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Volumn 2, Issue 8, 2006, Pages 0777-0789

Staphylococcus aureus redirects central metabolism to increase iron availability

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HEMIN; IRON; LACTIC ACID; PROTEIN FUR; STAPHYLOCOCCUS PROTEIN; UNCLASSIFIED DRUG; HEME; IRON BINDING PROTEIN; IRON UPTAKE REGULATION PROTEIN, BACTERIA; IRON-UPTAKE REGULATION PROTEIN, BACTERIA; REPRESSOR PROTEIN; TRANSFERRIN;

EID: 33748043648     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.0020087     Document Type: Article
Times cited : (174)

References (47)
  • 2
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the Fur protein
    • Escolar L, Perez-Martin J, de Lorenzo V (1999) Opening the iron box: Transcriptional metalloregulation by the Fur protein. J Bacteriol 181: 6223-6229.
    • (1999) J Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 3
    • 0038385189 scopus 로고    scopus 로고
    • Identification of a novel iron regulated staphylococcal surface protein with haptoglobin-haemoglobin binding activity
    • Dryla A, Gelbmann D, Von Gabain A, Nagy E (2003) Identification of a novel iron regulated staphylococcal surface protein with haptoglobin-haemoglobin binding activity. Mol Microbiol 49: 37-53.
    • (2003) Mol Microbiol , vol.49 , pp. 37-53
    • Dryla, A.1    Gelbmann, D.2    Von Gabain, A.3    Nagy, E.4
  • 4
    • 0037423231 scopus 로고    scopus 로고
    • Passage of heme-iron across the envelope of Staphylococcus aureus
    • Mazmanian SK, Skaar EP, Gaspar AH, Humayun M, Gornicki P, et al. (2003) Passage of heme-iron across the envelope of Staphylococcus aureus. Science 299: 906-909.
    • (2003) Science , vol.299 , pp. 906-909
    • Mazmanian, S.K.1    Skaar, E.P.2    Gaspar, A.H.3    Humayun, M.4    Gornicki, P.5
  • 5
    • 0034113354 scopus 로고    scopus 로고
    • Molecular characterization of the ferric-uptake regulator, fur, from Staphylococcus aureus
    • Xiong A, Singh VK, Cabrera G, Jayaswal RK (2000) Molecular characterization of the ferric-uptake regulator, fur, from Staphylococcus aureus. Microbiology 146 (Pt 3):: 659-668.
    • (2000) Microbiology , vol.146 , Issue.3 PART , pp. 659-668
    • Xiong, A.1    Singh, V.K.2    Cabrera, G.3    Jayaswal, R.K.4
  • 6
    • 0035150765 scopus 로고    scopus 로고
    • In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis
    • Horsburgh MJ, Ingham E, Foster SJ (2001) In Staphylococcus aureus, Fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis. J Bacteriol 183: 468-475.
    • (2001) J Bacteriol , vol.183 , pp. 468-475
    • Horsburgh, M.J.1    Ingham, E.2    Foster, S.J.3
  • 7
    • 3543068251 scopus 로고    scopus 로고
    • Regulog analysis: Detection of conserved regulatory networks across bacteria: Application to Staphylococcus aureus
    • Alkema WB, Lenhard B, Wasserman WW (2004) Regulog analysis: Detection of conserved regulatory networks across bacteria: Application to Staphylococcus aureus. Genome Res 14: 1362-1373.
    • (2004) Genome Res , vol.14 , pp. 1362-1373
    • Alkema, W.B.1    Lenhard, B.2    Wasserman, W.W.3
  • 8
    • 4644310922 scopus 로고    scopus 로고
    • Iron-source preference of Staphylococcus aureus infections
    • Skaar EP, Humayun M, Bae T, DeBord KL, Schneewind O (2004) Iron-source preference of Staphylococcus aureus infections. Science 305: 1626-1628.
    • (2004) Science , vol.305 , pp. 1626-1628
    • Skaar, E.P.1    Humayun, M.2    Bae, T.3    DeBord, K.L.4    Schneewind, O.5
  • 9
    • 1642283048 scopus 로고    scopus 로고
    • Iron-regulated surface determinants (Isd) of Staphylococcus aureus: Stealing iron from heme
    • Skaar EP, Schneewind O (2004) Iron-regulated surface determinants (Isd) of Staphylococcus aureus: Stealing iron from heme. Microbes Infect 6: 390-397.
    • (2004) Microbes Infect , vol.6 , pp. 390-397
    • Skaar, E.P.1    Schneewind, O.2
  • 10
    • 0345791519 scopus 로고    scopus 로고
    • IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus
    • Skaar EP, Gaspar AH, Schneewind O (2004) IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus. J Biol Chem 279: 436-443.
    • (2004) J Biol Chem , vol.279 , pp. 436-443
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 11
    • 13244296905 scopus 로고    scopus 로고
    • Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases
    • Wu R, Skaar EP, Zhang R, Joachimiak G, Gornicki P, et al. (2005) Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases. J Biol Chem 280: 2840-2846.
    • (2005) J Biol Chem , vol.280 , pp. 2840-2846
    • Wu, R.1    Skaar, E.P.2    Zhang, R.3    Joachimiak, G.4    Gornicki, P.5
  • 12
    • 4444351205 scopus 로고    scopus 로고
    • Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression
    • Gerbasi VR, Weaver CM, Hill S, Friedman DB, Link AJ (2004) Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression. Mol Cell Biol 24: 8276-8287.
    • (2004) Mol Cell Biol , vol.24 , pp. 8276-8287
    • Gerbasi, V.R.1    Weaver, C.M.2    Hill, S.3    Friedman, D.B.4    Link, A.J.5
  • 13
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard
    • Alban A, David SO, Bjorkesten L, Andersson C, Sloge E, et al. (2003) A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 3: 36-44.
    • (2003) Proteomics , vol.3 , pp. 36-44
    • Alban, A.1    David, S.O.2    Bjorkesten, L.3    Andersson, C.4    Sloge, E.5
  • 14
    • 1542406246 scopus 로고    scopus 로고
    • Proteome analysis of human colon cancer by two-dimensional difference gel electrophoresis and mass spectrometry
    • Friedman DB, Hill S, Keller JW, Merchant NB, Levy SE, et al. (2004) Proteome analysis of human colon cancer by two-dimensional difference gel electrophoresis and mass spectrometry. Proteomics 4: 793-811.
    • (2004) Proteomics , vol.4 , pp. 793-811
    • Friedman, D.B.1    Hill, S.2    Keller, J.W.3    Merchant, N.B.4    Levy, S.E.5
  • 15
    • 27744583045 scopus 로고    scopus 로고
    • All about DIGE: Quantification technology for differential-display 2D-gel proteomics
    • Lilley KS, Friedman DB (2004) All about DIGE: Quantification technology for differential-display 2D-gel proteomics. Exp Rev Proteomics 1: 401-409.
    • (2004) Exp Rev Proteomics , vol.1 , pp. 401-409
    • Lilley, K.S.1    Friedman, D.B.2
  • 16
    • 0348141912 scopus 로고    scopus 로고
    • Role of siderophore biosynthesis in virulence of Staphylococcus aureus: Identification and characterization of genes involved in production of a siderophore
    • Dale SE, Doherty-Kirby A, Lajoie G, Heinrichs DE (2004) Role of siderophore biosynthesis in virulence of Staphylococcus aureus: Identification and characterization of genes involved in production of a siderophore. Infect Immun 72: 29-37.
    • (2004) Infect Immun , vol.72 , pp. 29-37
    • Dale, S.E.1    Doherty-Kirby, A.2    Lajoie, G.3    Heinrichs, D.E.4
  • 17
    • 0033907955 scopus 로고    scopus 로고
    • Identification and characterization of a membrane permease involved in iron-hydroxamate transport in Staphylococcus aureus
    • Sebulsky MT, Hohnstein D, Hunter MD, Heinrichs DE (2000) Identification and characterization of a membrane permease involved in iron-hydroxamate transport in Staphylococcus aureus. J Bacteriol 182: 4394-4400.
    • (2000) J Bacteriol , vol.182 , pp. 4394-4400
    • Sebulsky, M.T.1    Hohnstein, D.2    Hunter, M.D.3    Heinrichs, D.E.4
  • 18
    • 3042777261 scopus 로고    scopus 로고
    • Proteomic analysis of a ferric uptake regulator mutant of Helicobacter pylori: Regulation of Helicobacter pylori gene expression by ferric uptake regulator and iron
    • Lee HW, Choe YH, Kim DK, Jung SY, Lee NG (2004) Proteomic analysis of a ferric uptake regulator mutant of Helicobacter pylori: regulation of Helicobacter pylori gene expression by ferric uptake regulator and iron. Proteomics 4: 2014-2027.
    • (2004) Proteomics , vol.4 , pp. 2014-2027
    • Lee, H.W.1    Choe, Y.H.2    Kim, D.K.3    Jung, S.Y.4    Lee, N.G.5
  • 19
    • 28444438519 scopus 로고    scopus 로고
    • Iron and fur regulation in Vibrio cholerae and the role of fur in virulence
    • Mey AR, Wyckoff EE, Kanukurthy V, Fisher CR, Payne SM (2005) Iron and fur regulation in Vibrio cholerae and the role of fur in virulence. Infect Immun 73: 8167-8178.
    • (2005) Infect Immun , vol.73 , pp. 8167-8178
    • Mey, A.R.1    Wyckoff, E.E.2    Kanukurthy, V.3    Fisher, C.R.4    Payne, S.M.5
  • 20
    • 3042816068 scopus 로고    scopus 로고
    • Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis
    • Delany I, Rappuoli R, Scarlato V (2004) Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis. Mol Microbiol 52: 1081-1090.
    • (2004) Mol Microbiol , vol.52 , pp. 1081-1090
    • Delany, I.1    Rappuoli, R.2    Scarlato, V.3
  • 21
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • Masse E, Vanderpool CK, Gottesman S (2005) Effect of RyhB small RNA on global iron use in Escherichia coli. J Bacteriol 187: 6962-6971.
    • (2005) J Bacteriol , vol.187 , pp. 6962-6971
    • Masse, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 22
    • 0034046748 scopus 로고    scopus 로고
    • Fur positive regulation of iron superoxide dismutase in Escherichia coli: Functional analysis of the sodB promoter
    • Dubrac S, Touati D (2000) Fur positive regulation of iron superoxide dismutase in Escherichia coli: Functional analysis of the sodB promoter. J Bacteriol 182: 3802-3808.
    • (2000) J Bacteriol , vol.182 , pp. 3802-3808
    • Dubrac, S.1    Touati, D.2
  • 23
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon
    • Baichoo N, Wang T, Ye R, Helmann JD (2002) Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. Mol Microbiol 45: 1613-1629.
    • (2002) Mol Microbiol , vol.45 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 24
    • 0041744003 scopus 로고    scopus 로고
    • Correlation of acetate catabolism and growth yield in Staphylococcus aureus: Implications for host-pathogen interactions
    • Somerville GA, Said-Salim B, Wickman JM, Raffel SJ, Kreiswirth BN, et al. (2003) Correlation of acetate catabolism and growth yield in Staphylococcus aureus: implications for host-pathogen interactions. Infect Immun 71: 4724-4732.
    • (2003) Infect Immun , vol.71 , pp. 4724-4732
    • Somerville, G.A.1    Said-Salim, B.2    Wickman, J.M.3    Raffel, S.J.4    Kreiswirth, B.N.5
  • 25
    • 0034640272 scopus 로고    scopus 로고
    • Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium
    • Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, et al. (2000) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275: 14031-14037.
    • (2000) J Biol Chem , vol.275 , pp. 14031-14037
    • Fillinger, S.1    Boschi-Muller, S.2    Azza, S.3    Dervyn, E.4    Branlant, G.5
  • 26
    • 0035016446 scopus 로고    scopus 로고
    • Zur: A Zn(2p)-responsive regulatory element of Staphylococcus aureus
    • Lindsay JA, Foster SJ (2001) zur: A Zn(2p)-responsive regulatory element of Staphylococcus aureus. Microbiology 147: 1259-1266.
    • (2001) Microbiology , vol.147 , pp. 1259-1266
    • Lindsay, J.A.1    Foster, S.J.2
  • 27
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh MJ, Clements MO, Crossley H, Ingham E, Foster SJ (2001) PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect Immun 69: 3744-3754.
    • (2001) Infect Immun , vol.69 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 28
    • 0036015643 scopus 로고    scopus 로고
    • MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake
    • Horsburgh MJ, Wharton SJ, Cox AG, Ingham E, Peacock S, et al. (2002) MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake. Mol Microbiol 44: 1269-1286.
    • (2002) Mol Microbiol , vol.44 , pp. 1269-1286
    • Horsburgh, M.J.1    Wharton, S.J.2    Cox, A.G.3    Ingham, E.4    Peacock, S.5
  • 29
    • 0013801741 scopus 로고
    • Carbohydrate metabolism of iron-rich and iron-poor Staphylococcus aureus
    • Theodore TS, Schade AL (1965) Carbohydrate metabolism of iron-rich and iron-poor Staphylococcus aureus. J Gen Microbiol 40: 385-395.
    • (1965) J Gen Microbiol , vol.40 , pp. 385-395
    • Theodore, T.S.1    Schade, A.L.2
  • 30
    • 0018070907 scopus 로고
    • The effect of acid pH and citrate on the release and exchange of iron on rat transferrin
    • Okada S, Rossmann MD, Brown EB (1978) The effect of acid pH and citrate on the release and exchange of iron on rat transferrin. Biochim Biophys Acta 543: 72-81.
    • (1978) Biochim Biophys Acta , vol.543 , pp. 72-81
    • Okada, S.1    Rossmann, M.D.2    Brown, E.B.3
  • 31
    • 27744497470 scopus 로고    scopus 로고
    • Analysis of a heme-dependent signal transduction system in Corynebacterium diphtheriae: Deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter
    • Bibb LA, King ND, Kunkle CA, Schmitt MP (2005) Analysis of a heme-dependent signal transduction system in Corynebacterium diphtheriae: Deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter. Infect Immun 73: 7406-7412.
    • (2005) Infect Immun , vol.73 , pp. 7406-7412
    • Bibb, L.A.1    King, N.D.2    Kunkle, C.A.3    Schmitt, M.P.4
  • 32
    • 0034783889 scopus 로고    scopus 로고
    • Heme utilization in Bordetella avium is regulated by RhuI, a heme-responsive extracytoplasmic function sigma factor
    • Kirby AE, Metzger DJ, Murphy ER, Connell TD (2001) Heme utilization in Bordetella avium is regulated by RhuI, a heme-responsive extracytoplasmic function sigma factor. Infect Immun 69: 6951-6961.
    • (2001) Infect Immun , vol.69 , pp. 6951-6961
    • Kirby, A.E.1    Metzger, D.J.2    Murphy, E.R.3    Connell, T.D.4
  • 33
    • 0037309146 scopus 로고    scopus 로고
    • Heme-responsive transcriptional activation of Bordetella bhu genes
    • Vanderpool CK, Armstrong SK (2003) Heme-responsive transcriptional activation of Bordetella bhu genes. J Bacteriol 185: 909-917.
    • (2003) J Bacteriol , vol.185 , pp. 909-917
    • Vanderpool, C.K.1    Armstrong, S.K.2
  • 34
    • 0030850117 scopus 로고    scopus 로고
    • The sae locus of Staphylococcus aureus controls exoprotein synthesis at the transcriptional level
    • Giraudo AT, Cheung AL, Nagel R (1997) The sae locus of Staphylococcus aureus controls exoprotein synthesis at the transcriptional level. Arch Microbiol 168: 53-58.
    • (1997) Arch Microbiol , vol.168 , pp. 53-58
    • Giraudo, A.T.1    Cheung, A.L.2    Nagel, R.3
  • 35
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Masse E, Gottesman S (2002) A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci U S A 99: 4620-4625.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 36
    • 3042840984 scopus 로고    scopus 로고
    • Identification of tandem duplicate regulatory small RNAs in Pseudomonas aeruginosa involved in iron homeostasis
    • Wilderman PJ, Sowa NA, FitzGerald DJ, FitzGerald PC, Gottesman S, et al. (2004) Identification of tandem duplicate regulatory small RNAs in Pseudomonas aeruginosa involved in iron homeostasis. Proc Natl Acad Sci U S A 101: 9792-9797.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9792-9797
    • Wilderman, P.J.1    Sowa, N.A.2    FitzGerald, D.J.3    FitzGerald, P.C.4    Gottesman, S.5
  • 37
    • 20444473805 scopus 로고    scopus 로고
    • Characterization of the small untranslated RNA RyhB and its regulon in Vibrio cholerae
    • Davis BM, Quinones M, Pratt J, Ding Y, Waldor MK (2005) Characterization of the small untranslated RNA RyhB and its regulon in Vibrio cholerae. J Bacteriol 187: 4005-4014.
    • (2005) J Bacteriol , vol.187 , pp. 4005-4014
    • Davis, B.M.1    Quinones, M.2    Pratt, J.3    Ding, Y.4    Waldor, M.K.5
  • 38
    • 28244485425 scopus 로고    scopus 로고
    • Fur regulates acid resistance in Shigella flexneri via RyhB and ydeP
    • Oglesby AG, Murphy ER, Iyer VR, Payne SM (2005) Fur regulates acid resistance in Shigella flexneri via RyhB and ydeP. Mol Microbiol 58: 1354-1367.
    • (2005) Mol Microbiol , vol.58 , pp. 1354-1367
    • Oglesby, A.G.1    Murphy, E.R.2    Iyer, V.R.3    Payne, S.M.4
  • 39
    • 26444600764 scopus 로고    scopus 로고
    • Small RNA genes expressed from Staphylococcus aureus genomic and pathogenicity islands with specific expression among pathogenic strains
    • Pichon C, Felden B (2005) Small RNA genes expressed from Staphylococcus aureus genomic and pathogenicity islands with specific expression among pathogenic strains. Proc Natl Acad Sci U S A 102: 14249-14254.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14249-14254
    • Pichon, C.1    Felden, B.2
  • 40
    • 0036840950 scopus 로고    scopus 로고
    • Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary-phase survival
    • Somerville GA, Chaussee MS, Morgan CI, Fitzgerald JR, Dorward DW, et al. (2002) Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary-phase survival. Infect Immun 70: 6373-6382.
    • (2002) Infect Immun , vol.70 , pp. 6373-6382
    • Somerville, G.A.1    Chaussee, M.S.2    Morgan, C.I.3    Fitzgerald, J.R.4    Dorward, D.W.5
  • 41
    • 0242575010 scopus 로고    scopus 로고
    • Synthesis and deformylation of Staphylococcus aureus delta-toxin are linked to tricarboxylic acid cycle activity
    • Somerville GA, Cockayne A, Durr M, Peschel A, Otto M, et al. (2003) Synthesis and deformylation of Staphylococcus aureus delta-toxin are linked to tricarboxylic acid cycle activity. J Bacteriol 185: 6686-6694.
    • (2003) J Bacteriol , vol.185 , pp. 6686-6694
    • Somerville, G.A.1    Cockayne, A.2    Durr, M.3    Peschel, A.4    Otto, M.5
  • 42
    • 0014076134 scopus 로고
    • Relation between iron uptake, pH of growth medium, and penicillinase formation in Staphylococcus aureus
    • Cohen S, Sweeney HM, Leitner F (1967) Relation between iron uptake, pH of growth medium, and penicillinase formation in Staphylococcus aureus. J Bacteriol 93: 1227-1235.
    • (1967) J Bacteriol , vol.93 , pp. 1227-1235
    • Cohen, S.1    Sweeney, H.M.2    Leitner, F.3
  • 43
    • 0037133213 scopus 로고    scopus 로고
    • An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis
    • Mazmanian SK, Ton-That H, Su K, Schneewind O (2002) An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proc Natl Acad Sci USA 99: 2293-2298.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2293-2298
    • Mazmanian, S.K.1    Ton-That, H.2    Su, K.3    Schneewind, O.4
  • 44
    • 4344649571 scopus 로고    scopus 로고
    • Staphylococcus aureus virulence genes identified by bursa aurealis mutagenesis and nematode killing
    • Bae T, Banger AK, Wallace A, Glass EM, Aslund F, et al. (2004) Staphylococcus aureus virulence genes identified by bursa aurealis mutagenesis and nematode killing. Proc Natl Acad Sci U S A 101: 12312-12317.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 12312-12317
    • Bae, T.1    Banger, A.K.2    Wallace, A.3    Glass, E.M.4    Aslund, F.5
  • 45
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D, Flugge UI (1984) A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal Biochem 138: 141-143.
    • (1984) Anal Biochem , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 46
    • 33748091244 scopus 로고    scopus 로고
    • Quantitative proteomics for two-dimensional gels using difference gel electrophoresis (DIGE)
    • Matthiesen R, editor. Totowa (New Jersey): Humana Press
    • Friedman DB (2006) Quantitative proteomics for two-dimensional gels using difference gel electrophoresis (DIGE). In: Matthiesen R, editor. Mass spectrometry data analysis in proteomics. Totowa (New Jersey): Humana Press.
    • (2006) Mass Spectrometry Data Analysis in Proteomics
    • Friedman, D.B.1
  • 47
    • 0030722862 scopus 로고    scopus 로고
    • Iron release from recombinant N-lobe and single point Asp63 mutants of human transferrin by EDTA
    • He QY, Mason AB, Woodworth RC (1997) Iron release from recombinant N-lobe and single point Asp63 mutants of human transferrin by EDTA. Biochem J 328 (Pt 2): 439-445.
    • (1997) Biochem J , vol.328 , Issue.2 PART , pp. 439-445
    • He, Q.Y.1    Mason, A.B.2    Woodworth, R.C.3


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