| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Yonatan B Tzur, Bradley M Hersh, H Robert Horvitz, Yosef Gruenbau. Fate of the nuclear lamina during Caenorhabditis elegans apoptosis. Journal of structural biology. vol 137. issue 1-2. 2002-12-09. PMID:12064941. |
caenorhabditis elegans has a single lamin protein, ce-lamin, and a caspase, ced-3, that is responsible for most if not all somatic apoptosis. |
2002-12-09 |
2023-08-12 |
caenorhabditis_elegans |
| J Parrish, L Li, K Klotz, D Ledwich, X Wang, D Xu. Mitochondrial endonuclease G is important for apoptosis in C. elegans. Nature. vol 412. issue 6842. 2001-07-26. PMID:11452313. |
here we report the characterization of the cps-6 gene, which appears to function downstream of, or in parallel to, the cell-death protease ced-3 of caenorhabditis elegans in the dna degradation process during apoptosis. |
2001-07-26 |
2023-08-12 |
human |
| S Conus, T Rossé, C Borne. Failure of Bcl-2 family members to interact with Apaf-1 in normal and apoptotic cells. Cell death and differentiation. vol 7. issue 10. 2001-05-24. PMID:11279541. |
ced-9 blocks programmed cell death (apoptosis) in the nematode c. elegans by binding to and neutralizing ced-4, an essential activator of the aspartate-directed cysteine protease (caspase) ced-3. |
2001-05-24 |
2023-08-12 |
caenorhabditis_elegans |
| A Cellerino, M Bähr, S Isenman. Apoptosis in the developing visual system. Cell and tissue research. vol 301. issue 1. 2000-12-07. PMID:10928281. |
two classes of molecules are particularly important in the context of apoptosis control in the nervous system: intracellular effectors homologous to the caenorhabditis elegans ced-3, -4, and -9 proteins, which in mammals correspond to the proteases of the caspase family, apaf-1, and the members of the bcl-2 protein family, and neurotrophic factors. |
2000-12-07 |
2023-08-12 |
caenorhabditis_elegans |
| S Gaumer, I Guénal, S Brun, L Théodore, B Mignott. Bcl-2 and Bax mammalian regulators of apoptosis are functional in Drosophila. Cell death and differentiation. vol 7. issue 9. 2000-11-14. PMID:11042675. |
studies of apoptosis in c. elegans have allowed the identification of three genes, ced-3, ced-4 and ced-9. |
2000-11-14 |
2023-08-12 |
caenorhabditis_elegans |
| S L Chan, K S Yee, K M Tan, V C Y. The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3 substrate that associates with CED-4 and mediates apoptosis in mammalian cells. The Journal of biological chemistry. vol 275. issue 24. 2000-07-20. PMID:10764728. |
the caenorhabditis elegans sex determination protein fem-1 is a ced-3 substrate that associates with ced-4 and mediates apoptosis in mammalian cells. |
2000-07-20 |
2023-08-12 |
caenorhabditis_elegans |
| S L Chan, K S Yee, K M Tan, V C Y. The Caenorhabditis elegans sex determination protein FEM-1 is a CED-3 substrate that associates with CED-4 and mediates apoptosis in mammalian cells. The Journal of biological chemistry. vol 275. issue 24. 2000-07-20. PMID:10764728. |
fem-1 is cleaved in vitro by the c. elegans caspase, ced-3, generating an n-terminal cleavage product that corresponds to the minimal effector domain for apoptosis. |
2000-07-20 |
2023-08-12 |
caenorhabditis_elegans |
| M R Aliso. Identifying and quantifying apoptosis: a growth industry in the face of death. The Journal of pathology. vol 188. issue 2. 2000-02-29. PMID:10398152. |
apoptosis remains one of the hottest topics in cell biology, and great strides are being made in unravelling the complex interplay between the various regulatory molecules, particularly between the mammalian homologues of the nematode caenorhabditis elegans death regulatory proteins ced-3, ced-4 and ced-9. |
2000-02-29 |
2023-08-12 |
caenorhabditis_elegans |
| F Ceccon. Apaf1 and the apoptotic machinery. Cell death and differentiation. vol 6. issue 11. 2000-02-29. PMID:10578178. |
the killer gene ced-3 encodes a cystein-aspartate protease (caspase), which is the archetype of a family of conserved proteins known as effectors of apoptosis in mammals. |
2000-02-29 |
2023-08-12 |
human |
| M O Hengartne. Programmed cell death in the nematode C. elegans. Recent progress in hormone research. vol 54. 1999-12-08. PMID:10548877. |
the proximal cause of apoptosis in c. elegans is the activation of the caspase homolog ced-3 from the inactive zymogen (proced-3) into the mature protease. |
1999-12-08 |
2023-08-12 |
caenorhabditis_elegans |
| K Urase, T Momoi, E Fujita, K Isahara, Y Uchiyama, A Tokunaga, K Nakayama, N Motoyam. Bcl-xL is a negative regulator of caspase-3 activation in immature neurons during development. Brain research. Developmental brain research. vol 116. issue 1. 1999-10-07. PMID:10446348. |
caspases and bcl-xl, the mammalian homologues of the caenorhabditis elegans (c. elegans) ced-3 and ced-9 genes, respectively, regulate apoptosis of various cells. |
1999-10-07 |
2023-08-12 |
mouse |
| C Borner, L Monne. Apoptosis without caspases: an inefficient molecular guillotine? Cell death and differentiation. vol 6. issue 6. 1999-09-08. PMID:10381652. |
since the discovery that the cysteine protease ced-3 was essential for developmental death in the nematode c. elegans, the search has been on to identify homologous proteases governing mammalian apoptosis. |
1999-09-08 |
2023-08-12 |
mouse |
| M Miwa, S Hanai, P Poltronieri, M Uchida, K Uchid. Functional analysis of poly(ADP-ribose) polymerase in Drosophila melanogaster. Molecular and cellular biochemistry. vol 193. issue 1-2. 1999-08-09. PMID:10331645. |
although the consensus cleavage site of ced-3 like protease during apoptosis is conserved from human to xenopus laevis parps, it is neither conserved in the corresponding region of drosophila nor sarcophaga peregrina. |
1999-08-09 |
2023-08-12 |
human |
| S Bajusz, I Fauszt, K Németh, E Barabás, A Juhász, M Patthy, P I Baue. Peptidyl beta-homo-aspartals (3-amino-4-carboxybutyraldehydes): new specific inhibitors of caspases. Biopolymers. vol 51. issue 1. 1999-07-26. PMID:10380358. |
ice has been identified as a unique cysteine protease, which cleaves asp-x bonds, shows resistance to e-64 (an inhibitor of most cysteine proteases) and has a primary structure that is homologous to ced-3, a protein required for apoptosis (programmed cell death) in the nematode caenorhabditis elegans, and to mammalian cysteine proteases that initiate and execute apoptosis, e.g., apopain/cpp32/caspase-3. |
1999-07-26 |
2023-08-12 |
caenorhabditis_elegans |
| D Wu, P J Chen, S Chen, Y Hu, G Nuñez, R E Elli. C. elegans MAC-1, an essential member of the AAA family of ATPases, can bind CED-4 and prevent cell death. Development (Cambridge, England). vol 126. issue 9. 1999-06-22. PMID:10101135. |
we observe a similar effect in mammalian cells, where expression of mac-1 can prevent ced-4 and ced-3 from inducing apoptosis. |
1999-06-22 |
2023-08-12 |
caenorhabditis_elegans |
| B R Rueda, I R Hendry, J L Tilly, D L Hamerni. Accumulation of caspase-3 messenger ribonucleic acid and induction of caspase activity in the ovine corpus luteum following prostaglandin F2alpha treatment in vivo. Biology of reproduction. vol 60. issue 5. 1999-06-03. PMID:10208968. |
caspase-3, a vertebrate homologue of the protein encoded by the caenorhabditis elegans cell death gene, ced-3, induces apoptosis when overexpressed in eukaryotic cells. |
1999-06-03 |
2023-08-12 |
human |
| R Robles, X J Tao, A M Trbovich, D V Maravel, R Nahum, G I Perez, K I Tilly, J L Till. Localization, regulation and possible consequences of apoptotic protease-activating factor-1 (Apaf-1) expression in granulosa cells of the mouse ovary. Endocrinology. vol 140. issue 6. 1999-06-03. PMID:10342853. |
these data, combined with previous observations regarding the role of homologs of the two other c. elegans cell death regulatory genes, ced-9 (bcl-2 family members) and ced-3 (caspases), in atresia fully support the hypothesis that granulosa cell apoptosis is precisely coordinated by all three major arms of a cell death program conserved through evolution. |
1999-06-03 |
2023-08-12 |
mouse |
| S C Chow, E A Slee, M MacFarlane, G M Cohe. Caspase-1 is not involved in CD95/Fas-induced apoptosis in Jurkat T cells. Experimental cell research. vol 246. issue 2. 1999-03-15. PMID:9925765. |
caspase-1, the first caspase discovered, was initially implicated in mammalian apoptosis because of its similarity to the gene product ced-3. |
1999-03-15 |
2023-08-12 |
Not clear |
| L del Peso, V M González, G Núñe. Caenorhabditis elegans EGL-1 disrupts the interaction of CED-9 with CED-4 and promotes CED-3 activation. The Journal of biological chemistry. vol 273. issue 50. 1999-01-14. PMID:9837929. |
expression of ced-4 and ced-3 resulted in decreased survival and apoptosis of mammalian cells, activities that could be inhibited by ced-9. |
1999-01-14 |
2023-08-12 |
caenorhabditis_elegans |
| Y Kondo, J Liu, T Haqqi, B P Barna, S Kond. Involvement of interleukin-1beta-converting enzyme in apoptosis of irradiated retinoblastomas. Investigative ophthalmology & visual science. vol 39. issue 13. 1998-12-21. PMID:9856788. |
to investigate whether interleukin-1beta-converting enzyme (ice), a mammalian homologue of the caenorhabditis elegans cell death gene ced-3, is involved in gamma-irradiation-induced apoptosis (programmed cell death) of human retinoblastoma cells. |
1998-12-21 |
2023-08-12 |
human |