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Volumn 76, Issue 20, 2002, Pages 10383-10392

A structural model of pestivirus Erns based on disulfide bond connectivity and homology modeling reveals an extremely rare vicinal disulfide

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CARBOXY TERMINAL SEQUENCE; DIMERIZATION; DISULFIDE BOND; ENZYME ACTIVITY; GENE INSERTION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; OPEN READING FRAME; PESTIVIRUS; PRIORITY JOURNAL; PROTEIN DEGRADATION; VIRUS ENVELOPE; VIRUS GENOME;

EID: 0036785507     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.20.10383-10392.2002     Document Type: Article
Times cited : (33)

References (32)
  • 2
    • 0028382370 scopus 로고
    • The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues
    • Blake, C. C., M. Ghosh, K. Harlos, A. Avezoux, and C. Anthony. 1994. The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues. Nat. Struct. Biol. 1:102-105.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 102-105
    • Blake, C.C.1    Ghosh, M.2    Harlos, K.3    Avezoux, A.4    Anthony, C.5
  • 3
    • 0030830396 scopus 로고    scopus 로고
    • A subunit vaccine based on glycoprotein E2 of bovine virus diarrhea virus induces fetal protection in sheep against homologous challenge
    • Bruschke, C. J., R. J. Moormann, J. T. van Oirschot, and P. A. van Rijn. 1997. A subunit vaccine based on glycoprotein E2 of bovine virus diarrhea virus induces fetal protection in sheep against homologous challenge. Vaccine 15:1940-1945.
    • (1997) Vaccine , vol.15 , pp. 1940-1945
    • Bruschke, C.J.1    Moormann, R.J.2    Van Oirschot, J.T.3    Van Rijn, P.A.4
  • 5
    • 0024041479 scopus 로고
    • Molecular cloning and nucleotide sequence of the pestivirus bovine viral diarrhea virus
    • Colett, M. S., R. Larson, C. Gold, D. Strick, D. K. Anderson, and A. F. Purchio. 1988. Molecular cloning and nucleotide sequence of the pestivirus bovine viral diarrhea virus. Virology 165:191-199.
    • (1988) Virology , vol.165 , pp. 191-199
    • Colett, M.S.1    Larson, R.2    Gold, C.3    Strick, D.4    Anderson, D.K.5    Purchio, A.F.6
  • 6
    • 0033572736 scopus 로고    scopus 로고
    • Evolution of oligomeric proteins. The unusual case of a dimeric ribonuclease
    • D'Alessio, G. 1999. Evolution of oligomeric proteins. The unusual case of a dimeric ribonuclease. Eur. J. Biochem. 266:699-708.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 699-708
    • D'Alessio, G.1
  • 8
    • 0028294275 scopus 로고
    • Glycoprotein E2 of classical swine fever virus: Expression in insect cells and identification as a ribonuclease
    • Hulst, M. M., G. Himes, E. Newbigin, and R. J. Moormann. 1994. Glycoprotein E2 of classical swine fever virus: expression in insect cells and identification as a ribonuclease. Virology 200:558-565.
    • (1994) Virology , vol.200 , pp. 558-565
    • Hulst, M.M.1    Himes, G.2    Newbigin, E.3    Moormann, R.J.4
  • 9
    • 0030704752 scopus 로고    scopus 로고
    • Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors
    • Hulst, M. M., and R. J. Moormann. 1997. Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors. J. Gen. Virol. 78:2779-2787.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2779-2787
    • Hulst, M.M.1    Moormann, R.J.2
  • 11
    • 0033955991 scopus 로고    scopus 로고
    • Interactions of bovine viral diarrhoea virus glycoprotein E(rns) with cell surface glycosaminoglycans
    • Iqbal, M., H. Flick-Smith, and J. W. McCauley. 2000. Interactions of bovine viral diarrhoea virus glycoprotein E(rns) with cell surface glycosaminoglycans. J. Gen. Virol. 81:451-459.
    • (2000) J. Gen. Virol. , vol.81 , pp. 451-459
    • Iqbal, M.1    Flick-Smith, H.2    McCauley, J.W.3
  • 12
    • 0022975251 scopus 로고
    • Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues
    • Kao, P. N., and A. Karlin. 1986. Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues. J. Biol. Chem. 261:8085-8088.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8085-8088
    • Kao, P.N.1    Karlin, A.2
  • 13
    • 0029134624 scopus 로고
    • Classical swine fever virus: Independent induction of protective immunity by two structural glycoproteins
    • Konig, M., T. Lengsfeld, T. Pauly, R. Stark, and H. J. Thiel. 1995. Classical swine fever virus: independent induction of protective immunity by two structural glycoproteins. J. Virol. 69:6479-6486.
    • (1995) J. Virol. , vol.69 , pp. 6479-6486
    • Konig, M.1    Lengsfeld, T.2    Pauly, T.3    Stark, R.4    Thiel, H.J.5
  • 14
    • 0029927855 scopus 로고    scopus 로고
    • The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0 A resolution
    • Kurihara, H., T. Nonaka, Y. Mitsui, K. Ohgi, M. Irie, and K. T. Nakamura. 1996. The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0 A resolution. J. Mol. Biol. 255:310-320.
    • (1996) J. Mol. Biol. , vol.255 , pp. 310-320
    • Kurihara, H.1    Nonaka, T.2    Mitsui, Y.3    Ohgi, K.4    Irie, M.5    Nakamura, K.T.6
  • 15
    • 0037085304 scopus 로고    scopus 로고
    • Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop
    • Langedijk, J. P. 2002. Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop. J. Biol. Chem. 277:5308-5314.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5308-5314
    • Langedijk, J.P.1
  • 17
    • 0035977011 scopus 로고    scopus 로고
    • Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility
    • Matsuura, T., H. Sakai, M. Unno, K. Ida, M. Sato, F. Sakiyama, and S. Norioka. 2001. Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility. J. Biol. Chem. 276:45261-45269.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45261-45269
    • Matsuura, T.1    Sakai, H.2    Unno, M.3    Ida, K.4    Sato, M.5    Sakiyama, F.6    Norioka, S.7
  • 18
    • 0345148344 scopus 로고    scopus 로고
    • rns of the pestivirus classical swine fever virus lead to virus attenuation
    • rns of the pestivirus classical swine fever virus lead to virus attenuation. J. Virol. 73:10224-10235.
    • (1999) J. Virol. , vol.73 , pp. 10224-10235
    • Meyers, G.1    Saalmüller, A.2    Büttner, M.3
  • 19
    • 0030030337 scopus 로고    scopus 로고
    • Infectious RNA transcribed from an engineered full-length cDNA template of the genome of a pestivirus
    • Moormann, R. J., H. G. van Gennip, G. K. Miedema, M. M. Hulst, and P. A. van Rijn. 1996. Infectious RNA transcribed from an engineered full-length cDNA template of the genome of a pestivirus. J. Virol. 70:763-770.
    • (1996) J. Virol. , vol.70 , pp. 763-770
    • Moormann, R.J.1    Van Gennip, H.G.2    Miedema, G.K.3    Hulst, M.M.4    Van Rijn, P.A.5
  • 20
    • 0034643337 scopus 로고    scopus 로고
    • Development of a classical swine fever subunit marker vaccine and companion diagnostic test
    • Moormann, R. J. M., A. Bouma, J. H. Kramps, C. Terpstra, and A. J. De Smit. 2000. Development of a classical swine fever subunit marker vaccine and companion diagnostic test. Vet. Microbiol. 73:209-219.
    • (2000) Vet. Microbiol. , vol.73 , pp. 209-219
    • Moormann, R.J.M.1    Bouma, A.2    Kramps, J.H.3    Terpstra, C.4    De Smit, A.J.5
  • 21
    • 0032775385 scopus 로고    scopus 로고
    • Crystal structure of a ribonuclease from the seeds of bitter gourd (Momordica charantia) at 1.75 A resolution
    • Nakagawa, A., I. Tanaka, R. Sakai, T. Nakashima, G. Funatsu, and M. Kimura. 1999. Crystal structure of a ribonuclease from the seeds of bitter gourd (Momordica charantia) at 1.75 A resolution. Biochim. Biophys. Acta 1433:253-260.
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 253-260
    • Nakagawa, A.1    Tanaka, I.2    Sakai, R.3    Nakashima, T.4    Funatsu, G.5    Kimura, M.6
  • 22
    • 0027238125 scopus 로고
    • Processing of the envelope glycoproteins of pestiviruses
    • Rumenapf, T., G. Unger, J. H. Strauss, and H. J. Thiel. 1993. Processing of the envelope glycoproteins of pestiviruses. J. Virol. 67:3288-3294.
    • (1993) J. Virol. , vol.67 , pp. 3288-3294
    • Rumenapf, T.1    Unger, G.2    Strauss, J.H.3    Thiel, H.J.4
  • 23
    • 0027433731 scopus 로고
    • Identification of a structural glycoprotein of an RNA virus as a ribonuclease
    • Schneider, R., G. Unger, R. Stark, E. Schneider-Scherzer, and H. J. Thiel. 1993. Identification of a structural glycoprotein of an RNA virus as a ribonuclease. Science 261:1169-1171.
    • (1993) Science , vol.261 , pp. 1169-1171
    • Schneider, R.1    Unger, G.2    Stark, R.3    Schneider-Scherzer, E.4    Thiel, H.J.5
  • 24
    • 0013784519 scopus 로고
    • Reactions of cyanate with functional groups of proteins. 3. Reactions with amino and carboxyl groups
    • Stark, G. R. 1965. Reactions of cyanate with functional groups of proteins. 3. Reactions with amino and carboxyl groups. Biochemistry 4:1030-1036.
    • (1965) Biochemistry , vol.4 , pp. 1030-1036
    • Stark, G.R.1
  • 26
    • 0025955758 scopus 로고
    • Hog cholera virus: Molecular composition of virions from a pestivirus
    • Erratum, 66:612, 1992
    • Thiel, H. J., R. Stark, E. Weiland, T. Rumenapf, and G. Meyers. 1991. Hog cholera virus: molecular composition of virions from a pestivirus. J. Virol. 65:4705-4712. (Erratum, 66:612, 1992.)
    • (1991) J. Virol. , vol.65 , pp. 4705-4712
    • Thiel, H.J.1    Stark, R.2    Weiland, E.3    Rumenapf, T.4    Meyers, G.5
  • 27
    • 0031172075 scopus 로고    scopus 로고
    • Mammalian Rh/T2/S-glycoprotein ribonuclease family genes: Cloning of a human member located in a region of chromosome 6 (6q27) frequently deleted in human malignancies
    • Trubia, M., L. Sessa, and R. Taramelli. 1997. Mammalian Rh/T2/S-glycoprotein ribonuclease family genes: cloning of a human member located in a region of chromosome 6 (6q27) frequently deleted in human malignancies. Genomics 42:342-344.
    • (1997) Genomics , vol.42 , pp. 342-344
    • Trubia, M.1    Sessa, L.2    Taramelli, R.3
  • 31
    • 0030586029 scopus 로고    scopus 로고
    • Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin
    • Yang, X., and K. Moffat. 1996. Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin. Structure 4:837-852.
    • (1996) Structure , vol.4 , pp. 837-852
    • Yang, X.1    Moffat, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.