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Metacaspases
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A Caspase-Related Protease Regulates Apoptosis in Yeast
Madeo, F., Herker, E., Maldener, C., Wissing, S., Lächelt, S., Herlan, M., Fehr, M., Lauber, K., Sigrist, S. J., Wesselborg, S., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00501-4 · Cited by 872
Structural Basis for the Inhibition of Caspase-3 by XIAP
Riedl, S. J., Renatus, M., Schwarzenbacher, R., Zhou, Q., Sun, C., Fesik, S. W., Liddington, R. C., & Salvesen, G. S. (2001) · Cell · doi:10.1016/s0092-8674(01)00274-4 · Cited by 792
Solomon, M., Belenghi, B., Delledonne, M., Menachem, E., & Levine, A. (1999) · The Plant Cell · doi:10.1105/tpc.11.3.431 · Cited by 760
Human Caspases: Activation, Specificity, and Regulation
Pop, C., & Salvesen, G. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r800084200 · Cited by 754
Chronological aging leads to apoptosis in yeast
Herker, E., Jungwirth, H., Lehmann, K. A., Maldener, C., Fröhlich, K.-U., Wissing, S., Büttner, S., Fehr, M., Sigrist, S., & Madeo, F. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310014 · Cited by 548
A micrococcal nuclease homologue in RNAi effector complexes
Caudy, A. A., Ketting, R. F., Hammond, S. M., Denli, A. M., Bathoorn, A. M. P., Tops, B. B. J., Silva, J. M., Myers, M. M., Hannon, G. J., & Plasterk, R. H. A. (2003) · Nature · doi:10.1038/nature01956 · Cited by 473
Uren, A. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00094-0 · Cited by 459
Arabidopsis Type I Metacaspases Control Cell Death
Coll, N. S., Vercammen, D., Smidler, A., Clover, C., Van Breusegem, F., Dangl, J. L., & Epple, P. (2010) · Science · doi:10.1126/science.1194980 · Cited by 425
Self-citationVercammen, D., van de Cotte, B., Jaeger, G. D., Eeckhout, D., Casteels, P., Vandepoele, K., Vandenberghe, I. H. M., BEEUMEN, J. V., Inzé, D., & Breusegem, F. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406329200 · Cited by 357
Coffeen, W. C., & Wolpert, T. J. (2004) · The Plant Cell · doi:10.1105/tpc.017947 · Cited by 274
Watanabe, N., & Lam, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413527200 · Cited by 264
Self-citationCysteine protease mcII-Pa executes programmed cell death during plant embryogenesis
Bozhkov, P. V., Suarez, M. F., Filonova, L. H., Daniel, G., Zamyatnin, A. A., Rodriguez-Nieto, S., Zhivotovsky, B., & Smertenko, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506948102 · Cited by 256
Self-citationBelenghi, B., Romero-Puertas, M. C., Vercammen, D., Brackenier, A., Inzé, D., Delledonne, M., & Van Breusegem, F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608931200 · Cited by 232
Self-citationSundström, J. F., Vaculova, A., Smertenko, A. P., Savenkov, E. I., Golovko, A., Minina, E., Tiwari, B. S., Rodriguez-Nieto, S., Zamyatnin, A. A., Välineva, T., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1979 · Cited by 212
Self-citationSerpin1 of Arabidopsis thaliana is a Suicide Inhibitor for Metacaspase 9
Vercammen, D., Belenghi, B., van de Cotte, B., Beunens, T., Gavigan, J.-A., Rycke, R. M. D., Brackenier, A., Inzé, D., Harris, J. L., & Breusegem, F. V. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.09.010 · Cited by 197
Physiological regulation of yeast cell death in multicellular colonies is triggered by ammonia
Váchová, L., & Palková, Z. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200410064 · Cited by 194
Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II
Yang, J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf463 · Cited by 190
Vercammen, D., Declercq, W., Vandenabeele, P., & Van Breusegem, F. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200705193 · Cited by 188
Self-citationAravind, L., & Koonin, E. V. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10060 · Cited by 185
Bidle, K. D., Haramaty, L., Barcelos e Ramos, J., & Falkowski, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701240104 · Cited by 183
Watanabe, N., & Lam, E. (2011) · The Plant Journal · doi:10.1111/j.1365-313x.2011.04554.x · Cited by 170
Self-citationMetacaspase Yca1 is required for clearance of insoluble protein aggregates
Lee, R. E. C., Brunette, S., Puente, L. G., & Megeney, L. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006610107 · Cited by 164
Bozhkov, P. V., Filonova, L. H., Suárez, M. F., Helmersson, A., Smertenko, A., Zhivotovsky, B., & von Arnold, S. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401330 · Cited by 159
Self-citationCaspase-dependent and caspase-independent cell death pathways in yeast
Madeo, F., Carmona‐Gutiérrez, D., Ring, J., Büttner, S., Eisenberg, T., & Kroemer, G. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.02.117 · Cited by 148
Szallies, A., Kubata, B. K., & Duszenko, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02608-x · Cited by 141
Structural and kinetic determinants of protease substrates
Timmer, J. C., Zhu, W., Pop, C., Regan, T. W., Snipas, S. J., Eroshkin, A. M., Riedl, S. J., & Salvesen, G. S. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1668 · Cited by 136
Lee, N., Gannavaram, S., Selvapandiyan, A., & Debrabant, A. (2007) · Eukaryotic Cell · doi:10.1128/ec.00123-07 · Cited by 135
Bidle, K. D., & Bender, S. J. (2007) · Eukaryotic Cell · doi:10.1128/ec.00296-07 · Cited by 132
Wu, X., Chang, W., Cheng, A., Sun, L., & Lou, H. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.01.001 · Cited by 130
Yang, J., Välineva, T., Hong, J., Bu, T., Yao, Z., Jensen, O. N., Frilander, M. J., & Silvennoinen, O. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm470 · Cited by 124
An essential role for the Leishmania major metacaspase in cell cycle progression
Ambit, A., Fasel, N. J., Coombs, G. H., & Mottram, J. C. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402232 · Cited by 120
Multiple Signaling Pathways Regulate Yeast Cell Death during the Response to Mating Pheromones
Zhang, N.-N., Dudgeon, D. D., Paliwal, S., Levchenko, A., Grote, E., & Cunningham, K. W. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-03-0177 · Cited by 117
Helms, M. J., Ambit, A., Appleton, P. L., Tetley, L., Coombs, G. H., & Mottram, J. C. (2006) · Journal of Cell Science · doi:10.1242/jcs.02809 · Cited by 113
Frey, N. F. D., Müller, P., Jammes, F., Kizis, D., Leung, J., Perrot‐Rechenmann, C., & Bianchi, M. W. (2010) · The Plant Cell · doi:10.1105/tpc.109.070680 · Cited by 103
A Non-Death Role of the Yeast Metacaspase: Yca1p Alters Cell Cycle Dynamics
Lee, R., Puente, L. G., Kærn, M., & Megeney, L. A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002956 · Cited by 102
Calcium-dependent Activation and Autolysis of Arabidopsis Metacaspase 2d
Watanabe, N., & Lam, E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.194340 · Cited by 97
Self-citationViruses activate a genetically conserved cell death pathway in a unicellular organism
Ivanovska, I., & Hardwick, J. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503069 · Cited by 96
Cao, Y., Huang, S., Dai, B., Zhu, Z., Lu, H., Dong, L., Cao, Y., Wang, Y., Gao, P., Chai, Y., et al. (2008) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2008.11.001 · Cited by 94
Moss, C., Westrop, G. D., Juliano, L., Coombs, G. H., & Mottram, J. C. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.009 · Cited by 93
Richie, D. L., Miley, M. D., Bhabhra, R., Robson, G. D., Rhodes, J. C., & Askew, D. S. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05534.x · Cited by 93
Guaragnella, N., Pereira, C., Sousa, M. J., Antonacci, L., Passarella, S., Côrte‐Real, M., Marra, E., & Giannattasio, S. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.050 · Cited by 88
Metacaspases are caspases. Doubt no more
Carmona‐Gutiérrez, D., Fröhlich, K.-U., Kroemer, G., & Madeo, F. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2009.198 · Cited by 87
Hamann, A., Brust, D., & Osiewacz, H. D. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05839.x · Cited by 86
The multifunctional human p100 protein 'hooks' methylated ligands
Shaw, N., Zhao, M., Cheng, C., Xu, H., Saarikettu, J., Li, Y., Da, Y., Yao, Z., Silvennoinen, O., Yang, J., et al. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1269 · Cited by 85
Wadskog, I., Maldener, C., Proksch, A., Madeo, F., & Adler, L. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-02-0114 · Cited by 83
Scadden, A. D. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.005 · Cited by 79
Methods for the proteomic identification of protease substrates
Agard, N. J., & Wells, J. A. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.07.026 · Cited by 72
Molecular Characterization of Propolis-Induced Cell Death in Saccharomyces cerevisiae
de Castro, P. A., Savoldi, M., Bonatto, D., de Barros, M. H., Goldman, M. H. S., Berretta, A. A., & Goldman, G. H. (2010) · Eukaryotic Cell · doi:10.1128/ec.00256-10 · Cited by 69
MS‐driven protease substrate degradomics
Impens, F., Colaert, N., Helsens, K., Plasman, K., Damme, P. V., Vandekerckhove, J. S., & Gevaert, K. (2010) · PROTEOMICS · doi:10.1002/pmic.200900418 · Cited by 62
Guaragnella, N., Bobba, A., Passarella, S., Marra, E., & Giannattasio, S. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.11.072 · Cited by 53
Bre1p-mediated histone H2B ubiquitylation regulates apoptosis in Saccharomyces cerevisiae
Walter, D., Matter, A., & Fahrenkrog, B. (2010) · Journal of Cell Science · doi:10.1242/jcs.065938 · Cited by 45
Colabardini, A. C., de Castro, P. A., de Gouvêa, P. F., Savoldi, M., Malavazi, I., Goldman, M. H. S., & Goldman, G. H. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07403.x · Cited by 45
Metacaspases are not caspases – always doubt
Enoksson, M., & Salvesen, G. S. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.45 · Cited by 42
Caspase-dependent and -independent lipotoxic cell-death pathways in fission yeast
Low, C. P., Shui, G., Liew, L. P., Büttner, S., Madeo, F., Dawes, I. W., Wenk, M. R., & Yang, H. (2008) · Journal of Cell Science · doi:10.1242/jcs.028977 · Cited by 40
Palermo, V., Falcone, C., Calvani, M., & Mazzoni, C. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00587.x · Cited by 39
Murik, O., & Kaplan, A. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2009.01957.x · Cited by 39
Hao, L., Goodwin, P. H., & Hsiang, T. (2007) · Plant Cell Reports · doi:10.1007/s00299-007-0387-7 · Cited by 39
Calnexin Regulates Apoptosis Induced by Inositol Starvation in Fission Yeast
Guérin, R., Beauregard, P. B., Leroux, A., & Rokeach, L. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006244 · Cited by 36
Functional characterization of human proapoptotic molecules in yeast S. cerevisiae
Guscetti, F., Nath, N., & Denko, N. C. (2005) · The FASEB Journal · doi:10.1096/fj.04-2316fje · Cited by 30
Aspasing Out Metacaspases and Caspases: Proteases of Many Trades
Bozhkov, P. V., Smertenko, A., & Zhivotovsky, B. (2010) · Science Signaling · doi:10.1126/scisignal.3152pe48 · Cited by 20
Self-citationSripriya, P., Vedantam, L. V., & Podile, A. R. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22217 · Cited by 18
Structure, expression and function of Allomyces arbuscula CDP II (metacaspase) gene
Ojha, M., Cattaneo, A., Hugh, S., Pawlowski, J. W., & Cox, J. A. (2010) · Gene · doi:10.1016/j.gene.2010.02.014 · Cited by 15
Cited by
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Metadata
- Authors
- Tsiatsiani, L., Van Breusegem, F., Gallois, P., Zavialov, A., Lam, E., & Bozhkov, P. V.
- Venue
- Cell Death & Differentiation
- Published
- 2011-05-20
- Volume
- 18
- Issue
- 8
- Pages
- 1279-1288
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- OpenAlex
- W4232254803
- Cited by
- 323
- References
- 62
- FWCI
- 9.87
- Type
- journal article
- Language
- en
- Open access
- bronze
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