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Volumn 43, Issue D1, 2015, Pages D283-D289

Expediting topology data gathering for the TOPDB database

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; ARTICLE; INFORMATION PROCESSING; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DATABASE; PROTEIN GLYCOSYLATION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; RELIABILITY; TOPOLOGY DATA BANK OF TRANSMEMBRANE PROTEINS DATABASE; CHEMISTRY; PROTEIN CONFORMATION;

EID: 84941351784     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku1119     Document Type: Article
Times cited : (36)

References (60)
  • 1
    • 10244252813 scopus 로고    scopus 로고
    • Transmembrane proteins in the Protein Data Bank: Identification and classification
    • Tusnády, G. E., Dosztányi, Z. and Simon, I. (2004) Transmembrane proteins in the Protein Data Bank: identification and classification. Bioinformatics, 20, 2964-2972.
    • (2004) Bioinformatics , vol.20 , pp. 2964-2972
    • Tusnády, G.E.1    Dosztányi, Z.2    Simon, I.3
  • 2
    • 13444280419 scopus 로고    scopus 로고
    • PDB TM: Selection and membrane localization of transmembrane proteins in the protein data bank
    • Tusnády, G., Dosztányi, Z. and Simon, I. (2005) PDB TM: selection and membrane localization of transmembrane proteins in the protein data bank. Nucleic Acids Res., 33, D275-D278.
    • (2005) Nucleic Acids Res. , vol.33 , pp. D275-D278
    • Tusnády, G.1    Dosztányi, Z.2    Simon, I.3
  • 3
    • 84874677954 scopus 로고    scopus 로고
    • PDBTM: Protein Data Bank of transmembrane proteins after 8 years
    • Kozma, D., Simon, I. and Tusnády, G. E. (2013) PDBTM: Protein Data Bank of transmembrane proteins after 8 years. Nucleic Acids Res., 41, D524-D529.
    • (2013) Nucleic Acids Res. , vol.41 , pp. D524-D529
    • Kozma, D.1    Simon, I.2    Tusnády, G.E.3
  • 4
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil, C. and Beckwith, J. (1985) TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. U. S. A., 82, 8129-8133.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 6
    • 0025053613 scopus 로고
    • Beta-lactamase as a probe of membrane protein assembly and protein export
    • Broome-Smith, J. K., Tadayyon, M. and Zhang, Y. (1990) Beta-lactamase as a probe of membrane protein assembly and protein export. Mol. Microbiol., 4, 1637-1644.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1637-1644
    • Broome-Smith, J.K.1    Tadayyon, M.2    Zhang, Y.3
  • 7
    • 0025099013 scopus 로고
    • Genetic and biochemical evaluation of eucaryotic membrane protein topology: Multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Sengstag, C., Stirling, C., Schekman, R. and Rine, J. (1990) Genetic and biochemical evaluation of eucaryotic membrane protein topology: multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mol. Cell. Biol., 10, 672-680.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 672-680
    • Sengstag, C.1    Stirling, C.2    Schekman, R.3    Rine, J.4
  • 9
    • 58849150788 scopus 로고    scopus 로고
    • Non-invasive topology analysis of membrane proteins in the secretory pathway
    • Brach, T., Soyk, S., Müller, C., Hinz, G., Hell, R., Brandizzi, F. and Meyer, A. J. (2009) Non-invasive topology analysis of membrane proteins in the secretory pathway. Plant J., 57, 534-541.
    • (2009) Plant J. , vol.57 , pp. 534-541
    • Brach, T.1    Soyk, S.2    Müller, C.3    Hinz, G.4    Hell, R.5    Brandizzi, F.6    Meyer, A.J.7
  • 10
    • 0020961266 scopus 로고
    • Transmembrane orientation of an early biosynthetic form of acetylcholine receptor delta subunit determined by proteolytic dissection in conjunction with monoclonal antibodies
    • Anderson, D. J., Blobel, G., Tzartos, S., Gullick, W. and Lindstrom, J. (1983) Transmembrane orientation of an early biosynthetic form of acetylcholine receptor delta subunit determined by proteolytic dissection in conjunction with monoclonal antibodies. J. Neurosci., 3, 1773-1784.
    • (1983) J. Neurosci. , vol.3 , pp. 1773-1784
    • Anderson, D.J.1    Blobel, G.2    Tzartos, S.3    Gullick, W.4    Lindstrom, J.5
  • 11
    • 0025958720 scopus 로고
    • Permissive sites and topology of an outer membrane protein with a reporter epitope
    • Charbit, A., Ronco, J., Michel, V., Werts, C. and Hofnung, M. (1991) Permissive sites and topology of an outer membrane protein with a reporter epitope. J. Bacteriol., 173, 262-275.
    • (1991) J. Bacteriol. , vol.173 , pp. 262-275
    • Charbit, A.1    Ronco, J.2    Michel, V.3    Werts, C.4    Hofnung, M.5
  • 12
    • 0027508383 scopus 로고
    • Reporter epitopes: A novel approach to examine transmembrane topology of integral membrane proteins applied to the alpha 1 subunit of the nicotinic acetylcholine receptor
    • Anand, R., Bason, L., Saedi, M. S., Gerzanich, V., Peng, X. and Lindstrom, J. (1993) Reporter epitopes: a novel approach to examine transmembrane topology of integral membrane proteins applied to the alpha 1 subunit of the nicotinic acetylcholine receptor. Biochemistry, 32, 9975-9984.
    • (1993) Biochemistry , vol.32 , pp. 9975-9984
    • Anand, R.1    Bason, L.2    Saedi, M.S.3    Gerzanich, V.4    Peng, X.5    Lindstrom, J.6
  • 13
    • 0029918133 scopus 로고    scopus 로고
    • Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofuorescence
    • Kast, C., Canfeld, V., Levenson, R. and Gros, P. (1996) Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofuorescence. J. Biol. Chem., 271, 9240-9248.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9240-9248
    • Kast, C.1    Canfeld, V.2    Levenson, R.3    Gros, P.4
  • 14
    • 0030685129 scopus 로고    scopus 로고
    • Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofuorescence
    • Kast, C. and Gros, P. (1997) Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofuorescence. J. Biol. Chem., 272, 26479-26487.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26479-26487
    • Kast, C.1    Gros, P.2
  • 15
    • 0032562137 scopus 로고    scopus 로고
    • Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein
    • Kast, C. and Gros, P. (1998) Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein. Biochemistry, 37, 2305-2313.
    • (1998) Biochemistry , vol.37 , pp. 2305-2313
    • Kast, C.1    Gros, P.2
  • 16
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I. M. and von Heijne, G. (1993) Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem., 268, 5798-5801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 17
    • 84882259886 scopus 로고    scopus 로고
    • Mass spectrometry investigation of glycosylation on the NXS/T sites in recombinant glycoproteins
    • Sokolowska, I., Ngounou Wetie, A. G., Roy, U., Woods, A. G. and Darie, C. C. (2013) Mass spectrometry investigation of glycosylation on the NXS/T sites in recombinant glycoproteins. Biochim. Biophys. Acta, 1834, 1474-1483.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1474-1483
    • Sokolowska, I.1    Ngounou Wetie, A.G.2    Roy, U.3    Woods, A.G.4    Darie, C.C.5
  • 20
    • 84893178816 scopus 로고    scopus 로고
    • Characterization of the membrane proteome and N-glycoproteome in BV-2 mouse microglia by liquid chromatography-tandem mass spectrometry
    • Han, D., Moon, S., Kim, Y., Min, H. and Kim, Y. (2014) Characterization of the membrane proteome and N-glycoproteome in BV-2 mouse microglia by liquid chromatography-tandem mass spectrometry. BMC Genomics, 15, 95.
    • (2014) BMC Genomics , vol.15 , pp. 95
    • Han, D.1    Moon, S.2    Kim, Y.3    Min, H.4    Kim, Y.5
  • 21
    • 0032700184 scopus 로고    scopus 로고
    • Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques
    • Loo, T. W. and Clarke, D. M. (1999) Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques. Biochim. Biophys. Acta, 1461, 315-325.
    • (1999) Biochim. Biophys. Acta , vol.1461 , pp. 315-325
    • Loo, T.W.1    Clarke, D.M.2
  • 22
    • 70350350024 scopus 로고    scopus 로고
    • New structural arrangement of the extracellular regions of the phosphate transporter SLC20A1, the receptor for gibbon ape leukemia virus
    • Farrell, K. B., Tusnady, G. E. and Eiden, M. V. (2009) New structural arrangement of the extracellular regions of the phosphate transporter SLC20A1, the receptor for gibbon ape leukemia virus. J. Biol. Chem., 284, 29979-29987.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29979-29987
    • Farrell, K.B.1    Tusnady, G.E.2    Eiden, M.V.3
  • 23
    • 0037474222 scopus 로고    scopus 로고
    • Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1
    • Zhu, Q., Lee, D. W. K. and Casey, J. R. (2003) Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1. J. Biol. Chem., 278, 3112-3120.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3112-3120
    • Zhu, Q.1    Lee, D.W.K.2    Casey, J.R.3
  • 24
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. (2003) Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta, 1612, 1-40.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 25
    • 16344362822 scopus 로고    scopus 로고
    • TMDET: Web server for detecting transmembrane regions of proteins by using their 3D coordinates
    • Tusnády, G. E., Dosztányi, Z. and Simon, I. (2005) TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates. Bioinformatics, 21, 1276-1277.
    • (2005) Bioinformatics , vol.21 , pp. 1276-1277
    • Tusnády, G.E.1    Dosztányi, Z.2    Simon, I.3
  • 26
    • 34547618240 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in positioning of peripheral proteins in membranes
    • Lomize, A. L., Pogozheva, I. D., Lomize, M. A. and Mosberg, H. I. (2007) The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Struct. Biol., 7, 44.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 44
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 27
    • 84861060898 scopus 로고    scopus 로고
    • OPM database and PPM web server: Resources for positioning of proteins in membranes
    • Lomize, M. A., Pogozheva, I. D., Joo, H., Mosberg, H. I. and Lomize, A. L. (2012) OPM database and PPM web server: resources for positioning of proteins in membranes. Nucleic Acids Res., 40, D370-D376.
    • (2012) Nucleic Acids Res. , vol.40 , pp. D370-D376
    • Lomize, M.A.1    Pogozheva, I.D.2    Joo, H.3    Mosberg, H.I.4    Lomize, A.L.5
  • 28
    • 84861038844 scopus 로고    scopus 로고
    • Knowledge-based potential for positioning membrane-associated structures and assessing residue-specific energetic contributions
    • Schramm, C. A., Hannigan, B. T., Donald, J. E., Keasar, C., Saven, J. G., Degrado, W. F. and Samish, I. (2012) Knowledge-based potential for positioning membrane-associated structures and assessing residue-specific energetic contributions. Structure, 20, 924-935.
    • (2012) Structure , vol.20 , pp. 924-935
    • Schramm, C.A.1    Hannigan, B.T.2    Donald, J.E.3    Keasar, C.4    Saven, J.G.5    Degrado, W.F.6    Samish, I.7
  • 30
    • 33847155026 scopus 로고    scopus 로고
    • Algorithms for incorporating prior topological information in HMMs: Application to transmembrane proteins
    • Bagos, P. G., Liakopoulos, T. D. and Hamodrakas, S. J. (2006) Algorithms for incorporating prior topological information in HMMs: application to transmembrane proteins. BMC Bioinformatics, 7, 189.
    • (2006) BMC Bioinformatics , vol.7 , pp. 189
    • Bagos, P.G.1    Liakopoulos, T.D.2    Hamodrakas, S.J.3
  • 31
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnády, G. E. and Simon, I. (2001) The HMMTOP transmembrane topology prediction server. Bioinformatics, 17, 849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnády, G.E.1    Simon, I.2
  • 32
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction -The Phobius web server
    • Käll, L., Krogh, A. and Sonnhammer, E. L. L. (2007) Advantages of combined transmembrane topology and signal peptide prediction-the Phobius web server. Nucleic Acids Res., 35, W429-W432.
    • (2007) Nucleic Acids Res. , vol.35 , pp. W429-W432
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.L.3
  • 33
    • 0344406716 scopus 로고    scopus 로고
    • Reliability measures for membrane protein topology prediction algorithms
    • Melén, K., Krogh, A. and von Heijne, G. (2003) Reliability measures for membrane protein topology prediction algorithms. J. Mol. Biol., 327, 735-744.
    • (2003) J. Mol. Biol. , vol.327 , pp. 735-744
    • Melén, K.1    Krogh, A.2    Von Heijne, G.3
  • 34
    • 22244451035 scopus 로고    scopus 로고
    • Improved membrane protein topology prediction by domain assignments
    • Bernsel, A. and von Heijne, G. (2005) Improved membrane protein topology prediction by domain assignments. Protein Sci., 14, 1723-1728.
    • (2005) Protein Sci. , vol.14 , pp. 1723-1728
    • Bernsel, A.1    Von Heijne, G.2
  • 35
    • 33645297088 scopus 로고    scopus 로고
    • The use of functional domains to improve transmembrane protein topology prediction
    • Xu, E. W., Kearney, P. and Brown, D. G. (2006) The use of functional domains to improve transmembrane protein topology prediction. J. Bioinform. Comput. Biol., 4, 109-123.
    • (2006) J. Bioinform. Comput. Biol. , vol.4 , pp. 109-123
    • Xu, E.W.1    Kearney, P.2    Brown, D.G.3
  • 38
    • 45449101527 scopus 로고    scopus 로고
    • TOPDOM: Database of domains and motifs with conservative location in transmembrane proteins
    • Tusnády, G. E., Kalmár, L., Hegyi, H., Tompa, P. and Simon, I. (2008) TOPDOM: database of domains and motifs with conservative location in transmembrane proteins. Bioinformatics, 24, 1469-1470.
    • (2008) Bioinformatics , vol.24 , pp. 1469-1470
    • Tusnády, G.E.1    Kalmár, L.2    Hegyi, H.3    Tompa, P.4    Simon, I.5
  • 39
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnády, G. E. and Simon, I. (1998) Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J. Mol. Biol., 283, 489-506.
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnády, G.E.1    Simon, I.2
  • 40
    • 48749084114 scopus 로고    scopus 로고
    • MemBrain: Improving the accuracy of predicting transmembrane helices
    • Shen, H. and Chou, J. J. (2008) MemBrain: improving the accuracy of predicting transmembrane helices. PLoS One, 3, e2399.
    • (2008) PLoS One , vol.3 , pp. e2399
    • Shen, H.1    Chou, J.J.2
  • 41
    • 67649472570 scopus 로고    scopus 로고
    • Transmembrane protein topology prediction using support vector machines
    • Nugent, T. and Jones, D. T. (2009) Transmembrane protein topology prediction using support vector machines. BMC Bioinformatics, 10, 159.
    • (2009) BMC Bioinformatics , vol.10 , pp. 159
    • Nugent, T.1    Jones, D.T.2
  • 42
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: Improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund, H. and Elofsson, A. (2008) OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics, 24, 1662-1668.
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 43
    • 57149112523 scopus 로고    scopus 로고
    • Transmembrane topology and signal peptide prediction using dynamic Bayesian networks
    • Reynolds, S. M., Käll, L., Riffe, M. E., Bilmes, J. A. and Noble, W. S. (2008) Transmembrane topology and signal peptide prediction using dynamic bayesian networks. PLoS Comput. Biol., 4, e1000213.
    • (2008) PLoS Comput. Biol. , vol.4 , pp. e1000213
    • Reynolds, S.M.1    Käll, L.2    Riffe, M.E.3    Bilmes, J.A.4    Noble, W.S.5
  • 44
    • 3042579686 scopus 로고    scopus 로고
    • Best alpha-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information
    • Viklund, H. and Elofsson, A. (2004) Best alpha-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information. Protein Sci., 13, 1908-1917.
    • (2004) Protein Sci. , vol.13 , pp. 1908-1917
    • Viklund, H.1    Elofsson, A.2
  • 47
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • Chen, R., Jiang, X., Sun, D., Han, G., Wang, F., Ye, M., Wang, L. and Zou, H. (2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J. Proteome Res., 8, 651-661.
    • (2009) J. Proteome Res. , vol.8 , pp. 651-661
    • Chen, R.1    Jiang, X.2    Sun, D.3    Han, G.4    Wang, F.5    Ye, M.6    Wang, L.7    Zou, H.8
  • 50
    • 79954493200 scopus 로고    scopus 로고
    • Rapid membrane protein topology prediction
    • Hennerdal, A. and Elofsson, A. (2011) Rapid membrane protein topology prediction. Bioinformatics, 27, 1322-1323.
    • (2011) Bioinformatics , vol.27 , pp. 1322-1323
    • Hennerdal, A.1    Elofsson, A.2
  • 51
    • 84862192588 scopus 로고    scopus 로고
    • Accurate de novo structure prediction of large transmembrane protein domains using fragment-assembly and correlated mutation analysis
    • Nugent, T. and Jones, D. T. (2012) Accurate de novo structure prediction of large transmembrane protein domains using fragment-assembly and correlated mutation analysis. Proc. Natl. Acad. Sci. U. S. A., 109, E1540-E1547.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. E1540-E1547
    • Nugent, T.1    Jones, D.T.2
  • 53
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley, D. O., Rapp, M., Granseth, E., Melén, K., Drew, D. and von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science, 308, 1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melén, K.4    Drew, D.5    Von Heijne, G.6
  • 54
    • 33746616385 scopus 로고    scopus 로고
    • A global topology map of the Saccharomyces cerevisiae membrane proteome
    • Kim, H., Melén, K., Osterberg, M. and von Heijne, G. (2006) A global topology map of the Saccharomyces cerevisiae membrane proteome. Proc. Natl. Acad. Sci. U. S. A., 103, 11142-11147.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11142-11147
    • Kim, H.1    Melén, K.2    Osterberg, M.3    Von Heijne, G.4
  • 55
    • 70449378220 scopus 로고    scopus 로고
    • MetaTM - A consensus method for transmembrane protein topology prediction
    • Klammer, M., Messina, D. N., Schmitt, T. and Sonnhammer, E. L. (2009) MetaTM - a consensus method for transmembrane protein topology prediction. BMC Bioinformatics, 10, 314.
    • (2009) BMC Bioinformatics , vol.10 , pp. 314
    • Klammer, M.1    Messina, D.N.2    Schmitt, T.3    Sonnhammer, E.L.4
  • 57
    • 77950663547 scopus 로고    scopus 로고
    • CoBaltDB: Complete bacterial and archaeal orfeomes subcellular localization database and associated resources
    • Goudenège, D., Avner, S., Lucchetti-Miganeh, C. and Barloy-Hubler, F. (2010) CoBaltDB: Complete bacterial and archaeal orfeomes subcellular localization database and associated resources. BMC Microbiol., 10, 88.
    • (2010) BMC Microbiol. , vol.10 , pp. 88
    • Goudenège, D.1    Avner, S.2    Lucchetti-Miganeh, C.3    Barloy-Hubler, F.4
  • 58
    • 78651331297 scopus 로고    scopus 로고
    • TMPad: An integrated structural database for helix-packing folds in transmembrane proteins
    • Lo, A., Cheng, C.-W., Chiu, Y.-Y., Sung, T.-Y. and Hsu, W.-L. (2011) TMPad: an integrated structural database for helix-packing folds in transmembrane proteins. Nucleic Acids Res., 39, D347-D355.
    • (2011) Nucleic Acids Res. , vol.39 , pp. D347-D355
    • Lo, A.1    Cheng, C.-W.2    Chiu, Y.-Y.3    Sung, T.-Y.4    Hsu, W.-L.5
  • 59
    • 84885459056 scopus 로고    scopus 로고
    • Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli
    • Butler, E. K., Davis, R. M., Bari, V., Nicholson, P. A. and Ruiz, N. (2013) Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli. J. Bacteriol., 195, 4639-4649.
    • (2013) J. Bacteriol. , vol.195 , pp. 4639-4649
    • Butler, E.K.1    Davis, R.M.2    Bari, V.3    Nicholson, P.A.4    Ruiz, N.5
  • 60
    • 84864491623 scopus 로고    scopus 로고
    • CMWeb: An interactive on-line tool for analysing residue-residue contacts and contact prediction methods
    • Kozma, D., Simon, I. and Tusnády, G. E. (2012) CMWeb: an interactive on-line tool for analysing residue-residue contacts and contact prediction methods. Nucleic Acids Res., 40, W329-W333.
    • (2012) Nucleic Acids Res. , vol.40 , pp. W329-W333
    • Kozma, D.1    Simon, I.2    Tusnády, G.E.3


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