Boo, a novel negative regulator of cell death, interacts with Apaf‐1
dc.contributor.author | Song, Qizhong | en_US |
dc.contributor.author | Kuang, Yongping | en_US |
dc.contributor.author | Dixit, Vishva M. | en_US |
dc.contributor.author | Vincenz, Claudius | en_US |
dc.date.accessioned | 2014-01-08T20:34:25Z | |
dc.date.available | 2014-01-08T20:34:25Z | |
dc.date.issued | 1999-01-04 | en_US |
dc.identifier.citation | Song, Qizhong; Kuang, Yongping; Dixit, Vishva M.; Vincenz, Claudius (1999). "Boo, a novel negative regulator of cell death, interacts with Apaf‐1." The EMBO Journal 18(1): 167-178. <http://hdl.handle.net/2027.42/102073> | en_US |
dc.identifier.issn | 0261-4189 | en_US |
dc.identifier.issn | 1460-2075 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/102073 | |
dc.publisher | John Wiley & Sons, Ltd | en_US |
dc.subject.other | Ovary | en_US |
dc.subject.other | Apaf‐1 | en_US |
dc.subject.other | Apoptosis | en_US |
dc.subject.other | Boo | en_US |
dc.subject.other | Caspase‐9 | en_US |
dc.title | Boo, a novel negative regulator of cell death, interacts with Apaf‐1 | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.identifier.pmid | 9878060 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102073/1/emboj7591454.pdf | |
dc.identifier.doi | 10.1093/emboj/18.1.167 | en_US |
dc.identifier.source | The EMBO Journal | en_US |
dc.identifier.citedreference | Ried HL and Jaffe N ( 1994 ) Radiation‐induced changes in long‐term survivors of childhood cancer after treatment with radiation therapy. Semin Roentgenol, 29, 6 – 14. | en_US |
dc.identifier.citedreference | Ratts VS, Flaws JA, Kolp R, Sorenson CM and Tilly JL ( 1995 ) Ablation of bcl‐2 gene expression decreases the numbers of oocytes and primordial follicles established in the post‐natal female mouse gonad. Endocrinology, 136, 3665 – 3668. | en_US |
dc.identifier.citedreference | Reed JC ( 1994 ) Bcl‐2 and the regulation of programmed cell death. J Cell Biol, 124, 1 – 6. | en_US |
dc.identifier.citedreference | Ross AJ, Waymire KG, Moss JE, Parlow AF, Skinner MK, Russell LD and MacGregor GR ( 1998 ) Testicular degeneration in Bclw‐defient mice. Nature Genet, 18, 251 – 256. | en_US |
dc.identifier.citedreference | Sattler M et al. ( 1997 ) Structure of Bcl‐x L –Bax peptide complex: recognition between regulators of apoptosis. Science, 275, 983 – 986. | en_US |
dc.identifier.citedreference | Sedlak TW, Oltvai ZN, Yang E, Wang K, Boise LH, Thompson CB and Korsmeyer SJ ( 1995 ) Multiple bcl‐2 family members demonstrate selective dimerizations with bax. Proc Natl Acad Sci USA, 92, 7834 – 7838. | en_US |
dc.identifier.citedreference | Shaham S and Horvitz HR ( 1996a ) An alternatively spliced C.elegans ced‐4 RNA encodes a novel cell death inhibitor. Cell, 86, 201 – 208. | en_US |
dc.identifier.citedreference | Shaham S and Horvitz HR ( 1996b ) Developing Caenorhabditis elegans neurons may contain both cell‐death protective and killer activities. Genes Dev, 10, 578 – 591. | en_US |
dc.identifier.citedreference | Simonian PL, Grillot DAM, Merino R and Nunez G ( 1996 ) Bax can antagonize Bcl‐XL during etoposide and cisplatin‐induced cell death independently of its heterodimerization with Bcl‐XL. J Biol Chem, 271, 22764 – 22772. | en_US |
dc.identifier.citedreference | Spector MS, Desnoyers S, Hoeppner DJ and Hengartner MO ( 1997 ) Interaction between the C.elegans cell‐death regulators CED‐9 and CED‐4. Nature, 385, 653 – 656. | en_US |
dc.identifier.citedreference | Thompson CB ( 1995 ) Apoptosis in the pathogenesis and treatment of disease. Science, 267, 1456 – 1462. | en_US |
dc.identifier.citedreference | Tilly JL ( 1996 ) Apoptosis and ovarian function. Rev Reprod, 1, 162 – 172. | en_US |
dc.identifier.citedreference | Tilly JL, Tilly KI, Kenton ML and Johnson AL ( 1995 ) Expression of members of the bcl‐2 gene family in the immature rat ovary: equine chorionic gonadotropin‐mediated inhibition of granulosa cell apoptosis is associated with decreased bax and constitutive bcl‐2 and bcl‐xlong messenger ribonucleic acid levels. Endocrinology, 136, 232 – 241. | en_US |
dc.identifier.citedreference | Vaux DL, Haecker G and Strasser A ( 1994 ) An evolutionary perspective on apoptosis. Cell, 76, 777 – 779. | en_US |
dc.identifier.citedreference | White E ( 1996 ) Life, death and the pursuit of apoptosis. Genes Dev, 10, 1 – 15. | en_US |
dc.identifier.citedreference | Wu D, Wallen HD, Inohara N and Nunez G ( 1997a ) Interaction and regulation of the Caenorhabditis elegans death protease CED‐3 by CED‐4 and CED‐9. J Biol Chem, 272, 21449 – 21454. | en_US |
dc.identifier.citedreference | Wu D, Wallen HD and Nunez G ( 1997b ) Interaction and regulation of subcellular localization of CED‐4 by CED‐9. Science, 275, 1126 – 1129. | en_US |
dc.identifier.citedreference | Yin XM, Oltvai ZN and Korsmeyer SJ ( 1994 ) BH1 and BH2 domains of Bcl‐2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature, 369, 321 – 323. | en_US |
dc.identifier.citedreference | Yuan J, Shaham S, Ledoux S, Ellis HM and Horvitz HR ( 1993 ) The C.elegans cell death gene ced‐3 encodes a protein similar to mammalian interleukin‐1β‐converting enzyme. Cell, 75, 641 – 652. | en_US |
dc.identifier.citedreference | Zha H, Aime‐Sempe C, Sato T and Reed JC ( 1996 ) Proapoptotic protein Bax heterodimerizes with Bcl‐2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem, 271, 7440 – 7444. | en_US |
dc.identifier.citedreference | Zou H, Henzel WJ, Liu X, Lutschg A and Wang X ( 1997 ) Apaf‐1, a human protein homologous to C.elegans CED‐4, participates in cytochrome c ‐dependent activation of caspase‐3. Cell, 90, 405 – 413. | en_US |
dc.identifier.citedreference | Armstrong RC et al. ( 1996 ) Fas‐induced activation of the cell death‐related protease CPP32 is inhibited by Bcl‐2 and by ICE family protease inhibitors. J Biol Chem, 271, 16850 – 16855. | en_US |
dc.identifier.citedreference | Beaumont HM and Mandl AM ( 1962 ) A quantitative and cytological study of oogonia and oocytes in the foetal and neonatal rat. Proc R Soc Lond (Ser B), 155, 557 – 579. | en_US |
dc.identifier.citedreference | Bergeron L et al. ( 1998 ) Defects in regulation of apoptosis in caspase‐2‐deficient mice. Genes Dev, 12, 1304 – 1314. | en_US |
dc.identifier.citedreference | Boise LH, Gottschalk AR, Quintans J and Thompson CB ( 1995 ) Bcl‐2 and Bcl‐2‐related proteins in apoptosis regulation. Curr Top Microbiol, 200, 107 – 121. | en_US |
dc.identifier.citedreference | Brown R ( 1997 ) The bcl‐2 family of proteins. Br Med Bull, 53, 466 – 477. | en_US |
dc.identifier.citedreference | Cheng EH‐Y, Levine B, Boise LH, Thompson CB and Hardwick M ( 1996 ) Bax‐independent inhibition of apoptosis by bcl‐xL. Nature, 379, 554 – 556. | en_US |
dc.identifier.citedreference | Cheng EH, Nicholas J, Bellows DS, Hayward GS, Guo HG, Reitz MS and Hardwick JM ( 1997 ) A Bcl‐2 homolog encoded by Kaposi sarcoma‐associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak. Proc Natl Acad Sci USA, 94, 690 – 694. | en_US |
dc.identifier.citedreference | Chinnaiyan AM and Dixit VM ( 1996 ) The cell‐death machine. Curr Biol, 6, 555 – 562. | en_US |
dc.identifier.citedreference | Chinnaiyan AM, Orth K, O'Rourke K, Duan H, Poirier GG and Dixit VM ( 1996 ) Molecular ordering of the cell death pathway: bcl‐2 and bcl‐xL function upstream of the CED‐3‐like apoptotic proteases. J Biol Chem, 271, 4573 – 4576. | en_US |
dc.identifier.citedreference | Chinnaiyan AM, O'Rourke K, Lane BR and Dixit VM ( 1997 ) Interaction of CED‐4 with CED‐3 and CED‐9: a molecular framework for cell death. Science, 275, 1122 – 1126. | en_US |
dc.identifier.citedreference | Chittenden T, Flemington C, Houghton AB, Ebb RG, Gallo GJ, Elangovan B, Chinnadurai G and Lutz RJ ( 1995a ) A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. EMBO J, 14, 5589 – 5596. | en_US |
dc.identifier.citedreference | Chittenden T, Harrington EA, O'Connor R, Flemington C, Lutz RJ, Evan GI and Guild BC ( 1995b ) Induction of apoptosis by the Bcl‐2 homologue Bak. Nature, 374, 733 – 736. | en_US |
dc.identifier.citedreference | Cohen GM ( 1997 ) Caspases: the executioners of apoptosis. Biochem J, 326, 1 – 16. | en_US |
dc.identifier.citedreference | Duan H and Dixit VM ( 1997 ) RAIDD is a new ‘death’ adaptor molecule. Nature, 385, 86 – 89. | en_US |
dc.identifier.citedreference | Duan H, Orth K, Chinnaiyan AM, Poirier GG, Froelich CJ, He WW and Dixit VM ( 1996 ) ICE‐LAP6, a novel member of the ICE/Ced‐3 gene family, is activated by the cytotoxic T cell protease granzyme B. J Biol Chem, 271, 16720 – 16724. | en_US |
dc.identifier.citedreference | Ellis HM and Horvitz HR ( 1986 ) Genetic control of programmed cell death in the nematode Caenorhabditis elegans. Cell, 44, 817 – 829. | en_US |
dc.identifier.citedreference | Familiari G, Caggiati A, Nottola SA, Ermini M, Di Benedetto MR and Motta PM ( 1993 ) Ultrastructure of human ovarian primordial follicles after combination chemotherapy for Hodgkin's disease. Human Reprod, 8, 2080 – 2087. | en_US |
dc.identifier.citedreference | Farrow SN and Brown R ( 1996 ) New members of the bcl‐2 family and their protein partners. Curr Opin Genet Dev, 6, 45 – 49. | en_US |
dc.identifier.citedreference | Furuchi T, Masuko K, Nishimune Y, Obinata M and Matsui Y ( 1996 ) Inhibition of testicular germ cell apoptosis and differentiation in mice misexpressing Bcl‐2 in spermatogonia. Development, 122, 1703 – 1709. | en_US |
dc.identifier.citedreference | Gibson L et al. ( 1996 ) bcl‐w, a novel member of the bcl‐2 family, promotes cell survival. Oncogene, 13, 665 – 675. | en_US |
dc.identifier.citedreference | Golstein P ( 1997 ) Controlling cell death. Science, 275, 1081 – 1082. | en_US |
dc.identifier.citedreference | Gonzalez‐Garcia M, Perez‐Ballestero R, Ding L, Duan L, Boise LH, Thompson CB and Nunez G ( 1994 ) bcl‐XL is the major bcl‐x mRNA form expressed during murine development and its product localizes to mitochondria. Development, 120, 3033 – 3042. | en_US |
dc.identifier.citedreference | Hengartner MO and Horvitz HR ( 1994a ) Activation of C.elegans cell death protein CED‐9 by an amino‐acid substitution in a domain conserved in Bcl‐2. Nature, 369, 318 – 320. | en_US |
dc.identifier.citedreference | Hengartner MO and Horvitz HR ( 1994b ) C.elegans cell survival gene ced‐9 encodes a functional homolog of the mammalian proto‐oncogene bcl‐2. Cell, 76, 665 – 676. | en_US |
dc.identifier.citedreference | Hengartner MO and Horvitz HR ( 1994c ) Programmed cell death in Caenorhabditis elegans. Curr Opin Genet Dev, 4, 581 – 586. | en_US |
dc.identifier.citedreference | Hengartner MO, Ellis RE and Horovitz HR ( 1992 ) Caenorhabditis elegans gene ced‐9 protects cells from programmed cell death. Nature, 356, 494 – 499. | en_US |
dc.identifier.citedreference | Henkart P ( 1996 ) ICE family protease: mediators of all apoptotic cell death? Immunity, 4, 195 – 201. | en_US |
dc.identifier.citedreference | Hsu SY, Kaipia A, McGee E, Lomeli M and Hsueh AJ ( 1997 ) Bok is a pro‐apoptotic Bcl‐2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti‐apoptotic Bcl‐2 family members. Proc Natl Acad Sci USA, 94, 12401 – 12406. | en_US |
dc.identifier.citedreference | Hu Y, Benedict MA, Wu D, Inohara N and Nunez G ( 1998 ) Bcl‐XL interacts with Apaf‐1 and inhibits Apaf‐1‐dependent caspase‐9 activation. Proc Natl Acad Sci USA, 95, 4386 – 4391. | en_US |
dc.identifier.citedreference | Huang DC, Cory S and Strasser A ( 1997 ) Bcl‐2, Bcl‐XL and adenovirus protein E1B19kD are functionally equivalent in their ability to inhibit cell death. Oncogene, 14, 405 – 414. | en_US |
dc.identifier.citedreference | Huang DC, Adams JM and Cory S ( 1998 ) The conserved N‐terminal BH4 domain of Bcl‐2 homologues is essential for inhibition of apoptosis and interaction with CED‐4. EMBO J, 17, 1029 – 1039. | en_US |
dc.identifier.citedreference | Humke EW, Ni J and Dixit VM ( 1998 ) ERICE, a novel FLICE‐activatable caspase. J Biol Chem, 273, 15702 – 15707. | en_US |
dc.identifier.citedreference | Inohara N, Ekhterae D, Garcia I, Carrio R, Merino J, Merry A, Chen S and Nunez G ( 1998a ) Mtd, a novel Bcl‐2 family member activates apoptosis in the absence of heterodimerization with Bcl‐2 and Bcl‐XL. J Biol Chem, 273, 8705 – 8710. | en_US |
dc.identifier.citedreference | Inohara N et al. ( 1998b ) Diva, a Bcl‐2 homologue that binds directly to Apaf‐1 and induces BH3‐independent cell death. J Biol Chem, 273, 32479 – 32490. | en_US |
dc.identifier.citedreference | Knudson CM, Tung KS, Tourtellotte WG, Brown GA and Korsmeyer SJ ( 1995 ) Bax‐deficient mice with lymphoid hyperplasia and male germ cell death. Science, 270, 96 – 99. | en_US |
dc.identifier.citedreference | Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W and Reed JC ( 1993 ) Investigation of the subcellular distribution of the bcl‐2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum and outer mitochondrial membranes. Cancer Res, 53, 4701 – 4714. | en_US |
dc.identifier.citedreference | Kroemer G ( 1997 ) The proto‐oncogene Bcl‐2 and its role in regulating apoptosis. Nature Med, 3, 614 – 620. | en_US |
dc.identifier.citedreference | Kumar S and Harvey NL ( 1995 ) Role of multiple cellular proteases in the execution of programmed cell death. FEBS Lett, 375, 169 – 173. | en_US |
dc.identifier.citedreference | Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES and Wang X ( 1997 ) Cytochrome c and dATP‐dependent formation of Apaf‐1/caspase‐9 complex initiates an apoptotic protease cascade. Cell, 91, 479 – 489. | en_US |
dc.identifier.citedreference | O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S and Huang DC ( 1998 ) Bim: a novel member of the Bcl‐2 family that promotes apoptosis. EMBO J, 17, 384 – 395. | en_US |
dc.identifier.citedreference | Oltvai ZN, Milliman CL and Korsmeyer SJ ( 1993 ) Bcl‐2 hetero‐ dimerizes in vivo with a conserved homolog, BAX, that accelerates programmed cell death. Cell, 74, 609 – 619. | en_US |
dc.identifier.citedreference | Ottilie S et al. ( 1997 ) Dimerization properties of human BAD. Identification of a BH‐3 domain and analysis of its binding to mutant BCL‐2 and BCL‐XL proteins. J Biol Chem, 272, 30866 – 30872. | en_US |
dc.identifier.citedreference | Pan G, O'Rourke K and Dixit VM ( 1998 ) Caspase‐9, Bcl‐XL and Apaf‐1 form a ternary complex. J Biol Chem, 273, 5841 – 5845. | en_US |
dc.identifier.citedreference | Perez GI, Knudson CM, Leykin L, Korsmeyer SJ and Tilly JL ( 1997 ) Apoptosis‐associated signaling pathways are required for chemotherapy‐mediated female germ cell destruction. Nature Med, 3, 1228 – 1232. | en_US |
dc.identifier.citedreference | Raff MC ( 1992 ) Social controls on cell survival and cell death. Nature, 356, 397 – 400. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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