All Relations between apoptosis and ced-3

Publication Sentence Publish Date Extraction Date Species
N L Harvey, J A Trapani, T Fernandes-Alnemri, G Litwack, E S Alnemri, S Kuma. Processing of the Nedd2 precursor by ICE-like proteases and granzyme B. Genes to cells : devoted to molecular & cellular mechanisms. vol 1. issue 7. 1997-04-25. PMID:9078393. because of their similarity to the cacnorhabditis elegans cell death protein ced-3, the ice-like proteins are thought to play a key role in the execution of apoptosis. 1997-04-25 2023-08-12 Not clear
T Mukasa, K Urase, M Y Momoi, I Kimura, T Momo. Specific expression of CPP32 in sensory neurons of mouse embryos and activation of CPP32 in the apoptosis induced by a withdrawal of NGF. Biochemical and biophysical research communications. vol 231. issue 3. 1997-04-16. PMID:9070890. we isolated mouse cpp32/apopain cdna, a mammalian homologue most closely related to ced-3 in c. elegans, and examined the involvement of cpp32 in the apoptosis of nervous system during development. 1997-04-16 2023-08-12 mouse
N J McCarthy, M K Whyte, C S Gilbert, G I Eva. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. The Journal of cell biology. vol 136. issue 1. 1997-02-20. PMID:9008715. there is increasing evidence for a central role in mammalian apoptosis of the interleukin-1 beta-converting enzyme (ice) family of cysteine proteases, homologues of the product of the nematode "death" gene, ced-3. 1997-02-20 2023-08-12 Not clear
K Kuida, T S Zheng, S Na, C Kuan, D Yang, H Karasuyama, P Rakic, R A Flavel. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature. vol 384. issue 6607. 1996-12-13. PMID:8934524. the identification of the caenorhabditis elegans cell death gene, ced-3, as a prototype of the interleukin-1beta converting enzyme (ice) protease family has led to extensive evidence implicating these enzymes in apoptosis. 1996-12-13 2023-08-12 mouse
Y Tsujimot. [Prevention of cell death by Bcl-2 family genes]. Nihon rinsho. Japanese journal of clinical medicine. vol 54. issue 7. 1996-11-26. PMID:8741684. proteases encoded by ced-3 and ice gene family appear to play a key role in driving apoptosis. 1996-11-26 2023-08-12 Not clear
K Orth, K O'Rourke, G S Salvesen, V M Dixi. Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases. The Journal of biological chemistry. vol 271. issue 35. 1996-10-10. PMID:8702858. using a cell-free apoptosis system, recombinant ice proteases and both biochemical and morphological criteria, we demonstrate an ordering of the mammalian ices that are most related to the caenorhabditis elegans death protease ced-3. 1996-10-10 2023-08-12 caenorhabditis_elegans
T S Juan, I K McNiece, N A Jenkins, D J Gilbert, N G Copeland, F A Fletche. Molecular characterization of mouse and rat CPP32 beta gene encoding a cysteine protease resembling interleukin-1 beta converting enzyme and CED-3. Oncogene. vol 13. issue 4. 1996-10-10. PMID:8761296. both ice and ced-3, when introduced into cultured cells, induce apoptosis, indicating that this type of cysteine protease may play an important role in the process of programmed cell death. 1996-10-10 2023-08-12 mouse
Y P Goldberg, D W Nicholson, D M Rasper, M A Kalchman, H B Koide, R K Graham, M Bromm, P Kazemi-Esfarjani, N A Thornberry, J P Vaillancourt, M R Hayde. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nature genetics. vol 13. issue 4. 1996-09-05. PMID:8696339. apopain, a human counterpart of the nematode cysteine protease death-gene product, ced-3, has a key role in proteolytic events leading to apoptosis. 1996-09-05 2023-08-12 human
K Orth, A M Chinnaiyan, M Garg, C J Froelich, V M Dixi. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. The Journal of biological chemistry. vol 271. issue 28. 1996-08-29. PMID:8663580. the ced-3/ice-like protease mch2 is activated during apoptosis and cleaves the death substrate lamin a. phylogenetic analysis of the ced-3/ice family of cysteine proteases suggests the existence of a subfamily most related to the caenorhabditis elegans death gene ced-3 and includes yama (cpp32, apopain), lap3 (mch3, cmh1), and mch2. 1996-08-29 2023-08-12 caenorhabditis_elegans
E Fujita, T Mukasa, T Tsukahara, K Arahata, S Omura, T Momo. Enhancement of CPP32-like activity in the TNF-treated U937 cells by the proteasome inhibitors. Biochemical and biophysical research communications. vol 224. issue 1. 1996-08-29. PMID:8694836. cpp32, which is most closely related to ced-3 in the apoptotic protease in c. elegance, is activated during apoptosis induced by anti-fas and tnf. 1996-08-29 2023-08-12 Not clear
J Rotonda, D W Nicholson, K M Fazil, M Gallant, Y Gareau, M Labelle, E P Peterson, D M Rasper, R Ruel, J P Vaillancourt, N A Thornberry, J W Becke. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nature structural biology. vol 3. issue 7. 1996-08-15. PMID:8673606. cysteine proteases related to mammalian interleukin-1 beta converting enzyme (ice) and to its caenorhabditis elegans homologue, ced-3, play a critical role in the biochemical events that culminate in apoptosis. 1996-08-15 2023-08-12 human
D Xue, S Shaham, H R Horvit. The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes & development. vol 10. issue 9. 1996-07-26. PMID:8654923. the caenorhabditis elegans cell-death gene ced-3 encodes a protein similar to mammalian interleukin-1beta-converting enzyme (ice), a cysteine protease implicated in mammalian apoptosis. 1996-07-26 2023-08-12 human
D Xue, S Shaham, H R Horvit. The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes & development. vol 10. issue 9. 1996-07-26. PMID:8654923. our results suggest that different mammalian ced-3/ice-like proteases may have distinct roles in mammalian apoptosis and that cpp32 is a candidate for being a mammalian functional equivalent of ced-3. 1996-07-26 2023-08-12 human
M Hugunin, L J Quintal, J A Mankovich, T Ghayu. Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product. The Journal of biological chemistry. vol 271. issue 7. 1996-07-02. PMID:8631956. the caenorhabditis elegans cell death gene, ced-3, encodes one of the two proteins required for apoptosis in this organism. 1996-07-02 2023-08-12 caenorhabditis_elegans
M Hugunin, L J Quintal, J A Mankovich, T Ghayu. Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product. The Journal of biological chemistry. vol 271. issue 7. 1996-07-02. PMID:8631956. aurintricarboxylic acid, an inhibitor of apoptosis in mammalian cells, blocked ced-3 autocatalytic activity, suggesting that an aurintricarboxylic acid-sensitive ced-3/ice-related protease might be involved in the apoptosis pathway(s) in mammalian cells. 1996-07-02 2023-08-12 caenorhabditis_elegans
J Hasegawa, S Kamada, W Kamiike, S Shimizu, T Imazu, H Matsuda, Y Tsujimot. Involvement of CPP32/Yama(-like) proteases in Fas-mediated apoptosis. Cancer research. vol 56. issue 8. 1996-06-14. PMID:8620480. interleukin-1beta-converting enzyme (ice), which shows substantial homology to the product of the cell death gene, ced-3, of caenorhabditis elegans, is reported to be involved in fas-mediated apoptosis. 1996-06-14 2023-08-12 human
H Duan, A M Chinnaiyan, P L Hudson, J P Wing, W W He, V M Dixi. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. The Journal of biological chemistry. vol 271. issue 3. 1996-03-11. PMID:8576161. ice-lap3, a novel mammalian homologue of the caenorhabditis elegans cell death protein ced-3 is activated during fas- and tumor necrosis factor-induced apoptosis. 1996-03-11 2023-08-12 caenorhabditis_elegans
T Fernandes-Alnemri, A Takahashi, R Armstrong, J Krebs, L Fritz, K J Tomaselli, L Wang, Z Yu, C M Croce, G Salveso. Mch3, a novel human apoptotic cysteine protease highly related to CPP32. Cancer research. vol 55. issue 24. 1996-01-22. PMID:8521391. recent evidence suggests that mammalian cysteine proteases related to caenorhabditis elegans ced-3 are key components of mammalian programmed cell death or apoptosis. 1996-01-22 2023-08-12 human
S Kondo, B P Barna, T Morimura, J Takeuchi, J Yuan, A Akbasak, G H Barnet. Interleukin-1 beta-converting enzyme mediates cisplatin-induced apoptosis in malignant glioma cells. Cancer research. vol 55. issue 24. 1996-01-22. PMID:8521409. we show here that cis-diamminedichloroplatinum (cisplatin) induces the expression of interleukin-1 beta-converting enzyme (ice), a mammalian homologue of the caenorhabditis elegans cell death gene ced-3, in murine and human malignant glioma cells during apoptosis regardless of their p53 status. 1996-01-22 2023-08-12 human
J P Vasilakos, T Ghayur, R T Carroll, D A Giegel, J M Saunders, L Quintal, K M Keane, B D Shiver. IL-1 beta converting enzyme (ICE) is not required for apoptosis induced by lymphokine deprivation in an IL-2-dependent T cell line. Journal of immunology (Baltimore, Md. : 1950). vol 155. issue 7. 1995-10-27. PMID:7561038. the cysteine protease, il-1 beta converting enzyme (ice), is implicated in apoptosis based on its structural similarity to the pcd gene, ced-3, in caenorhabditis elegans and the induction of pcd in fibroblasts transfected with recombinant ice. 1995-10-27 2023-08-12 caenorhabditis_elegans