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Volumn 2013, Issue , 2013, Pages

In silico determination and validation of baumannii acinetobactin utilization a structure and ligand binding site

Author keywords

[No Author keywords available]

Indexed keywords

IRON REGULATED OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; UNCLASSIFIED DRUG; IRON; LIGAND; MEMBRANE PROTEIN;

EID: 84884887649     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/172784     Document Type: Article
Times cited : (32)

References (57)
  • 1
    • 78649892086 scopus 로고    scopus 로고
    • Deciphering the iron response in Acinetobacter baumannii: A proteomics approach
    • 2-s2.0-78649892086 10.1016/j.jprot.2010.07.010
    • Nwugo C. C., Gaddy J. A., Zimbler D. L., Actis L. A., Deciphering the iron response in Acinetobacter baumannii: a proteomics approach. Journal of Proteomics 2011 74 1 44 58 2-s2.0-78649892086 10.1016/j.jprot.2010.07.010
    • (2011) Journal of Proteomics , vol.74 , Issue.1 , pp. 44-58
    • Nwugo, C.C.1    Gaddy, J.A.2    Zimbler, D.L.3    Actis, L.A.4
  • 2
    • 4444347184 scopus 로고    scopus 로고
    • T
    • Mihara K., Tanabe T., Yamakawa Y., Funahashi T., Nakao H., Narimatsu S., Yamamoto S., Identification and transcriptional organization of a gene cluster involved in biosynthesis and transport of acinetobactin, a siderophore produced by Acinetobacter baumannii ATCC 19606T. Microbiology 2004 150 8 2587 2597 2-s2.0-4444347184 (Pubitemid 39177437)
    • (2004) Microbiology , vol.150 , Issue.8 , pp. 2587-2597
    • Mihara, K.1    Tanabe, T.2    Yamakawa, Y.3    Funahashi, T.4    Nakao, H.5    Narimatsu, S.6    Yamamoto, S.7
  • 3
    • 24644432870 scopus 로고    scopus 로고
    • Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa
    • DOI 10.1016/j.jmb.2005.08.004, PII S0022283605009046
    • Cobessi D., Celia H., Pattus F., Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. Journal of Molecular Biology 2005 352 4 893 904 2-s2.0-24644432870 10.1016/j.jmb.2005.08.004 (Pubitemid 41267075)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.4 , pp. 893-904
    • Cobessi, D.1    Celia, H.2    Pattus, F.3
  • 4
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • DOI 10.1146/annurev.micro.61.080706.093245
    • Bos M. P., Robert V., Tommassen J., Biogenesis of the gram-negative bacterial outer membrane. Annual Review of Microbiology 2007 61 191 214 2-s2.0-35348906348 10.1146/annurev.micro.61.080706.093245 (Pubitemid 350058206)
    • (2007) Annual Review of Microbiology , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 5
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • DOI 10.1126/science.1078973
    • Voulhoux R., Bos M. P., Geurtsen J., Mols M., Tommassen J., Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 2003 299 5604 262 265 2-s2.0-0037428132 10.1126/science.1078973 (Pubitemid 36125214)
    • (2003) Science , vol.299 , Issue.5604 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 6
    • 59449102274 scopus 로고    scopus 로고
    • Iron acquisition functions expressed by the human pathogen Acinetobacter baumannii
    • 2-s2.0-59449102274 10.1007/s10534-008-9202-3
    • Zimbler D. L., Penwell W. F., Gaddy J. A., Menke S. M., Tomaras A. P., Connerly P. L., Actis L. A., Iron acquisition functions expressed by the human pathogen Acinetobacter baumannii. BioMetals 2009 22 1 23 32 2-s2.0-59449102274 10.1007/s10534-008-9202-3
    • (2009) BioMetals , vol.22 , Issue.1 , pp. 23-32
    • Zimbler, D.L.1    Penwell, W.F.2    Gaddy, J.A.3    Menke, S.M.4    Tomaras, A.P.5    Connerly, P.L.6    Actis, L.A.7
  • 7
    • 19044393300 scopus 로고    scopus 로고
    • Monoclonal antibodies against the iron regulated outer membrane proteins of Acinetobacter baumannii are bactericidal
    • 2-s2.0-19044393300
    • Goel V. K., Kapil A., Monoclonal antibodies against the iron regulated outer membrane proteins of Acinetobacter baumannii are bactericidal. BMC Microbiology 2001 1, article 16 2-s2.0-19044393300
    • (2001) BMC Microbiology , vol.116
    • Goel, V.K.1    Kapil, A.2
  • 8
    • 84878084578 scopus 로고    scopus 로고
    • Basic protein structure prediction for the biologist: A review
    • Mihasan M., Basic protein structure prediction for the biologist: a review. Archives of Biological Sciences 2010 62 857 871
    • (2010) Archives of Biological Sciences , vol.62 , pp. 857-871
    • Mihasan, M.1
  • 9
    • 27844505722 scopus 로고    scopus 로고
    • Advances in protein structure prediction and de novo protein design: A review
    • DOI 10.1016/j.ces.2005.04.009, PII S0009250905002988, Biomolecular Engineering
    • Floudas C. A., Fung H. K., McAllister S. R., Mönnigmann M., Rajgaria R., Advances in protein structure prediction and de novo protein design: a review. Chemical Engineering Science 2006 61 3 966 988 2-s2.0-27844505722 10.1016/j.ces.2005.04.009 (Pubitemid 41655853)
    • (2006) Chemical Engineering Science , vol.61 , Issue.3 , pp. 966-988
    • Floudas, C.A.1    Fung, H.K.2    McAllister, S.R.3    Monnigmann, M.4    Rajgaria, R.5
  • 11
    • 33751099863 scopus 로고    scopus 로고
    • Prediction of residues in discontinuous B-cell epitopes using protein 3D structures
    • DOI 10.1110/ps.062405906
    • Andersen P. H., Nielsen M., Lund O., Prediction of residues in discontinuous B-cell epitopes using protein 3D structures. Protein Science 2009 15 11 2558 2567 2-s2.0-33751099863 (Pubitemid 44771693)
    • (2006) Protein Science , vol.15 , Issue.11 , pp. 2558-2567
    • Andersen, P.H.1    Nielsen, M.2    Lund, O.3
  • 12
    • 0030020734 scopus 로고    scopus 로고
    • Topology prediction of membrane proteins
    • Argos P., Persson B., Topology prediction of membrane proteins. Protein Science 1996 5 2 363 371 2-s2.0-0030020734 (Pubitemid 26054293)
    • (1996) Protein Science , vol.5 , Issue.2 , pp. 363-371
    • Persson, B.1    Argos, P.2
  • 13
    • 29144526714 scopus 로고    scopus 로고
    • Protein structure prediction: Inroads to biology
    • DOI 10.1016/j.molcel.2005.12.005, PII S1097276505018472
    • Petrey D., Honig B., Protein structure prediction: inroads to biology. Molecular Cell 2005 20 6 811 819 2-s2.0-29144526714 10.1016/j.molcel.2005.12.005 (Pubitemid 41814871)
    • (2005) Molecular Cell , vol.20 , Issue.6 , pp. 811-819
    • Petrey, D.1    Honig, B.2
  • 14
    • 80052342097 scopus 로고    scopus 로고
    • An in silico DNA vaccine against Listeria monocytogenes
    • 2-s2.0-80052342097 10.1016/j.vaccine.2011.07.040
    • Jahangiri A., Rasooli I., Gargari S. L. M., Owlia P., Rahbar M. R., Amani J., Khalili S., An in silico DNA vaccine against Listeria monocytogenes. Vaccine 2011 29 40 6948 6958 2-s2.0-80052342097 10.1016/j.vaccine.2011.07.040
    • (2011) Vaccine , vol.29 , Issue.40 , pp. 6948-6958
    • Jahangiri, A.1    Rasooli, I.2    Gargari, S.L.M.3    Owlia, P.4    Rahbar, M.R.5    Amani, J.6    Khalili, S.7
  • 15
    • 84859931126 scopus 로고    scopus 로고
    • Precise detection of L monocytogenes hitting its highly conserved region possessing several specific antibody binding sites
    • 2-s2.0-84859931126 10.1016/j.jtbi.2012.04.010
    • Jahangiri A., Rasooli I., Rahbar M. R., Khalili S., Amani J., Zanoos K. A., Precise detection of L. monocytogenes hitting its highly conserved region possessing several specific antibody binding sites. Journal of Theoretical Biology 2012 305 15 23 2-s2.0-84859931126 10.1016/j.jtbi.2012.04.010
    • (2012) Journal of Theoretical Biology , vol.305 , pp. 15-23
    • Jahangiri, A.1    Rasooli, I.2    Rahbar, M.R.3    Khalili, S.4    Amani, J.5    Zanoos, K.A.6
  • 16
    • 77954557401 scopus 로고    scopus 로고
    • In silico analysis of antibody triggering biofilm associated protein in Acinetobacter baumannii
    • 2-s2.0-77954557401 10.1016/j.jtbi.2010.06.014
    • Rahbar M. R., Rasooli I., Gargari S. L. M., Amani J., Fattahian Y., In silico analysis of antibody triggering biofilm associated protein in Acinetobacter baumannii. Journal of Theoretical Biology 2010 266 2 275 290 2-s2.0-77954557401 10.1016/j.jtbi.2010.06.014
    • (2010) Journal of Theoretical Biology , vol.266 , Issue.2 , pp. 275-290
    • Rahbar, M.R.1    Rasooli, I.2    Gargari, S.L.M.3    Amani, J.4    Fattahian, Y.5
  • 17
    • 81055138205 scopus 로고    scopus 로고
    • A potential in silico antibody-antigen based diagnostic test for precise identification of Acinetobacter baumannii
    • 2-s2.0-81055138205 10.1016/j.jtbi.2011.10.026
    • Rahbar M. R., Rasooli I., Gargari S. L. M., Sandstrom G., Amani J., Fattahian Y., Jahangiri A., Jalali M., A potential in silico antibody-antigen based diagnostic test for precise identification of Acinetobacter baumannii. Journal of Theoretical Biology 2012 294 29 39 2-s2.0-81055138205 10.1016/j.jtbi.2011.10.026
    • (2012) Journal of Theoretical Biology , vol.294 , pp. 29-39
    • Rahbar, M.R.1    Rasooli, I.2    Gargari, S.L.M.3    Sandstrom, G.4    Amani, J.5    Fattahian, Y.6    Jahangiri, A.7    Jalali, M.8
  • 18
    • 33744791187 scopus 로고    scopus 로고
    • Structure of TonB in complex with FhuA, E coli outer membrane receptor
    • DOI 10.1126/science.1128057
    • Pawelek P. D., Croteau N., Ng-Thow-Hing C., Khursigara C. M., Moiseeva N., Allaire M., Coulton J. W., Structure of TonB in complex with FhuA, E. coli outer membrane receptor. Science 2006 312 5778 1399 1402 2-s2.0-33744791187 10.1126/science.1128057 (Pubitemid 43839555)
    • (2006) Science , vol.312 , Issue.5778 , pp. 1399-1402
    • Pawelek, P.D.1    Croteau, N.2    Ng-Thow-Hing, C.3    Khursigara, C.M.4    Moiseeva, N.5    Allaire, M.6    Coulton, J.W.7
  • 19
    • 0033990053 scopus 로고    scopus 로고
    • The NCBI. Publicly available tools and resources on the Web
    • 2-s2.0-0033990053
    • Jenuth J. P., The NCBI. Publicly available tools and resources on the Web. Methods in Molecular Biology 2000 132 301 312 2-s2.0-0033990053
    • (2000) Methods in Molecular Biology , vol.132 , pp. 301-312
    • Jenuth, J.P.1
  • 20
    • 0029933671 scopus 로고    scopus 로고
    • Effective protein sequence comparison
    • DOI 10.1016/S0076-6879(96)66017-0
    • Pearson W. R., Effective protein sequence comparison. Methods in Enzymology 1996 266 227 258 2-s2.0-0029933671 (Pubitemid 26165871)
    • (1996) Methods in Enzymology , vol.266 , pp. 227-258
    • Pearson, W.R.1
  • 21
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity search
    • DOI 10.1038/ng0393-266
    • Gish W., States D. J., Identification of protein coding regions by database similarity search. Nature Genetics 1993 3 3 266 272 2-s2.0-0027399530 10.1038/ng0393-266 (Pubitemid 23096565)
    • (1993) Nature Genetics , vol.3 , Issue.3 , pp. 266-272
    • Gish, W.1    States, D.J.2
  • 22
    • 33645734536 scopus 로고    scopus 로고
    • Protein structure modeling in the proteomics era
    • DOI 10.1586/14789450.1.1.97
    • Fiser A., Protein structure modeling in the proteomics era. Expert Review of Proteomics 2004 1 1 97 110 2-s2.0-33645734536 10.1586/14789450.1.1.97 (Pubitemid 43826433)
    • (2004) Expert Review of Proteomics , vol.1 , Issue.1 , pp. 97-110
    • Fiser, A.1
  • 23
    • 23144440940 scopus 로고    scopus 로고
    • PRALINE: A multiple sequence alignment toolbox that integrates homology-extended and secondary structure information
    • DOI 10.1093/nar/gki390
    • Simossis V. A., Heringa J., PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information. Nucleic Acids Research 2005 33 2 W289 W294 2-s2.0-23144440940 10.1093/nar/gki390 (Pubitemid 44529928)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Simossis, V.A.1    Heringa, J.2
  • 24
    • 3242883431 scopus 로고    scopus 로고
    • PRED-TMBB: A web server for predicting the topology of β-barrel outer membrane proteins
    • DOI 10.1093/nar/gkh417
    • Bagos P. G., Liakopoulos T. D., Spyropoulos I. C., Hamodrakas S. J., PRED-TMBB: a web server for predicting the topology of β -barrel outer membrane proteins. Nucleic Acids Research 2004 32 W400 W404 2-s2.0-3242883431 10.1093/nar/gkh417 (Pubitemid 38997367)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Bagos, P.G.1    Liakopoulos, T.D.2    Spyropoulos, I.C.3    Hamodrakas, S.J.4
  • 25
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C., Deleage G., SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Computer Applications in the Biosciences 1995 11 6 681 684 2-s2.0-0029595442 (Pubitemid 26032758)
    • (1995) Computer Applications in the Biosciences , vol.11 , Issue.6 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 26
    • 33747825121 scopus 로고    scopus 로고
    • 2: Protein structure prediction server
    • DOI 10.1093/nar/gkl187
    • Chen C., Hwang J., Yang J., (PS)2: protein structure prediction server. Nucleic Acids Research 2006 34 W152 W157 2-s2.0-33747825121 10.1093/nar/gkl187 (Pubitemid 44529754)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS.
    • Chen, C.-C.1    Hwang, J.-K.2    Yang, J.-M.3
  • 27
    • 0036740806 scopus 로고    scopus 로고
    • ESyPred3D: Prediction of proteins 3D structures
    • 2-s2.0-0036740806
    • Lambert C., Léonard N., de Bolle X., Depiereux E., ESyPred3D: prediction of proteins 3D structures. Bioinformatics 2002 18 9 1250 1256 2-s2.0-0036740806
    • (2002) Bioinformatics , vol.18 , Issue.9 , pp. 1250-1256
    • Lambert, C.1    Léonard, N.2    De Bolle, X.3    Depiereux, E.4
  • 28
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • DOI 10.1002/prot.1168
    • Bates P. A., Kelley L. A., MacCallum R. M., Sternberg M. J. E., Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins 2001 45 5 39 46 2-s2.0-0035747672 10.1002/prot.1168 (Pubitemid 34113166)
    • (2001) Proteins: Structure, Function and Genetics , vol.45 , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.E.4
  • 29
    • 0036172167 scopus 로고    scopus 로고
    • Geno3D: Automatic comparative molecular modelling of protein
    • Combet C., Jambon M., Deléage G., Geourjon C., Geno3D: automatic comparative molecular modelling of protein. Bioinformatics 2002 18 1 213 214 2-s2.0-0036172167 (Pubitemid 34145058)
    • (2002) Bioinformatics , vol.18 , Issue.1 , pp. 213-214
    • Combet, C.1    Jambon, M.2    Deleage, G.3    Geourjon, C.4
  • 30
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • DOI 10.1186/1471-2105-9-40
    • Zhang Y., I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 2008 9, article 40 2-s2.0-39449115394 10.1186/1471-2105-9-40 (Pubitemid 351267364)
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 31
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • 2-s2.0-77954065271
    • Roy A., Kucukural A., Zhang Y., I-TASSER: a unified platform for automated protein structure and function prediction. Nature Protocols 2010 5 4 725 738 2-s2.0-77954065271
    • (2010) Nature Protocols , vol.5 , Issue.4 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 32
    • 79251470739 scopus 로고    scopus 로고
    • Proteins: Sequence to structure and function - Current status
    • 2-s2.0-79251470739 10.2174/138920310794109094
    • Shenoy S. R., Jayaram B., Proteins: sequence to structure and function-current status. Current Protein and Peptide Science 2010 11 7 498 514 2-s2.0-79251470739 10.2174/138920310794109094
    • (2010) Current Protein and Peptide Science , vol.11 , Issue.7 , pp. 498-514
    • Shenoy, S.R.1    Jayaram, B.2
  • 33
    • 77950518894 scopus 로고    scopus 로고
    • Protein folding requires crowd control in a simulated cell
    • 2-s2.0-77950518894 10.1016/j.jmb.2010.01.074
    • Jefferys B. R., Kelley L. A., Sternberg M. J. E., Protein folding requires crowd control in a simulated cell. Journal of Molecular Biology 2010 397 5 1329 1338 2-s2.0-77950518894 10.1016/j.jmb.2010.01.074
    • (2010) Journal of Molecular Biology , vol.397 , Issue.5 , pp. 1329-1338
    • Jefferys, B.R.1    Kelley, L.A.2    Sternberg, M.J.E.3
  • 34
    • 34250851687 scopus 로고    scopus 로고
    • LOMETS: A local meta-threading-server for protein structure prediction
    • DOI 10.1093/nar/gkm251
    • Wu S., Zhang Y., LOMETS: a local meta-threading-server for protein structure prediction. Nucleic Acids Research 2007 35 10 3375 3382 2-s2.0-34250851687 10.1093/nar/gkm251 (Pubitemid 47073600)
    • (2007) Nucleic Acids Research , vol.35 , Issue.10 , pp. 3375-3382
    • Wu, S.1    Zhang, Y.2
  • 36
    • 0041620407 scopus 로고    scopus 로고
    • VADAR: A web server for quantitative evaluation of protein structure quality
    • DOI 10.1093/nar/gkg565
    • Willard L., Ranjan A., Zhang H., Monzavi H., Boyko R. F., Sykes B. D., Wishart D. S., VADAR: a web server for quantitative evaluation of protein structure quality. Nucleic Acids Research 2003 31 13 3316 3319 2-s2.0-0041620407 10.1093/nar/gkg565 (Pubitemid 37442148)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3316-3319
    • Willard, L.1    Ranjan, A.2    Zhang, H.3    Monzavi, H.4    Boyko, R.F.5    Sykes, B.D.6    Wishart, D.S.7
  • 37
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • 2-s2.0-34547566446 10.1093/nar/gkm290
    • Wiederstein M., Sippl M. J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Research 2007 35 W407 W410 2-s2.0-34547566446 10.1093/nar/gkm290
    • (2007) Nucleic Acids Research , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 38
    • 40549141792 scopus 로고    scopus 로고
    • QMEAN: A comprehensive scoring function for model quality assessment
    • DOI 10.1002/prot.21715
    • Benkert P., Tosatto S. C. E., Schomburg D., QMEAN: a comprehensive scoring function for model quality assessment. Proteins 2008 71 1 261 277 2-s2.0-40549141792 10.1002/prot.21715 (Pubitemid 351358609)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.1 , pp. 261-277
    • Benkert, P.1    Tosatto, S.C.E.2    Schomburg, D.3
  • 39
    • 81255123286 scopus 로고    scopus 로고
    • Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization
    • 2-s2.0-81255123286 10.1016/j.bpj.2011.10.024
    • Xu D., Zhang Y., Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization. Biophysical Journal 2011 101 10 2525 2534 2-s2.0-81255123286 10.1016/j.bpj.2011.10.024
    • (2011) Biophysical Journal , vol.101 , Issue.10 , pp. 2525-2534
    • Xu, D.1    Zhang, Y.2
  • 40
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • 2-s2.0-0033824470
    • Holm L., Park J., DaliLite workbench for protein structure comparison. Bioinformatics 2000 16 6 566 567 2-s2.0-0033824470
    • (2000) Bioinformatics , vol.16 , Issue.6 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 41
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • 2-s2.0-77954288774 10.1093/nar/gkq366
    • Holm L., Rosenström P., Dali server: conservation mapping in 3D. Nucleic Acids Research 2010 38 2 W545 W549 2-s2.0-77954288774 10.1093/nar/gkq366
    • (2010) Nucleic Acids Research , vol.38 , Issue.2
    • Holm, L.1    Rosenström, P.2
  • 42
    • 84864460609 scopus 로고    scopus 로고
    • COFACTOR: An accurate comparative algorithm for structure-based protein function annotation
    • Roy A., Yang J., Zhang Y., COFACTOR: an accurate comparative algorithm for structure-based protein function annotation. Nucleic Acids Research 2012 40 W471 W477
    • (2012) Nucleic Acids Research , vol.40
    • Roy, A.1    Yang, J.2    Zhang, Y.3
  • 43
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: A server for predicting protein function from 3D structure
    • DOI 10.1093/nar/gki414
    • Laskowski R. A., Watson J. D., Thornton J. M., ProFunc: a server for predicting protein function from 3D structure. Nucleic Acids Research 2005 33 2 W89 W93 2-s2.0-22544441094 10.1093/nar/gki414 (Pubitemid 44529886)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 44
    • 80054736579 scopus 로고    scopus 로고
    • Pyochelin enantiomers and their outer-membrane siderophore transporters in fluorescent pseudomonads: Structural bases for unique enantiospecific recognition
    • 2-s2.0-80054736579 10.1021/ja205504z
    • Brillet K., Reimmann C., Mislin G. L. A., Noël S., Rognan D., Schalk I. J., Cobessi D., Pyochelin enantiomers and their outer-membrane siderophore transporters in fluorescent pseudomonads: structural bases for unique enantiospecific recognition. Journal of the American Chemical Society 2011 133 41 16503 16509 2-s2.0-80054736579 10.1021/ja205504z
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.41 , pp. 16503-16509
    • Brillet, K.1    Reimmann, C.2    Mislin, G.L.A.3    Noël, S.4    Rognan, D.5    Schalk, I.J.6    Cobessi, D.7
  • 45
    • 0029913746 scopus 로고    scopus 로고
    • Acinetobacter spp as nosocomial pathogens: Microbiological, clinical, and epidemiological features
    • Bergogne-Bérézin E., Towner K. J., Acinetobacter spp. as nosocomial pathogens: microbiological, clinical, and epidemiological features. Clinical Microbiology Reviews 1996 9 2 148 165 2-s2.0-0029913746 (Pubitemid 26123943)
    • (1996) Clinical Microbiology Reviews , vol.9 , Issue.2 , pp. 148-165
    • Bergogne-Berezin, E.1    Towner, K.J.2
  • 47
    • 14144255323 scopus 로고    scopus 로고
    • The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 A resolution
    • DOI 10.1016/j.jmb.2005.01.021
    • Cobessi D., Celia H., Folschweiller N., Schalk I. J., Abdallah M. A., Pattus F., The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 A resolution. Journal of Molecular Biology 2005 347 1 121 134 2-s2.0-14144255323 10.1016/j.jmb.2005.01.021 (Pubitemid 40283633)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.1 , pp. 121-134
    • Cobessi, D.1    Celia, H.2    Folschweiller, N.3    Schalk, I.J.4    Abdallah, M.A.5    Pattus, F.6
  • 48
    • 20844443081 scopus 로고    scopus 로고
    • Homology modelling of transferrin-binding protein A from Neisseria meningitidis
    • DOI 10.1093/protein/gzi024
    • Oakhill J. S., Sutton B. J., Gorringe A. R., Evans R. W., Homology modelling of transferrin-binding protein A from Neisseria meningitidis. Protein Engineering, Design and Selection 2005 18 5 221 228 2-s2.0-20844443081 10.1093/protein/gzi024 (Pubitemid 40863426)
    • (2005) Protein Engineering, Design and Selection , vol.18 , Issue.5 , pp. 221-228
    • Oakhill, J.S.1    Sutton, B.J.2    Gorringe, A.R.3    Evans, R.W.4
  • 49
    • 13244259253 scopus 로고    scopus 로고
    • Evaluation of methods for predicting the topology of β-barrel outer membrane proteins and a consensus prediction method
    • DOI 10.1186/1471-2105-6-7
    • Bagos P. G., Liakopoulos T. D., Hamodrakas S. J., Evaluation of methods for predicting the topology of β -barrel outer membrane proteins and a consensus prediction method. BMC Bioinformatics 2005 6, article 7 2-s2.0-13244259253 10.1186/1471-2105-6-7 (Pubitemid 40195448)
    • (2005) BMC Bioinformatics , vol.6 , pp. 7
    • Bagos, P.G.1    Liakopoulos, T.D.2    Hamodrakas, S.J.3
  • 50
    • 50049089034 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake
    • 2-s2.0-50049089034 10.1016/j.bbamem.2007.07.026
    • Krewulak K. D., Vogel H. J., Structural biology of bacterial iron uptake. Biochimica et Biophysica Acta 2008 1778 9 1781 1804 2-s2.0-50049089034 10.1016/j.bbamem.2007.07.026
    • (2008) Biochimica et Biophysica Acta , vol.1778 , Issue.9 , pp. 1781-1804
    • Krewulak, K.D.1    Vogel, H.J.2
  • 51
    • 79953302147 scopus 로고    scopus 로고
    • Recent insights into iron import by bacteria
    • 2-s2.0-79953302147 10.1016/j.cbpa.2011.01.005
    • Braun V., Hantke K., Recent insights into iron import by bacteria. Current Opinion in Chemical Biology 2011 15 2 328 334 2-s2.0-79953302147 10.1016/j.cbpa.2011.01.005
    • (2011) Current Opinion in Chemical Biology , vol.15 , Issue.2 , pp. 328-334
    • Braun, V.1    Hantke, K.2
  • 53
    • 34250851687 scopus 로고    scopus 로고
    • LOMETS: A local meta-threading-server for protein structure prediction
    • DOI 10.1093/nar/gkm251
    • Wu S., Zhang Y., LOMETS: a local meta-threading-server for protein structure prediction. Nucleic Acids Research 2007 35 10 3375 3382 2-s2.0-34250851687 10.1093/nar/gkm251 (Pubitemid 47073600)
    • (2007) Nucleic Acids Research , vol.35 , Issue.10 , pp. 3375-3382
    • Wu, S.1    Zhang, Y.2
  • 54
    • 0242292013 scopus 로고    scopus 로고
    • From protein structure to biochemical function?
    • DOI 10.1023/A:1026127927612
    • Laskowski R. A., Watson J. D., Thornton J. M., From protein structure to biochemical function? Journal of Structural and Functional Genomics 2003 4 2-3 167 177 2-s2.0-0242292013 10.1023/A:1026127927612 (Pubitemid 37356271)
    • (2003) Journal of Structural and Functional Genomics , vol.4 , Issue.2-3 , pp. 167-177
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 55
    • 0347479229 scopus 로고    scopus 로고
    • Molecular Basis of Bacterial Outer Membrane Permeability Revisited
    • DOI 10.1128/MMBR.67.4.593-656.2003
    • Nikaido H., Molecular basis of bacterial outer membrane permeability revisited. Microbiology and Molecular Biology Reviews 2003 67 4 593 656 2-s2.0-0347479229 10.1128/MMBR.67.4.593-656.2003 (Pubitemid 37549772)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.4 , pp. 593-656
    • Nikaido, H.1
  • 56
    • 84881228096 scopus 로고    scopus 로고
    • Immune response variations to Salmonella enterica serovar Typhi recombinant porin proteins in mice
    • Toobak H., Rasooli I., Talei D., Jahangiri A., Owlia P., Astaneh S. D. A., Immune response variations to Salmonella enterica serovar Typhi recombinant porin proteins in mice. Biologicals 2013 41 4 224 230
    • (2013) Biologicals , vol.41 , Issue.4 , pp. 224-230
    • Toobak, H.1    Rasooli, I.2    Talei, D.3    Jahangiri, A.4    Owlia, P.5    Astaneh, S.D.A.6


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