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Volumn 52, Issue 2, 2007, Pages 249-257

Expression, purification and characterization of recombinant severe acute respiratory syndrome coronavirus non-structural protein 1

Author keywords

Coronavirus; Non structural protein 1; Nspl; SARS; Severe acute respiratory syndrome; Size exclusion chromatography multi angle light scattering

Indexed keywords

PEPTIDE HYDROLASE; RECOMBINANT PROTEIN; VIRUS PROTEIN;

EID: 33846416887     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.11.005     Document Type: Article
Times cited : (2)

References (29)
  • 5
    • 33646942954 scopus 로고    scopus 로고
    • The widening scope of coronaviruses
    • Kahn J.S. The widening scope of coronaviruses. Curr. Opin. Pediatr. 18 (2006) 42-47
    • (2006) Curr. Opin. Pediatr. , vol.18 , pp. 42-47
    • Kahn, J.S.1
  • 6
    • 0002257116 scopus 로고    scopus 로고
    • Coronaviruses
    • Knipe D.M., Roizman B., Howley P.M., Straus S.E., Fields B.N., Griffin D.E., Martin M.A., and Lamb R.A. (Eds), Lippincott Williams & Wilkins, Philadelphia
    • Holmes K.V. Coronaviruses. In: Knipe D.M., Roizman B., Howley P.M., Straus S.E., Fields B.N., Griffin D.E., Martin M.A., and Lamb R.A. (Eds). Fields Virology (2001), Lippincott Williams & Wilkins, Philadelphia 1187-1203
    • (2001) Fields Virology , pp. 1187-1203
    • Holmes, K.V.1
  • 7
    • 13444282434 scopus 로고    scopus 로고
    • Evidence of a novel human coronavirus that is associated with respiratory tract disease in infants and young children
    • Esper F., Weibel C., Ferguson D., Landry M.L., and Kahn J.S. Evidence of a novel human coronavirus that is associated with respiratory tract disease in infants and young children. J. Infect. Dis. 191 (2005) 492-498
    • (2005) J. Infect. Dis. , vol.191 , pp. 492-498
    • Esper, F.1    Weibel, C.2    Ferguson, D.3    Landry, M.L.4    Kahn, J.S.5
  • 13
    • 13744252665 scopus 로고    scopus 로고
    • Complete genomic sequence of human coronavirus OC43: molecular clock analysis suggests a relatively recent zoonotic coronavirus transmission event
    • Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P., Vandamme A.M., and Van Ranst M. Complete genomic sequence of human coronavirus OC43: molecular clock analysis suggests a relatively recent zoonotic coronavirus transmission event. J. Virol. 79 (2005) 1595-1604
    • (2005) J. Virol. , vol.79 , pp. 1595-1604
    • Vijgen, L.1    Keyaerts, E.2    Moes, E.3    Thoelen, I.4    Wollants, E.5    Lemey, P.6    Vandamme, A.M.7    Van Ranst, M.8
  • 15
    • 10044268025 scopus 로고    scopus 로고
    • Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity
    • Harcourt B.H., Jukneliene D., Kanjanahaluethai A., Bechill J., Severson K.M., Smith C.M., Rota P.A., and Baker S.C. Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity. J. Virol. 78 (2004) 13600-13612
    • (2004) J. Virol. , vol.78 , pp. 13600-13612
    • Harcourt, B.H.1    Jukneliene, D.2    Kanjanahaluethai, A.3    Bechill, J.4    Severson, K.M.5    Smith, C.M.6    Rota, P.A.7    Baker, S.C.8
  • 16
    • 4444246734 scopus 로고    scopus 로고
    • Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins
    • Prentice E., McAuliffe J., Lu X., Subbarao K., and Denison M.R. Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins. J. Virol. 78 (2004) 9977-9986
    • (2004) J. Virol. , vol.78 , pp. 9977-9986
    • Prentice, E.1    McAuliffe, J.2    Lu, X.3    Subbarao, K.4    Denison, M.R.5
  • 17
    • 13544275676 scopus 로고    scopus 로고
    • Characterization of viral proteins encoded by the SARS-coronavirus genome
    • Tan Y.J., Lim S.G., and Hong W. Characterization of viral proteins encoded by the SARS-coronavirus genome. Antiviral Res. 65 (2005) 69-78
    • (2005) Antiviral Res. , vol.65 , pp. 69-78
    • Tan, Y.J.1    Lim, S.G.2    Hong, W.3
  • 18
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • Gosert R., Kanjanahaluethai A., Egger D., Bienz K., and Baker S.C. RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J. Virol. 76 (2002) 3697-3708
    • (2002) J. Virol. , vol.76 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 19
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice E., Jerome W.G., Yoshimori T., Mizushima N., and Denison M.R. Coronavirus replication complex formation utilizes components of cellular autophagy. J. Biol. Chem. 279 (2004) 10136-10141
    • (2004) J. Biol. Chem. , vol.279 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 20
    • 24944485104 scopus 로고    scopus 로고
    • Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replication
    • Brockway S.M., and Denison M.R. Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replication. Virology 340 (2005) 209-223
    • (2005) Virology , vol.340 , pp. 209-223
    • Brockway, S.M.1    Denison, M.R.2
  • 21
    • 2442650226 scopus 로고    scopus 로고
    • Cleavage between replicase proteins p28 and p65 of mouse hepatitis virus is not required for virus replication
    • Denison M.R., Yount B., Brockway S.M., Graham R.L., Sims A.C., Lu X., and Baric R.S. Cleavage between replicase proteins p28 and p65 of mouse hepatitis virus is not required for virus replication. J. Virol. 78 (2004) 5957-5965
    • (2004) J. Virol. , vol.78 , pp. 5957-5965
    • Denison, M.R.1    Yount, B.2    Brockway, S.M.3    Graham, R.L.4    Sims, A.C.5    Lu, X.6    Baric, R.S.7
  • 22
    • 33748046163 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression by promoting host mRNA degradation
    • Kamitani W., Narayanan K., Huang C., Lokugamage K., Ikegami T., Ito N., Kubo H., and Makino S. Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression by promoting host mRNA degradation. Proc. Natl. Acad. Sci. USA 103 (2006) 12885-12890
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12885-12890
    • Kamitani, W.1    Narayanan, K.2    Huang, C.3    Lokugamage, K.4    Ikegami, T.5    Ito, N.6    Kubo, H.7    Makino, S.8
  • 23
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade M.A., Chacon P., Merelo J.J., and Moran F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 24
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: a protein structure and structural feature prediction server
    • Cheng J., Randall A.Z., Sweredoski M.J., and Baldi P. SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res. 33 (2005) W72-W76
    • (2005) Nucleic Acids Res. , vol.33
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 26
    • 13444266488 scopus 로고    scopus 로고
    • A simple and fast secondary structure prediction method using hidden neural networks
    • Lin K., Simossis V.A., Taylor W.R., and Heringa J. A simple and fast secondary structure prediction method using hidden neural networks. Bioinformatics 21 (2005) 152-159
    • (2005) Bioinformatics , vol.21 , pp. 152-159
    • Lin, K.1    Simossis, V.A.2    Taylor, W.R.3    Heringa, J.4
  • 27
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • Adamczak R., Porollo A., and Meller J. Combining prediction of secondary structure and solvent accessibility in proteins. Proteins 59 (2005) 467-475
    • (2005) Proteins , vol.59 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 28
    • 0030931336 scopus 로고    scopus 로고
    • Seventy-five percent accuracy in protein secondary structure prediction
    • Frishman D., and Argos P. Seventy-five percent accuracy in protein secondary structure prediction. Proteins 27 (1997) 329-335
    • (1997) Proteins , vol.27 , pp. 329-335
    • Frishman, D.1    Argos, P.2
  • 29
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew E., and Williams K.R. Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biomol. Tech. 10 (1999) 51-63
    • (1999) J. Biomol. Tech. , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.