메뉴 건너뛰기




Volumn 1, Issue 19, 2013, Pages 2463-2475

Chitosan nanomagnets for effective extraction and sensitive mass spectrometric detection of pathogenic bacterial endotoxin from human urine

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY-BASED SEPARATION; BACTERIAL ENDOTOXINS; BACTERIAL INFECTIONS; CLINICAL SAMPLES; DEGREE OF SENSITIVITY; LIPOPOLYSACCHARIDES; MAGNETIC NANO-PARTICLES; SURFACE-MODIFIED;

EID: 84876931920     PISSN: 20507518     EISSN: 2050750X     Source Type: Journal    
DOI: 10.1039/c3tb20079e     Document Type: Article
Times cited : (95)

References (81)
  • 1
    • 0345711193 scopus 로고
    • Non specific transport through the outer membrane
    • ed. M. Inouye, John Wiley & Sons, Inc., New York
    • H. Nikaido, Non specific transport through the outer membrane, in Bacterial outer membranes: biogenesis and functions, ed., M. Inouye, John Wiley & Sons, Inc., New York, 1979, pp. 361-405
    • (1979) Bacterial Outer Membranes: Biogenesis and Functions , pp. 361-405
    • Nikaido, H.1
  • 2
    • 0018587209 scopus 로고
    • The outer membrane of gram-negative bacteria
    • H. Nikaido T. Nakae The outer membrane of gram-negative bacteria Adv. Microb. Physiol. 1979 19 163 250
    • (1979) Adv. Microb. Physiol. , vol.19 , pp. 163-250
    • Nikaido, H.1    Nakae, T.2
  • 5
    • 0024042262 scopus 로고
    • Roles of porin and beta-lactamase in beta-lactam resistance of Pseudomonas aeruginosa
    • R. E. Hancock W. A. Woodruff Roles of porin and beta-lactamase in beta-lactam resistance of Pseudomonas aeruginosa Clin. Infect. Dis. 1988 10 770 775
    • (1988) Clin. Infect. Dis. , vol.10 , pp. 770-775
    • Hancock, R.E.1    Woodruff, W.A.2
  • 6
    • 0021063524 scopus 로고
    • Reduced sensitivity to beta-lactam antibiotics arising during ceftazidime treatment of Pseudomonas aeruginosa infections
    • A. King K. Shannon S. Eykyn I. Phillips Reduced sensitivity to beta-lactam antibiotics arising during ceftazidime treatment of Pseudomonas aeruginosa infections J. Antimicrob. Chemother. 1983 12 363 370
    • (1983) J. Antimicrob. Chemother. , vol.12 , pp. 363-370
    • King, A.1    Shannon, K.2    Eykyn, S.3    Phillips, I.4
  • 7
    • 0031952858 scopus 로고    scopus 로고
    • Beta-lactamase inhibitors are substrates for the ultidrug efflux pumps of Pseudomonas aeruginosa
    • X. Z. Li L. Zhang R. Srikumar K. Poole Beta-lactamase inhibitors are substrates for the ultidrug efflux pumps of Pseudomonas aeruginosa Antimicrob. Agents Chemother. 1998 42 399 403
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 399-403
    • Li, X.Z.1    Zhang, L.2    Srikumar, R.3    Poole, K.4
  • 9
    • 0029826961 scopus 로고    scopus 로고
    • In vivo oral efficacy of levofloxacin for treatment of systemic Pseudomonas aeruginosa infections in a murine model of septicemia
    • S. K. Yagel J. F. Barrett D. J. Amaratunga M. B. Frosco In vivo oral efficacy of levofloxacin for treatment of systemic Pseudomonas aeruginosa infections in a murine model of septicemia Antimicrob. Agents Chemother. 1996 40 2 2894 2897
    • (1996) Antimicrob. Agents Chemother. , vol.40 , Issue.2 , pp. 2894-2897
    • Yagel, S.K.1    Barrett, J.F.2    Amaratunga, D.J.3    Frosco, M.B.4
  • 10
    • 0027494050 scopus 로고
    • Multiple antibiotic resistance in Pseudomonas aeruginosa: Evidence for involvement of an efflux operon
    • K. Poole K. Krebes C. Mcnally S. J. Neshat Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon J. Bacteriol. 1993 175 22 7363 7372
    • (1993) J. Bacteriol. , vol.175 , Issue.22 , pp. 7363-7372
    • Poole, K.1    Krebes, K.2    McNally, C.3    Neshat, S.J.4
  • 11
    • 0009463610 scopus 로고
    • Pseudomonas aeruginosa infections
    • ed. R. Germanier, Academic, New York, 317-351
    • S. Cryz, Pseudomonas aeruginosa infections, in Bacterial vaccine, ed., R. Germanier, Academic, New York, 1984, pp. 317-351
    • (1984) Bacterial Vaccine
    • Cryz, S.1
  • 12
    • 0021809838 scopus 로고
    • The contribution of exoproducts to virulence of Pseudomonas aeruginosa
    • T. I. Nicas B. H. Iglewski The contribution of exoproducts to virulence of Pseudomonas aeruginosa Can. J. Microbiol. 1985 31 4 387 392
    • (1985) Can. J. Microbiol. , vol.31 , Issue.4 , pp. 387-392
    • Nicas, T.I.1    Iglewski, B.H.2
  • 13
    • 0020825597 scopus 로고
    • Toxins of Pseudomonas aeruginosa: New perspectives
    • D. E. Woods B. H. Iglewski Toxins of Pseudomonas aeruginosa: new perspectives Clin. Infect. Dis. 1983 5 715 722
    • (1983) Clin. Infect. Dis. , vol.5 , pp. 715-722
    • Woods, D.E.1    Iglewski, B.H.2
  • 14
    • 0021327584 scopus 로고
    • Protection against fatal Pseudomonas aeruginosa burn wound sepsis by immunization with lipopolysaccharide and high-molecular-weight polysaccharide
    • S. J. Cryz E. Furer R. Germanier Protection against fatal Pseudomonas aeruginosa burn wound sepsis by immunization with lipopolysaccharide and high-molecular-weight polysaccharide Infect. Immun. 1984 4 3 795 799
    • (1984) Infect. Immun. , vol.4 , Issue.3 , pp. 795-799
    • Cryz, S.J.1    Furer, E.2    Germanier, R.3
  • 15
    • 0032831499 scopus 로고    scopus 로고
    • Genetics of antigen biosynthesis in Pseudomonas aeruginosa
    • H. L. Rocchetta L. L. Burrow J. S. Lam Genetics of antigen biosynthesis in Pseudomonas aeruginosa Microbiol. Mol. Biol. Rev. 1999 63 3 523 553
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , Issue.3 , pp. 523-553
    • Rocchetta, H.L.1    Burrow, L.L.2    Lam, J.S.3
  • 16
    • 0031458161 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa antigens as potential vaccines
    • E. S. Stanislavesky J. S. Lam Pseudomonas aeruginosa antigens as potential vaccines FEMS Microbiol. Rev. 1997 21 3 243 277
    • (1997) FEMS Microbiol. Rev. , vol.21 , Issue.3 , pp. 243-277
    • Stanislavesky, E.S.1    Lam, J.S.2
  • 17
    • 0025078706 scopus 로고
    • Polysaccharide antigens of Pseudomonas aeruginosa
    • Y. Knirel Polysaccharide antigens of Pseudomonas aeruginosa Crit. Rev. Microbiol. 1990 17 4 273 304
    • (1990) Crit. Rev. Microbiol. , vol.17 , Issue.4 , pp. 273-304
    • Knirel, Y.1
  • 19
    • 0032831499 scopus 로고    scopus 로고
    • Genetics of O-antigen biosynthesis in Pseudomonas aeruginosa
    • H. L. Rocchetta L. L. Burrows J. S. Lam Genetics of O-antigen biosynthesis in Pseudomonas aeruginosa Microbiol. Mol. Biol. Rev. 1999 63 3 523 553
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , Issue.3 , pp. 523-553
    • Rocchetta, H.L.1    Burrows, L.L.2    Lam, J.S.3
  • 21
    • 0034026605 scopus 로고    scopus 로고
    • Structural characterization of the outer core and the O-chain linkage region of lipopolysaccharide from Pseudomonas aeruginosa serotype O5
    • I. Sadovskaya J. R. Brisson P. Thibault J. C. Richards J. S. Lam E. Altman Structural characterization of the outer core and the O-chain linkage region of lipopolysaccharide from Pseudomonas aeruginosa serotype O5 Eur. J. Biochem. 2000 267 6 1640 1650
    • (2000) Eur. J. Biochem. , vol.267 , Issue.6 , pp. 1640-1650
    • Sadovskaya, I.1    Brisson, J.R.2    Thibault, P.3    Richards, J.C.4    Lam, J.S.5    Altman, E.6
  • 22
    • 0036233571 scopus 로고    scopus 로고
    • Structural studies on the core and the O-polysaccharide repeating unit of Pseudomonas aeruginosa immunotype 1 lipopolysaccharide
    • O. V. Bystrova A. S. Shashkov N. A. Kocharova Y. A. Knirel B. Lindner U. Zähringer G. B. Pier Structural studies on the core and the O-polysaccharide repeating unit of Pseudomonas aeruginosa immunotype 1 lipopolysaccharide Eur. J. Biochem. 2002 269 8 2194 2203
    • (2002) Eur. J. Biochem. , vol.269 , Issue.8 , pp. 2194-2203
    • Bystrova, O.V.1    Shashkov, A.S.2    Kocharova, N.A.3    Knirel, Y.A.4    Lindner, B.5    Zähringer, U.6    Pier, G.B.7
  • 23
    • 0036136149 scopus 로고    scopus 로고
    • WbjA adds glucose to complete the O-antigen trisaccharide repeating unit of the lipopolysaccharide of Pseudomonas aeruginosa serogroup O11
    • C. R. Dean A. Datta R. W. Carlson J. B. Goldberg WbjA adds glucose to complete the O-antigen trisaccharide repeating unit of the lipopolysaccharide of Pseudomonas aeruginosa serogroup O11 J. Bacteriol. 2002 184 1 323 326
    • (2002) J. Bacteriol. , vol.184 , Issue.1 , pp. 323-326
    • Dean, C.R.1    Datta, A.2    Carlson, R.W.3    Goldberg, J.B.4
  • 24
    • 0032145539 scopus 로고    scopus 로고
    • Structural elucidation of the lipopolysaccharide core regions of the wild-type strain PAO1 and O-chain-deficient mutant strains AK1401 and AK1012 from Pseudomonas aeruginosa serotype O5
    • I. Sadovskaya J. R. Brisson J. S. Lam J. C. Richards E. Altman Structural elucidation of the lipopolysaccharide core regions of the wild-type strain PAO1 and O-chain-deficient mutant strains AK1401 and AK1012 from Pseudomonas aeruginosa serotype O5 Eur. J. Biochem. 1998 255 3 673 684
    • (1998) Eur. J. Biochem. , vol.255 , Issue.3 , pp. 673-684
    • Sadovskaya, I.1    Brisson, J.R.2    Lam, J.S.3    Richards, J.C.4    Altman, E.5
  • 25
    • 0345097421 scopus 로고    scopus 로고
    • Structure of a highly phosphorylated lipopolysaccharide core in the Delta algC mutants derived from Pseudomonas aeruginosa wild-type strains PAO1 (serogroup O5) and PAC1R (serogroup O3)
    • O. Kooistra G. Bedoux L. Brecker B. Lindner P. Sanchez-Carballo D. Haras U. Zähringer Structure of a highly phosphorylated lipopolysaccharide core in the Delta algC mutants derived from Pseudomonas aeruginosa wild-type strains PAO1 (serogroup O5) and PAC1R (serogroup O3) Carbohydr. Res. 2003 338 23 2667 2677
    • (2003) Carbohydr. Res. , vol.338 , Issue.23 , pp. 2667-2677
    • Kooistra, O.1    Bedoux, G.2    Brecker, L.3    Lindner, B.4    Sanchez-Carballo, P.5    Haras, D.6    Zähringer, U.7
  • 26
    • 0344538424 scopus 로고    scopus 로고
    • Elucidation of the structure of an alanine-lacking core tetrasaccharide trisphosphate from the lipopolysaccharide of Pseudomonas aeruginosa mutant H4
    • P. M. Sanchez-Carballo E. T. Rietschel P. Kosma U. Zähringer Elucidation of the structure of an alanine-lacking core tetrasaccharide trisphosphate from the lipopolysaccharide of Pseudomonas aeruginosa mutant H4 Eur. J. Biochem. 1999 261 2 500 508
    • (1999) Eur. J. Biochem. , vol.261 , Issue.2 , pp. 500-508
    • Sanchez-Carballo, P.M.1    Rietschel, E.T.2    Kosma, P.3    Zähringer, U.4
  • 28
    • 0027918090 scopus 로고
    • Site-specific carbohydrate identification in recombinant proteins using MALD-TOF MS
    • M. C. Huberty J. E. Vath W. Yu S. A. Martin Site-specific carbohydrate identification in recombinant proteins using MALD-TOF MS Anal. Chem. 1993 65 20 2791 2800
    • (1993) Anal. Chem. , vol.65 , Issue.20 , pp. 2791-2800
    • Huberty, M.C.1    Vath, J.E.2    Yu, W.3    Martin, S.A.4
  • 29
    • 23044435003 scopus 로고    scopus 로고
    • Derivatization for stabilizing sialic acids in MALDI-MS
    • S. Sekiya S. Y. Wada Y. K. Tanaka Derivatization for stabilizing sialic acids in MALDI-MS Anal. Chem. 2005 77 15 4962 4968
    • (2005) Anal. Chem. , vol.77 , Issue.15 , pp. 4962-4968
    • Sekiya, S.1    Wada, S.Y.2    Tanaka, Y.K.3
  • 30
    • 41449096385 scopus 로고    scopus 로고
    • Ionic liquid matrixes optimized for MALDI-MS of sulfated/sialylated/ neutral oligosaccharides and glycopeptides
    • Y. Fukuyama S. Nakaya Y. Yamazaki K. Tanaka Ionic liquid matrixes optimized for MALDI-MS of sulfated/sialylated/neutral oligosaccharides and glycopeptides Anal. Chem. 2008 80 6 2171 2179
    • (2008) Anal. Chem. , vol.80 , Issue.6 , pp. 2171-2179
    • Fukuyama, Y.1    Nakaya, S.2    Yamazaki, Y.3    Tanaka, K.4
  • 31
    • 0030587060 scopus 로고    scopus 로고
    • Analysis of acidic oligosaccharides and glycopeptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Y. Fukuyama S. Nakaya Y. Yamazaki K. Tanaka Analysis of acidic oligosaccharides and glycopeptides by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry Anal. Chem. 1996 68 18 3215 3223
    • (1996) Anal. Chem. , vol.68 , Issue.18 , pp. 3215-3223
    • Fukuyama, Y.1    Nakaya, S.2    Yamazaki, Y.3    Tanaka, K.4
  • 34
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10 000 Daltons
    • M. Karas F. Hillenkamp Laser desorption ionization of proteins with molecular masses exceeding 10 000 Daltons Anal. Chem. 1988 60 20 2299 2301
    • (1988) Anal. Chem. , vol.60 , Issue.20 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 35
    • 0025512408 scopus 로고
    • Laser desorption ionization mass spectrometry of large biomolecules
    • M. Karas U. Bahr Laser desorption ionization mass spectrometry of large biomolecules TrAC, Trends Anal. Chem. 1990 9 10 321 325
    • (1990) TrAC, Trends Anal. Chem. , vol.9 , Issue.10 , pp. 321-325
    • Karas, M.1    Bahr, U.2
  • 36
    • 0035151362 scopus 로고    scopus 로고
    • Phyloproteomics: Species identification of Enterobacteriaceae using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • G. C. Conway S. C. Smole D. A. Sarraeino R. D. Arbeit P. E. Leopold Phyloproteomics: species identification of Enterobacteriaceae using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry J. Mol. Microbiol. Biotechnol. 2001 3 1 103 112
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , Issue.1 , pp. 103-112
    • Conway, G.C.1    Smole, S.C.2    Sarraeino, D.A.3    Arbeit, R.D.4    Leopold, P.E.5
  • 38
    • 39749093671 scopus 로고    scopus 로고
    • Highly efficient classification and identification of human pathogenic bacteria by MALDI-TOF MS
    • S. Y. Hsieh C. L. Tseng Y. S. Lee A. Kuo C. F. Sun H. Lin Y. J. K. Chen Highly efficient classification and identification of human pathogenic bacteria by MALDI-TOF MS Mol. Cell. Proteomics 2008 7 8 448 456
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.8 , pp. 448-456
    • Hsieh, S.Y.1    Tseng, C.L.2    Lee, Y.S.3    Kuo, A.4    Sun, C.F.5    Lin, H.6    Chen, Y.J.K.7
  • 39
    • 45149125131 scopus 로고    scopus 로고
    • Evaluation of matrix-assisted laser desorption ionization-time-of-flight mass spectrometry in comparison to 16S rRNA gene sequencing for species identification of nonfermenting bacteria
    • A. Mellmann J. Cloud T. Maier U. Keckevoet I. Ramminger P. Iwen J. Dunn G. Hall D. Wilson P. Lasala M. Kostrzewa D. Harmsen Evaluation of matrix-assisted laser desorption ionization-time-of-flight mass spectrometry in comparison to 16S rRNA gene sequencing for species identification of nonfermenting bacteria J. Clin. Microbiol. 2008 46 8 1946 1954
    • (2008) J. Clin. Microbiol. , vol.46 , Issue.8 , pp. 1946-1954
    • Mellmann, A.1    Cloud, J.2    Maier, T.3    Keckevoet, U.4    Ramminger, I.5    Iwen, P.6    Dunn, J.7    Hall, G.8    Wilson, D.9    Lasala, P.10    Kostrzewa, M.11    Harmsen, D.12
  • 40
    • 0037232281 scopus 로고    scopus 로고
    • Detection and treatment of bloodstream infection: Laboratory reporting and antimicrobial management
    • E. L. Munson D. J. Diekema S. E. Beekmann K. C. Chapin G. V. Doern Detection and treatment of bloodstream infection: laboratory reporting and antimicrobial management J. Clin. Microbiol. 2003 41 1 495 497
    • (2003) J. Clin. Microbiol. , vol.41 , Issue.1 , pp. 495-497
    • Munson, E.L.1    Diekema, D.J.2    Beekmann, S.E.3    Chapin, K.C.4    Doern, G.V.5
  • 41
    • 67651108596 scopus 로고    scopus 로고
    • Ongoing revolution in bacteriology: Routine identification of bacteria by matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • P. Seng M. Drancourt F. Gouriet B. La Scola P. E. Fournier J. M. Rolain D. Raoult Ongoing revolution in bacteriology: routine identification of bacteria by matrix-assisted laser desorption ionization time-of-flight mass spectrometry Clin. Infect. Dis. 2009 49 4 543 150
    • (2009) Clin. Infect. Dis. , vol.49 , Issue.4 , pp. 543-150
    • Seng, P.1    Drancourt, M.2    Gouriet, F.3    La Scola, B.4    Fournier, P.E.5    Rolain, J.M.6    Raoult, D.7
  • 42
    • 0036149342 scopus 로고    scopus 로고
    • Sample preparation of Gram-positive bacteria for identification by matrix assisted laser desorption/ionization time-of-flight
    • S. C. Smole L. A. King P. E. Leopold R. D. Arbeit Sample preparation of Gram-positive bacteria for identification by matrix assisted laser desorption/ionization time-of-flight J. Microbiol. Methods 2002 48 2-3 107 115
    • (2002) J. Microbiol. Methods , vol.48 , Issue.23 , pp. 107-115
    • Smole, S.C.1    King, L.A.2    Leopold, P.E.3    Arbeit, R.D.4
  • 43
    • 79956303518 scopus 로고    scopus 로고
    • 3-Mercaptopropionic acid modified ZnSe quantum dots as the matrix for direct surface-assisted laser desorption/ionization mass spectrometric analysis of peptides/proteins from sodium salt solution
    • H. F. Wu F. T. Chung 3-Mercaptopropionic acid modified ZnSe quantum dots as the matrix for direct surface-assisted laser desorption/ionization mass spectrometric analysis of peptides/proteins from sodium salt solution Rapid Commun. Mass Spectrom. 2011 25 12 1779 1786
    • (2011) Rapid Commun. Mass Spectrom. , vol.25 , Issue.12 , pp. 1779-1786
    • Wu, H.F.1    Chung, F.T.2
  • 44
    • 66449135386 scopus 로고    scopus 로고
    • Quantum dots laser desorption/ionization MS: Multifunctional CdSe quantum dots as the matrix, concentrating probes and acceleration for microwave enzymatic digestion for peptide analysis and high resolution detection of proteins in a linear MALDI-TOF MS
    • K. Shrivas S. K. Kailasa H. F. Wu Quantum dots laser desorption/ ionization MS: multifunctional CdSe quantum dots as the matrix, concentrating probes and acceleration for microwave enzymatic digestion for peptide analysis and high resolution detection of proteins in a linear MALDI-TOF MS Proteomics 2009 9 10 2656 2667
    • (2009) Proteomics , vol.9 , Issue.10 , pp. 2656-2667
    • Shrivas, K.1    Kailasa, S.K.2    Wu, H.F.3
  • 45
    • 84862791918 scopus 로고    scopus 로고
    • Functionalized quantum dots with dopamine dithiocarbamate as the matrix for the quantification of efavirenz in human plasma and as affinity probes for rapid identification of microwave tryptic digested proteins in MALDI-TOF-MS
    • S. K. Kailasa H. F. Wu Functionalized quantum dots with dopamine dithiocarbamate as the matrix for the quantification of efavirenz in human plasma and as affinity probes for rapid identification of microwave tryptic digested proteins in MALDI-TOF-MS J. Proteomics 2012 75 10 2924 2933
    • (2012) J. Proteomics , vol.75 , Issue.10 , pp. 2924-2933
    • Kailasa, S.K.1    Wu, H.F.2
  • 46
    • 84867740778 scopus 로고    scopus 로고
    • A method to detect metal-drug complexes and their interactions with pathogenic bacteria via graphene nanosheet assist laser desorption/ionization mass spectrometry and biosensors
    • H. N. Abdelhamid H. F. Wu A method to detect metal-drug complexes and their interactions with pathogenic bacteria via graphene nanosheet assist laser desorption/ionization mass spectrometry and biosensors Anal. Chim. Acta 2012 751 94 104
    • (2012) Anal. Chim. Acta , vol.751 , pp. 94-104
    • Abdelhamid, H.N.1    Wu, H.F.2
  • 47
    • 84863251361 scopus 로고    scopus 로고
    • One-pot synthesis of dopamine dithiocarbamate functionalized gold nanoparticles for quantitative analysis of small molecules and phosphopeptides in SALDI- and MALDI-MS
    • S. K. Kailasa H. F. Wu One-pot synthesis of dopamine dithiocarbamate functionalized gold nanoparticles for quantitative analysis of small molecules and phosphopeptides in SALDI- and MALDI-MS Analyst 2012 137 7 1629 1638
    • (2012) Analyst , vol.137 , Issue.7 , pp. 1629-1638
    • Kailasa, S.K.1    Wu, H.F.2
  • 48
    • 0034096182 scopus 로고    scopus 로고
    • Characterisation of bacteria by matrix-assisted laser desorption/ionisation and electrospray mass spectrometry
    • B. L. Van Baar Characterisation of bacteria by matrix-assisted laser desorption/ionisation and electrospray mass spectrometry FEMS Microbiol. Rev. 2000 24 2 193 219
    • (2000) FEMS Microbiol. Rev. , vol.24 , Issue.2 , pp. 193-219
    • Van Baar, B.L.1
  • 49
    • 84862561043 scopus 로고    scopus 로고
    • Wound infection kinetics probed by MALDI-MS: Rapid profiling of Staphylococcus aureus in mice
    • J. L. Narayana J. Gopal H. F. Wu Wound infection kinetics probed by MALDI-MS: rapid profiling of Staphylococcus aureus in mice Analyst 2012 137 14 3372 3380
    • (2012) Analyst , vol.137 , Issue.14 , pp. 3372-3380
    • Narayana, J.L.1    Gopal, J.2    Wu, H.F.3
  • 50
    • 84860525394 scopus 로고    scopus 로고
    • Cell population based mass spectrometry using platinum nanodots for algal and fungal studies
    • M. Manikandan H. F. Wu N. Hasan Cell population based mass spectrometry using platinum nanodots for algal and fungal studies Biosens. Bioelectron. 2012 35 1 493 497
    • (2012) Biosens. Bioelectron. , vol.35 , Issue.1 , pp. 493-497
    • Manikandan, M.1    Wu, H.F.2    Hasan, N.3
  • 51
    • 84455208297 scopus 로고    scopus 로고
    • Ionic solution and nanoparticle assisted MALDI-MS as bacterial biosensors for rapid analysis of yogurt
    • C. H. Lee J. Gopal H. F. Wu Ionic solution and nanoparticle assisted MALDI-MS as bacterial biosensors for rapid analysis of yogurt Biosens. Bioelectron. 2012 31 1 77 83
    • (2012) Biosens. Bioelectron. , vol.31 , Issue.1 , pp. 77-83
    • Lee, C.H.1    Gopal, J.2    Wu, H.F.3
  • 52
    • 84862806667 scopus 로고    scopus 로고
    • Biofunctionalization of nanoparticle assisted mass spectrometry as biosensors for rapid detection of plant associated bacteria
    • F. Ahmad M. Siddiqui O. O. Babalola H. F. Wu Biofunctionalization of nanoparticle assisted mass spectrometry as biosensors for rapid detection of plant associated bacteria Biosens. Bioelectron. 2012 35 1 235 242
    • (2012) Biosens. Bioelectron. , vol.35 , Issue.1 , pp. 235-242
    • Ahmad, F.1    Siddiqui, M.2    Babalola, O.O.3    Wu, H.F.4
  • 53
    • 84862786223 scopus 로고    scopus 로고
    • Rapid and direct detection of in vivo kinetics of pathogenic bacterial infection from mouse blood and urine
    • J. Gopal C. H. Lee H. F. Wu Rapid and direct detection of in vivo kinetics of pathogenic bacterial infection from mouse blood and urine J. Proteomics 2012 75 10 2972 2982
    • (2012) J. Proteomics , vol.75 , Issue.10 , pp. 2972-2982
    • Gopal, J.1    Lee, C.H.2    Wu, H.F.3
  • 55
    • 0029120274 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of phospholipids
    • D. J. Harvey Matrix-assisted laser desorption/ionization mass spectrometry of phospholipids J. Mass Spectrom. 1995 30 1333 1346
    • (1995) J. Mass Spectrom. , vol.30 , pp. 1333-1346
    • Harvey, D.J.1
  • 56
    • 1442339662 scopus 로고    scopus 로고
    • In situ MALDI-TOF MS regional analysis of neutral phospholipids in lens tissue
    • M. Rujoi R. Estrada M. C. Yappert In situ MALDI-TOF MS regional analysis of neutral phospholipids in lens tissue Anal. Chem. 2004 76 6 1657 1663
    • (2004) Anal. Chem. , vol.76 , Issue.6 , pp. 1657-1663
    • Rujoi, M.1    Estrada, R.2    Yappert, M.C.3
  • 57
    • 0033080774 scopus 로고    scopus 로고
    • Lipid analysis by matrix-assisted laser desorption and ionization mass spectrometry: A methodological approach
    • J. Schiller J. Arnhold S. Benard M. Muller S. Reichl K. Arnold Lipid analysis by matrix-assisted laser desorption and ionization mass spectrometry: a methodological approach Anal. Biochem. 1999 267 1 46 56
    • (1999) Anal. Biochem. , vol.267 , Issue.1 , pp. 46-56
    • Schiller, J.1    Arnhold, J.2    Benard, S.3    Muller, M.4    Reichl, S.5    Arnold, K.6
  • 58
    • 0027409199 scopus 로고
    • Gas chromatography-mass spectrometry methods for analysis of 2- and 3-hydroxylated fatty acids: Application for endotoxin measurement
    • Z. Mielniczuk E. Mielniczuk L. Larsson Gas chromatography-mass spectrometry methods for analysis of 2- and 3-hydroxylated fatty acids: application for endotoxin measurement J. Microbiol. Methods 1993 17 91 102
    • (1993) J. Microbiol. Methods , vol.17 , pp. 91-102
    • Mielniczuk, Z.1    Mielniczuk, E.2    Larsson, L.3
  • 59
    • 29244477536 scopus 로고    scopus 로고
    • Shotgun lipidomics identifies cardiolipin depletion in diabetic myocardium linking altered substrate utilization with mitochondrial dysfunction
    • X. Han J. Yang H. Cheng K. Yang D. R. Abendschein R. W. Gross Shotgun lipidomics identifies cardiolipin depletion in diabetic myocardium linking altered substrate utilization with mitochondrial dysfunction Biochemistry 2005 44 50 16684 16694
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16684-16694
    • Han, X.1    Yang, J.2    Cheng, H.3    Yang, K.4    Abendschein, D.R.5    Gross, R.W.6
  • 60
    • 33746268123 scopus 로고    scopus 로고
    • Characterization of cardiolipin as the sodiated ions by positive-ion electrospray ionization with multiple stage quadrupole ion-trap mass spectrometry
    • F. F. Hsu J. Turk Characterization of cardiolipin as the sodiated ions by positive-ion electrospray ionization with multiple stage quadrupole ion-trap mass spectrometry J. Am. Soc. Mass Spectrom. 2006 17 8 1146 1157
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , Issue.8 , pp. 1146-1157
    • Hsu, F.F.1    Turk, J.2
  • 61
    • 33344470892 scopus 로고    scopus 로고
    • Characterization of cardiolipin from Escherichia coli by electrospray ionization with multiple stage quadrupole ion-trap mass spectrometric analysis of [M - 2H + Na]-ions
    • F. F. Hsu J. Turk Characterization of cardiolipin from Escherichia coli by electrospray ionization with multiple stage quadrupole ion-trap mass spectrometric analysis of [M - 2H + Na]-ions J. Am. Soc. Mass Spectrom. 2006 17 3 420 429
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , Issue.3 , pp. 420-429
    • Hsu, F.F.1    Turk, J.2
  • 62
    • 77950618109 scopus 로고    scopus 로고
    • Separation and characterization of cardiolipin molecular species by reverse-phase ion pair high-performance liquid chromatography-mass spectrometry
    • P. E. Minkler C. L. Hoppel Separation and characterization of cardiolipin molecular species by reverse-phase ion pair high-performance liquid chromatography-mass spectrometry J. Lipid Res. 2010 51 4 856 865
    • (2010) J. Lipid Res. , vol.51 , Issue.4 , pp. 856-865
    • Minkler, P.E.1    Hoppel, C.L.2
  • 64
    • 33847060357 scopus 로고    scopus 로고
    • Direct MALDI-MS analysis of cardiolipin from rat organs sections
    • H. Y. Wang S. N. Jackson A. S. Woods Direct MALDI-MS analysis of cardiolipin from rat organs sections J. Am. Soc. Mass Spectrom. 2007 18 3 567 577
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , Issue.3 , pp. 567-577
    • Wang, H.Y.1    Jackson, S.N.2    Woods, A.S.3
  • 65
    • 0033603353 scopus 로고    scopus 로고
    • 3 in Escherichia coli K12. Detection of 4-amino-4-deoxy-L-arabinose, phosphoethanolamine and palmitate
    • 3 in Escherichia coli K12. Detection of 4-amino-4-deoxy-L-arabinose, phosphoethanolamine and palmitate J. Biol. Chem. 1999 274 26 18503 18514
    • (1999) J. Biol. Chem. , vol.274 , Issue.26 , pp. 18503-18514
    • Zhou, Z.1    Lin, S.2    Cotter, R.J.3    Raetz, C.4
  • 66
    • 0035875750 scopus 로고    scopus 로고
    • Helicobacter mustelae lipid A structure differs from that of Helicobacter pylori
    • H. Therisod M. Monteiro M. Perry M. Caroff Helicobacter mustelae lipid A structure differs from that of Helicobacter pylori FEBS Lett. 2001 499 1-2 1 5
    • (2001) FEBS Lett. , vol.499 , Issue.12 , pp. 1-5
    • Therisod, H.1    Monteiro, M.2    Perry, M.3    Caroff, M.4
  • 67
    • 0030029484 scopus 로고    scopus 로고
    • Separation and characterization of O-deacylated lipooligosaccharides and glycans derived from Moraxella catarrhalis using capillary electrophoresis- electrospray mass spectrometry and tandem mass spectrometry
    • J. Kelly H. Masoud M. Perry J. Richards P. Thibauld Separation and characterization of O-deacylated lipooligosaccharides and glycans derived from Moraxella catarrhalis using capillary electrophoresis-electrospray mass spectrometry and tandem mass spectrometry Anal. Biochem. 1996 233 1 15 30
    • (1996) Anal. Biochem. , vol.233 , Issue.1 , pp. 15-30
    • Kelly, J.1    Masoud, H.2    Perry, M.3    Richards, J.4    Thibauld, P.5
  • 68
    • 38249042435 scopus 로고
    • Direct fatty acid profiling of complex lipids in intact algae by fast-atom-bombardment mass spectrometry
    • M. M. Ross R. A. Neihof J. E. Campana Direct fatty acid profiling of complex lipids in intact algae by fast-atom-bombardment mass spectrometry Anal. Chim. Acta 1986 181 149 157
    • (1986) Anal. Chim. Acta , vol.181 , pp. 149-157
    • Ross, M.M.1    Neihof, R.A.2    Campana, J.E.3
  • 70
    • 0023639410 scopus 로고
    • Profiling of bacteria by fast atom bombardment mass spectrometry
    • D. N. Heller R. J. Cotter C. Fenselau O. M. Uy Profiling of bacteria by fast atom bombardment mass spectrometry Anal. Chem. 1987 59 2806 2809
    • (1987) Anal. Chem. , vol.59 , pp. 2806-2809
    • Heller, D.N.1    Cotter, R.J.2    Fenselau, C.3    Uy, O.M.4
  • 71
    • 0027336821 scopus 로고
    • 252Cf plasma desorption mass spectrometry applied to the analysis of underivatized rough-type endotoxin preparations
    • M. Caroff C. Deprun D. Karibian 252Cf plasma desorption mass spectrometry applied to the analysis of underivatized rough-type endotoxin preparations J. Biol. Chem. 1993 268 12321 12324
    • (1993) J. Biol. Chem. , vol.268 , pp. 12321-12324
    • Caroff, M.1    Deprun, C.2    Karibian, D.3
  • 72
    • 0030977560 scopus 로고    scopus 로고
    • Structural characterization of the lipids A of three Bordetella bronchiseptica strains: Variability of fatty acid substitution
    • H. Zarrouk D. Karibian S. Bodie M. B. Perry J. C. Richards M. Caroff Structural characterization of the lipids A of three Bordetella bronchiseptica strains: variability of fatty acid substitution J. Bacteriol. 1997 179 11 3756 3760
    • (1997) J. Bacteriol. , vol.179 , Issue.11 , pp. 3756-3760
    • Zarrouk, H.1    Karibian, D.2    Bodie, S.3    Perry, M.B.4    Richards, J.C.5    Caroff, M.6
  • 74
    • 78951488892 scopus 로고    scopus 로고
    • Characterization of chitosan magnetic nanoparticles for in situ delivery of tissue plasminogen activator
    • J. P. Chen P. C. Yang Y. H. Ma T. Wu Characterization of chitosan magnetic nanoparticles for in situ delivery of tissue plasminogen activator Carbohydr. Polym. 2011 84 1 364 372
    • (2011) Carbohydr. Polym. , vol.84 , Issue.1 , pp. 364-372
    • Chen, J.P.1    Yang, P.C.2    Ma, Y.H.3    Wu, T.4
  • 76
    • 35348949138 scopus 로고    scopus 로고
    • Analysis of low molecular weight acids by negative mode matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • R. Shroff A. Muck A. Svatos Analysis of low molecular weight acids by negative mode matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Rapid Commun. Mass Spectrom. 2007 21 4 3295 3300
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , Issue.4 , pp. 3295-3300
    • Shroff, R.1    Muck, A.2    Svatos, A.3
  • 77
    • 84867324894 scopus 로고    scopus 로고
    • Rapid and direct detection of attomole adenosine triphosphate (ATP) by MALDI-MS using rutile titania chips
    • M. Manikandan N. Hasan H. F. Wu Rapid and direct detection of attomole adenosine triphosphate (ATP) by MALDI-MS using rutile titania chips Analyst 2012 137 5128 5134
    • (2012) Analyst , vol.137 , pp. 5128-5134
    • Manikandan, M.1    Hasan, N.2    Wu, H.F.3
  • 78
    • 78650866068 scopus 로고    scopus 로고
    • The lipid A phosphate position determines differential host Toll-like receptor 4 responses to phylogenetically related symbiotic and pathogenic bacteria
    • S. R. Coats A. B. Berezow T. T. To S. Jain B. W. Bainbridge K. P. Banani R. P. Darveau The lipid A phosphate position determines differential host Toll-like receptor 4 responses to phylogenetically related symbiotic and pathogenic bacteria Infect. Immun. 2011 79 1 203 210
    • (2011) Infect. Immun. , vol.79 , Issue.1 , pp. 203-210
    • Coats, S.R.1    Berezow, A.B.2    To, T.T.3    Jain, S.4    Bainbridge, B.W.5    Banani, K.P.6    Darveau, R.P.7
  • 79
    • 84867805923 scopus 로고    scopus 로고
    • Quantum dot applications endowing novelty to analytical proteomics
    • H. F. Wu J. Gopal H. N. Abdelhamid N. Hasan Quantum dot applications endowing novelty to analytical proteomics Proteomics 2012 12 19-20 2949 2961
    • (2012) Proteomics , vol.12 , Issue.1920 , pp. 2949-2961
    • Wu, H.F.1    Gopal, J.2    Abdelhamid, H.N.3    Hasan, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.