메뉴 건너뛰기




Volumn 71, Issue 2, 1997, Pages 1576-1582

Interaction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducers

Author keywords

[No Author keywords available]

Indexed keywords

TUMOR NECROSIS FACTOR ALPHA;

EID: 1842407248     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.2.1576-1582.1997     Document Type: Article
Times cited : (48)

References (52)
  • 1
    • 0028349539 scopus 로고
    • Molecular mechanisms of tumor necrosis factor-induced cytotoxicity. What we do understand and what we do not
    • Review
    • Beyaert, R., and W. Fiers. 1994. Molecular mechanisms of tumor necrosis factor-induced cytotoxicity. What we do understand and what we do not. FEBS Lett. 340:9-16. (Review.)
    • (1994) FEBS Lett. , vol.340 , pp. 9-16
    • Beyaert, R.1    Fiers, W.2
  • 2
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death
    • Boldin, M. P., T. M. Goncharov, Y. V. Goltsev, and D. Wallach. 1996. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death. Cell 85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 3
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin, M. P., E. E. Varfolomeev, Z. Pancer, I. L. Mett, J. H. Camonis, and D. Wallach. 1995. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J. Biol. Chem. 270:7795-7798.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 4
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Review
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature 349:117-127. (Review.)
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 7
    • 0026770670 scopus 로고
    • Putative GTP-binding protein. Gtrl, associated with the function of the Pho84 inorganic phosphate transporter in Saccharomyces cerevisiae
    • Bun-Ya, M., S. Harashima, and Y. Oshima. 1992 Putative GTP-binding protein. Gtrl, associated with the function of the Pho84 inorganic phosphate transporter in Saccharomyces cerevisiae. Mol. Cell. Biol. 12:2958-2966.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2958-2966
    • Bun-Ya, M.1    Harashima, S.2    Oshima, Y.3
  • 8
    • 0024557043 scopus 로고
    • Epidermal growth factor receptor is down-regulated by a 10,400 mw protein encoded by the E3 region of adenovirus
    • Carlin, C. R., A. E. Tollefson, H. A. Brady, B. L. Hoffman, and W. S. M. Wold. 1989. Epidermal growth factor receptor is down-regulated by a 10,400 mw protein encoded by the E3 region of adenovirus. Cell 57:135-144.
    • (1989) Cell , vol.57 , pp. 135-144
    • Carlin, C.R.1    Tollefson, A.E.2    Brady, H.A.3    Hoffman, B.L.4    Wold, W.S.M.5
  • 9
    • 0028351930 scopus 로고
    • Lipid modifications of G proteins
    • Review
    • Casey, P. J. 1994. Lipid modifications of G proteins. Curr. Opin. Cell Biol. 6:219-225. (Review.)
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 219-225
    • Casey, P.J.1
  • 11
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A. M., K. O'Rourke, M. Tewari, and V. M. Dixit. 1995. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81:505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 12
    • 0028059445 scopus 로고
    • Functional complementation of the adenovirus E1B 19-kilodalton protein with Bcl-2 in the inhibition of apoptosis in infected cells
    • Chiou, S. K., C. C. Tseng, L. Rao, and E. White. 1994. Functional complementation of the adenovirus E1B 19-kilodalton protein with Bcl-2 in the inhibition of apoptosis in infected cells. J. Virol. 68:6553-6566.
    • (1994) J. Virol. , vol.68 , pp. 6553-6566
    • Chiou, S.K.1    Tseng, C.C.2    Rao, L.3    White, E.4
  • 14
    • 0025734783 scopus 로고
    • The T/E1A-binding domain of the retinoblastoma product can interact selectively with a sequence-specific DNA-binding protein
    • Chittenden, T., D. M. Livingston, and W. G. Kaelin, Jr. 1991. The T/E1A-binding domain of the retinoblastoma product can interact selectively with a sequence-specific DNA-binding protein. Cell 65:1073-1082.
    • (1991) Cell , vol.65 , pp. 1073-1082
    • Chittenden, T.1    Livingston, D.M.2    Kaelin Jr., W.G.3
  • 15
    • 0029066697 scopus 로고
    • Contenders in FasL/TNF death signaling
    • Review
    • Cleveland, J. L., and J. N. Ihle. 1995. Contenders in FasL/TNF death signaling. Cell 81:479-482. (Review.)
    • (1995) Cell , vol.81 , pp. 479-482
    • Cleveland, J.L.1    Ihle, J.N.2
  • 18
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 20
    • 0023881028 scopus 로고
    • A 14,700 MW protein from the E3 region of adenovirus inhibits cytolysis by tumor necrosis factor
    • Gooding, L. R., L. W. Elmore, A. E. Tollefson, H. A. Brady, and W. S. M. Wold. 1988. A 14,700 MW protein from the E3 region of adenovirus inhibits cytolysis by tumor necrosis factor. Cell 53:341-346.
    • (1988) Cell , vol.53 , pp. 341-346
    • Gooding, L.R.1    Elmore, L.W.2    Tollefson, A.E.3    Brady, H.A.4    Wold, W.S.M.5
  • 21
    • 0025812952 scopus 로고
    • The 10,400- and 14,500-dalton proteins encoded by region E3 of adenovirus function together to protect many but not all mouse cell lines against lysis by tumor necrosis factor
    • Gooding, L. R., T. S. Ranheim, A. E. Tollefson, L. Aquino, P. J. Duerksen-Hughes, T. M. Horton, and W. S. M. Wold. 1991. The 10,400- and 14,500-dalton proteins encoded by region E3 of adenovirus function together to protect many but not all mouse cell lines against lysis by tumor necrosis factor. J. Virol. 65:4114-4123.
    • (1991) J. Virol. , vol.65 , pp. 4114-4123
    • Gooding, L.R.1    Ranheim, T.S.2    Tollefson, A.E.3    Aquino, L.4    Duerksen-Hughes, P.J.5    Horton, T.M.6    Wold, W.S.M.7
  • 22
    • 0025029079 scopus 로고
    • The adenovirus E3-14.7K protein is a general inhibitor of tumor necrosis factor-mediated cytolysis
    • Gooding, L. R., I. O. Sofola, A. E. Tollefson, P. J. Duerksen-Hughes, and W. S. M. Wold. 1990. The adenovirus E3-14.7K protein is a general inhibitor of tumor necrosis factor-mediated cytolysis. J. Immunol. 145:3080-3086.
    • (1990) J. Immunol. , vol.145 , pp. 3080-3086
    • Gooding, L.R.1    Sofola, I.O.2    Tollefson, A.E.3    Duerksen-Hughes, P.J.4    Wold, W.S.M.5
  • 23
    • 0029664296 scopus 로고    scopus 로고
    • ICE family proteases: Mediators of all apoptotic cell death?
    • Henkart, P. A. 1996. ICE family proteases: mediators of all apoptotic cell death? Immunity 4:195-201.
    • (1996) Immunity , vol.4 , pp. 195-201
    • Henkart, P.A.1
  • 24
    • 0025815367 scopus 로고
    • Adenovirus E3 14.7K protein functions in the absence of other adenovirus proteins to protect transfected cells from tumor necrosis factor cytolysis
    • Horton. T. M., T. S. Ranheim, L. Aquino, D. I. Kusher, S. K. Saha, C. F. Ware, W. S. M. Wold, and L. R. Gooding. 1991. Adenovirus E3 14.7K protein functions in the absence of other adenovirus proteins to protect transfected cells from tumor necrosis factor cytolysis. J. Virol. 65:2629-2639.
    • (1991) J. Virol. , vol.65 , pp. 2629-2639
    • Horton, T.M.1    Ranheim, T.S.2    Aquino, L.3    Kusher, D.I.4    Saha, S.K.5    Ware, C.F.6    Wold, W.S.M.7    Gooding, L.R.8
  • 25
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu, H., J. Huang, H.-B. Shu, V. Baichwal, and D. V. Goeddel. 1996. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4:387-396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.-B.3    Baichwal, V.4    Goeddel, D.V.5
  • 26
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu, H., B. H. Shu, M. G. Pan, and D. V. Goeddel. 1996. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84:299-308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, B.H.2    Pan, M.G.3    Goeddel, D.V.4
  • 27
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • Hsu, H., J. Xiong, and D. V. Goeddel. 1995. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell 81:495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 28
    • 0027943499 scopus 로고
    • A novel RING finger protein interacts with the cytoplasmic domain of CD40
    • Hu, H. M., K. O'Rourke, M. S. Boguski, and V. M. Dixit. 1994. A novel RING finger protein interacts with the cytoplasmic domain of CD40. J. Biol. Chem. 269:30069-30072.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30069-30072
    • Hu, H.M.1    O'Rourke, K.2    Boguski, M.S.3    Dixit, V.M.4
  • 30
    • 0028297068 scopus 로고
    • The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling
    • Review
    • Kolesnick, R., and D. W. Golde. 1994. The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell 77:325-328. (Review.)
    • (1994) Cell , vol.77 , pp. 325-328
    • Kolesnick, R.1    Golde, D.W.2
  • 31
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Review
    • Martin, S. J. and D. R. Green. 1995. Protease activation during apoptosis: death by a thousand cuts? Cell 82:349-352. (Review.)
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 32
    • 0029045520 scopus 로고
    • Getting to know you: Viruses meet CD40 ligand
    • Comment
    • McFadden, G. 1995. Getting to know you: viruses meet CD40 ligand. Nat. Med. 1:408-409. (Comment.)
    • (1995) Nat. Med. , vol.1 , pp. 408-409
    • McFadden, G.1
  • 33
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos, G., M. Birkenbach, R. Yalamanchili, T. VanArsdale, C. Ware, and E. Kieff. 1995. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell 80:389-399.
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1    Birkenbach, M.2    Yalamanchili, R.3    VanArsdale, T.4    Ware, C.5    Kieff, E.6
  • 35
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe, M., S. C. Wong, W. J. Henzel, and D. V. Goeddel. 1994. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 78:681-692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 36
    • 0025923344 scopus 로고
    • Modulation of phospholipase A2 activity in zymogen granule membranes by GTP[S]; evidence for GTP-binding protein regulation
    • Rubin, R. P., M. Withiam-Leitch, and S. G. Laychock. 1991. Modulation of phospholipase A2 activity in zymogen granule membranes by GTP[S]; evidence for GTP-binding protein regulation. Biochem. Biophys. Res. Commun. 177:22-26.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 22-26
    • Rubin, R.P.1    Withiam-Leitch, M.2    Laychock, S.G.3
  • 37
    • 0028940364 scopus 로고
    • An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3
    • Schreiber-Agus, N., L. Chin, K. Chen, R. Torres, G. Rao, P. Guida, A. I. Skolultchi, and R. A. DePinho. 1995. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80:777-786.
    • (1995) Cell , vol.80 , pp. 777-786
    • Schreiber-Agus, N.1    Chin, L.2    Chen, K.3    Torres, R.4    Rao, G.5    Guida, P.6    Skolultchi, A.I.7    DePinho, R.A.8
  • 38
    • 0027970842 scopus 로고
    • Evolutionary relationships and functional conservation among vertebrate Max-associated proteins: The zebra fish homolog of Mxi1
    • Schreiber-Agus, N., L. Chin, K. Chen, R. Torres, C. T. Thomson, J. C. Sacchettini, and R. A. DePinho. 1994. Evolutionary relationships and functional conservation among vertebrate Max-associated proteins: the zebra fish homolog of Mxi1. Oncogene 9:3167-3177.
    • (1994) Oncogene , vol.9 , pp. 3167-3177
    • Schreiber-Agus, N.1    Chin, L.2    Chen, K.3    Torres, R.4    Thomson, C.T.5    Sacchettini, J.C.6    DePinho, R.A.7
  • 39
    • 0028849086 scopus 로고
    • Cloning of a novel family of mammalian GTP-binding proteins (RagA, RacB, RagB') with remote similarity to the ras-related GTPases
    • Schurmann, A., A. Brauers, S. Mabmann, W. Becker, and H. G. Joost 1995. Cloning of a novel family of mammalian GTP-binding proteins (RagA, RacB, RagB') with remote similarity to the ras-related GTPases. J. Biol. Chem. 270:28982-28988.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28982-28988
    • Schurmann, A.1    Brauers, A.2    Mabmann, S.3    Becker, W.4    Joost, H.G.5
  • 40
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
    • Review
    • Smith, C. A., T. Farrah, and R. G. Goodwin. 1994. The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell 76:959-962. (Review.)
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 41
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song, H. Y., J. D. Dunbar, Y. X. Zhang, D. Guo, and D. B. Donner. 1995. Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 270:3574-3581.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3574-3581
    • Song, H.Y.1    Dunbar, J.D.2    Zhang, Y.X.3    Guo, D.4    Donner, D.B.5
  • 42
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger, B. Z., P. Leder, T. H. Lee, E. Kim, and B. Seed. 1995. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 81:513-523.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 44
    • 0028139267 scopus 로고
    • The adenovirus E3 14.7K protein, an antagonist of tumor necrosis factor cytolysis, increases the virulence of vaccinia virus in SCID mice
    • Tufariello, J., S. Cho, and M. S. Horwitz. 1994. The adenovirus E3 14.7K protein, an antagonist of tumor necrosis factor cytolysis, increases the virulence of vaccinia virus in SCID mice. Proc. Natl. Acad. Sci. USA 91:10987-10991.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10987-10991
    • Tufariello, J.1    Cho, S.2    Horwitz, M.S.3
  • 45
    • 0028049104 scopus 로고
    • The adenovirus E3 14.7-kilodalton protein which inhibits cytolysis by tumor necrosis factor increases the virulence of vaccinia virus in a murine pneumonia model
    • Tufariello, J., S. Cho, and M. S. Horwitz. 1994. The adenovirus E3 14.7-kilodalton protein which inhibits cytolysis by tumor necrosis factor increases the virulence of vaccinia virus in a murine pneumonia model. J. Virol. 68:453-462.
    • (1994) J. Virol. , vol.68 , pp. 453-462
    • Tufariello, J.1    Cho, S.2    Horwitz, M.S.3
  • 47
    • 0030046508 scopus 로고    scopus 로고
    • Life, death, and the pursuit of apoptosis
    • White, E. 1996. Life, death, and the pursuit of apoptosis. Genes Dev. 10:1-15.
    • (1996) Genes Dev. , vol.10 , pp. 1-15
    • White, E.1
  • 48
    • 0026773471 scopus 로고
    • The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor alpha
    • White, E., P. Sabbatini, M. Debbas, W. S. M. Wold, D. I. Kusher, and L. R. Gooding. 1992. The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor alpha. Mol. Cell. Biol. 12:2570-2580.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2570-2580
    • White, E.1    Sabbatini, P.2    Debbas, M.3    Wold, W.S.M.4    Kusher, D.I.5    Gooding, L.R.6
  • 49
    • 0028061798 scopus 로고
    • Adenovirus proteins that subvert host defenses
    • Review
    • Wold, W. S. M., T. W. Hermiston, and A. E. Tollefson. 1994. Adenovirus proteins that subvert host defenses. Trends Microbiol. 2:437-443. (Review.)
    • (1994) Trends Microbiol. , vol.2 , pp. 437-443
    • Wold, W.S.M.1    Hermiston, T.W.2    Tollefson, A.E.3
  • 51
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan, J., S. Shaham, S. Ledoux, H. M. Ellis, and H. R. Horvitz. 1993. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 75:641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 52
    • 0026474669 scopus 로고
    • The adenovirus E3 region 14.7 kDa protein, heat and sodium arsinate inhibit the TNF-induced release of arachidonic acid
    • Zilli, D., C. Voelkel-Johnson, T. Skinner, and S. M. Laster. 1992. The adenovirus E3 region 14.7 kDa protein, heat and sodium arsinate inhibit the TNF-induced release of arachidonic acid. Biochem. Biophys. Res. Commun. 188:177-183.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 177-183
    • Zilli, D.1    Voelkel-Johnson, C.2    Skinner, T.3    Laster, S.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.