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harakiri , a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival‐promoting proteins Bcl‐2 and Bcl‐X L

dc.contributor.authorInohara, Naohiroen_US
dc.contributor.authorDing, Liyunen_US
dc.contributor.authorChen, Shuen_US
dc.contributor.authorNúñez, Gabrielen_US
dc.date.accessioned2014-01-08T20:34:41Z
dc.date.available2014-01-08T20:34:41Z
dc.date.issued1997-04-01en_US
dc.identifier.citationInohara, Naohiro; Ding, Liyun; Chen, Shu; Núñez, Gabriel (1997). " harakiri , a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survivalâ promoting proteins Bclâ 2 and Bclâ X L ." The EMBO Journal 16(7): 1686-1694. <http://hdl.handle.net/2027.42/102121>en_US
dc.identifier.issn0261-4189en_US
dc.identifier.issn1460-2075en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/102121
dc.publisherJohn Wiley & Sons, Ltden_US
dc.subject.otherHrken_US
dc.subject.otherBcl‐2 Familyen_US
dc.subject.otherApoptosisen_US
dc.subject.otherProgrammed Cell Deathen_US
dc.titleharakiri , a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival‐promoting proteins Bcl‐2 and Bcl‐X Len_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.identifier.pmid9130713en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/102121/1/emboj7590158.pdf
dc.identifier.doi10.1093/emboj/16.7.1686en_US
dc.identifier.sourceThe EMBO Journalen_US
dc.identifier.citedreferenceSwaroop A and Xu J ( 1993 ) cDNA libraries from human tissues and cell lines. Cytogenet Cell Genet, 64, 292 – 294.en_US
dc.identifier.citedreferenceMerino R, Grillot DA, Simonian PL, Muthukkumar S, Fanslow WC, Bondada S and Núñez G ( 1995 ) Modulation of anti‐IgM‐induced B cell apoptosis by Bcl‐X L and CD40 in WEHI‐231 cells: dissociation from cell cycle arrest and dependence of the antibody–IgM receptor interaction. J Immunol, 155, 3830 – 3838.en_US
dc.identifier.citedreferenceMotoyama N et al. ( 1995 ) Massive cell death of immature hematopoietic cells and neurons in Bcl‐x‐deficient mice. Science, 267, 1506 – 1510.en_US
dc.identifier.citedreferenceMuchmore SW et al. ( 1996 ) X‐ray and NMR structure of human Bcl‐xL, an inhibitor of programmed cell death. Nature, 381, 335 – 341.en_US
dc.identifier.citedreferenceNúñez G, London L, Hockenbery D, Alexander M, McKearn JP and Korsmeyer SJ ( 1990 ) Deregulated Bcl‐2 gene expression selectively prolongs survival of growth factor‐deprived hemopoietic cell lines. J Immunol, 144, 3602 – 3610.en_US
dc.identifier.citedreferenceOltvai ZN and Korsmeyer SJ ( 1994 ) Checkpoints of dueling dimers foil death wishes. Cell, 79, 189 – 192.en_US
dc.identifier.citedreferenceOltvai ZN, Milliman CL and Korsmeyer SJ ( 1993 ) Bcl‐2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell, 74, 609 – 619.en_US
dc.identifier.citedreferenceSato T et al. ( 1994 ) Interactions among members of the Bcl‐2 family analyzed with a yeast two‐hybrid system. Proc Natl Acad Sci USA, 91, 9283 – 9242.en_US
dc.identifier.citedreferenceShaw G and Kamen R ( 1986 ) A conserved AU sequence from the 3′ untranslated region of GM‐CSF mRNA mediates selective mRNA degradation. Cell, 46, 659 – 667.en_US
dc.identifier.citedreferenceSimonian PL, Grillot DAM, Merino R and Núñez G ( 1996 ) Bax can antagonize Bcl‐X L during etoposide and cisplatin‐induced cell death independently of its heterodimerization with Bcl‐X L. J Biol Chem, 271, 22764 – 22772.en_US
dc.identifier.citedreferenceTakayama S, Sato T, Krajewski S, Kochel K, Irie S, Millan JA and Reed JC ( 1995 ) Cloning and functional analysis of BAG‐1: a novel Bcl‐2‐binding protein with anti‐cell death activity. Cell, 80, 279 – 284.en_US
dc.identifier.citedreferenceThompson CB ( 1995 ) Apoptosis in the pathogenesis and treatment of disease. Science, 267, 1456 – 1462.en_US
dc.identifier.citedreferenceVaux DL, Cory S and Adams JM ( 1988 ) Bcl‐2 gene promotes haemopoietic cell survival and cooperates with c‐myc to immortalize pre‐B cells. Nature, 335, 440 – 442.en_US
dc.identifier.citedreferenceVeis DJ, Sorenson CM, Shutter JR and Korsmeyer SJ ( 1993 ) Bcl‐2‐deficient mice demonstrate fulminant lymphoid apoptosis, polycystic disease, and hypopigmented hair. Cell, 75, 229 – 240.en_US
dc.identifier.citedreferenceWang HG, Takayama S, Rapp UR and Reed JC ( 1996 ) Bcl‐2 interacting protein, BAG‐1, binds to and activates the kinase Raf‐1. Proc Natl Acad Sci USA, 93, 7063 – 7068.en_US
dc.identifier.citedreferenceWhite E ( 1996 ) Life, death and the pursuit of apoptosis. Genes Dev, 10, 1 – 15.en_US
dc.identifier.citedreferenceWhite E, Cipriani R, Sabbatini P and Denton A ( 1991 ) Adenovirus E1B 19‐kilodalton protein overcomes the cytotoxicity of E1A proteins. J Virol, 65, 2968 – 2978.en_US
dc.identifier.citedreferenceYamagata K, Sanders LK, Kaufmann WE, Yee Y, Barnes CA, Nathans D and Worley PF ( 1994 ) RheB, a growth factor‐ and synaptic activity‐regulated gene, encodes a novel Ras‐related protein. J Biol Chem, 269, 16333 – 16339.en_US
dc.identifier.citedreferenceYang E, Zha J, Jockel J, Boise LH, Thompson CB and Korsmeyer SJ ( 1995 ) Bacl, a heterodimeric partner for Bcl‐xL and Bcl‐2, displaces Bax and promotes cell death. Cell, 80, 285 – 291.en_US
dc.identifier.citedreferenceZha H, Aimé‐Sempé 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.citedreferenceAskew D, Ashmun R, Simmons B and Cleveland J ( 1991 ) Constitutive c‐ myc expression in an IL‐3‐dependent myeloid cell line suppresses cell cycle arrest and accelerates apoptosis. Oncogene, 6, 1915 – 1922.en_US
dc.identifier.citedreferenceBoise LH, González‐García M, Postema CE, Ding L, Lindsten T, Turka LA, Mao X, Núñez G and Thompson CB ( 1993 ) bcl‐x, a bcl‐2 related gene that functions as a dominant regulator of apoptotic cell death. Cell, 74, 597 – 608.en_US
dc.identifier.citedreferenceBoise LH, Minn AJ, Noel PJ, June CH, Accavitti MA, Lindsten T and Thompson CB ( 1995 ) CD28 costimulation can promote T cell survival by enhancing the expression of Bcl‐X L. Immunity, 3, 87 – 98.en_US
dc.identifier.citedreferenceBoyd JM, Malstrom S, Subramanian T, Venkatesh LK, Schaeper U, Elangovan B, D'Sa‐Eipper C and Chinnadural G ( 1994 ) Adenovirus E1B and 19 kDa and Bcl‐2 proteins interact with a common set of cellular proteins. Cell, 79, 341 – 351.en_US
dc.identifier.citedreferenceBoyd JM et al. ( 1995 ) Bik, a novel death‐inducing protein shares a distinct sequence motif with Bcl‐2 family proteins and interacts with viral and cellular survival‐promoting proteins. Oncogene, 11, 1921 – 1928.en_US
dc.identifier.citedreferenceChinnaiyan 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‐X L function upstream of the CED‐3‐like apoptotic proteases. J Biol Chem, 271, 4573 – 4576.en_US
dc.identifier.citedreferenceChittenden T, Harrington EA, O'Connor R, Flemington C, Lutz RJ, Evan GI and Guild BC ( 1995a ) Induction of apoptosis by the Bcl‐2 homologue Bak. Nature, 374, 733 – 736.en_US
dc.identifier.citedreferenceChittenden T, Flemington C, Houghton AB, Ebb GE, Gallo GJ, Elangovan B, Chinnadurai G and Lutz RJ ( 1995b ) 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.citedreferenceClarke MF et al. ( 1995 ) A recombinant bcl‐x s adenovirus selectively induces apoptosis in cancer cells, but not normal bone marrow cells. Proc Natl Acad Sci USA, 92, 11024 – 11028.en_US
dc.identifier.citedreferenceDuke RC and Cohen JJ ( 1994 ) Morphological and biochemical assays of apoptosis. In Coligan,J.E., Kruisbeek,A.M., Margulies,D.H., Shevach,E.M. and Strober,W. (eds), Current Protocols in Immunology Current Protocols, NY, pp. 3.17.1 – 3.17.3.en_US
dc.identifier.citedreferenceEvan GI, Wyllie AH, Gilbert CS, Littlewood TD, Land H, Brooks M, Waters CM, Penn LZ and Hancock DC ( 1992 ) Induction of apoptosis in fibroblasts by c‐myc protein. Cell, 69, 119 – 128.en_US
dc.identifier.citedreferenceFarrow SN, White JH, Martinou I, Raven T, Pun KT, Grinham CJ, Martinou JC and Brown R ( 1995 ) Cloning of a bcl‐2 homologue by interaction with adenovirus E1B 19K. Nature, 374, 731 – 733.en_US
dc.identifier.citedreferenceFeilotter HE, Hannon GJ, Ruddell CJ and Beach D ( 1994 ) Construction of an improved host strain for two hybrid screening. Nucleic Acids Res, 22, 1502 – 1503.en_US
dc.identifier.citedreferenceFernandez‐Sarabia MJ and Bischoff JR ( 1993 ) Bcl‐2 associates with the ras‐related protein R‐ras p23. Nature, 366, 274 – 275.en_US
dc.identifier.citedreferenceGonzález‐García M, Pérez‐Ballestero R, Ding L, Duan L, Boise LH, Thompson CB and Núñez G ( 1994 ) bcl‐x L 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.citedreferenceHan J, Sabbatini P, Perez D, Rao L, Modha D and White E ( 1996a ) The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53‐inducible and death‐promoting Bax protein. Genes Dev, 10, 461 – 477.en_US
dc.identifier.citedreferenceHan J, Sabbatini P and White E ( 1996b ) Induction of apoptosis by human Nbk/Bik, a BH3‐containing protein that interacts with E1B 19K. Mol Cell Biol, 16, 5857 – 5864.en_US
dc.identifier.citedreferenceHannon GJ, Demetrick D and Beach D ( 1993 ) Isolation of the Rb‐related p130 through its interaction with CDK2 and cyclins. Genes Dev, 7, 2378 – 2391.en_US
dc.identifier.citedreferenceHockenbery D, Núñez G, Milliman C, Scheiber RD and Korsmeyer SJ ( 1991 ) Bcl‐2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature, 348, 334 – 336.en_US
dc.identifier.citedreferenceKrajewski S, Tanaka S, Takeyama 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.owningcollnameInterdisciplinary and Peer-Reviewed


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