References
- Methods Archive Exp. Pathol. v.13 Patterns of cell death Walker,N.I.;B.V.Harmon;G.C.Gobe;J.F.R.Kerr
- J. Pathol. v.142 Chromatin cleavage in apoptosis: Association with condensed chromatin morphology and dependence on macromolecular synthesis Wyllie,A.H.;R.G.Morris;A.L.Smith;D.Dunlop
- Int. Rev. Cytol. v.68 Cell death: the significance of apoptosis Wyllie,A.H.;J.F.R.Kerr;A.R.Currie https://doi.org/10.1016/S0074-7696(08)62312-8
- Annu. Rev. Cell Biol. v.7 Mechanisms and functions of cell death Ellis,R.E.;J.Yuan;H.R.Horvitz https://doi.org/10.1146/annurev.cb.07.110191.003311
- Science v.262 Programmed cell death and the control of cell survival: Lessons form nervous system Raff,M.C.;B.A.Barres;J.F.Burne;H.S.Coles;Y.Ishizaki;M.D.Jacobson https://doi.org/10.1126/science.8235590
- Bio. Rev. Cambridge Phil. Soc. v.26 Cell death in nornal vertebrated ontogeny Glucksmann,A.
- Br. J. Cancer v.26 Apoptosis: A basic biological phenomenon with wideranging implications in tissue kinetics Kerr,J.F.R.;A.H.Wyllie;A.H.Currie https://doi.org/10.1038/bjc.1972.33
- Semin. Immunol. v.9 The molecular regulation of lymphocyte apoptosis Lenardo,M.J. https://doi.org/10.1006/smim.1996.0050
- Dev. Biol. v.138 Genetic mosaic analysis of ced-3 and ced-4, two genes that control programmed cell death in the nematode C. elegans Yuan,J.Y.;R.H.Horvitz https://doi.org/10.1016/0012-1606(90)90174-H
- Nature v.356 Caenorhabditis elegans gene ced-9 protects cells from programmed cell death Hengartner,M.O.;R.E.Ellis;R.H.Horvitz https://doi.org/10.1038/356494a0
- Cell v.76 C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2 Hengartner,M.O.;R.H.Horvitz https://doi.org/10.1016/0092-8674(94)90506-1
- Cell v.75 The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β converting enzyme Yuan,J.Y.;S.Shaham;S.Ledoux;M.H.Ellis;R.H.Horvitz https://doi.org/10.1016/0092-8674(93)90485-9
- Science v.275 Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death Chinnaiyan,A.M.;K.O'Rourke;B.R.Lane;V.M.Dixit https://doi.org/10.1126/science.275.5303.1122
- Cell v.30 Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of capases-3 Zou,H.;W.J.Henzel;X.Liu;A.Lutschg;X.Wang
- Cell v.81 Yma/CPP32β, a mammalian homolog of ced-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-reibose) polymerase Tewari,M.;L.Quan;K.O'Rourke;S.Desonoyers;Z.Zeng;D.R.Beidler;G.G.Poirier;G.S.Salvesen;V.M.Dixit https://doi.org/10.1016/0092-8674(95)90541-3
- Science v.254 Prevention of apoptosis by a baculovirus gene during infection of insect cells Clem,R.J.;M.Fechheimer;L.K.Miller https://doi.org/10.1126/science.1962198
- Cell v.85 A license to kill Fraser,A.;G.Evan https://doi.org/10.1016/S0092-8674(00)81005-3
- Trends Biotechnol. v.16 Overcoming apoptosis: New methods for improving protein-expression systems Mastrangelo,A.J.;M.J.Betenbaugh https://doi.org/10.1016/S0167-7799(97)01159-1
- Biochim. Biophysis. Acta v.1366 Mitochondria as a regulator of apoptosis-doubt no more Susin,S.A.;N.Zamzami;G.Kroemer https://doi.org/10.1016/S0005-2728(98)00110-8
- Cell v.86 Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Liu,X.;C.N.Kim;J.Yang;X.Wang https://doi.org/10.1016/S0092-8674(00)80085-9
- Mol. Cell v.1 Autoactivation of pro-caspase-9 by Apaf-1-mediated oligomerization Srinivasula,S.M.;M.Ahmad;T.Fernandes-Alnemri;E.S.Alnemri https://doi.org/10.1016/S1097-2765(00)80095-7
- Drug Resist. Updat. v.2 Activation and role of caspases in chemocherapy-induced apoptosis Schmitt,E.;A.T.Snae;R.Bertrand https://doi.org/10.1054/drup.1999.0065
- Nature v.391 Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Rosse,T.;R.Olivier;L.Monney;M.Rager;S.Conus;I.Fellay;B.Jansen;C.Borner https://doi.org/10.1038/35160
- J. Biol. Chem. v.273 Pro-caspase-3 is a major physiologic target of caspase-8 Stennicke,H.R.;J.M.Jurgensmeier;H.Shin https://doi.org/10.1074/jbc.273.42.27084
- Science v.228 Involvement of the bcl-2 gene in human follicular lymphoma Tsujimoto,Y.;J.Cossman;E.Jaff;C.Croce https://doi.org/10.1126/science.3874430
- Nature v.348 Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death Hockenbery,D.;G.Nunez;C.Milliman;R.D.Screiber;S.Korsmeyer https://doi.org/10.1038/348334a0
- J. Virol. v.67 An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif Crook,N.E.;R.J.Clem;L.K.Miller
- J. Virol. v.68 An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motif Birnbaum,M.J.;R.J.Clem;L.K.Miller
- Genes Dev. v.13 IAP family proteins Suppressor of apoptosis Deveraux,Q.L.;J.C.Reed https://doi.org/10.1101/gad.13.3.239
- Nature v.388 X-linked IAP is a direct inhibitor of cell-death proteases Deveraux,Q.L.;R.Takahashi;G.S.Salvesen;J.C.Reed https://doi.org/10.1038/40792
- EMBO J. v.16 The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases Roy,N.;Q.L.Deveraux;R.Takahashi;G.S.Salvesen;J.C.Reed https://doi.org/10.1093/emboj/16.23.6914
- Cancer Res. v.58 IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas(CD95), Bax, caspases, and anticancer drugs Tamm,I.;Y.Wang;E.Sausville;D.A.Scudiero;N.Vigna;T.Oltersdorf;J.C.Reed
- EMBO J. v.17 IAP block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases Deveraux,Q.L.;N.Roy;H.R.Stennicke;T.Van Arsdale;Q.Zhou;S.M.Srinivasula;E.S.Alnemri;G.S.Salvesen;J.C.Reed https://doi.org/10.1093/emboj/17.8.2215
- Cell v.83 The TNFR2-TRAF signaling complex contains two novel proteins related to baculovirus inhibitor of apoptosis proteins Rothe,M.;M.G.Pan;W.J.Henzel;T.M.Ayers;D.V.Goeddel https://doi.org/10.1016/0092-8674(95)90149-3
- Annu. Rev. Genet. v.22 The heat shock proteins Linquist,S.;E.A.Craig https://doi.org/10.1146/annurev.ge.22.120188.003215
- Adv. Protein Chem. v.44 Structure and mechanism of 70-kDa heat-shock-related proteins Mckey,D.B. https://doi.org/10.1016/S0065-3233(08)60564-1
- Biol. Chem. v.379 Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death Arrigo,A.P.
- Cell v.92 The Hsp70 and Hsp60 chaperone machines Bukau,B.;A.L.Horwich https://doi.org/10.1016/S0092-8674(00)80928-9
- EMBO J. v.11 Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity Jaattela,M.;D.Wissing;P.A.Bauer;G.C.Li
- EMBO J. v.17 Hsp70 exerts its anti-apoptotic function downstream of cspase-3-like proteases Jaattela,M.;D.Wissing;K.Kokholm;T.Kallunki;M.Egeblad https://doi.org/10.1093/emboj/17.21.6124
- EMBO J. v.15 Human hsp27, Drosophila hsp27 and human α-crystallin expression-mediated increase in glutathion is essential for the protective activity of these proteins against TNFα-Iinduced cell death Mehlen,P.;C.Kretz-Remy;X.Preville;A.P.Arrigo
- Science v.267 Apoptosis in the pathogenesis and treatment of disease Thompson,C.B. https://doi.org/10.1126/science.7878464
- Biochem. Biophys. Res. Commun. v.266 Apoptosis in human disease: A new skin for the old ceremony Fadeel,B.;S.Orrenius;B.Zhivotovsky https://doi.org/10.1006/bbrc.1999.1888
- Cell v.69 Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme Ray,C.A.;R.A.Black;S.R.Kronheim;T.A.Greenstreet;P.R.Sleath;G.S.Salvesen;D.J.Pickup https://doi.org/10.1016/0092-8674(92)90223-Y
- Science v.263 Prevention of vertebrate neuronal death by the crmA gene Gagliardini,V.;P.A.Fernandez;R.K.Lee;H.C.Drexler;R.J.Rotello;M.C.Fishman;J.Yuan https://doi.org/10.1126/science.8303301
- Proc. Natl. Acad. Sci. USA v.97 Transgenic mice neuronally expressing baculoviral p35 are resistant to diverse types of induced apoptosis, including seizure-associated neurodeg-eneration Viswanath,V.;Z.Wu;C.Fonck;Q.Wei;R.Boonplueang;J.K.Andersen https://doi.org/10.1073/pnas.030365297
- EMBO J. v.19 Targeted expression of baculovirus p35 caspase inhibitor in oligodendrocytes protects mice against autoimmune-mediated demyelination Hisahara,S.;T.Araki;F.Sugiyama;K.Yagami;M.Suzuki;K.Abe;K.Yamamura;J.Miyazaki;T.Momoi;T.Saruta;C.C.Bernard;H.Okano;M.Miura https://doi.org/10.1093/emboj/19.3.341
- Biochem. Biophys. Res. Commun. v.264 Marked induction of the IAP family antiapoptotic proteins survivin and XIAP by VEGF in vascular endothelial cells Tran,J.;J.Rak;C.Sheehan;S.D.Saibil;E.LaCasse;R.G.Korneluk;R.S.Kerbel https://doi.org/10.1006/bbrc.1999.1589
- Biotechnol. Bioeng. v.55 Extension of Sp2/0 hybridoma cell viability through interleukin-6 supplementation Chung,J.D.;C.Zabel;A.J.Sinskey;G.Stephanopoulos https://doi.org/10.1002/(SICI)1097-0290(19970720)55:2<439::AID-BIT21>3.0.CO;2-A
- Biotechnol. Bioeng. v.54 Prevention of hybridoma cell death by bcl-2 during suboptimal culture conditions Simpson,N.H.;A.E.Milner;M.Al-Rubeai https://doi.org/10.1002/(SICI)1097-0290(19970405)54:1<1::AID-BIT1>3.0.CO;2-K
- Biotechnol. Bioeng. v.71 Overexpression of bcl-2 inhibits sodium butyrate-induced apoptosis in Chinese hamster ovary cells resulting in enhanced humanized antibody production Kim,N.S.;G.M.Lee https://doi.org/10.1002/1097-0290(2000)71:3<184::AID-BIT1008>3.0.CO;2-W
- Biotechnol. Bioeng. v.78 Inhibition of sodium butyrate-induced apoptosis in recombinant Chinese hamster ovary cells by constitutively expressing antisense RNA of caspase-3 Kim,N.S.;G.M.Lee https://doi.org/10.1002/bit.10191
- Biotechnol. Bioeng. v.67 Part I. Bcl-2 and Bcl-x(L) limit apoptosis upon infection with alphavirus vectors Mastrangelo,A.J.;J.M.Hardwick;F.Bex;M.J.Betenbaugh https://doi.org/10.1002/(SICI)1097-0290(20000305)67:5<544::AID-BIT5>3.0.CO;2-#
- Biotechnol. Bioeng. v.67 Part Ⅱ. Overexpression of bcl-2 family members enhances survival of mammalian cells in response to various culture insults Mastrangelo,A.J.;J.M.Hardwick;S.Zou;M.J.Betenbaugh https://doi.org/10.1002/(SICI)1097-0290(20000305)67:5<555::AID-BIT6>3.0.CO;2-T
- Biotechnol. Bioeng. v.77 Inhibiting apoptosis in mammalian cell culture using the caspase inhibitor XIAP and deletion mutants Sauerwald,T.M.;M.J.Betenbaugh;G.A.Oyler https://doi.org/10.1002/bit.10154
- Biotechnol. Bioeng. v.81 Transfection of NS0 myeloma fusion partner cells with HSP70 gene results in higher hybridoma yield by improving cellular resistance to apoptosis Lasunskaia,E.B.;I.I.Fridlianskaia;Z.A.Darieva;M.S.Da Silva;M.M.Kanashiro;B.A.Margulis https://doi.org/10.1002/bit.10493
- Biotechnol. Bioeng. v.63 Apoptosis-resistant E1B-19K-expressing NS/0 myeloma cells exhibit increased viability and chimeric antibody productivity under perfusion culture conditions Mercille,S;B.Massie https://doi.org/10.1002/(SICI)1097-0290(19990605)63:5<529::AID-BIT3>3.0.CO;2-X
- Biotechnol. Tech. v.10 Silkworm hemolymph as a subsitute for fetal bovine serum in insect cell culture Ha,S.H.;T.H.Park;S.E.Kim
- Biotechnol. Bioprocess Eng. v.3 Oxidation-deficient silkworm hemolymph as a medium supplement for insect cell culture Kim,E.J.;J.Y.Choi;S.E.Kim;T.H.Park https://doi.org/10.1007/BF02932508
- J. Microbiol. Biotechnol. v.9 Reduction of FBS concentration through adaptation process in mammalian cell culture and addition of silkworm hemolymph in insect cell culture Kim,E.J.;T.H.Park
- Biotechnol. Lett. v.19 Utilization of silkworm hemolymph for production of recombinant protein in an insect cell-baculovirus system Ha,S.H.;T.H.Park https://doi.org/10.1023/A:1018484309194
- Biotechnol. Prog. v.15 Kinetic effect of silkworm hemolymph on the delayed host cell death in an insect cell-baculovirus system Rhee,W.J.;E.J.Kim;T.H.Park https://doi.org/10.1021/bp990093s
- Biochem. Biophys. Res. Commun. v.271 Silkworm hemolymph inhibits baculovirus-induced insect cell apoptosis Rhee,W.J.;T.H.Park https://doi.org/10.1006/bbrc.2000.2592
- J. Microbiol. Biotechnol. v.11 no.5 Flow cytometric analysis of the effect of silkworm hemolymph on the baculovirus-induced insect cell apoptosis Rhee,W.J.;T.H.Park
- Biochem. Biophys. Res. Commun. v.295 Silkworm hemolymph as a potent inhibitor of apoptosis in Sf9 cells Rhee,W.J.;E.J.Kim;T.H.Park https://doi.org/10.1016/S0006-291X(02)00746-5
- Biotechnol. Prog. v.18 Inhibition of human cell apoptosis by silkworm hemolymph Choi,S.S.;W.J.Rhee;T.H.Park https://doi.org/10.1021/bp020001q
- Biochem. Biophys. Res. Commun. v.285 Isolation and characterization of an apoptosis-inhibiting component from the hemolymph of Bombyx mori Kim,E.J.;W.J.Rhee;T.H.Park https://doi.org/10.1006/bbrc.2001.5148
- Biochim. Biophys. Acta v.670 Molecular properties and biosynthesis of major plasma proteins in Bombyx mori Izumi,S.;J.Fujie;S.Yamada;S.Tomino https://doi.org/10.1016/0005-2795(81)90013-1
- Develop. Biol. v.97 Development and sex-dependent regulation of storage protein synthesis in the silkworm, Bombyx mori Mine,E.;S.Izumi;M.Katsuki;S.Tomino https://doi.org/10.1016/0012-1606(83)90090-8
- Biochim. Biophys. Acta v.949 Structure and expression of mRNA coding for major plasma proteins of Bombyx mori Sakai,N.;S.Mori;S.Izumi;K.Haino Fukushima;T.Ogura;H.Maekawa;S.Tomino https://doi.org/10.1016/0167-4781(88)90086-3
- Ph. D. Thesis, Seoul National University Isolation of a Novel Anti-apoptotic Protein from the Hemolymph of Bombyx mori and Its Application to Animal Cell Culture Kim,E.J.
- Biotechnol. Adv. v.9 Production scale insect cell culture Agathos,S.N. https://doi.org/10.1016/0734-9750(91)90404-J
- Curr. Opin. Genet. Dev. v.3b Baculoviruses: High level expression on insect cells Miller,L.K.
- Invertebrate Cell System Infectivity of baculovirus to cultured cells Granados,R.R.;Y.Hashimoto;J.Mitsuhashi(ed.)