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Volumn 80, Issue 18, 2006, Pages 9073-9081

Oligomerization of hantavirus nucleocapsid protein: Analysis of the N-terminal coiled-coil domain

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GC; GLYCOPROTEIN GN; NUCLEOCAPSID PROTEIN; RIBONUCLEOPROTEIN; RNA; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

EID: 33748479919     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00515-06     Document Type: Article
Times cited : (25)

References (44)
  • 1
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • Akey, D. L., V. N. Malashkevich, and P. S. Kim. 2001. Buried polar residues in coiled-coil interfaces. Biochemistry 40:6352-6360.
    • (2001) Biochemistry , vol.40 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 7
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard, P., J. Stetefeld, and S. V. Strelkov. 2001. Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 11:82-88.
    • (2001) Trends Cell Biol. , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 8
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan, D. C., C. T. Chutkowski, and P. S. Kim. 1998. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. USA 95:15613-15617.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 9
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: An automated docking and discrimination method for the prediction of protein complexes
    • Comeau, S. R., D. W. Gatchell, S. Vajda, and C. J. Camacho. 2004. ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20:45-50.
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 10
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled coils
    • Crick, F. H. C. 1953. The packing of α-helices: simple coiled coils. Acta Crystallogr. 6:689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 12
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: A simple approach to improve protein structure predictions
    • Ginalski, K., A. Elofsson, D. Fischer, and L. Rychlewski. 2003. 3D-Jury: a simple approach to improve protein structure predictions. Bioinformatics 19:1015-1018.
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 13
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 14
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus, K., C. Barrett, and R. Hughey. 1998. Hidden Markov models for detecting remote protein homologies. Bioinformatics 14:846-856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 16
    • 0141454820 scopus 로고    scopus 로고
    • Mapping of the regions involved in homotypic interactions of Tula hantavirus N protein
    • Kaukinen, P., A. Vaheri, and A. Plyusnin. 2003. Mapping of the regions involved in homotypic interactions of Tula hantavirus N protein. J. Virol. 77:10910-10916.
    • (2003) J. Virol. , vol.77 , pp. 10910-10916
    • Kaukinen, P.1    Vaheri, A.2    Plyusnin, A.3
  • 17
    • 0037370962 scopus 로고    scopus 로고
    • Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitin-related modifier-1, SUMO-1
    • Kaukinen, P., A. Vaheri, and A. Plyusnin. 2003. Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitin-related modifier-1, SUMO-1. Virus Res. 92:37-45.
    • (2003) Virus Res. , vol.92 , pp. 37-45
    • Kaukinen, P.1    Vaheri, A.2    Plyusnin, A.3
  • 18
    • 10044281964 scopus 로고    scopus 로고
    • Oligomerization of hantavirus N protein: C-terminal alpha-helices interact to form a shared hydrophobic space
    • Kaukinen, P., V. Kumar, K. Tulimaki, P. Engelhardt, A. Vaheri, and A. Plyusnin. 2004. Oligomerization of hantavirus N protein: C-terminal alpha-helices interact to form a shared hydrophobic space. J. Virol. 78:13669-13677.
    • (2004) J. Virol. , vol.78 , pp. 13669-13677
    • Kaukinen, P.1    Kumar, V.2    Tulimaki, K.3    Engelhardt, P.4    Vaheri, A.5    Plyusnin, A.6
  • 19
    • 23844454526 scopus 로고    scopus 로고
    • Hantavirus nucleocapsid protein: A multifunctional molecule with both housekeeping and ambassadorial duties
    • Kaukinen, P., A. Vaheri, and A. Plyusnin. 2005. Hantavirus nucleocapsid protein: a multifunctional molecule with both housekeeping and ambassadorial duties. Arch. Virol. 150:1693-1713.
    • (2005) Arch. Virol. , vol.150 , pp. 1693-1713
    • Kaukinen, P.1    Vaheri, A.2    Plyusnin, A.3
  • 20
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3DPSSM
    • Kelley, L. A., C. M. McCallum, and M. J. Sternberg. 2000. Enhanced genome annotation using structural profiles in the program 3DPSSM. J. Mol. Biol. 299:501-522.
    • (2000) J. Mol. Biol. , vol.299 , pp. 501-522
    • Kelley, L.A.1    McCallum, C.M.2    Sternberg, M.J.3
  • 21
    • 2442700154 scopus 로고    scopus 로고
    • Tula hantavirus L protein is a 250 kDa perinuclear membrane-associated protein
    • Kukkonen, S. K. J., A. Vaheri, and A. Plyusnin. 2004. Tula hantavirus L protein is a 250 kDa perinuclear membrane-associated protein. J. Gen. Virol. 85:1181-1189.
    • (2004) J. Gen. Virol. , vol.85 , pp. 1181-1189
    • Kukkonen, S.K.J.1    Vaheri, A.2    Plyusnin, A.3
  • 22
    • 0242552701 scopus 로고    scopus 로고
    • Association of the nucleocapsid protein of the Seoul and Hantaan hantaviruses with small ubiquitin-like modifier-1-related molecules
    • Lee, B. H., K. Yoshimatsu, A. Maeda, K. Ochiai, M. Morimatsu, K. Araki, M. Ogino, S. Morikawa, and J. Arikawa. 2003. Association of the nucleocapsid protein of the Seoul and Hantaan hantaviruses with small ubiquitin-like modifier-1-related molecules. Virus Res. 98:83-91.
    • (2003) Virus Res. , vol.98 , pp. 83-91
    • Lee, B.H.1    Yoshimatsu, K.2    Maeda, A.3    Ochiai, K.4    Morimatsu, M.5    Araki, K.6    Ogino, M.7    Morikawa, S.8    Arikawa, J.9
  • 24
    • 0026481821 scopus 로고
    • Bank vole monoclonal antibodies against Puumala virus envelope glycoproteins: Identification of epitopes involved in neutralization
    • Lundkvist, Å., and B. Niklasson. 1992. Bank vole monoclonal antibodies against Puumala virus envelope glycoproteins: identification of epitopes involved in neutralization. Arch. Virol. 126:93-105.
    • (1992) Arch. Virol. , vol.126 , pp. 93-105
    • Lundkvist, Å.1    Niklasson, B.2
  • 25
    • 0030296262 scopus 로고    scopus 로고
    • Characterization of Tula virus antigenic determinants defined by monoclonal antibodies raised against baculovirus-expressed nucleocapsid protein
    • Lundkvist, Å., O. Vapalahti, A. Plyusnin, K. B. Sjolander, B. Niklasson, and A. Vaheri. 1996. Characterization of Tula virus antigenic determinants defined by monoclonal antibodies raised against baculovirus-expressed nucleocapsid protein. Virus Res. 45:29-44.
    • (1996) Virus Res. , vol.45 , pp. 29-44
    • Lundkvist, Å.1    Vapalahti, O.2    Plyusnin, A.3    Sjolander, K.B.4    Niklasson, B.5    Vaheri, A.6
  • 26
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 27
    • 0037455554 scopus 로고    scopus 로고
    • The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9)
    • Maeda, A., B. H. Lee, K. Yoshimatsu, M. Saijo, I. Kurane, J. Arikawa, and S. Morikawa. 2003. The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9). Virology 305:288-297.
    • (2003) Virology , vol.305 , pp. 288-297
    • Maeda, A.1    Lee, B.H.2    Yoshimatsu, K.3    Saijo, M.4    Kurane, I.5    Arikawa, J.6    Morikawa, S.7
  • 28
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: Stability, specificity, and biological implications
    • Mason, J. M., and K. M. Arndt. 2004. Coiled coil domains: stability, specificity, and biological implications. Chembiochem 6:170-176.
    • (2004) Chembiochem , vol.6 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 29
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., K. Bryson, and D. T. Jones. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 30
    • 3242713982 scopus 로고    scopus 로고
    • Trimeric hantavirus nucleocapsid protein binds specifically to the viral RNA panhandle
    • Mir, M, A., and A. T. Panganiban. 2004. Trimeric hantavirus nucleocapsid protein binds specifically to the viral RNA panhandle. J. Virol. 78:8281-8288.
    • (2004) J. Virol. , vol.78 , pp. 8281-8288
    • Mir, M.A.1    Panganiban, A.T.2
  • 31
    • 31044439245 scopus 로고    scopus 로고
    • The bunyavirus nucleocapsid protein is an RNA chaperone: Possible roles in viral RNA panhandle formation and genome replication
    • Mir, M. A., and A. T. Panganiban. 2006. The bunyavirus nucleocapsid protein is an RNA chaperone: possible roles in viral RNA panhandle formation and genome replication. RNA 12:272-282.
    • (2006) RNA , vol.12 , pp. 272-282
    • Mir, M.A.1    Panganiban, A.T.2
  • 32
    • 0032509105 scopus 로고    scopus 로고
    • Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods
    • Park, J., K. Karplus, C. Barrett, R. Hughey, D. Haussler, T. Hubbard, and C. Chothia. 1998. Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods. J. Mol. Biol. 284:1201-1210.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1201-1210
    • Park, J.1    Karplus, K.2    Barrett, C.3    Hughey, R.4    Haussler, D.5    Hubbard, T.6    Chothia, C.7
  • 33
    • 0037372265 scopus 로고    scopus 로고
    • An Antiviral peptide targets a coiled-coil domain of the human T-cell leukemia virus envelope glycoprotein
    • Pinon, J. D., S. M. Kelly, N. C. Price, J. U. Flanagan, and D. W. Brighty. 2003. An Antiviral peptide targets a coiled-coil domain of the human T-cell leukemia virus envelope glycoprotein. J. Virol. 77:3281-3290.
    • (2003) J. Virol. , vol.77 , pp. 3281-3290
    • Pinon, J.D.1    Kelly, S.M.2    Price, N.C.3    Flanagan, J.U.4    Brighty, D.W.5
  • 34
    • 0031948195 scopus 로고    scopus 로고
    • Role of actin microfilaments in Black Creek Canal virus morphogenesis
    • Ravkov, E. V., S. T. Nichol, C. J. Peters, and R. W. Compans. 1998. Role of actin microfilaments in Black Creek Canal virus morphogenesis. J. Virol. 72:2865-2870.
    • (1998) J. Virol. , vol.72 , pp. 2865-2870
    • Ravkov, E.V.1    Nichol, S.T.2    Peters, C.J.3    Compans, R.W.4
  • 35
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B, 1996. PHD: predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266:525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 37
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons, K. T., C. Kooperberg, E. Huang, and D. Baker. 1997. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268:209-225.
    • (1997) J. Mol. Biol. , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 38
    • 0032929780 scopus 로고    scopus 로고
    • Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins
    • Simons, K. T., I. Ruczinski, C. Kooperberg, B. A. Fox, C. Bystroff, and D. Baker. 1999. Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins. Proteins 34:82-95.
    • (1999) Proteins , vol.34 , pp. 82-95
    • Simons, K.T.1    Ruczinski, I.2    Kooperberg, C.3    Fox, B.A.4    Bystroff, C.5    Baker, D.6
  • 41
    • 0036122461 scopus 로고    scopus 로고
    • The RNA binding domain of the Hantaan virus N protein maps to a central, conserved region
    • Xu, X., W. Severson, N. Villegas, C. S. Schmaljohn, and C. B. Jonsson. 2002. The RNA binding domain of the Hantaan virus N protein maps to a central, conserved region. J. Virol. 76:3301-3308.
    • (2002) J. Virol. , vol.76 , pp. 3301-3308
    • Xu, X.1    Severson, W.2    Villegas, N.3    Schmaljohn, C.S.4    Jonsson, C.B.5
  • 42
    • 0037225705 scopus 로고    scopus 로고
    • The multimerization of hantavirus nucleocapsid protein depends on type-specific epitopes
    • Yoshimatsu, K., B. H. Lee, K. Araki, M. Morimatsu, M. Ogino, H. Ebihara, and J. Arikawa. 2003. The multimerization of hantavirus nucleocapsid protein depends on type-specific epitopes. J. Virol. 77:943-952.
    • (2003) J. Virol. , vol.77 , pp. 943-952
    • Yoshimatsu, K.1    Lee, B.H.2    Araki, K.3    Morimatsu, M.4    Ogino, M.5    Ebihara, H.6    Arikawa, J.7
  • 43
    • 0030841383 scopus 로고    scopus 로고
    • Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms
    • Wiltscheck, R., R. A. Kammerer, S. A. Dames, T. Schulthess, M. J. Blommers, J. Engel, and A. T. Alexandrescu. 1997. Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms. Protein Sci. 6:1734-1745.
    • (1997) Protein Sci. , vol.6 , pp. 1734-1745
    • Wiltscheck, R.1    Kammerer, R.A.2    Dames, S.A.3    Schulthess, T.4    Blommers, M.J.5    Engel, J.6    Alexandrescu, A.T.7
  • 44
    • 0030987407 scopus 로고    scopus 로고
    • MultiCoil: A program for predicting two- and three-stranded coiled coils
    • Wolf, E., P. Kim, and B. Berger. 1997. MultiCoil: a program for predicting two- and three-stranded coiled coils. Protein Sci. 6:1179-1189.
    • (1997) Protein Sci. , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.2    Berger, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.