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Volumn 10, Issue 7, 2014, Pages

The CD27L and CTP1L Endolysins Targeting Clostridia Contain a Built-in Trigger and Release Factor

Author keywords

[No Author keywords available]

Indexed keywords

ENDOLYSIN; PROTEINASE; VIRAL PROTEIN;

EID: 84905385283     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004228     Document Type: Article
Times cited : (38)

References (49)
  • 1
    • 84870725981 scopus 로고    scopus 로고
    • Tools from viruses: bacteriophage successes and beyond
    • doi:10.1016/j.virol.2012.09.017
    • Henry M, Debarbieux L, (2012) Tools from viruses: bacteriophage successes and beyond. Virology 434: 151-161 doi:10.1016/j.virol.2012.09.017.
    • (2012) Virology , vol.434 , pp. 151-161
    • Henry, M.1    Debarbieux, L.2
  • 2
    • 84881593673 scopus 로고    scopus 로고
    • Gut solutions to a gut problem: bacteriocins, probiotics and bacteriophage for control of Clostridium difficile infection
    • doi:10.1099/jmm.0.058933-0
    • Rea MC, Alemayehu D, Ross RP, Hill C, (2013) Gut solutions to a gut problem: bacteriocins, probiotics and bacteriophage for control of Clostridium difficile infection. J Med Microbiol 62: 1369-1378 doi:10.1099/jmm.0.058933-0.
    • (2013) J Med Microbiol , vol.62 , pp. 1369-1378
    • Rea, M.C.1    Alemayehu, D.2    Ross, R.P.3    Hill, C.4
  • 3
    • 84880755457 scopus 로고    scopus 로고
    • Evaluation of bacteriophage therapy to control Clostridium difficile and toxin production in an in vitro human colon model system
    • doi:10.1016/j.anaerobe.2013.05.001
    • Meader E, Mayer MJ, Steverding D, Carding SR, Narbad A, (2013) Evaluation of bacteriophage therapy to control Clostridium difficile and toxin production in an in vitro human colon model system. Anaerobe 22: 25-30 doi:10.1016/j.anaerobe.2013.05.001.
    • (2013) Anaerobe , vol.22 , pp. 25-30
    • Meader, E.1    Mayer, M.J.2    Steverding, D.3    Carding, S.R.4    Narbad, A.5
  • 4
    • 84863673580 scopus 로고    scopus 로고
    • Current state of Clostridium difficile treatment options
    • doi:10.1093/cid/cis355
    • Venugopal AA, Johnson S, (2012) Current state of Clostridium difficile treatment options. Clin Infect Dis Off Publ Infect Dis Soc Am 55 (Suppl 2): S71-76 doi:10.1093/cid/cis355.
    • (2012) Clin Infect Dis Off Publ Infect Dis Soc Am , vol.55 , Issue.SUPPL. 2
    • Venugopal, A.A.1    Johnson, S.2
  • 5
    • 53849135601 scopus 로고    scopus 로고
    • Molecular characterization of a Clostridium difficile bacteriophage and its cloned biologically active endolysin
    • doi:10.1128/JB.00686-08
    • Mayer MJ, Narbad A, Gasson MJ, (2008) Molecular characterization of a Clostridium difficile bacteriophage and its cloned biologically active endolysin. J Bacteriol 190: 6734-6740 doi:10.1128/JB.00686-08.
    • (2008) J Bacteriol , vol.190 , pp. 6734-6740
    • Mayer, M.J.1    Narbad, A.2    Gasson, M.J.3
  • 6
    • 22544471225 scopus 로고    scopus 로고
    • Bacteriophage endolysins-current state of research and applications
    • doi:10.1016/j.mib.2005.06.002
    • Loessner MJ, (2005) Bacteriophage endolysins-current state of research and applications. Curr Opin Microbiol 8: 480-487 doi:10.1016/j.mib.2005.06.002.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 480-487
    • Loessner, M.J.1
  • 7
    • 80053609598 scopus 로고    scopus 로고
    • Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range
    • doi:10.1128/JB.00439-11
    • Mayer MJ, Garefalaki V, Spoerl R, Narbad A, Meijers R, (2011) Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range. J Bacteriol 193: 5477-5486 doi:10.1128/JB.00439-11.
    • (2011) J Bacteriol , vol.193 , pp. 5477-5486
    • Mayer, M.J.1    Garefalaki, V.2    Spoerl, R.3    Narbad, A.4    Meijers, R.5
  • 8
    • 35948990424 scopus 로고    scopus 로고
    • Taking aim on bacterial pathogens: from phage therapy to enzybiotics
    • doi:10.1016/j.mib.2007.08.002
    • Hermoso JA, García JL, García P, (2007) Taking aim on bacterial pathogens: from phage therapy to enzybiotics. Curr Opin Microbiol 10: 461-472 doi:10.1016/j.mib.2007.08.002.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 461-472
    • Hermoso, J.A.1    García, J.L.2    García, P.3
  • 10
    • 76649100791 scopus 로고    scopus 로고
    • Micron-scale holes terminate the phage infection cycle
    • doi:10.1073/pnas.0914030107
    • Dewey JS, Savva CG, White RL, Vitha S, Holzenburg A, et al. (2010) Micron-scale holes terminate the phage infection cycle. Proc Natl Acad Sci U S A 107: 2219-2223 doi:10.1073/pnas.0914030107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2219-2223
    • Dewey, J.S.1    Savva, C.G.2    White, R.L.3    Vitha, S.4    Holzenburg, A.5
  • 11
    • 0141594766 scopus 로고    scopus 로고
    • Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1
    • Hermoso JA, Monterroso B, Albert A, Galán B, Ahrazem O, et al. (2003) Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. Struct Lond Engl 1993 11: 1239-1249.
    • (2003) Struct Lond Engl 1993 , vol.11 , pp. 1239-1249
    • Hermoso, J.A.1    Monterroso, B.2    Albert, A.3    Galán, B.4    Ahrazem, O.5
  • 12
    • 33846431990 scopus 로고    scopus 로고
    • The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis
    • doi:10.1016/j.jmb.2006.11.056
    • Porter CJ, Schuch R, Pelzek AJ, Buckle AM, McGowan S, et al. (2007) The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis. J Mol Biol 366: 540-550 doi:10.1016/j.jmb.2006.11.056.
    • (2007) J Mol Biol , vol.366 , pp. 540-550
    • Porter, C.J.1    Schuch, R.2    Pelzek, A.J.3    Buckle, A.M.4    McGowan, S.5
  • 13
    • 27444432629 scopus 로고    scopus 로고
    • Structure and lytic activity of a Bacillus anthracis prophage endolysin
    • doi:10.1074/jbc.M502723200
    • Low LY, Yang C, Perego M, Osterman A, Liddington RC, (2005) Structure and lytic activity of a Bacillus anthracis prophage endolysin. J Biol Chem 280: 35433-35439 doi:10.1074/jbc.M502723200.
    • (2005) J Biol Chem , vol.280 , pp. 35433-35439
    • Low, L.Y.1    Yang, C.2    Perego, M.3    Osterman, A.4    Liddington, R.C.5
  • 14
    • 77955971676 scopus 로고    scopus 로고
    • Genomic sequence and characterization of the virulent bacteriophage phiCTP1 from Clostridium tyrobutyricum and heterologous expression of its endolysin
    • doi:10.1128/AEM.00989-10
    • Mayer MJ, Payne J, Gasson MJ, Narbad A, (2010) Genomic sequence and characterization of the virulent bacteriophage phiCTP1 from Clostridium tyrobutyricum and heterologous expression of its endolysin. Appl Environ Microbiol 76: 5415-5422 doi:10.1128/AEM.00989-10.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5415-5422
    • Mayer, M.J.1    Payne, J.2    Gasson, M.J.3    Narbad, A.4
  • 15
    • 11844266530 scopus 로고    scopus 로고
    • Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme
    • doi:10.1126/science.1105143
    • Xu M, Arulandu A, Struck DK, Swanson S, Sacchettini JC, et al. (2005) Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science 307: 113-117 doi:10.1126/science.1105143.
    • (2005) Science , vol.307 , pp. 113-117
    • Xu, M.1    Arulandu, A.2    Struck, D.K.3    Swanson, S.4    Sacchettini, J.C.5
  • 16
    • 84864504723 scopus 로고    scopus 로고
    • X-ray crystal structure of the streptococcal specific phage lysin PlyC
    • doi:10.1073/pnas.1208424109
    • McGowan S, Buckle AM, Mitchell MS, Hoopes JT, Gallagher DT, et al. (2012) X-ray crystal structure of the streptococcal specific phage lysin PlyC. Proc Natl Acad Sci 109: 12752-7 doi:10.1073/pnas.1208424109 Available: http://www.pnas.org/content/early/2012/07/17/1208424109 Accessed 24 January 2013.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 12752-12757
    • McGowan, S.1    Buckle, A.M.2    Mitchell, M.S.3    Hoopes, J.T.4    Gallagher, D.T.5
  • 17
    • 0032919371 scopus 로고    scopus 로고
    • Protein folds and families: sequence and structure alignments
    • Holm L, Sander C, (1999) Protein folds and families: sequence and structure alignments. Nucleic Acids Res 27: 244-247.
    • (1999) Nucleic Acids Res , vol.27 , pp. 244-247
    • Holm, L.1    Sander, C.2
  • 18
    • 33751066117 scopus 로고    scopus 로고
    • The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls
    • doi:10.1016/j.jmb.2006.08.069
    • Korndörfer IP, Danzer J, Schmelcher M, Zimmer M, Skerra A, et al. (2006) The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls. J Mol Biol 364: 678-689 doi:10.1016/j.jmb.2006.08.069.
    • (2006) J Mol Biol , vol.364 , pp. 678-689
    • Korndörfer, I.P.1    Danzer, J.2    Schmelcher, M.3    Zimmer, M.4    Skerra, A.5
  • 19
    • 34548300011 scopus 로고    scopus 로고
    • Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1
    • doi:10.1074/jbc.M704317200
    • Pérez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, et al. (2007) Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1. J Biol Chem 282: 24990-24999 doi:10.1074/jbc.M704317200.
    • (2007) J Biol Chem , vol.282 , pp. 24990-24999
    • Pérez-Dorado, I.1    Campillo, N.E.2    Monterroso, B.3    Hesek, D.4    Lee, M.5
  • 21
    • 79953734276 scopus 로고    scopus 로고
    • Macromolecular complexes in crystals and solutions
    • doi:10.1107/S0907444911007232
    • Krissinel E, (2011) Macromolecular complexes in crystals and solutions. Acta Crystallogr D Biol Crystallogr 67: 376-385 doi:10.1107/S0907444911007232.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 376-385
    • Krissinel, E.1
  • 22
    • 12944249776 scopus 로고
    • A discussion of the solution for the best rotation to relate two sets of vectors
    • doi:10.1107/S0567739478001680
    • Kabsch W, (1978) A discussion of the solution for the best rotation to relate two sets of vectors. Acta Crystallogr Sect A 34: 827-828 doi:10.1107/S0567739478001680.
    • (1978) Acta Crystallogr Sect A , vol.34 , pp. 827-828
    • Kabsch, W.1
  • 23
    • 0029185933 scopus 로고
    • CRYSOL - a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates
    • doi:10.1107/S0021889895007047
    • Svergun D, Barberato C, Koch MHJ, (1995) CRYSOL - a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates. J Appl Crystallogr 28: 768-773 doi:10.1107/S0021889895007047.
    • (1995) J Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 24
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • doi:10.1107/S0021889812007662
    • Petoukhov MV, Franke D, Shkumatov AV, Tria G, Kikhney AG, et al. (2012) New developments in the ATSAS program package for small-angle scattering data analysis. J Appl Crystallogr 45: 342-350 doi:10.1107/S0021889812007662.
    • (2012) J Appl Crystallogr , vol.45 , pp. 342-350
    • Petoukhov, M.V.1    Franke, D.2    Shkumatov, A.V.3    Tria, G.4    Kikhney, A.G.5
  • 25
    • 18744396951 scopus 로고    scopus 로고
    • Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid
    • doi:10.1038/nmeth739
    • Hino N, Okazaki Y, Kobayashi T, Hayashi A, Sakamoto K, et al. (2005) Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid. Nat Methods 2: 201-206 doi:10.1038/nmeth739.
    • (2005) Nat Methods , vol.2 , pp. 201-206
    • Hino, N.1    Okazaki, Y.2    Kobayashi, T.3    Hayashi, A.4    Sakamoto, K.5
  • 26
    • 0036349994 scopus 로고    scopus 로고
    • Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer
    • Fernández-Tornero C, García E, López R, Giménez-Gallego G, Romero A, (2002) Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer. J Mol Biol 321: 163-173.
    • (2002) J Mol Biol , vol.321 , pp. 163-173
    • Fernández-Tornero, C.1    García, E.2    López, R.3    Giménez-Gallego, G.4    Romero, A.5
  • 27
    • 80255133188 scopus 로고    scopus 로고
    • A stable phage lysin (Cpl-1) dimer with increased antipneumococcal activity and decreased plasma clearance
    • doi:10.1016/j.ijantimicag.2011.08.009
    • Resch G, Moreillon P, Fischetti VA, (2011) A stable phage lysin (Cpl-1) dimer with increased antipneumococcal activity and decreased plasma clearance. Int J Antimicrob Agents 38: 516-521 doi:10.1016/j.ijantimicag.2011.08.009.
    • (2011) Int J Antimicrob Agents , vol.38 , pp. 516-521
    • Resch, G.1    Moreillon, P.2    Fischetti, V.A.3
  • 28
    • 84861219631 scopus 로고    scopus 로고
    • Allostery and the Monod-Wyman-Changeux Model After 50 Years
    • doi:10.1146/annurev-biophys-050511-102222
    • Changeux J-P, (2011) Allostery and the Monod-Wyman-Changeux Model After 50 Years. Annu Rev Biophys 41: 103-33 doi:10.1146/annurev-biophys-050511-102222 Available: http://www.ncbi.nlm.nih.gov/pubmed/22224598 Accessed 3 April 2012.
    • (2011) Annu Rev Biophys , vol.41 , pp. 103-133
    • Changeux, J.-P.1
  • 29
    • 80053201228 scopus 로고    scopus 로고
    • Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins
    • doi:10.1074/jbc.M111.244160
    • Low LY, Yang C, Perego M Osterman A, Liddington R, (2011) Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins. J Biol Chem 286: 34391-34403 doi:10.1074/jbc.M111.244160.
    • (2011) J Biol Chem , vol.286 , pp. 34391-34403
    • Low, L.Y.1    Yang, C.2    Perego M Osterman, A.3    Liddington, R.4
  • 30
    • 65549169054 scopus 로고    scopus 로고
    • Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike
    • doi:10.1016/j.molcel.2009.04.009
    • Xiang Y, Leiman PG, Li L, Grimes S, Anderson DL, et al. (2009) Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike. Mol Cell 34: 375-386 doi:10.1016/j.molcel.2009.04.009.
    • (2009) Mol Cell , vol.34 , pp. 375-386
    • Xiang, Y.1    Leiman, P.G.2    Li, L.3    Grimes, S.4    Anderson, D.L.5
  • 31
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • doi:10.1074/jbc.M703062200
    • Egerer M, Giesemann T, Jank T, Satchell KJF, Aktories K, (2007) Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. J Biol Chem 282: 25314-25321 doi:10.1074/jbc.M703062200.
    • (2007) J Biol Chem , vol.282 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Satchell, K.J.F.4    Aktories, K.5
  • 32
    • 33947502604 scopus 로고    scopus 로고
    • Autocatalytic cleavage of Clostridium difficile toxin B
    • doi:10.1038/nature05622
    • Reineke J, Tenzer S, Rupnik M, Koschinski A, Hasselmayer O, et al. (2007) Autocatalytic cleavage of Clostridium difficile toxin B. Nature 446: 415-419 doi:10.1038/nature05622.
    • (2007) Nature , vol.446 , pp. 415-419
    • Reineke, J.1    Tenzer, S.2    Rupnik, M.3    Koschinski, A.4    Hasselmayer, O.5
  • 33
    • 84861142923 scopus 로고    scopus 로고
    • Genomic sequence of bacteriophage ATCC 8074-B1 and activity of its endolysin and engineered variants against Clostridium sporogenes
    • doi:10.1128/AEM.07884-11
    • Mayer MJ, Gasson MJ, Narbad A, (2012) Genomic sequence of bacteriophage ATCC 8074-B1 and activity of its endolysin and engineered variants against Clostridium sporogenes. Appl Environ Microbiol 78: 3685-3692 doi:10.1128/AEM.07884-11.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 3685-3692
    • Mayer, M.J.1    Gasson, M.J.2    Narbad, A.3
  • 34
    • 84857129636 scopus 로고    scopus 로고
    • Insights into cis-autoproteolysis reveal a reactive state formed through conformational rearrangement
    • doi:10.1073/pnas.1113633109
    • Buller AR, Freeman MF, Wright NT, Schildbach JF, Townsend CA, (2012) Insights into cis-autoproteolysis reveal a reactive state formed through conformational rearrangement. Proc Natl Acad Sci U S A 109: 2308-2313 doi:10.1073/pnas.1113633109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 2308-2313
    • Buller, A.R.1    Freeman, M.F.2    Wright, N.T.3    Schildbach, J.F.4    Townsend, C.A.5
  • 35
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • doi:10.1146/annurev.biochem.69.1.447
    • Paulus H, (2000) Protein splicing and related forms of protein autoprocessing. Annu Rev Biochem 69: 447-496 doi:10.1146/annurev.biochem.69.1.447.
    • (2000) Annu Rev Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 38
    • 84860285553 scopus 로고    scopus 로고
    • Completion of autobuilt protein models using a database of protein fragments
    • doi:10.1107/S0907444911039655
    • Cowtan K, (2012) Completion of autobuilt protein models using a database of protein fragments. Acta Crystallogr D Biol Crystallogr 68: 328-335 doi:10.1107/S0907444911039655.
    • (2012) Acta Crystallogr D Biol Crystallogr , vol.68 , pp. 328-335
    • Cowtan, K.1
  • 40
    • 74549194551 scopus 로고    scopus 로고
    • Molecular replacement with MOLREP
    • doi:10.1107/S0907444909042589
    • Vagin A, Teplyakov A, (2010) Molecular replacement with MOLREP. Acta Crystallogr D Biol Crystallogr 66: 22-25 doi:10.1107/S0907444909042589.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 22-25
    • Vagin, A.1    Teplyakov, A.2
  • 43
    • 0141484613 scopus 로고    scopus 로고
    • PRIMUS: a Windows PC-based system for small-angle scattering data analysis
    • doi:10.1107/S0021889803012779
    • Konarev PV, Volkov VV, Sokolova AV, Koch MHJ, Svergun DI, (2003) PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J Appl Crystallogr 36: 1277-1282 doi:10.1107/S0021889803012779.
    • (2003) J Appl Crystallogr , vol.36 , pp. 1277-1282
    • Konarev, P.V.1    Volkov, V.V.2    Sokolova, A.V.3    Koch, M.H.J.4    Svergun, D.I.5
  • 45
    • 0026244044 scopus 로고
    • GNOM - a program package for small-angle scattering data processing
    • doi:10.1107/S002188989100081X
    • Semenyuk AV, Svergun DI, (1991) GNOM - a program package for small-angle scattering data processing. J Appl Crystallogr 24: 537-540 doi:10.1107/S002188989100081X.
    • (1991) J Appl Crystallogr , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 46
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • doi:10.1107/S0021889809000338
    • Franke D, Svergun DI, (2009) DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J Appl Crystallogr 42: 342-346 doi:10.1107/S0021889809000338.
    • (2009) J Appl Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 47
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • doi:10.1107/S0021889803000268
    • Volkov VV, Svergun DI, (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Crystallogr 36: 860-864 doi:10.1107/S0021889803000268.
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 48
    • 23644445334 scopus 로고    scopus 로고
    • Photo-cross-linking interacting proteins with a genetically encoded benzophenone
    • doi:10.1038/nmeth0505-377
    • Farrell IS, Toroney R, Hazen JL, Mehl RA, Chin JW, (2005) Photo-cross-linking interacting proteins with a genetically encoded benzophenone. Nat Methods 2: 377-384 doi:10.1038/nmeth0505-377.
    • (2005) Nat Methods , vol.2 , pp. 377-384
    • Farrell, I.S.1    Toroney, R.2    Hazen, J.L.3    Mehl, R.A.4    Chin, J.W.5
  • 49
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins
    • doi:10.1093/nar/gkg556
    • Gouet P, Robert X, Courcelle E, (2003) ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 31: 3320-3323 doi:10.1093/nar/gkg556.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3


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