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Volumn 87, Issue 16, 2013, Pages 9199-9207

Frog virus 3 open reading frame 97R localizes to the endoplasmic reticulum and induces nuclear invaginations

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; B CELL LYMPHOMA 2 HOMOLOGY 1 DOMAIN PROTEIN; MYELOID CELL LEUKEMIA 1 PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84881239571     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00637-13     Document Type: Article
Times cited : (9)

References (39)
  • 1
    • 0013908835 scopus 로고
    • Viruses and renal carcinoma of Rana pipiens
    • Granoff A, Came PE, Breeze DC. 1966. Viruses and renal carcinoma of Rana pipiens. 1. The isolation and properties of virus from normal and tumor tissue. Virology 29:133-148.
    • (1966) Virology , vol.29 , pp. 133-148
    • Granoff, A.1    Came, P.E.2    Breeze, D.C.3
  • 2
    • 2542454676 scopus 로고    scopus 로고
    • Comparative genomic analyses of frog virus 3, type species of the genus Ranavirus (family Iridoviridae)
    • Tan WGH, Barkman TJ, Chinchar VG, Essani K. 2004. Comparative genomic analyses of frog virus 3, type species of the genus Ranavirus (family Iridoviridae). Virology 323:70-84.
    • (2004) Virology , vol.323 , pp. 70-84
    • Tan, W.G.H.1    Barkman, T.J.2    Chinchar, V.G.3    Essani, K.4
  • 5
    • 33846848887 scopus 로고    scopus 로고
    • Comparative genomic analysis of the family Iridoviridae: reannotating and defining the core set of iridovirus genes
    • Eaton H, Metcalf J, Penny E, Tcherepanov V, Upton C, Brunetti C. 2007. Comparative genomic analysis of the family Iridoviridae: reannotating and defining the core set of iridovirus genes. Virol. J. 4:11-27.
    • (2007) Virol. J. , vol.4 , pp. 11-27
    • Eaton, H.1    Metcalf, J.2    Penny, E.3    Tcherepanov, V.4    Upton, C.5    Brunetti, C.6
  • 6
    • 0036791781 scopus 로고    scopus 로고
    • Viral homologs of BCL-2: role of apoptosis in the regulation of virus infection
    • Cuconati A, White E. 2002. Viral homologs of BCL-2: role of apoptosis in the regulation of virus infection. Genes Dev. 16:2465-2478.
    • (2002) Genes Dev. , vol.16 , pp. 2465-2478
    • Cuconati, A.1    White, E.2
  • 9
    • 1942521233 scopus 로고    scopus 로고
    • Morphological changes contribute to apoptotic cell death and are affected by caspase-3 and caspase-6 inhibitors during red sea bream iridovirus permissive replication
    • Imajoh M, Sugiura H, Oshima S. 2004. Morphological changes contribute to apoptotic cell death and are affected by caspase-3 and caspase-6 inhibitors during red sea bream iridovirus permissive replication. Virology 322:220-230.
    • (2004) Virology , vol.322 , pp. 220-230
    • Imajoh, M.1    Sugiura, H.2    Oshima, S.3
  • 13
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang CX, Youle RJ. 2009. The role of mitochondria in apoptosis. Annu. Rev. Genet. 43:95-118.
    • (2009) Annu. Rev. Genet , vol.43 , pp. 95-118
    • Wang, C.X.1    Youle, R.J.2
  • 15
    • 64849113485 scopus 로고    scopus 로고
    • Control of mitochondrial apoptosis by the Bcl-2 family
    • Brunelle JK, Letai A. 2009. Control of mitochondrial apoptosis by the Bcl-2 family. J. Cell Sci. 122:437-441.
    • (2009) J. Cell Sci. , vol.122 , pp. 437-441
    • Brunelle, J.K.1    Letai, A.2
  • 16
    • 0038481271 scopus 로고    scopus 로고
    • Mitochondrial regulation of apoptosis
    • Mayer B, Oberbauer R. 2003. Mitochondrial regulation of apoptosis. News Physiol. Sci. 18:89-94.
    • (2003) News Physiol. Sci. , vol.18 , pp. 89-94
    • Mayer, B.1    Oberbauer, R.2
  • 18
    • 0033965412 scopus 로고    scopus 로고
    • Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins
    • Lutz RJ. 2000. Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins. Biochem. Soc. Trans. 28: 51-56.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 51-56
    • Lutz, R.J.1
  • 19
    • 0034747351 scopus 로고    scopus 로고
    • Comparison of the eIF-2 alpha homologous proteins of seven ranaviruses (Iridoviridae)
    • Essbauer S, Bremont M, Ahne W. 2001. Comparison of the eIF-2 alpha homologous proteins of seven ranaviruses (Iridoviridae). Virus Genes 23: 347-359.
    • (2001) Virus Genes , vol.23 , pp. 347-359
    • Essbauer, S.1    Bremont, M.2    Ahne, W.3
  • 20
    • 66749084358 scopus 로고    scopus 로고
    • Complete sequence determination of a novel reptile iridovirus isolated from soft-shelled turtle and evolutionary analysis of Iridoviridae
    • Huang Y, Huang X, Liu H, Gong J, Ouyang Z, Cui H, Cao J, Zhao Y, Wang X, Jiang Y, Qin Q. 2009. Complete sequence determination of a novel reptile iridovirus isolated from soft-shelled turtle and evolutionary analysis of Iridoviridae. BMC Genomics 10:224-238.
    • (2009) BMC Genomics , vol.10 , pp. 224-238
    • Huang, Y.1    Huang, X.2    Liu, H.3    Gong, J.4    Ouyang, Z.5    Cui, H.6    Cao, J.7    Zhao, Y.8    Wang, X.9    Jiang, Y.10    Qin, Q.11
  • 21
    • 33645154135 scopus 로고    scopus 로고
    • Cellular response to endoplasmic reticulum stress: a matter of life or death
    • Boyce M, Yuan J. 2006. Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ. 13:363-373.
    • (2006) Cell Death Differ. , vol.13 , pp. 363-373
    • Boyce, M.1    Yuan, J.2
  • 22
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M, Kaufman RJ. 2005. ER stress and the unfolded protein response. Mutat. Res. 569:29-63.
    • (2005) Mutat. Res. , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 24
    • 11144245597 scopus 로고    scopus 로고
    • Vaccinia virus F1L protein is a tail-anchored protein that functions at the mitochondria to inhibit apoptosis
    • Stewart TL, Wasilenko ST, Barry M. 2005. Vaccinia virus F1L protein is a tail-anchored protein that functions at the mitochondria to inhibit apoptosis. J. Virol. 79:1084-1098.
    • (2005) J. Virol. , vol.79 , pp. 1084-1098
    • Stewart, T.L.1    Wasilenko, S.T.2    Barry, M.3
  • 25
    • 0033118409 scopus 로고    scopus 로고
    • Complexes containing activating transcription factor (ATF)/cAMPresponsive-element-binding protein (CREB) interact with the CCAAT enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response
    • Fawcett TW, Martindale JL, Guyton KZ, Hai T, Holbrook NJ. 1999. Complexes containing activating transcription factor (ATF)/cAMPresponsive-element-binding protein (CREB) interact with the CCAAT enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response. Biochem. J. 339:135-141.
    • (1999) Biochem. J. , vol.339 , pp. 135-141
    • Fawcett, T.W.1    Martindale, J.L.2    Guyton, K.Z.3    Hai, T.4    Holbrook, N.J.5
  • 26
    • 60249089101 scopus 로고    scopus 로고
    • Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them?
    • Kumarswamy R, Chandna S. 2009. Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them? Mitochondrion 9:1-8.
    • (2009) Mitochondrion , vol.9 , pp. 1-8
    • Kumarswamy, R.1    Chandna, S.2
  • 29
    • 68549134924 scopus 로고    scopus 로고
    • Transcriptome analysis of frog virus 3, the type species of the genus Ranavirus, family Iridoviridae
    • Majji S, Thodima V, Sample R, Whitley D, Deng Y, Mao J, Chinchar VG. 2009. Transcriptome analysis of frog virus 3, the type species of the genus Ranavirus, family Iridoviridae. Virology 391:293-303.
    • (2009) Virology , vol.391 , pp. 293-303
    • Majji, S.1    Thodima, V.2    Sample, R.3    Whitley, D.4    Deng, Y.5    Mao, J.6    Chinchar, V.G.7
  • 30
    • 0003903343 scopus 로고    scopus 로고
    • Molecular cloning: a laboratory manual
    • 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Russell D. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001)
    • Sambrook, J.1    Russell, D.2
  • 32
    • 33646846666 scopus 로고    scopus 로고
    • Mcl-1 interacts with truncated Bid and inhibits its induction of cytochrome c release and its role in receptor-mediated apoptosis
    • Clohessy JG, Zhuang J, de Boer J, Gil-Gomez G, Brady HJM. 2006. Mcl-1 interacts with truncated Bid and inhibits its induction of cytochrome c release and its role in receptor-mediated apoptosis. J. Biol. Chem. 281:5750-5759.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5750-5759
    • Clohessy, J.G.1    Zhuang, J.2    de Boer, J.3    Gil-Gomez, G.4    Brady, H.J.M.5
  • 33
    • 0032439347 scopus 로고    scopus 로고
    • 3T3 cells have nuclear invaginations containing F-actin
    • Clubb BH, Locke M. 1998. 3T3 cells have nuclear invaginations containing F-actin. Tissue Cell 30:684-691.
    • (1998) Tissue Cell , vol.30 , pp. 684-691
    • Clubb, B.H.1    Locke, M.2
  • 34
    • 0041423293 scopus 로고    scopus 로고
    • Nuclear envelope irregularity is induced by RET/PTC during interphase
    • Fischer AH, Taysavang P, Jhiang SM. 2003. Nuclear envelope irregularity is induced by RET/PTC during interphase. Am. J. Pathol. 163:1091-1100.
    • (2003) Am. J. Pathol. , vol.163 , pp. 1091-1100
    • Fischer, A.H.1    Taysavang, P.2    Jhiang, S.M.3
  • 35
    • 72249101914 scopus 로고    scopus 로고
    • Astrocyte elevated gene-1: far more than just a gene regulated in astrocytes
    • Sarkar D, Emdad L, Lee SG, Yoo BK, Su ZZ, Fisher PB. 2009. Astrocyte elevated gene-1: far more than just a gene regulated in astrocytes. Cancer Res. 79:8529-8535.
    • (2009) Cancer Res. , vol.79 , pp. 8529-8535
    • Sarkar, D.1    Emdad, L.2    Lee, S.G.3    Yoo, B.K.4    Su, Z.Z.5    Fisher, P.B.6
  • 36
    • 0035208243 scopus 로고    scopus 로고
    • Intranuclear endoplasmic reticulum induced by Nopp140 mimics the nucleolar channel system of human endometrium
    • Isaac C, Pollard JW, Meier UT. 2001. Intranuclear endoplasmic reticulum induced by Nopp140 mimics the nucleolar channel system of human endometrium. J. Cell Sci. 114:4253-4264.
    • (2001) J. Cell Sci. , vol.114 , pp. 4253-4264
    • Isaac, C.1    Pollard, J.W.2    Meier, U.T.3
  • 38
  • 39
    • 0037089070 scopus 로고    scopus 로고
    • Trafficking of tail-anchored proteins: transport from the endoplasmic reticulum to the plasma membrane and sorting between surface domains in polarised epithelial cells
    • Bulbarelli A, Sprocati T, Barberi M, Pedrazzini E, Borgese N. 2002. Trafficking of tail-anchored proteins: transport from the endoplasmic reticulum to the plasma membrane and sorting between surface domains in polarised epithelial cells. J. Cell Sci. 115:1689-1702.
    • (2002) J. Cell Sci. , vol.115 , pp. 1689-1702
    • Bulbarelli, A.1    Sprocati, T.2    Barberi, M.3    Pedrazzini, E.4    Borgese, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.