메뉴 건너뛰기




Volumn 16, Issue 11-12, 2016, Pages 1767-1774

MALDI imaging mass spectrometry of Pacific White Shrimp L. vannamei and identification of abdominal muscle proteins

Author keywords

Biomedicine; Electron transfer dissociation; Flightin; Imaging mass spectrometry; Top down proteomics

Indexed keywords

ABDOMINAL MUSCLE PROTEIN; CONNECTIN; DNA; FLIGHTIN; MUSCLE PROTEIN; TROPONIN I; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84974802783     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201500531     Document Type: Article
Times cited : (7)

References (45)
  • 1
    • 84904422596 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry: spatial molecular analysis to enable a new age of discovery
    • Gessel, M. M., Norris, J. L., Caprioli, R. M., MALDI imaging mass spectrometry: spatial molecular analysis to enable a new age of discovery. J. Proteomics 2014 107, 71–82.
    • (2014) J. Proteomics , vol.107 , pp. 71-82
    • Gessel, M.M.1    Norris, J.L.2    Caprioli, R.M.3
  • 2
    • 84865170415 scopus 로고    scopus 로고
    • Imaging mass spectrometry of thin tissue sections: a decade of collective efforts
    • Chaurand, P., Imaging mass spectrometry of thin tissue sections: a decade of collective efforts. J. Proteomics 2012 75, 4883–4892.
    • (2012) J. Proteomics , vol.75 , pp. 4883-4892
    • Chaurand, P.1
  • 3
    • 84920408182 scopus 로고    scopus 로고
    • Mass spectrometry imaging of biomolecular information
    • Spengler, B., Mass spectrometry imaging of biomolecular information. Anal. Chem. 2015 87, 64–82.
    • (2015) Anal. Chem. , vol.87 , pp. 64-82
    • Spengler, B.1
  • 4
    • 78651243767 scopus 로고    scopus 로고
    • Imaging mass spectrometry for the assessment of drugs and metabolites in tissue
    • Trim, P. J., Francese, S., Clench, M. R., Imaging mass spectrometry for the assessment of drugs and metabolites in tissue. Bioanalysis 2009 1, 309–319.
    • (2009) Bioanalysis , vol.1 , pp. 309-319
    • Trim, P.J.1    Francese, S.2    Clench, M.R.3
  • 5
    • 84894427320 scopus 로고    scopus 로고
    • A critical evaluation of the current state-of-the-art in quantitative imaging mass spectrometry
    • Ellis, S. R., Bruinen, A. L., Heeren, R. M., A critical evaluation of the current state-of-the-art in quantitative imaging mass spectrometry. Anal. Bioanal. Chem. 2014 406, 1275–1289.
    • (2014) Anal. Bioanal. Chem. , vol.406 , pp. 1275-1289
    • Ellis, S.R.1    Bruinen, A.L.2    Heeren, R.M.3
  • 6
    • 33748865022 scopus 로고    scopus 로고
    • Direct molecular analysis of whole-body animal tissue sections by imaging MALDI mass spectrometry
    • Khatib-Shahidi, S., Andersson, M., Herman, J. L., Gillespie, T. A., Caprioli, R. M., Direct molecular analysis of whole-body animal tissue sections by imaging MALDI mass spectrometry. Anal. Chem. 2006 78, 6448–6456.
    • (2006) Anal. Chem. , vol.78 , pp. 6448-6456
    • Khatib-Shahidi, S.1    Andersson, M.2    Herman, J.L.3    Gillespie, T.A.4    Caprioli, R.M.5
  • 7
    • 79955802352 scopus 로고    scopus 로고
    • Direct molecular analysis of whole-body animal tissue sections by MALDI imaging mass spectrometry
    • Reyzer, M. L., Chaurand, P., Angel, P. M., Caprioli, R. M., Direct molecular analysis of whole-body animal tissue sections by MALDI imaging mass spectrometry. Methods Mol. Biol. 2010 656, 285–301.
    • (2010) Methods Mol. Biol. , vol.656 , pp. 285-301
    • Reyzer, M.L.1    Chaurand, P.2    Angel, P.M.3    Caprioli, R.M.4
  • 8
    • 84869025464 scopus 로고    scopus 로고
    • Direct imaging of single cells and tissue at sub-cellular spatial resolution using transmission geometry MALDI MS
    • Zavalin, A., Todd, E. M., Rawhouser, P. D., Yang, J. et al., Direct imaging of single cells and tissue at sub-cellular spatial resolution using transmission geometry MALDI MS. J. Mass Spectrom. 2012 47, 1473–1481.
    • (2012) J. Mass Spectrom. , vol.47 , pp. 1473-1481
    • Zavalin, A.1    Todd, E.M.2    Rawhouser, P.D.3    Yang, J.4
  • 9
    • 85039706375 scopus 로고    scopus 로고
    • Tissue protein imaging at 1 mum laser spot diameter for high spatial resolution and high imaging speed using transmission geometry MALDI TOF MS
    • Zavalin, A., Yang, J., Hayden, K., Vestal, M., Caprioli, R. M., Tissue protein imaging at 1 mum laser spot diameter for high spatial resolution and high imaging speed using transmission geometry MALDI TOF MS. Anal. Bioanal. Chem. 2015 407, 2337–2342.
    • (2015) Anal. Bioanal. Chem. , vol.407 , pp. 2337-2342
    • Zavalin, A.1    Yang, J.2    Hayden, K.3    Vestal, M.4    Caprioli, R.M.5
  • 10
    • 84878264150 scopus 로고    scopus 로고
    • Mass spectrometry imaging with high resolution in mass and space
    • Rompp, A., Spengler, B., Mass spectrometry imaging with high resolution in mass and space. Histochem. Cell Biol. 2013 139, 759–783.
    • (2013) Histochem. Cell Biol. , vol.139 , pp. 759-783
    • Rompp, A.1    Spengler, B.2
  • 11
    • 84946224898 scopus 로고    scopus 로고
    • High resolution mass spectrometry imaging of plant tissues: towards a plant metabolite atlas
    • Bhandari, D. R., Wang, Q., Friedt, W., Spengler, B. et al., High resolution mass spectrometry imaging of plant tissues: towards a plant metabolite atlas. Analyst 2015 140, 7696–7709.
    • (2015) Analyst , vol.140 , pp. 7696-7709
    • Bhandari, D.R.1    Wang, Q.2    Friedt, W.3    Spengler, B.4
  • 12
    • 79955806756 scopus 로고    scopus 로고
    • High-speed MALDI-TOF imaging mass spectrometry: rapid ion image acquisition and considerations for next generation instrumentation
    • Spraggins, J. M., Caprioli, R. M., High-speed MALDI-TOF imaging mass spectrometry: rapid ion image acquisition and considerations for next generation instrumentation. J. Am. Soc. Mass Spectrom. 2011 22, 1022–1031.
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1022-1031
    • Spraggins, J.M.1    Caprioli, R.M.2
  • 13
    • 84929004305 scopus 로고    scopus 로고
    • High-speed MALDI MS/MS imaging mass spectrometry using continuous raster sampling
    • Prentice, B. M., Chumbley, C. W., Caprioli, R. M., High-speed MALDI MS/MS imaging mass spectrometry using continuous raster sampling. J. Mass Spectrom. 2015 50, 703–710.
    • (2015) J. Mass Spectrom. , vol.50 , pp. 703-710
    • Prentice, B.M.1    Chumbley, C.W.2    Caprioli, R.M.3
  • 14
    • 84945950670 scopus 로고    scopus 로고
    • Use of advantageous, volatile matrices enabled by next-generation high-speed matrix-assisted laser desorption/ionization time-of-flight imaging employing a scanning laser beam
    • Ogrinc Potocnik, N., Porta, T., Becker, M., Heeren, R. M., Ellis, S. R., Use of advantageous, volatile matrices enabled by next-generation high-speed matrix-assisted laser desorption/ionization time-of-flight imaging employing a scanning laser beam. Rapid Commun. Mass Spectrom. 2015 29, 2195–2203.
    • (2015) Rapid Commun. Mass Spectrom. , vol.29 , pp. 2195-2203
    • Ogrinc Potocnik, N.1    Porta, T.2    Becker, M.3    Heeren, R.M.4    Ellis, S.R.5
  • 15
    • 64149100821 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometric imaging of complete rat sections using a triple quadrupole linear ion trap
    • Hopfgartner, G., Varesio, E., Stoeckli, M., Matrix-assisted laser desorption/ionization mass spectrometric imaging of complete rat sections using a triple quadrupole linear ion trap. Rapid Commun. Mass Spectrom. 2009 23, 733–736.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 733-736
    • Hopfgartner, G.1    Varesio, E.2    Stoeckli, M.3
  • 16
    • 33846886098 scopus 로고    scopus 로고
    • Mapping pharmaceuticals in tissues using MALDI imaging mass spectrometry
    • Hsieh, Y., Chen, J., Korfmacher, W. A., Mapping pharmaceuticals in tissues using MALDI imaging mass spectrometry. J. Pharmacol. Toxicol. Methods 2007 55, 193–200.
    • (2007) J. Pharmacol. Toxicol. Methods , vol.55 , pp. 193-200
    • Hsieh, Y.1    Chen, J.2    Korfmacher, W.A.3
  • 17
    • 84865200761 scopus 로고    scopus 로고
    • Mass spectrometry imaging for drug distribution studies
    • Prideaux, B., Stoeckli, M., Mass spectrometry imaging for drug distribution studies. J. Proteomics 2012 75, 4999–5013.
    • (2012) J. Proteomics , vol.75 , pp. 4999-5013
    • Prideaux, B.1    Stoeckli, M.2
  • 18
    • 84890485143 scopus 로고    scopus 로고
    • Whole-body tissue distribution study of drugs in neonate mice using desorption electrospray ionization mass spectrometry imaging
    • Liu, J., Gingras, J., Ganley, K. P., Vismeh, R. et al., Whole-body tissue distribution study of drugs in neonate mice using desorption electrospray ionization mass spectrometry imaging. Rapid Commun. Mass Spectrom. 2014 28, 185–190.
    • (2014) Rapid Commun. Mass Spectrom. , vol.28 , pp. 185-190
    • Liu, J.1    Gingras, J.2    Ganley, K.P.3    Vismeh, R.4
  • 19
    • 84865448064 scopus 로고    scopus 로고
    • Evaluation of an accurate mass approach for the simultaneous detection of drug and metabolite distributions via whole-body mass spectrometric imaging
    • Shahidi-Latham, S. K., Dutta, S. M., Prieto Conaway, M. C., Rudewicz, P. J., Evaluation of an accurate mass approach for the simultaneous detection of drug and metabolite distributions via whole-body mass spectrometric imaging. Anal. Chem. 2012 84, 7158–7165.
    • (2012) Anal. Chem. , vol.84 , pp. 7158-7165
    • Shahidi-Latham, S.K.1    Dutta, S.M.2    Prieto Conaway, M.C.3    Rudewicz, P.J.4
  • 21
    • 84940093295 scopus 로고    scopus 로고
    • Direct profiling of the phospholipid composition of adult Caenorhabditis elegans using whole-body imaging mass spectrometry
    • Hameed, S., Ikegami, K., Sugiyama, E., Matsushita, S. et al., Direct profiling of the phospholipid composition of adult Caenorhabditis elegans using whole-body imaging mass spectrometry. Anal. Bioanal. Chem. 2015 407, 7589–7602.
    • (2015) Anal. Bioanal. Chem. , vol.407 , pp. 7589-7602
    • Hameed, S.1    Ikegami, K.2    Sugiyama, E.3    Matsushita, S.4
  • 22
    • 84920393411 scopus 로고    scopus 로고
    • Analysis of Drosophila lipids by matrix-assisted laser desorption/ionization mass spectrometric imaging
    • Niehoff, A. C., Kettling, H., Pirkl, A., Chiang, Y. N. et al., Analysis of Drosophila lipids by matrix-assisted laser desorption/ionization mass spectrometric imaging. Anal. Chem. 2014 86, 11086–11092.
    • (2014) Anal. Chem. , vol.86 , pp. 11086-11092
    • Niehoff, A.C.1    Kettling, H.2    Pirkl, A.3    Chiang, Y.N.4
  • 23
    • 84947207432 scopus 로고    scopus 로고
    • Phospholipid topography of whole-body sections of the anopheles stephensi mosquito, characterized by high-resolution atmospheric-pressure scanning microprobe matrix-assisted laser desorption/ionization mass spectrometry imaging
    • Khalil, S. M., Rompp, A., Pretzel, J., Becker, K., Spengler, B., Phospholipid topography of whole-body sections of the anopheles stephensi mosquito, characterized by high-resolution atmospheric-pressure scanning microprobe matrix-assisted laser desorption/ionization mass spectrometry imaging. Anal. Chem. 2015 87, 11309–11316.
    • (2015) Anal. Chem. , vol.87 , pp. 11309-11316
    • Khalil, S.M.1    Rompp, A.2    Pretzel, J.3    Becker, K.4    Spengler, B.5
  • 24
    • 84929004304 scopus 로고    scopus 로고
    • Metabolite localization by atmospheric pressure high-resolution scanning microprobe matrix-assisted laser desorption/ionization mass spectrometry imaging in whole-body sections and individual organs of the rove beetle Paederus riparius
    • Bhandari, D. R., Schott, M., Rompp, A., Vilcinskas, A., Spengler, B., Metabolite localization by atmospheric pressure high-resolution scanning microprobe matrix-assisted laser desorption/ionization mass spectrometry imaging in whole-body sections and individual organs of the rove beetle Paederus riparius. Anal. Bioanal. Chem. 2015 407, 2189–2201.
    • (2015) Anal. Bioanal. Chem. , vol.407 , pp. 2189-2201
    • Bhandari, D.R.1    Schott, M.2    Rompp, A.3    Vilcinskas, A.4    Spengler, B.5
  • 25
    • 84906715055 scopus 로고    scopus 로고
    • Imaging of whole zebra fish (Danio rerio) by desorption electrospray ionization mass spectrometry
    • Chramow, A., Hamid, T. S., Eberlin, L. S., Girod, M., Ifa, D. R., Imaging of whole zebra fish (Danio rerio) by desorption electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom. 2014 28, 2084–2088.
    • (2014) Rapid Commun. Mass Spectrom. , vol.28 , pp. 2084-2088
    • Chramow, A.1    Hamid, T.S.2    Eberlin, L.S.3    Girod, M.4    Ifa, D.R.5
  • 26
    • 84929076361 scopus 로고    scopus 로고
    • Influence of desorption conditions on analyte sensitivity and internal energy in discrete tissue or whole body imaging by IR-MALDESI
    • Rosen, E. P., Bokhart, M. T., Ghashghaei, H. T., Muddiman, D. C., Influence of desorption conditions on analyte sensitivity and internal energy in discrete tissue or whole body imaging by IR-MALDESI. J. Am. Soc. Mass Spectrom. 2015 26, 899–910.
    • (2015) J. Am. Soc. Mass Spectrom. , vol.26 , pp. 899-910
    • Rosen, E.P.1    Bokhart, M.T.2    Ghashghaei, H.T.3    Muddiman, D.C.4
  • 27
    • 84929593559 scopus 로고    scopus 로고
    • Ambient mass spectrometry imaging metabolomics method provides novel insights into the action mechanism of drug candidates
    • He, J., Luo, Z., Huang, L., He, J. et al., Ambient mass spectrometry imaging metabolomics method provides novel insights into the action mechanism of drug candidates. Anal. Chem. 2015 87, 5372–5379.
    • (2015) Anal. Chem. , vol.87 , pp. 5372-5379
    • He, J.1    Luo, Z.2    Huang, L.3    He, J.4
  • 28
    • 84872312050 scopus 로고    scopus 로고
    • Orthogonal organic and aqueous-based washes of tissue sections to enhance protein sensitivity by MALDI imaging mass spectrometry
    • Thomas, A., Patterson, N. H., Laveaux Charbonneau, J., Chaurand, P., Orthogonal organic and aqueous-based washes of tissue sections to enhance protein sensitivity by MALDI imaging mass spectrometry. J. Mass Spectrom. 2013 48, 42–48.
    • (2013) J. Mass Spectrom. , vol.48 , pp. 42-48
    • Thomas, A.1    Patterson, N.H.2    Laveaux Charbonneau, J.3    Chaurand, P.4
  • 29
    • 84883618452 scopus 로고    scopus 로고
    • Optimization of whole-body zebrafish sectioning methods for mass spectrometry imaging
    • Nelson, K. A., Daniels, G. J., Fournie, J. W., Hemmer, M. J., Optimization of whole-body zebrafish sectioning methods for mass spectrometry imaging. J. Biomol. Tech. 2013 24, 119–127.
    • (2013) J. Biomol. Tech. , vol.24 , pp. 119-127
    • Nelson, K.A.1    Daniels, G.J.2    Fournie, J.W.3    Hemmer, M.J.4
  • 30
    • 78650776255 scopus 로고    scopus 로고
    • Virus diseases of farmed shrimp in the Western Hemisphere (the Americas): a review
    • Lightner, D. V., Virus diseases of farmed shrimp in the Western Hemisphere (the Americas): a review. J. Invertebr. Pathol. 2011 106, 110–130.
    • (2011) J. Invertebr. Pathol. , vol.106 , pp. 110-130
    • Lightner, D.V.1
  • 31
    • 84873038737 scopus 로고    scopus 로고
    • Mapping of neuropeptides in the crustacean stomatogastric nervous system by imaging mass spectrometry
    • Ye, H., Hui, L., Kellersberger, K., Li, L., Mapping of neuropeptides in the crustacean stomatogastric nervous system by imaging mass spectrometry. J. Am. Soc. Mass Spectrom. 2013 24, 134–147.
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 134-147
    • Ye, H.1    Hui, L.2    Kellersberger, K.3    Li, L.4
  • 32
  • 33
    • 84858342301 scopus 로고    scopus 로고
    • Visualization of neuropeptides in paraffin-embedded tissue sections of the central nervous system in the decapod crustacean, Penaeus monodon, by imaging mass spectrometry
    • Chansela, P., Goto-Inoue, N., Zaima, N., Sroyraya, M. et al., Visualization of neuropeptides in paraffin-embedded tissue sections of the central nervous system in the decapod crustacean, Penaeus monodon, by imaging mass spectrometry. Peptides 2012 34, 10–18.
    • (2012) Peptides , vol.34 , pp. 10-18
    • Chansela, P.1    Goto-Inoue, N.2    Zaima, N.3    Sroyraya, M.4
  • 34
    • 84858172592 scopus 로고    scopus 로고
    • Composition and localization of lipids in Penaeus merguiensis ovaries during the ovarian maturation cycle as revealed by imaging mass spectrometry
    • Chansela, P., Goto-Inoue, N., Zaima, N., Hayasaka, T. et al., Composition and localization of lipids in Penaeus merguiensis ovaries during the ovarian maturation cycle as revealed by imaging mass spectrometry. PLoS One 2012 7, e33154.
    • (2012) PLoS One , vol.7
    • Chansela, P.1    Goto-Inoue, N.2    Zaima, N.3    Hayasaka, T.4
  • 35
    • 84910673767 scopus 로고    scopus 로고
    • Deep and quantitative top-down proteomics in clinical and translational research
    • Kelleher, N. L., Thomas, P. M., Ntai, I., Compton, P. D., LeDuc, R. D., Deep and quantitative top-down proteomics in clinical and translational research. Expert Rev. Proteomics 2014 11, 649–651.
    • (2014) Expert Rev. Proteomics , vol.11 , pp. 649-651
    • Kelleher, N.L.1    Thomas, P.M.2    Ntai, I.3    Compton, P.D.4    LeDuc, R.D.5
  • 36
    • 84880551095 scopus 로고    scopus 로고
    • Spatially-directed protein identification from tissue sections by top-down LC-MS/MS with electron transfer dissociation
    • Schey, K. L., Anderson, D. M., Rose, K. L., Spatially-directed protein identification from tissue sections by top-down LC-MS/MS with electron transfer dissociation. Anal. Chem. 2013 85, 6767–6774.
    • (2013) Anal. Chem. , vol.85 , pp. 6767-6774
    • Schey, K.L.1    Anderson, D.M.2    Rose, K.L.3
  • 37
    • 84870694137 scopus 로고    scopus 로고
    • High-definition de novo sequencing of crustacean hyperglycemic hormone (CHH)-family neuropeptides
    • Jia, C., Hui, L., Cao, W., Lietz, C. B. et al., High-definition de novo sequencing of crustacean hyperglycemic hormone (CHH)-family neuropeptides. Mol. Cell. Proteomics 2012 11, 1951–1964.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1951-1964
    • Jia, C.1    Hui, L.2    Cao, W.3    Lietz, C.B.4
  • 38
    • 84946887927 scopus 로고    scopus 로고
    • Defining the neuropeptidome of the spiny lobster panulirus interruptus brain using a multidimensional mass spectrometry-based platform
    • Ye, H., Wang, J., Zhang, Z., Jia, C. et al., Defining the neuropeptidome of the spiny lobster panulirus interruptus brain using a multidimensional mass spectrometry-based platform. J. Proteome Res. 2015 14, 4776–4791.
    • (2015) J. Proteome Res. , vol.14 , pp. 4776-4791
    • Ye, H.1    Wang, J.2    Zhang, Z.3    Jia, C.4
  • 39
    • 84893657723 scopus 로고    scopus 로고
    • An evolutionary analysis of flightin reveals a conserved motif unique and widespread in Pancrustacea
    • Soto-Adames, F. N., Alvarez-Ortiz, P., Vigoreaux, J. O., An evolutionary analysis of flightin reveals a conserved motif unique and widespread in Pancrustacea. J. Mol. Evol. 2014 78, 24–37.
    • (2014) J. Mol. Evol. , vol.78 , pp. 24-37
    • Soto-Adames, F.N.1    Alvarez-Ortiz, P.2    Vigoreaux, J.O.3
  • 40
    • 0034739846 scopus 로고    scopus 로고
    • Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles
    • Reedy, M. C., Bullard, B., Vigoreaux, J. O., Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles. J. Cell Biol. 2000 151, 1483–1500.
    • (2000) J. Cell Biol. , vol.151 , pp. 1483-1500
    • Reedy, M.C.1    Bullard, B.2    Vigoreaux, J.O.3
  • 41
    • 73149087896 scopus 로고    scopus 로고
    • Flightin is necessary for length determination, structural integrity, and large bending stiffness of insect flight muscle thick filaments
    • Contompasis, J. L., Nyland, L. R., Maughan, D. W., Vigoreaux, J. O., Flightin is necessary for length determination, structural integrity, and large bending stiffness of insect flight muscle thick filaments. J. Mol. Biol. 2010 395, 340–348.
    • (2010) J. Mol. Biol. , vol.395 , pp. 340-348
    • Contompasis, J.L.1    Nyland, L.R.2    Maughan, D.W.3    Vigoreaux, J.O.4
  • 42
    • 79960989133 scopus 로고    scopus 로고
    • COOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle
    • Tanner, B. C., Miller, M. S., Miller, B. M., Lekkas, P. et al., COOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle. Am. J. Physiol. Cell Physiol. 2011 301, C383–391.
    • (2011) Am. J. Physiol. Cell Physiol. , vol.301 , pp. 383-391
    • Tanner, B.C.1    Miller, M.S.2    Miller, B.M.3    Lekkas, P.4
  • 43
    • 84897435957 scopus 로고    scopus 로고
    • Imaging mass spectrometry for assessing temporal proteomics: analysis of calprotectin in Acinetobacter baumannii pulmonary infection
    • Moore, J. L., Becker, K. W., Nicklay, J. J., Boyd, K. L. et al., Imaging mass spectrometry for assessing temporal proteomics: analysis of calprotectin in Acinetobacter baumannii pulmonary infection. Proteomics 2014 14, 820–828.
    • (2014) Proteomics , vol.14 , pp. 820-828
    • Moore, J.L.1    Becker, K.W.2    Nicklay, J.J.3    Boyd, K.L.4
  • 44
    • 84884257375 scopus 로고    scopus 로고
    • MntABC and MntH contribute to systemic Staphylococcus aureus infection by competing with calprotectin for nutrient manganese
    • Kehl-Fie, T. E., Zhang, Y., Moore, J. L., Farrand, A. J. et al., MntABC and MntH contribute to systemic Staphylococcus aureus infection by competing with calprotectin for nutrient manganese. Infect. Immun. 2013 81, 3395–3405.
    • (2013) Infect. Immun. , vol.81 , pp. 3395-3405
    • Kehl-Fie, T.E.1    Zhang, Y.2    Moore, J.L.3    Farrand, A.J.4
  • 45
    • 84903593111 scopus 로고    scopus 로고
    • Advanced mass spectrometry technologies for the study of microbial pathogenesis
    • Moore, J. L., Caprioli, R. M., Skaar, E. P., Advanced mass spectrometry technologies for the study of microbial pathogenesis. Curr. Opin. Microbiol. 2014 19, 45–51.
    • (2014) Curr. Opin. Microbiol. , vol.19 , pp. 45-51
    • Moore, J.L.1    Caprioli, R.M.2    Skaar, E.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.