메뉴 건너뛰기




Volumn 13, Issue 2, 2005, Pages 41-44

Enterovirus protein 2B po(u)res out the calcium: A viral strategy to survive?

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CYCLOHEXIMIDE; CYTOCHROME C; DACTINOMYCIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS PROTEIN 2B;

EID: 12944321845     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2004.12.005     Document Type: Short Survey
Times cited : (57)

References (28)
  • 1
    • 0036744013 scopus 로고    scopus 로고
    • The viral manipulation of the host cellular and immune environments to enhance propagation and survival: A focus on RNA viruses
    • S. Mahalingam The viral manipulation of the host cellular and immune environments to enhance propagation and survival: a focus on RNA viruses J. Leukoc. Biol. 72 2002 429 439
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 429-439
    • Mahalingam, S.1
  • 2
    • 0028977987 scopus 로고
    • Apoptosis-inducing and apoptosis-preventing functions of poliovirus
    • E.A. Tolskaya Apoptosis-inducing and apoptosis-preventing functions of poliovirus J. Virol. 69 1995 1181 1189
    • (1995) J. Virol. , vol.69 , pp. 1181-1189
    • Tolskaya, E.A.1
  • 3
    • 0034120437 scopus 로고    scopus 로고
    • Competing death programs in poliovirus-infected cells: Commitment switch in the middle of the infectious cycle
    • V.I. Agol Competing death programs in poliovirus-infected cells: commitment switch in the middle of the infectious cycle J. Virol. 74 2000 5534 5541
    • (2000) J. Virol. , vol.74 , pp. 5534-5541
    • Agol, V.I.1
  • 4
    • 2442475430 scopus 로고    scopus 로고
    • The coxsackievirus 2B protein suppresses apoptotic host cell responses by manipulating intracellular Ca2+ homeostasis
    • M. Campanella The coxsackievirus 2B protein suppresses apoptotic host cell responses by manipulating intracellular Ca2+ homeostasis J. Biol. Chem. 279 2004 18440 18450
    • (2004) J. Biol. Chem. , vol.279 , pp. 18440-18450
    • Campanella, M.1
  • 5
    • 0030928285 scopus 로고    scopus 로고
    • Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release
    • F.J.M. Van Kuppeveld Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release EMBO J. 16 1997 3519 3532
    • (1997) EMBO J. , vol.16 , pp. 3519-3532
    • Van Kuppeveld, F.J.M.1
  • 6
    • 0030834131 scopus 로고    scopus 로고
    • Poliovirus protein 2BC increases cytosolic free calcium concentrations
    • R. Aldabe Poliovirus protein 2BC increases cytosolic free calcium concentrations J. Virol. 71 1997 6214 6217
    • (1997) J. Virol. , vol.71 , pp. 6214-6217
    • Aldabe, R.1
  • 7
    • 0029951824 scopus 로고    scopus 로고
    • Coxsackie B3 virus protein 2B contains cationic amphipathic helix that is required for viral RNA replication
    • F.J.M. Van Kuppeveld Coxsackie B3 virus protein 2B contains cationic amphipathic helix that is required for viral RNA replication J. Virol. 70 1996 3876 3886
    • (1996) J. Virol. , vol.70 , pp. 3876-3886
    • Van Kuppeveld, F.J.M.1
  • 8
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 9
    • 0037428390 scopus 로고    scopus 로고
    • Determinants for membrane association and permeabilization of the coxsackievirus 2B protein and the identification of the Golgi complex as the target organelle
    • A.S. De Jong Determinants for membrane association and permeabilization of the coxsackievirus 2B protein and the identification of the Golgi complex as the target organelle J. Biol. Chem. 278 2003 1012 1021
    • (2003) J. Biol. Chem. , vol.278 , pp. 1012-1021
    • De Jong, A.S.1
  • 10
    • 0037174990 scopus 로고    scopus 로고
    • Viroporin-mediated membrane permeabilization. Pore formation by nonstructural poliovirus 2B protein
    • A. Agirre Viroporin-mediated membrane permeabilization. Pore formation by nonstructural poliovirus 2B protein J. Biol. Chem. 277 2002 40434 40441
    • (2002) J. Biol. Chem. , vol.277 , pp. 40434-40441
    • Agirre, A.1
  • 11
    • 0031908686 scopus 로고    scopus 로고
    • A protein linkage map of the P2 nonstructural proteins of poliovirus
    • A. Cuconati A protein linkage map of the P2 nonstructural proteins of poliovirus J. Virol. 72 1998 1297 1307
    • (1998) J. Virol. , vol.72 , pp. 1297-1307
    • Cuconati, A.1
  • 12
    • 0036203022 scopus 로고    scopus 로고
    • Multimerization reactions of coxsackievirus proteins 2B, 2C and 2BC: A mammalian two-hybrid analysis
    • A.S. De Jong Multimerization reactions of coxsackievirus proteins 2B, 2C and 2BC: a mammalian two-hybrid analysis J. Gen. Virol. 83 2002 783 793
    • (2002) J. Gen. Virol. , vol.83 , pp. 783-793
    • De Jong, A.S.1
  • 13
    • 0036721022 scopus 로고    scopus 로고
    • Homomultimerization of the coxsackievirus 2B protein in living cells visualized by fluorescence resonance energy transfer microscopy
    • F.J.M. Van Kuppeveld Homomultimerization of the coxsackievirus 2B protein in living cells visualized by fluorescence resonance energy transfer microscopy J. Virol. 76 2002 9446 9456
    • (2002) J. Virol. , vol.76 , pp. 9446-9456
    • Van Kuppeveld, F.J.M.1
  • 14
    • 2442529754 scopus 로고    scopus 로고
    • Mutational Analysis of Different Regions in the Coxsackievirus 2B Protein: Requirements for Homo-multimerization, Membrane Permeabilization, Subcellular Localization, and Virus Replication
    • A.S. De Jong Mutational Analysis of Different Regions in the Coxsackievirus 2B Protein: Requirements for Homo-multimerization, Membrane Permeabilization, Subcellular Localization, and Virus Replication J. Biol. Chem. 279 2004 19924 19935
    • (2004) J. Biol. Chem. , vol.279 , pp. 19924-19935
    • De Jong, A.S.1
  • 15
    • 0034688231 scopus 로고    scopus 로고
    • Poliovirus protease 3C(pro) kills cells by apoptosis
    • A. Barco Poliovirus protease 3C(pro) kills cells by apoptosis Virology 266 2000 352 360
    • (2000) Virology , vol.266 , pp. 352-360
    • Barco, A.1
  • 16
    • 0033959603 scopus 로고    scopus 로고
    • Poliovirus 2A protease induces apoptotic cell death
    • D. Goldstaub Poliovirus 2A protease induces apoptotic cell death Mol. Cell. Biol. 20 2000 1271 1277
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1271-1277
    • Goldstaub, D.1
  • 17
    • 0041887188 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL overexpression inhibits cytochrome c release, activation of multiple caspases, and virus release following coxsackievirus B3 infection
    • C.M. Carthy Bcl-2 and Bcl-xL overexpression inhibits cytochrome c release, activation of multiple caspases, and virus release following coxsackievirus B3 infection Virology 313 2003 147 157
    • (2003) Virology , vol.313 , pp. 147-157
    • Carthy, C.M.1
  • 18
    • 0035848736 scopus 로고    scopus 로고
    • Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event
    • M.G. Annis Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event Oncogene 20 2001 1939 1952
    • (2001) Oncogene , vol.20 , pp. 1939-1952
    • Annis, M.G.1
  • 19
    • 0038464650 scopus 로고    scopus 로고
    • Regulation of cell death: The calcium-apoptosis link
    • S. Orrenius Regulation of cell death: the calcium-apoptosis link Nat. Rev. Mol. Cell Biol. 4 2003 552 565
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 552-565
    • Orrenius, S.1
  • 20
    • 2542448093 scopus 로고    scopus 로고
    • Participation of endoplasmic reticulum and mitochondrial calcium handling in apoptosis: More than just neighborhood?
    • G. Szabadkai, and R. Rizzuto Participation of endoplasmic reticulum and mitochondrial calcium handling in apoptosis: more than just neighborhood? FEBS Lett. 567 2004 111 115
    • (2004) FEBS Lett. , vol.567 , pp. 111-115
    • Szabadkai, G.1    Rizzuto, R.2
  • 21
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • D. Boehning Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis Nat. Cell Biol. 5 2003 1051 1061
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1051-1061
    • Boehning, D.1
  • 22
    • 0037418843 scopus 로고    scopus 로고
    • BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis
    • L. Scorrano BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis Science 300 2003 135 139
    • (2003) Science , vol.300 , pp. 135-139
    • Scorrano, L.1
  • 23
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • M. Zhang, and R.J. Kaufman Signaling the unfolded protein response from the endoplasmic reticulum J. Biol. Chem. 279 2004 25935 25938
    • (2004) J. Biol. Chem. , vol.279 , pp. 25935-25938
    • Zhang, M.1    Kaufman, R.J.2
  • 24
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases
    • B.T. Chua Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases J. Biol. Chem. 275 2000 5131 5135
    • (2000) J. Biol. Chem. , vol.275 , pp. 5131-5135
    • Chua, B.T.1
  • 25
    • 0027422866 scopus 로고
    • Picornavirus nonstructural proteins: Emerging roles in virus replication and inhibition of host cell functions
    • A.G. Porter Picornavirus nonstructural proteins: emerging roles in virus replication and inhibition of host cell functions J. Virol. 67 1993 6917 6921
    • (1993) J. Virol. , vol.67 , pp. 6917-6921
    • Porter, A.G.1
  • 26
    • 0028188147 scopus 로고
    • Characteristics of the poliovirus replication complex
    • K. Bienz Characteristics of the poliovirus replication complex Arch. Virol. Suppl. 9 1994 147 157
    • (1994) Arch. Virol. Suppl. , vol.9 , pp. 147-157
    • Bienz, K.1
  • 27
    • 0028918959 scopus 로고
    • Inhibition of protein secretion by poliovirus proteins 2B and 3A
    • J.R. Doedens, and K. Kirkegaard Inhibition of protein secretion by poliovirus proteins 2B and 3A EMBO J. 14 1995 894 907
    • (1995) EMBO J. , vol.14 , pp. 894-907
    • Doedens, J.R.1    Kirkegaard, K.2
  • 28
    • 1642539980 scopus 로고    scopus 로고
    • Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen
    • A.J. Merz, and W.T. Wickner Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen J. Cell Biol. 164 2004 195 206
    • (2004) J. Cell Biol. , vol.164 , pp. 195-206
    • Merz, A.J.1    Wickner, W.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.