J., Lavandero, S., & Hetz, C. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037782 · Cited by 38
Schaeffer, E. L., Aquino, E. R. D. S., Novaes, B. D. A., Skaf, H. D., & Gattaz, W. F. (2010) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2010.08.019 · Cited by 38
Cortical ballooned neurons in progressive supranuclear palsy
Mori, H., Oda, M., & Mizuno, Y. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)12612-4 · Cited by 38
Oncosis, the possible cell death pathway in astrocytes after focal cerebral ischemia
Chu, X., Fu, X., Zou, L., Qi, C., Li, Z., Rao, Y., & Ma, K. (2007) · Brain Research · doi:10.1016/j.brainres.2007.02.061 · Cited by 36
Evidence of early involvement of apoptosis inducing factor-induced neuronal death in Alzheimer brain
Lee, J.-H., Cheon, Y. H., Woo, R., Song, D., Moon, C., & Baik, T. (2012) · Anatomy & Cell Biology · doi:10.5115/acb.2012.45.1.26 · Cited by 36
Tokarz, P., Kaarniranta, K., & Błasiak, J. (2015) · Rejuvenation Research · doi:10.1089/rej.2015.1717 · Cited by 36
Han, B., Wang, Q., Cui, G., Shen, X., & Zhu, Z. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.008 · Cited by 35
Oppenheim, R. W., Blomgren, K., Ethell, D. W., Koike, M., Komatsu, M., Prevette, D. M., Roth, K. A., Uchiyama, Y., Vinsant, S. L., & Zhu, C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4575-07.2008 · Cited by 35
A role for p53 in the β-amyloid-mediated regulation of the lysosomal system
Fogarty, M. P., McCormack, R. M., Noonan, J., Murphy, D. B., Gowran, A., & Campbell, V. A. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.09.018 · Cited by 35
Neniškytė, U., Fricker, M., & Brown, G. C. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.06.005 · Cited by 35
Self-citationVillunger, A., Labi, V., Bouillet, P., Adams, J. M., & Strasser, A. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.100 · Cited by 34
Adalbert, R., Nógrádi, A., Szabó, A., & Coleman, M. P. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05103.x · Cited by 34
Self-citationIV. On the early development of Lepidosteus osseus . — Preliminary notice
Beard, J. (1890) · Proceedings of the Royal Society of London · doi:10.1098/rspl.1889.0015 · Cited by 34
Thal, S. E., Zhu, C., Thal, S. C., Blomgren, K., & Plesnila, N. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.05.016 · Cited by 32
Fujino, Y., DeLucia, M. W., Davies, P., et al. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00593.x · Cited by 31
Cao, X., Zhang, Y., Zou, L., Xiao, H., Chu, Y., & Chu, X. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.05.040 · Cited by 31
Kanno, H., Ozawa, H., Tateda, S., Yahata, K., & Itoi, E. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0204-0 · Cited by 30
Effect of glutamate on lysosomal membrane permeabilization in primary cultured cortical neurons
Yan, M., Zhu, W., Zheng, X., Li, Y., Tang, L., Lu, B., Chen, W. K., Qiu, P., Leng, T., Lin, S., et al. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.4819 · Cited by 30
Muramatsu, Y., Furuichi, Y., Tojo, N., Moriguchi, A., Maemoto, T., Nakada, H., Hino, M., & Matsuoka, N. (2007) · Brain Research · doi:10.1016/j.brainres.2007.02.036 · Cited by 29
Nagamine, S., Yamazaki, T., Makioka, K., Fujita, Y., Ikeda, M., Takatama, M., Okamoto, K., Yokoo, H., & Ikeda, Y. (2015) · Neuropathology · doi:10.1111/neup.12277 · Cited by 28
Johnsen, H., & Horvitz, H. R. (2016) · BMC Biology · doi:10.1186/s12915-016-0262-5 · Cited by 28
Tanaka, H., Shimazaki, H., Kimura, M., Izuta, H., Tsuruma, K., Shimazawa, M., & Hara, H. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00180.x · Cited by 27
Loucks, F. A., Schroeder, E. K., Zommer, A. E., Hilger, S., Kelsey, N. A., Bouchard, R. J., Blackstone, C. D., Brewster, J. L., & Linseman, D. A. (2008) · Brain Research · doi:10.1016/j.brainres.2008.10.081 · Cited by 27
Involvement of presenilin holoprotein upregulation in calcium dyshomeostasis of Alzheimer's disease
Honarnejad, K., Jung, C. K. E., Lammich, S., Arzberger, T., Kretzschmar, H. A., & Herms, J. W. (2013) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12008 · Cited by 27
Pascotini, E. T., Flores, A. E., Kegler, A., Gabbi, P., Bochi, G. V., Algarve, T. D., Prado, A. L. C., Duarte, M. M. M. F., da Cruz, I. B. M., Moresco, R. N., et al. (2015) · Physiology & Behavior · doi:10.1016/j.physbeh.2015.08.005 · Cited by 26
Clarke, G. D., & Lumsden, C. J. (2004) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2004.10.028 · Cited by 26
Deletion of autophagy-related gene 7 in dopaminergic neurons prevents their loss induced by MPTP
Niu, X., Huang, H.-J., Zhang, J., Zhang, C., Chen, W., Sun, C., Ding, Y., & Liao, M. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.09.037 · Cited by 25
Dávila, D., Jimenez-Mateos, E. M., Mooney, C. M., Velasco, G., Henshall, D. C., & Prehn, J. H. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-08-0495 · Cited by 23
Neuronal Cell Death: An Overview of Its Different Forms in Central and Peripheral Neurons
Lossi, L., Castagna, C., & Merighi, A. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2152-2_1 · Cited by 23
Yamada, K., Goto, S., Yoshikawa, M., & Ushio, Y. (1996) · Neuroscience · doi:10.1016/0306-4522(96)00041-3 · Cited by 22
Fricker, M., Papadia, S., Hardingham, G. E., & Tolkovsky, A. M. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06804.x · Cited by 19
Self-citationMultiple mechanisms repress N-Bak mRNA translation in the healthy and apoptotic neurons
Jakobson, M., Jakobson, M., Llano, O., Palgi, J., & Arumäe, U. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.297 · Cited by 19
Gizatullina, Z. Z., Gaynutdinov, T. R., Svoboda, H., Jerzembek, D., Knabe, A., Vielhaber, S., Malešević, M., Heinze, H., Fischer, G. S., Striggow, F., et al. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.12.012 · Cited by 18
Molecular imaging of neurodegeneration by a novel cross-disease biomarker
Shirvan, A., Reshef, A., Yogev‐Falach, M., & Ziv, I. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.032 · Cited by 17
Martin, N. A., Bonner, H. P., Elkjaer, M. L., D’Orsi, B., Chen, G., König, H., Svensson, M., Deierborg, T., Pfeiffer, S., Prehn, J. H. M., et al. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00014 · Cited by 17
Dual Kinase Inhibition Affords Extended in vitro Neuroprotection in Amyloid-β Toxicity
Gourmaud, S., Mouton‐Liger, F., Abadie, C., MEURS, E. F., Paquet, C., & Hugon, J. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160509 · Cited by 17
Calpastatin modulates APP processing in the brains of β-amyloid depositing but not wild-type mice
Morales‐Corraliza, J., Berger, J. D., Mazzella, M. J., Veeranna, Neubert, T. A., Ghiso, J. A., Rao, M. V., Staufenbiel, M., Nixon, R. A., & Mathews, P. M. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.023 · Cited by 16
An angiogenic inhibitor, cyclic RGDfV, attenuates MPTP-induced dopamine neuron toxicity
Patel, A., Toia, G. V., Colletta, K., Bradaric, B. D., Carvey, P. M., & Hendey, B. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.06.004 · Cited by 15
Inhibition of Apoptosome Activation Protects Injured Motor Neurons from Cell Death
Kanungo, A., Hao, Z., Elia, A., Mak, T. W., & Henderson, J. T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800988200 · Cited by 14
Nixon, R. A. (2014) · BioEssays · doi:10.1002/bies.201400064 · Cited by 14
Kahraman, S., Siegel, A., Polster, B. M., & Fiskum, G. M. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9588-2 · Cited by 13
DeGiorgio, L. A., DeGiorgio, N., & Volpe, B. T. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00428-x · Cited by 13
Mimuro, M., Yoshida, M., Miyao, S., Harada, T., Ishiguro, K., & Hashizume, Y. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2009.11.002 · Cited by 13
Shibata, N., Kakita, A., Takahashi, H., Ihara, Y., Nobukuni, K., Fujimura, H., Sakoda, S., Sasaki, S., Yamamoto, T., & Kobayashi, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0580-6 · Cited by 13
Hunter, S., Minett, T., Polvikoski, T. M., Mukaetova‐Ladinska, E. B., & Brayne, C. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0141-2 · Cited by 12
DNase activation by hypoxia–acidosis parallels but is independent of programmed cell death
Thompson, J. W., Graham, R. M., & Webster, K. A. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.03.034 · Cited by 12
Efthimiadi, L., Farso, M. C., Quirion, R., & Krantic, S. M. (2012) · Neurodegenerative Diseases · doi:10.1159/000335911 · Cited by 11
Aoki, K., Uchihara, T., Nakamura, A., Komori, T., Arai, N., & Mizutani, T. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0740-z · Cited by 10
Advanced Neuroimaging Methods Towards Characterization of Early Stages of Alzheimer’s Disease
Sepulcre, J., & Masdeu, J. C. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2627-5_31 · Cited by 10
Salloway, S., & Sperling, R. A. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.1804 · Cited by 9
Entosis and Related Forms of Cell Death within Cells.
Wang, Y., & Wang, X. (2015) · Current Molecular Medicine · doi:10.2174/1566524015666151026100339 · Cited by 6
Liu, W., Chen, S.-Y., Cheng, J. C., Cheng, H.-J., & Huang, P. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.050 · Cited by 6
Zhu, J., Wang, W., Kong, L., Ma, C., Li, Y., Liu, B., & Tan, L. (2016) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-016-9959-0 · Cited by 3
Picture imperfect: Going beyond imaging amyloid in Alzheimer's disease
Kincaid, E. (2016) · Nature Medicine · doi:10.1038/nm1016-1067 · Cited by 2
(2000) · doi:10.1002/1097-4547(20000915)61:6<686::aid-jnr12>3.0.co;2-7
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.