메뉴 건너뛰기




Volumn 10, Issue 4, 2011, Pages 1657-1666

Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen staphylococcus aureus under iron-limited conditions

Author keywords

14N15N metabolic labeling; biotinylation; cell surface proteins; iron limitation; mass spectrometry; Staphylococcus aureus; trypsin shaving

Indexed keywords

CELL MEMBRANE PROTEIN; CYTOPLASM PROTEIN; IRON; LIPOPROTEIN; MEMBRANE PROTEIN; NITROGEN; NITROGEN 15; TRYPSIN;

EID: 79953718512     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr1009838     Document Type: Article
Times cited : (57)

References (66)
  • 2
    • 35349026669 scopus 로고    scopus 로고
    • Staphylococcus aureus virulence factors associated with infected skin lesions: Influence on the local immune response
    • DOI 10.1001/archderm.143.10.1259
    • Mertz, P. M.; Cardenas, T. C.; Snyder, R. V.; Kinney, M. A.; Davis, S. C.; Plano, L. R. Staphylococcus aureus virulence factors associated with infected skin lesions: influence on the local immune response Arch. Dermatol. 2007, 143, 1259-63 (Pubitemid 47607676)
    • (2007) Archives of Dermatology , vol.143 , Issue.10 , pp. 1259-1263
    • Mertz, P.M.1    Cardenas, T.C.P.2    Snyder, R.V.3    Kinney, M.A.4    Davis, S.C.5    Plano, L.R.W.6
  • 3
    • 37549045236 scopus 로고    scopus 로고
    • Community-associated MRSA (CA-MRSA): An emerging pathogen in infective endocarditis
    • Millar, B. C.; Prendergast, B. D.; Moore, J. E. Community-associated MRSA (CA-MRSA): an emerging pathogen in infective endocarditis J. Antimicrob. Chemother. 2008, 61, 1-7
    • (2008) J. Antimicrob. Chemother. , vol.61 , pp. 1-7
    • Millar, B.C.1    Prendergast, B.D.2    Moore, J.E.3
  • 5
    • 0019462948 scopus 로고
    • Identification and characterization of an exotoxin from Staphylococcus aureus associated with toxic-shock syndrome
    • Schlievert, P. M.; Shands, K. N.; Dan, B. B.; Schmid, G. P.; Nishimura, R. D. Identification and characterization of an exotoxin from Staphylococcus aureus associated with toxic-shock syndrome J. Infect. Dis. 1981, 143, 509-16 (Pubitemid 11111260)
    • (1981) Journal of Infectious Diseases , vol.143 , Issue.4 , pp. 509-516
    • Schlievert, P.M.1    Shands, K.N.2    Dan, B.B.3
  • 6
    • 34548523299 scopus 로고    scopus 로고
    • Severe sepsis attributable to community-associated methicillin-resistant Staphylococcus aureus: An emerging fatal problem
    • Castaldo, E. T.; Yang, E. Y. Severe sepsis attributable to community-associated methicillin-resistant Staphylococcus aureus: an emerging fatal problem Am. Surg. 2007, 73, 684-7 (Pubitemid 351396623)
    • (2007) American Surgeon , vol.73 , Issue.7 , pp. 684-687
    • Castaldo, E.T.1    Yang, E.Y.2
  • 7
    • 79953705318 scopus 로고    scopus 로고
    • discussion: 687-8
    • discussion: 687-8.
  • 8
    • 1642283048 scopus 로고    scopus 로고
    • Iron-regulated surface determinants (Isd) of Staphylococcus aureus: Stealing iron from heme
    • DOI 10.1016/j.micinf.2003.12.008, PII S1286457904000309
    • Skaar, E. P.; Schneewind, O. Iron-regulated surface determinants (Isd) of Staphylococcus aureus: stealing iron from heme Microbes Infect. 2004, 6, 390-7 (Pubitemid 38393820)
    • (2004) Microbes and Infection , vol.6 , Issue.4 , pp. 390-397
    • Skaar, E.P.1    Schneewind, O.2
  • 9
    • 33646907917 scopus 로고    scopus 로고
    • Iron acquisition and transport in Staphylococcus aureus
    • DOI 10.1007/s10534-005-4863-7, Special Issue on Microbial Iron Transport, Storage and Metabolism
    • Maresso, A. W.; Schneewind, O. Iron acquisition and transport in Staphylococcus aureus Biometals 2006, 19, 193-203 (Pubitemid 43794828)
    • (2006) BioMetals , vol.19 , Issue.2 , pp. 193-203
    • Maresso, A.W.1    Schneewind, O.2
  • 11
    • 66549117376 scopus 로고    scopus 로고
    • Iron-regulated surface determinant protein A mediates adhesion of Staphylococcus aureus to human corneocyte envelope proteins
    • Clarke, S. R.; Andre, G.; Walsh, E. J.; Dufrene, Y. F.; Foster, T. J.; Foster, S. J. Iron-regulated surface determinant protein A mediates adhesion of Staphylococcus aureus to human corneocyte envelope proteins Infect. Immun. 2009, 77, 2408-16
    • (2009) Infect. Immun. , vol.77 , pp. 2408-16
    • Clarke, S.R.1    Andre, G.2    Walsh, E.J.3    Dufrene, Y.F.4    Foster, T.J.5    Foster, S.J.6
  • 12
    • 28444440285 scopus 로고    scopus 로고
    • Proteomics-based consensus prediction of protein retention in a bacterial membrane
    • DOI 10.1002/pmic.200402080
    • Tjalsma, H.; van Dijl, J. M. Proteomics-based consensus prediction of protein retention in a bacterial membrane Proteomics 2005, 5, 4472-82 (Pubitemid 41739924)
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4472-4482
    • Tjalsma, H.1    Van Dijl, J.M.2
  • 13
    • 0027992980 scopus 로고
    • Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in Gram-positive bacteria
    • DOI 10.1111/j.1365-2958.1994.tb01271.x
    • Navarre, W. W.; Schneewind, O. Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria Mol. Microbiol. 1994, 14, 115-21 (Pubitemid 24312824)
    • (1994) Molecular Microbiology , vol.14 , Issue.1 , pp. 115-121
    • Navarre, W.W.1    Schneewind, O.2
  • 14
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S. K.; Liu, G.; Ton-That, H.; Schneewind, O. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall Science 1999, 285, 760-3
    • (1999) Science , vol.285 , pp. 760-3
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 20
    • 42049098165 scopus 로고    scopus 로고
    • Shedding & shaving: Disclosure of proteomic expressions on a bacterial face
    • DOI 10.1002/pmic.200700550
    • Tjalsma, H.; Lambooy, L.; Hermans, P. W.; Swinkels, D. W. Shedding & shaving: disclosure of proteomic expressions on a bacterial face Proteomics 2008, 8, 1415-28 (Pubitemid 351518552)
    • (2008) Proteomics , vol.8 , Issue.7 , pp. 1415-1428
    • Tjalsma, H.1    Lambooy, L.2    Hermans, P.W.3    Swinkels, D.W.4
  • 21
    • 77952372626 scopus 로고    scopus 로고
    • Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control
    • Solis, N.; Larsen, M. R.; Cordwell, S. J. Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control Proteomics 2010, 10, 2037-49
    • (2010) Proteomics , vol.10 , pp. 2037-49
    • Solis, N.1    Larsen, M.R.2    Cordwell, S.J.3
  • 25
    • 77949797684 scopus 로고    scopus 로고
    • Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach
    • Hempel, K.; Pane-Farre, J.; Otto, A.; Sievers, S.; Hecker, M.; Becher, D. Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach J. Proteome Res. 2010, 9, 1579-90
    • (2010) J. Proteome Res. , vol.9 , pp. 1579-90
    • Hempel, K.1    Pane-Farre, J.2    Otto, A.3    Sievers, S.4    Hecker, M.5    Becher, D.6
  • 29
    • 0018608677 scopus 로고
    • Genetics of staphylococcal enterotoxin B in methicillin-resistant isolates of Staphylococcus aureus
    • Shafer, W. M.; Iandolo, J. J. Genetics of staphylococcal enterotoxin B in methicillin-resistant isolates of Staphylococcus aureus Infect. Immun. 1979, 25, 902-11 (Pubitemid 9251893)
    • (1979) Infection and Immunity , vol.25 , Issue.3 , pp. 902-911
    • Shafer, W.M.1    Landolo, J.J.2
  • 30
    • 0346122950 scopus 로고    scopus 로고
    • A Correlation Algorithm for the Automated Quantitative Analysis of Shotgun Proteomics Data
    • DOI 10.1021/ac034790h
    • MacCoss, M. J.; Wu, C. C.; Liu, H.; Sadygov, R.; Yates, J. R., 3rd A correlation algorithm for the automated quantitative analysis of shotgun proteomics data Anal. Chem. 2003, 75, 6912-21 (Pubitemid 37523592)
    • (2003) Analytical Chemistry , vol.75 , Issue.24 , pp. 6912-6921
    • MacCoss, M.J.1    Wu, C.C.2    Liu, H.3    Sadygov, R.4    Yates III, J.R.5
  • 31
    • 5644280025 scopus 로고    scopus 로고
    • B in growth phase dependent regulation of virulence factors in Staphylococcus aureus
    • DOI 10.1002/pmic.200400937
    • Ziebandt, A. K.; Becher, D.; Ohlsen, K.; Hacker, J.; Hecker, M.; Engelmann, S. The influence of agr and sigmaB in growth phase dependent regulation of virulence factors in Staphylococcus aureus Proteomics 2004, 4, 3034-47 (Pubitemid 39372386)
    • (2004) Proteomics , vol.4 , Issue.10 , pp. 3034-3047
    • Ziebandt, A.-K.1    Becher, D.2    Ohlsen, K.3    Hacker, J.4    Hecker, M.5    Engelmann, S.6
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227, 680-5
    • (1970) Nature , vol.227 , pp. 680-5
    • Laemmli, U.K.1
  • 34
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L.; McDonald, W. H.; Yates, J. R., 3rd DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics J. Proteome Res. 2002, 1, 21-6
    • (2002) J. Proteome Res. , vol.1 , pp. 21-6
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 35
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 2001, 305, 567-80 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 36
    • 0031603460 scopus 로고    scopus 로고
    • Prediction of signal peptides and signal anchors by a hidden Markov model
    • Nielsen, H.; Krogh, A. Prediction of signal peptides and signal anchors by a hidden Markov model Proc. Int. Conf. Intell. Syst. Mol. Biol. 1998, 6, 122-30
    • (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.6 , pp. 122-30
    • Nielsen, H.1    Krogh, A.2
  • 37
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Bendtsen, J. D.; Nielsen, H.; von Heijne, G.; Brunak, S. Improved prediction of signal peptides: SignalP 3.0 J. Mol. Biol. 2004, 340, 783-95 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 38
    • 0036091972 scopus 로고    scopus 로고
    • DOLOP - Database of bacterial lipoproteins
    • Madan Babu, M.; Sankaran, K. DOLOP - database of bacterial lipoproteins Bioinformatics 2002, 18, 641-3 (Pubitemid 34521055)
    • (2002) Bioinformatics , vol.18 , Issue.4 , pp. 641-643
    • Babu, M.M.1    Sankaran, K.2
  • 39
    • 33750980713 scopus 로고    scopus 로고
    • Augur - A computational pipeline for whole genome microbial surface protein prediction and classification
    • DOI 10.1093/bioinformatics/btl466
    • Billion, A.; Ghai, R.; Chakraborty, T.; Hain, T. Augur - a computational pipeline for whole genome microbial surface protein prediction and classification Bioinformatics 2006, 22, 2819-20 (Pubitemid 44742404)
    • (2006) Bioinformatics , vol.22 , Issue.22 , pp. 2819-2820
    • Billion, A.1    Ghai, R.2    Chakraborty, T.3    Hain, T.4
  • 40
    • 33748927643 scopus 로고    scopus 로고
    • Surface Adhesins of Staphylococcus aureus
    • DOI 10.1016/S0065-2911(06)51004-5, PII S0065291106510045
    • Clarke, S. R.; Foster, S. J. Surface adhesins of Staphylococcus aureus Adv. Microb. Physiol. 2006, 51, 187-224 (Pubitemid 44436456)
    • (2006) Advances in Microbial Physiology , vol.51 , Issue.SUPPL. , pp. 187-224
    • Clarke, S.R.1    Foster, S.J.2
  • 41
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K.; Horton, P. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization Trends Biochem. Sci. 1999, 24, 34-6
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-6
    • Nakai, K.1    Horton, P.2
  • 42
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • DOI 10.1038/nmeth.1195, PII NMETH.1195
    • Park, S. K.; Venable, J. D.; Xu, T.; Yates, J. R., 3rd A quantitative analysis software tool for mass spectrometry-based proteomics Nat. Methods 2008, 5, 319-22 (Pubitemid 351459367)
    • (2008) Nature Methods , vol.5 , Issue.4 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates III, J.R.4
  • 44
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • DOI 10.1016/S1369-5274(03)00039-0
    • Kiley, P. J.; Beinert, H. The role of Fe-S proteins in sensing and regulation in bacteria Curr. Opin. Microbiol. 2003, 6, 181-5 (Pubitemid 36628663)
    • (2003) Current Opinion in Microbiology , vol.6 , Issue.2 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 45
    • 50249172221 scopus 로고    scopus 로고
    • Complementary analysis of the vegetative membrane proteome of the human pathogen Staphylococcus aureus
    • Wolff, S.; Hahne, H.; Hecker, M.; Becher, D. Complementary analysis of the vegetative membrane proteome of the human pathogen Staphylococcus aureus Mol. Cell. Proteomics 2008, 7, 1460-8
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1460-8
    • Wolff, S.1    Hahne, H.2    Hecker, M.3    Becher, D.4
  • 49
    • 34047266670 scopus 로고    scopus 로고
    • Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection
    • DOI 10.1111/j.1462-5822.2006.00858.x
    • Burlak, C.; Hammer, C. H.; Robinson, M. A.; Whitney, A. R.; McGavin, M. J.; Kreiswirth, B. N.; Deleo, F. R. Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection Cell Microbiol. 2007, 9, 1172-90 (Pubitemid 46547137)
    • (2007) Cellular Microbiology , vol.9 , Issue.5 , pp. 1172-1190
    • Burlak, C.1    Hammer, C.H.2    Robinson, M.-A.3    Whitney, A.R.4    Mcgavin, M.J.5    Kreiswirth, B.N.6    Deleo, F.R.7
  • 50
    • 48149085307 scopus 로고    scopus 로고
    • Relative quantitative comparisons of the extracellular protein profiles of Staphylococcus aureus UAMS-1 and its sarA, agr, and sarA agr regulatory mutants using one-dimensional polyacrylamide gel electrophoresis and nanocapillary liquid chromatography coupled with tandem mass spectrometry
    • Jones, R. C.; Deck, J.; Edmondson, R. D.; Hart, M. E. Relative quantitative comparisons of the extracellular protein profiles of Staphylococcus aureus UAMS-1 and its sarA, agr, and sarA agr regulatory mutants using one-dimensional polyacrylamide gel electrophoresis and nanocapillary liquid chromatography coupled with tandem mass spectrometry J. Bacteriol. 2008, 190, 5265-78
    • (2008) J. Bacteriol. , vol.190 , pp. 5265-78
    • Jones, R.C.1    Deck, J.2    Edmondson, R.D.3    Hart, M.E.4
  • 51
    • 77956509713 scopus 로고    scopus 로고
    • Comprehensive characterization of methicillin-resistant Staphylococcus aureus subsp. aureus COL secretome by two-dimensional liquid chromatography and mass spectrometry
    • Ravipaty, S.; Reilly, J. P. Comprehensive characterization of methicillin-resistant Staphylococcus aureus subsp. aureus COL secretome by two-dimensional liquid chromatography and mass spectrometry Mol. Cell. Proteomics 2010, 9, 1898-919
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1898-919
    • Ravipaty, S.1    Reilly, J.P.2
  • 52
    • 33746385346 scopus 로고    scopus 로고
    • Transcriptional modulation of some Staphylococcus aureus iron-regulated genes during growth in vitro and in a tissue cage model in vivo
    • DOI 10.1016/j.micinf.2006.01.022, PII S1286457906001092
    • Allard, M.; Moisan, H.; Brouillette, E.; Gervais, A. L.; Jacques, M.; Lacasse, P.; Diarra, M. S.; Malouin, F. Transcriptional modulation of some Staphylococcus aureus iron-regulated genes during growth in vitro and in a tissue cage model in vivo Microbes Infect. 2006, 8, 1679-90 (Pubitemid 44128871)
    • (2006) Microbes and Infection , vol.8 , Issue.7 , pp. 1679-1690
    • Allard, M.1    Moisan, H.2    Brouillette, E.3    Gervais, A.L.4    Jacques, M.5    Lacasse, P.6    Diarra, M.S.7    Malouin, F.8
  • 53
    • 67449138548 scopus 로고    scopus 로고
    • Lipoproteins in Staphylococcus aureus mediate inflammation by TLR2 and iron-dependent growth in vivo
    • Schmaler, M.; Jann, N. J.; Ferracin, F.; Landolt, L. Z.; Biswas, L.; Gotz, F.; Landmann, R. Lipoproteins in Staphylococcus aureus mediate inflammation by TLR2 and iron-dependent growth in vivo J. Immunol. 2009, 182, 7110-8
    • (2009) J. Immunol. , vol.182 , pp. 7110-8
    • Schmaler, M.1    Jann, N.J.2    Ferracin, F.3    Landolt, L.Z.4    Biswas, L.5    Gotz, F.6    Landmann, R.7
  • 54
    • 0026686089 scopus 로고
    • Cloning of the outer membrane high-affinity Fe(III)-pyochelin receptor of Pseudomonas aeruginosa
    • Ankenbauer, R. G. Cloning of the outer membrane high-affinity Fe(III)-pyochelin receptor of Pseudomonas aeruginosa J. Bacteriol. 1992, 174, 4401-9
    • (1992) J. Bacteriol. , vol.174 , pp. 4401-9
    • Ankenbauer, R.G.1
  • 55
    • 0029852317 scopus 로고    scopus 로고
    • Adhesion of Pseudomonas aeruginosa to respiratory mucins and expression of mucin-binding proteins are increased by limiting iron during growth
    • Scharfman, A.; Kroczynski, H.; Carnoy, C.; Van Brussel, E.; Lamblin, G.; Ramphal, R.; Roussel, P. Adhesion of Pseudomonas aeruginosa to respiratory mucins and expression of mucin-binding proteins are increased by limiting iron during growth Infect. Immun. 1996, 64, 5417-20 (Pubitemid 26404014)
    • (1996) Infection and Immunity , vol.64 , Issue.12 , pp. 5417-5420
    • Scharfman, A.1    Kroczynski, H.2    Carnoy, C.3    Van Brussel, E.4    Lamblin, G.5    Ramphal, R.6    Roussel, P.7
  • 56
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilis fur regulon and the iron starvation stimulon
    • DOI 10.1046/j.1365-2958.2002.03113.x
    • Baichoo, N.; Wang, T.; Ye, R.; Helmann, J. D. Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon Mol. Microbiol. 2002, 45, 1613-29 (Pubitemid 35231978)
    • (2002) Molecular Microbiology , vol.45 , Issue.6 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 60
    • 77149179065 scopus 로고    scopus 로고
    • Structural biology of heme binding in the Staphylococcus aureus Isd system
    • Grigg, J. C.; Ukpabi, G.; Gaudin, C. F.; Murphy, M. E. Structural biology of heme binding in the Staphylococcus aureus Isd system J. Inorg. Biochem. 2010, 104, 341-8
    • (2010) J. Inorg. Biochem. , vol.104 , pp. 341-8
    • Grigg, J.C.1    Ukpabi, G.2    Gaudin, C.F.3    Murphy, M.E.4
  • 61
    • 4644310922 scopus 로고    scopus 로고
    • Iron-source preference of Staphylococcus aureus infections
    • DOI 10.1126/science.1099930
    • Skaar, E. P.; Humayun, M.; Bae, T.; DeBord, K. L.; Schneewind, O. Iron-source preference of Staphylococcus aureus infections Science 2004, 305, 1626-8 (Pubitemid 39296358)
    • (2004) Science , vol.305 , Issue.5690 , pp. 1626-1628
    • Skaar, E.P.1    Humayun, M.2    Bae, T.3    DeBord, K.L.4    Schneewind, O.5
  • 62
    • 0034885056 scopus 로고    scopus 로고
    • Identification and characterization of fhuD1 and fhuD2, two genes involved in iron-hydroxamate uptake in Staphylococcus aureus
    • DOI 10.1128/JB.183.17.4994-5000.2001
    • Sebulsky, M. T.; Heinrichs, D. E. Identification and characterization of fhuD1 and fhuD2, two genes involved in iron-hydroxamate uptake in Staphylococcus aureus J. Bacteriol. 2001, 183, 4994-5000 (Pubitemid 32750926)
    • (2001) Journal of Bacteriology , vol.183 , Issue.17 , pp. 4994-5000
    • Sebulsky, M.T.1    Heinrichs, D.E.2
  • 63
    • 0346749526 scopus 로고    scopus 로고
    • The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus: Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport
    • DOI 10.1074/jbc.M305073200
    • Sebulsky, M. T.; Shilton, B. H.; Speziali, C. D.; Heinrichs, D. E. The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport J. Biol. Chem. 2003, 278, 49890-900 (Pubitemid 37548824)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 49890-49900
    • Sebulsky, M.T.1    Shilton, B.H.2    Speziali, C.D.3    Heinrichs, D.E.4
  • 64
    • 0032985815 scopus 로고    scopus 로고
    • Identification and characterization of SirA, an iron-regulated protein from Staphylococcus aureus
    • Heinrichs, J. H.; Gatlin, L. E.; Kunsch, C.; Choi, G. H.; Hanson, M. S. Identification and characterization of SirA, an iron-regulated protein from Staphylococcus aureus J. Bacteriol. 1999, 181, 1436-43 (Pubitemid 29110801)
    • (1999) Journal of Bacteriology , vol.181 , Issue.5 , pp. 1436-1443
    • Heinrichs, J.H.1    Gatlin, L.E.2    Kunsch, C.3    Choi, G.H.4    Hanson, M.S.5
  • 65
    • 10044255385 scopus 로고    scopus 로고
    • Involvement of SirABC in iron-siderophore import in Staphylococcus aureus
    • DOI 10.1128/JB.186.24.8356-8362.2004
    • Dale, S. E.; Sebulsky, M. T.; Heinrichs, D. E. Involvement of SirABC in iron-siderophore import in Staphylococcus aureus J. Bacteriol. 2004, 186, 8356-62 (Pubitemid 39603226)
    • (2004) Journal of Bacteriology , vol.186 , Issue.24 , pp. 8356-8362
    • Dale, S.E.1    Sebulsky, M.T.2    Heinrichs, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.