메뉴 건너뛰기




Volumn 4983 LNBI, Issue , 2008, Pages 146-158

Physicochemical correlation between amino acid sites in short sequences under selective pressure

Author keywords

Amino acid; Covariation; Physicochemical properties; Selection

Indexed keywords

ACID SITES; AMINO ACID; AMINO-ACID SEQUENCES; COVARIATION; IN-VITRO; INTERNATIONAL SYMPOSIUM; MHC CLASS; NATURAL SELECTION; PHYSICOCHEMICAL PROPERTIES; SELECTION; SELECTIVE PRESSURES; SHORT SEQUENCES;

EID: 50049106445     PISSN: 03029743     EISSN: 16113349     Source Type: Book Series    
DOI: 10.1007/978-3-540-79450-9_14     Document Type: Conference Paper
Times cited : (4)

References (61)
  • 1
    • 0030743758 scopus 로고    scopus 로고
    • Effectiveness of correlation analysis in identifying protein residues
    • Pollock, D., Taylor, W.: Effectiveness of correlation analysis in identifying protein residues. Protein Eng. 10(6), 647-657 (1997)
    • (1997) Protein Eng , vol.10 , Issue.6 , pp. 647-657
    • Pollock, D.1    Taylor, W.2
  • 2
    • 0020483945 scopus 로고
    • Evolution of proteins formed by beta-sheets. I. Plastocyanin and azurin
    • Chothia, C., Lesk, A.: Evolution of proteins formed by beta-sheets. I. Plastocyanin and azurin. J. Mol. Biol. 160(2), 309-323 (1982)
    • (1982) J. Mol. Biol , vol.160 , Issue.2 , pp. 309-323
    • Chothia, C.1    Lesk, A.2
  • 3
    • 0020429363 scopus 로고    scopus 로고
    • Lesk, A., C., C.: Evolution of proteins formed by beta-sheets. II. The core of the immunoglobulin domains. J. Mol. Biol. 160(2), 325-342 (1982)
    • Lesk, A., C., C.: Evolution of proteins formed by beta-sheets. II. The core of the immunoglobulin domains. J. Mol. Biol. 160(2), 325-342 (1982)
  • 4
    • 0022465940 scopus 로고
    • Analysis of mutations in the transmembrane region of the aspartate chemoreceptor in Escherichia coli
    • Oosawa, K., Simon, M.: Analysis of mutations in the transmembrane region of the aspartate chemoreceptor in Escherichia coli. Proc. Natl. Acad. Sci. USA 83(18), 6930-6934 (1986)
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , Issue.18 , pp. 6930-6934
    • Oosawa, K.1    Simon, M.2
  • 5
    • 0024084164 scopus 로고
    • Coordinated amino acid changes in homologous protein families
    • Altschuh, D., et al.: Coordinated amino acid changes in homologous protein families. Protein Eng. 2(3), 193-199 (1988)
    • (1988) Protein Eng , vol.2 , Issue.3 , pp. 193-199
    • Altschuh, D.1
  • 6
    • 0025327474 scopus 로고
    • Evolution of protein cores. Constraints in point mutations as observed in globin tertiary structure
    • Bordo, D., Argos, P.: Evolution of protein cores. Constraints in point mutations as observed in globin tertiary structure. J. Mol. Biol. 211(4), 975-988 (1990)
    • (1990) J. Mol. Biol , vol.211 , Issue.4 , pp. 975-988
    • Bordo, D.1    Argos, P.2
  • 7
    • 0033616825 scopus 로고    scopus 로고
    • Mutually compensatory mutations during evolution of the tetramerization domain of tumor supressor p53 lead to impaired hetero-oligomerization
    • Mateu, M., Fersht, A.: Mutually compensatory mutations during evolution of the tetramerization domain of tumor supressor p53 lead to impaired hetero-oligomerization. Proc. Natl. Acad. Sci. USA 96, 3595-3599 (1999)
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3595-3599
    • Mateu, M.1    Fersht, A.2
  • 8
    • 0024507791 scopus 로고
    • Alternative packing arrangements in the hydrophobic core of lambda repressor
    • Lim, W., Sauer, R.: Alternative packing arrangements in the hydrophobic core of lambda repressor. Nature 339(6219), 31-36 (1989)
    • (1989) Nature , vol.339 , Issue.6219 , pp. 31-36
    • Lim, W.1    Sauer, R.2
  • 9
    • 0026766573 scopus 로고
    • Structural and energetic consequences of disruptive mutations in a protein core
    • Lim, W., Farruggio, D., Sauer, R.: Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry 31(17), 4324-4333 (1992)
    • (1992) Biochemistry , vol.31 , Issue.17 , pp. 4324-4333
    • Lim, W.1    Farruggio, D.2    Sauer, R.3
  • 10
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Baldwin, E., et al.: The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science 262(5140), 1715-1718 (1993)
    • (1993) Science , vol.262 , Issue.5140 , pp. 1715-1718
    • Baldwin, E.1
  • 11
    • 0037449144 scopus 로고    scopus 로고
    • Systematic variation of Amino acid substitutions for stringent assesment of pairwise covariation
    • Govindarajan, S., et al.: Systematic variation of Amino acid substitutions for stringent assesment of pairwise covariation. J. Mol. Biol. 328, 1061-1069 (2003)
    • (2003) J. Mol. Biol , vol.328 , pp. 1061-1069
    • Govindarajan, S.1
  • 12
    • 0028832687 scopus 로고
    • Covariation of residues in the homeodomain sequence family
    • Clarke, N.: Covariation of residues in the homeodomain sequence family. Protein Sci. 4(11), 2269-2278 (1995)
    • (1995) Protein Sci , vol.4 , Issue.11 , pp. 2269-2278
    • Clarke, N.1
  • 13
    • 0035957360 scopus 로고    scopus 로고
    • Computational method to reduce the search space for directed protein evolution
    • Voigt, C., et al.: Computational method to reduce the search space for directed protein evolution. In: Proc. Natl. Acad. Sci. USA, vol. 98, pp. 3778-3783 (2001)
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3778-3783
    • Voigt, C.1
  • 14
    • 0033977832 scopus 로고    scopus 로고
    • Correlations among amino acid sites in bHLH protein domains: An information theoretic analysis
    • Atchley, W., et al.: Correlations among amino acid sites in bHLH protein domains: an information theoretic analysis. Mol. Biol. Evol. 17(1), 164-178 (2000)
    • (2000) Mol. Biol. Evol , vol.17 , Issue.1 , pp. 164-178
    • Atchley, W.1
  • 15
    • 0036301488 scopus 로고    scopus 로고
    • Detecting compensatory covariation signals in protein evolution using reconstructed ancestral sequences
    • Fukami-Kobayashi, K., Schreiber, D., Benner, S.: Detecting compensatory covariation signals in protein evolution using reconstructed ancestral sequences. J. Mol. Biol. 319, 729-743 (2002)
    • (2002) J. Mol. Biol , vol.319 , pp. 729-743
    • Fukami-Kobayashi, K.1    Schreiber, D.2    Benner, S.3
  • 16
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Göbel, U., et al.: Correlated mutations and residue contacts in proteins. Proteins 18(4), 309-317 (1994)
    • (1994) Proteins , vol.18 , Issue.4 , pp. 309-317
    • Göbel, U.1
  • 17
    • 0028125904 scopus 로고
    • How frequent are correlated changes in families of protein sequences?
    • Neher, E.: How frequent are correlated changes in families of protein sequences? Proc Natl Acad Sci USA 91(1), 98-102 (1994)
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.1 , pp. 98-102
    • Neher, E.1
  • 18
    • 0028084754 scopus 로고
    • Can three dimensional contacts in protein structures be predicted by analysis of correlated mutations?
    • Shindyalov, I., Kolchanov, N., Sander, C.: Can three dimensional contacts in protein structures be predicted by analysis of correlated mutations? Protein Eng. 7, 349-358 (1994)
    • (1994) Protein Eng , vol.7 , pp. 349-358
    • Shindyalov, I.1    Kolchanov, N.2    Sander, C.3
  • 19
    • 0027952860 scopus 로고
    • Compensating changes in protein multiple sequence alignments
    • Taylor, W., Hatrick, K.: Compensating changes in protein multiple sequence alignments. Protein Eng. 7(3), 341-348 (1994)
    • (1994) Protein Eng , vol.7 , Issue.3 , pp. 341-348
    • Taylor, W.1    Hatrick, K.2
  • 20
    • 1842624559 scopus 로고    scopus 로고
    • Bona fide predictions of protein secondary structure using transparent analyses of multiple sequence alignments
    • Benner, S., et al.: Bona fide predictions of protein secondary structure using transparent analyses of multiple sequence alignments. Chem. Rev. 97, 2725-2844 (1997)
    • (1997) Chem. Rev , vol.97 , pp. 2725-2844
    • Benner, S.1
  • 21
    • 0032619785 scopus 로고    scopus 로고
    • Evolutionary constraint networks in ligand-binding domains: An information-theoretic approach
    • Nagl, S., Freeman, J., Smith, T.: Evolutionary constraint networks in ligand-binding domains: an information-theoretic approach. Pac. Symp. Biocomput, 90-101 (1999)
    • (1999) Pac. Symp. Biocomput , vol.90-101
    • Nagl, S.1    Freeman, J.2    Smith, T.3
  • 22
    • 0034721944 scopus 로고    scopus 로고
    • Analysis of covariation in an SH3 domain sequence alignment: Applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions
    • Larson, S., Di Nardo, A., Davidson, A.: Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions. J. Mol. Biol. 303(3), 433-446 (2000)
    • (2000) J. Mol. Biol , vol.303 , Issue.3 , pp. 433-446
    • Larson, S.1    Di Nardo, A.2    Davidson, A.3
  • 23
    • 0035182669 scopus 로고    scopus 로고
    • Detection of conserved physico-chemical characteristics of proteins by analyzing clusters of positions with co-ordinated substitutions
    • Afonnikov, D., Oshchepkov, D., Kolchanov, N.: Detection of conserved physico-chemical characteristics of proteins by analyzing clusters of positions with co-ordinated substitutions. Bioinformatics 17(11), 1035-1046 (2001)
    • (2001) Bioinformatics , vol.17 , Issue.11 , pp. 1035-1046
    • Afonnikov, D.1    Oshchepkov, D.2    Kolchanov, N.3
  • 24
    • 16644373510 scopus 로고    scopus 로고
    • Detection of pairwise residue proximity by covariation analysis for 3-Dstructure prediction of G-protein-coupled receptors
    • Nemoto, W., et al.: Detection of pairwise residue proximity by covariation analysis for 3-Dstructure prediction of G-protein-coupled receptors. Protein. J. 23(6), 427-435 (2004)
    • (2004) Protein. J , vol.23 , Issue.6 , pp. 427-435
    • Nemoto, W.1
  • 25
    • 31044435608 scopus 로고    scopus 로고
    • Covariation analysis of local amino acid sequences in recurrent protein local structures
    • Wang, L.: Covariation analysis of local amino acid sequences in recurrent protein local structures. J. Bioinform. Comput. Biol. 3(6), 1391-1409 (2005)
    • (2005) J. Bioinform. Comput. Biol , vol.3 , Issue.6 , pp. 1391-1409
    • Wang, L.1
  • 26
    • 36749031067 scopus 로고    scopus 로고
    • Contact prediction using mutual information and neural nets
    • Shackelford, G., Karplus, K.: Contact prediction using mutual information and neural nets. Proteins 69(suppl. 8), 159-164 (2007)
    • (2007) Proteins , vol.69 , Issue.SUPPL. 8 , pp. 159-164
    • Shackelford, G.1    Karplus, K.2
  • 27
    • 0023660022 scopus 로고
    • Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus
    • Altschuh, D., et al.: Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus. J. Mol. Biol. 193(4), 693-707 (1987)
    • (1987) J. Mol. Biol , vol.193 , Issue.4 , pp. 693-707
    • Altschuh, D.1
  • 28
    • 0027297096 scopus 로고
    • Covariation of mutations in the V3 loop of human immunodeficiency virus type 1 envelope protein: An information theoretic analysis
    • Korber, B., et al.: Covariation of mutations in the V3 loop of human immunodeficiency virus type 1 envelope protein: an information theoretic analysis. Proc. Natl. Acad. Sci. USA 90(15), 7176-7180 (1993)
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , Issue.15 , pp. 7176-7180
    • Korber, B.1
  • 29
    • 30344486956 scopus 로고    scopus 로고
    • Covariability of selected amino acid positions for HIV type 1 subtypes C and B
    • Gilbert, P., Novitsky, V., Essex, M.: Covariability of selected amino acid positions for HIV type 1 subtypes C and B. AIDS Res. Hum. Retroviruses 21(12), 1016-1030 (2005)
    • (2005) AIDS Res. Hum. Retroviruses , vol.21 , Issue.12 , pp. 1016-1030
    • Gilbert, P.1    Novitsky, V.2    Essex, M.3
  • 30
    • 33646043172 scopus 로고    scopus 로고
    • Co-evolution of nelfinavir-resistant HIV-1 protease and the p1-p6 substrate
    • Kolli, M., Lastere, S., Schiffer, C.: Co-evolution of nelfinavir-resistant HIV-1 protease and the p1-p6 substrate. Virology 347(2), 405-409 (2006)
    • (2006) Virology , vol.347 , Issue.2 , pp. 405-409
    • Kolli, M.1    Lastere, S.2    Schiffer, C.3
  • 31
    • 0030970646 scopus 로고    scopus 로고
    • An analysis of simultaneous variation in protein structures
    • Chelvanayagam, G., et al.: An analysis of simultaneous variation in protein structures. Protein Eng. 10(4), 307-316 (1997)
    • (1997) Protein Eng , vol.10 , Issue.4 , pp. 307-316
    • Chelvanayagam, G.1
  • 32
    • 27944458910 scopus 로고    scopus 로고
    • Using information theory to search for co-evolving residues in proteins
    • Martin, L., et al.: Using information theory to search for co-evolving residues in proteins. Bioinformatics 21(22), 4116-4124 (2005)
    • (2005) Bioinformatics , vol.21 , Issue.22 , pp. 4116-4124
    • Martin, L.1
  • 33
    • 18544362952 scopus 로고    scopus 로고
    • Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions
    • Gloor, G., et al.: Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions. Biochemistry 44(19), 156-165 (2005)
    • (2005) Biochemistry , vol.44 , Issue.19 , pp. 156-165
    • Gloor, G.1
  • 34
    • 21044438202 scopus 로고    scopus 로고
    • The rate of compensatory mutation in the DNA bacteriophage phiX174
    • Poon, A., Chao, L.: The rate of compensatory mutation in the DNA bacteriophage phiX174. Genetics 170(3), 989-999 (2005)
    • (2005) Genetics , vol.170 , Issue.3 , pp. 989-999
    • Poon, A.1    Chao, L.2
  • 35
    • 36949019322 scopus 로고    scopus 로고
    • Detecting coevolution in and among protein domains
    • Yeang, C., Haussler, D.: Detecting coevolution in and among protein domains. PLoS Comput Biol. 3(11), e211 (2007)
    • (2007) PLoS Comput Biol , vol.3 , Issue.11
    • Yeang, C.1    Haussler, D.2
  • 36
  • 37
    • 0035009714 scopus 로고    scopus 로고
    • Relating amino acid sequence to phenotype: Analysis of peptide-binding data
    • Segal, M., Cummings, M., Hubbard, A.: Relating amino acid sequence to phenotype: analysis of peptide-binding data. Biometrics 57(2), 632-642 (2001)
    • (2001) Biometrics , vol.57 , Issue.2 , pp. 632-642
    • Segal, M.1    Cummings, M.2    Hubbard, A.3
  • 38
    • 34250679750 scopus 로고    scopus 로고
    • Epidemiology of hepatitis C virus infection
    • Alter, M.: Epidemiology of hepatitis C virus infection. World J. Gastroenterol. 13(17), 2436-2441 (2007)
    • (2007) World J. Gastroenterol , vol.13 , Issue.17 , pp. 2436-2441
    • Alter, M.1
  • 39
    • 0033458046 scopus 로고    scopus 로고
    • Natural History Of Hepatitis C
    • Alberti, A., Chemello, L., Benvegnu, L.: Natural History Of Hepatitis C. J. Hepatol. 31(supp. 1), 17-24 (1999)
    • (1999) J. Hepatol , vol.31 , Issue.SUPP. 1 , pp. 17-24
    • Alberti, A.1    Chemello, L.2    Benvegnu, L.3
  • 40
    • 23944467250 scopus 로고    scopus 로고
    • Adaptive immune responses in acute and chronic hepatitis C virus infection
    • Bowen, D., Walker, C.: Adaptive immune responses in acute and chronic hepatitis C virus infection. Nature 436, 946-952 (2005)
    • (2005) Nature , vol.436 , pp. 946-952
    • Bowen, D.1    Walker, C.2
  • 41
    • 0024509701 scopus 로고
    • Isolation Of A Cdna Clone Derived From A Bloodborne Non-A, Non-B Viral Hepatitis Genome
    • Choo, Q., et al.: Isolation Of A Cdna Clone Derived From A Bloodborne Non-A, Non-B Viral Hepatitis Genome. Science 244, 359-362 (1989)
    • (1989) Science , vol.244 , pp. 359-362
    • Choo, Q.1
  • 42
    • 0032809666 scopus 로고    scopus 로고
    • Evolution of the hypervariable region of hepatitis C virus
    • Smith, D.: Evolution of the hypervariable region of hepatitis C virus. J. Viral Hepat 6(suppl. 1), 41-46 (1999)
    • (1999) J. Viral Hepat , vol.6 , Issue.SUPPL. 1 , pp. 41-46
    • Smith, D.1
  • 43
    • 0034774844 scopus 로고    scopus 로고
    • Hypervariable region 1 of hepatitis C virus: Immunological decoy or biologically relevant domain?
    • Mondelli, M., et al.: Hypervariable region 1 of hepatitis C virus: immunological decoy or biologically relevant domain? Antiviral Res. 52(2), 153-159 (2001)
    • (2001) Antiviral Res , vol.52 , Issue.2 , pp. 153-159
    • Mondelli, M.1
  • 44
    • 13844253602 scopus 로고    scopus 로고
    • The Los Alamos hepatitis C sequence database
    • Kuiken, C., et al.: The Los Alamos hepatitis C sequence database. Bioinformatics 21(3), 379-384 (2005)
    • (2005) Bioinformatics , vol.21 , Issue.3 , pp. 379-384
    • Kuiken, C.1
  • 45
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J., Higgins, D., Gibson, T.: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic. Acids. Res. 22(22), 4673-4680 (1994)
    • (1994) Nucleic. Acids. Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 46
    • 18144406581 scopus 로고    scopus 로고
    • Solving the protein sequence metric problem
    • Atchley, W., et al.: Solving the protein sequence metric problem. Proc. Natl. Acad. Sci. USA 102(18), 6395-6400 (2005)
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.18 , pp. 6395-6400
    • Atchley, W.1
  • 48
    • 33845907935 scopus 로고    scopus 로고
    • Molecular architecture of the DNA-binding region and its relationship to classification of basic helix-loop-helix proteins
    • Atchley, W., Zhao, J.: Molecular architecture of the DNA-binding region and its relationship to classification of basic helix-loop-helix proteins. Mol. Biol. Evol. 24( 1 ), 192-202 (2007)
    • (2007) Mol. Biol. Evol , vol.24 , Issue.1 , pp. 192-202
    • Atchley, W.1    Zhao, J.2
  • 51
    • 0003980906 scopus 로고    scopus 로고
    • Midcontinent Ecological Science Center US Geological Survey Fort Collins, Colorado
    • Cade, B., Richards, J.: User Manual For BLOSSOM Statistical Software. Midcontinent Ecological Science Center US Geological Survey Fort Collins, Colorado (2001)
    • (2001) User Manual For BLOSSOM Statistical Software
    • Cade, B.1    Richards, J.2
  • 53
    • 50049097218 scopus 로고    scopus 로고
    • SPSS 15.0 for windows, SPSS Inc, Chicago IL (2006)
    • SPSS 15.0 for windows, SPSS Inc, Chicago IL (2006)
  • 54
    • 20844452182 scopus 로고    scopus 로고
    • Detection and reduction of evolutionary noise in correlated mutation analysis
    • Noivirt, O., Eisenstein, M., Horovitz, A.: Detection and reduction of evolutionary noise in correlated mutation analysis. Protein Eng. 18(5), 247-253 (2005)
    • (2005) Protein Eng , vol.18 , Issue.5 , pp. 247-253
    • Noivirt, O.1    Eisenstein, M.2    Horovitz, A.3
  • 55
    • 3242881590 scopus 로고    scopus 로고
    • CRASP: A program for analysis of coordinated substitutions in multiple alignments of protein sequences
    • Afonnikov, D., Kolchanov, N.: CRASP: a program for analysis of coordinated substitutions in multiple alignments of protein sequences. Nucleic. Acids. Res. 32, W64-W68 (2004)
    • (2004) Nucleic. Acids. Res , vol.32
    • Afonnikov, D.1    Kolchanov, N.2
  • 56
    • 50049092044 scopus 로고    scopus 로고
    • Math Works, T.: MATLAB, Natick, MA (2007)
    • Math Works, T.: MATLAB, Natick, MA (2007)
  • 57
    • 0034724418 scopus 로고    scopus 로고
    • Separation of phylogenetic and functional associations in biological sequences by using the parametric bootstrap
    • Wollenberg, K., Atchley, W.: Separation of phylogenetic and functional associations in biological sequences by using the parametric bootstrap. Proc. Natl. Acad. Sci. USA 97(7), 3288-3291 (2000)
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.7 , pp. 3288-3291
    • Wollenberg, K.1    Atchley, W.2
  • 58
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y., Hochberg, Y.: Controlling the false discovery rate: a practical and powerful approach to multiple testing. Journal of the Royal statistical Society, Series B 57(1), 289-300 (1995)
    • (1995) Journal of the Royal statistical Society, Series B , vol.57 , Issue.1 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 59
    • 0022203256 scopus 로고
    • Phylogenies and the comparative method
    • Felsenstein, J.: Phylogenies and the comparative method. Am. Nat. 125, 1-15 (1985)
    • (1985) Am. Nat , vol.125 , pp. 1-15
    • Felsenstein, J.1
  • 60
    • 0031901336 scopus 로고    scopus 로고
    • Long-term evolution of the hypervariable region of hepatitis C virus in a common-source-infected cohort
    • McAllister, J., et al.: Long-term evolution of the hypervariable region of hepatitis C virus in a common-source-infected cohort. J. Virol. 72(6), 4893-4905 (1998)
    • (1998) J. Virol , vol.72 , Issue.6 , pp. 4893-4905
    • McAllister, J.1
  • 61
    • 1842510015 scopus 로고    scopus 로고
    • High-resolution phylogenetic analysis of hepatitis C virus adaptation and its relationship to disease progression
    • Sheridan, I., et al.: High-resolution phylogenetic analysis of hepatitis C virus adaptation and its relationship to disease progression. J. Virol 78(7), 3447-3454 (2004)
    • (2004) J. Virol , vol.78 , Issue.7 , pp. 3447-3454
    • Sheridan, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.