메뉴 건너뛰기




Volumn 69, Issue , 2015, Pages 209-254

Biomarker Characterization by MALDI-TOF/MS

Author keywords

Biofluids; Biomarkers; Clinical diagnosis; Immunoaffinity; Mass spectrometry; Matrix assisted laser desorption ionization time of flight mass spectrometry; Multivariate statistics; Nanomaterial

Indexed keywords

BIOLOGICAL MARKER; NANOMATERIAL;

EID: 84945478141     PISSN: 00652423     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.acc.2015.01.001     Document Type: Chapter
Times cited : (40)

References (320)
  • 1
    • 78149447309 scopus 로고    scopus 로고
    • A review of clinical diagnostic applications of liquid chromatography-tandem mass spectrometry
    • Shushan B. A review of clinical diagnostic applications of liquid chromatography-tandem mass spectrometry. Mass Spectrom. Rev. 2010, 29:930-944.
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 930-944
    • Shushan, B.1
  • 2
    • 78649315174 scopus 로고    scopus 로고
    • Mass-spectrometry-based clinical proteomics-a review and prospective
    • Parker C.E., Pearson T.W., Anderson N.L., Borchers C.H. Mass-spectrometry-based clinical proteomics-a review and prospective. Analyst 2010, 135:1830-1838.
    • (2010) Analyst , vol.135 , pp. 1830-1838
    • Parker, C.E.1    Pearson, T.W.2    Anderson, N.L.3    Borchers, C.H.4
  • 3
    • 80053492663 scopus 로고    scopus 로고
    • Current and future applications of mass spectrometry to the clinical laboratory
    • Strathmann F.G., Hoofnagle A.N. Current and future applications of mass spectrometry to the clinical laboratory. Am. J. Clin. Pathol. 2011, 136:609-616.
    • (2011) Am. J. Clin. Pathol. , vol.136 , pp. 609-616
    • Strathmann, F.G.1    Hoofnagle, A.N.2
  • 4
    • 24944449608 scopus 로고    scopus 로고
    • A review of current applications of mass spectrometry for biomarker/molecular tracer elucidation
    • Simoneit B.R. A review of current applications of mass spectrometry for biomarker/molecular tracer elucidation. Mass Spectrom. Rev. 2005, 24:719-765.
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 719-765
    • Simoneit, B.R.1
  • 5
    • 79952628909 scopus 로고    scopus 로고
    • Protein profiling for cancer biomarker discovery using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and infrared imaging: a review
    • Bakry R., Rainer M., Huck C.W., Bonn G.K. Protein profiling for cancer biomarker discovery using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and infrared imaging: a review. Anal. Chim. Acta 2011, 690:26-34.
    • (2011) Anal. Chim. Acta , vol.690 , pp. 26-34
    • Bakry, R.1    Rainer, M.2    Huck, C.W.3    Bonn, G.K.4
  • 6
    • 84879614117 scopus 로고    scopus 로고
    • Insights into tandem mass spectrometry for the laboratory endocrinology
    • Pagotto U., Fanelli F., Pasquali R. Insights into tandem mass spectrometry for the laboratory endocrinology. Rev. Endocr. Metab. Disord. 2013, 14:141.
    • (2013) Rev. Endocr. Metab. Disord. , vol.14 , pp. 141
    • Pagotto, U.1    Fanelli, F.2    Pasquali, R.3
  • 7
    • 84856432103 scopus 로고    scopus 로고
    • The coming of age of liquid chromatography coupled to tandem mass spectrometry in the endocrinology laboratory
    • Carvalho V.M. The coming of age of liquid chromatography coupled to tandem mass spectrometry in the endocrinology laboratory. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2012, 883-884:50-58.
    • (2012) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , pp. 50-58
    • Carvalho, V.M.1
  • 8
    • 77952801705 scopus 로고    scopus 로고
    • Liquid chromatography-tandem mass spectrometry applications in endocrinology
    • Kushnir M.M., Rockwood A.L., Bergquist J. Liquid chromatography-tandem mass spectrometry applications in endocrinology. Mass Spectrom. Rev. 2010, 29:480-502.
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 480-502
    • Kushnir, M.M.1    Rockwood, A.L.2    Bergquist, J.3
  • 9
    • 35948932643 scopus 로고    scopus 로고
    • Liquid chromatography tandem-mass spectrometry (LC-MS/MS)-technique and applications in endocrinology
    • Vogeser M., Parhofer K.G. Liquid chromatography tandem-mass spectrometry (LC-MS/MS)-technique and applications in endocrinology. Exp. Clin. Endocrinol. Diabetes 2007, 115:559-570.
    • (2007) Exp. Clin. Endocrinol. Diabetes , vol.115 , pp. 559-570
    • Vogeser, M.1    Parhofer, K.G.2
  • 10
    • 68949206409 scopus 로고    scopus 로고
    • Applying mass spectrometry-based proteomics to genetics, genomics and network biology
    • Gstaiger M., Aebersold R. Applying mass spectrometry-based proteomics to genetics, genomics and network biology. Nat. Rev. Genet. 2009, 10:617-627.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 617-627
    • Gstaiger, M.1    Aebersold, R.2
  • 11
    • 0036288945 scopus 로고    scopus 로고
    • Application of tandem mass spectrometry to biochemical genetics and newborn screening
    • Carpenter K.H., Wiley V. Application of tandem mass spectrometry to biochemical genetics and newborn screening. Clin. Chim. Acta 2002, 322:1-10.
    • (2002) Clin. Chim. Acta , vol.322 , pp. 1-10
    • Carpenter, K.H.1    Wiley, V.2
  • 12
    • 77958606301 scopus 로고    scopus 로고
    • Application and use of various mass spectrometry methods in clinical microbiology
    • Emonet S., Shah H.N., Cherkaoui A., Schrenzel J. Application and use of various mass spectrometry methods in clinical microbiology. Clin. Microbiol. Infect. 2010, 16:1604-1613.
    • (2010) Clin. Microbiol. Infect. , vol.16 , pp. 1604-1613
    • Emonet, S.1    Shah, H.N.2    Cherkaoui, A.3    Schrenzel, J.4
  • 13
    • 33645088717 scopus 로고    scopus 로고
    • Mass spectrometry in drug discovery: a current review
    • Feng W.Y. Mass spectrometry in drug discovery: a current review. Curr. Drug Discov. Technol. 2004, 1:295-312.
    • (2004) Curr. Drug Discov. Technol. , vol.1 , pp. 295-312
    • Feng, W.Y.1
  • 14
    • 49049090526 scopus 로고    scopus 로고
    • Review of a current role of mass spectrometry for proteome research
    • Chen C.H. Review of a current role of mass spectrometry for proteome research. Anal. Chim. Acta 2008, 624:16-36.
    • (2008) Anal. Chim. Acta , vol.624 , pp. 16-36
    • Chen, C.H.1
  • 15
    • 0017099267 scopus 로고
    • A new method for the determination of the major metabolite of prostaglandin F2alpha in human urine based on stable isotope dilution and gas chromatography-mass spectrometry
    • Brash A.R., Draffan G.H., Clare R.A., Baillie T.A. A new method for the determination of the major metabolite of prostaglandin F2alpha in human urine based on stable isotope dilution and gas chromatography-mass spectrometry. Biochem. Soc. Trans. 1976, 4:706-708.
    • (1976) Biochem. Soc. Trans. , vol.4 , pp. 706-708
    • Brash, A.R.1    Draffan, G.H.2    Clare, R.A.3    Baillie, T.A.4
  • 16
    • 0017410099 scopus 로고
    • Determination of clonazepam and its 7-amino metabolite in plasma and blood by gas chromatography-chemical ionization mass spectrometry
    • Min B.H., Garland W.A. Determination of clonazepam and its 7-amino metabolite in plasma and blood by gas chromatography-chemical ionization mass spectrometry. J. Chromatogr. 1977, 139:121-133.
    • (1977) J. Chromatogr. , vol.139 , pp. 121-133
    • Min, B.H.1    Garland, W.A.2
  • 17
    • 0016952509 scopus 로고
    • Determination of debrisoquin and its 4-hydroxy metabolite in plasma by gas chromatography/mass spectrometry
    • Malcolm S.L., Marten T.R. Determination of debrisoquin and its 4-hydroxy metabolite in plasma by gas chromatography/mass spectrometry. Anal. Chem. 1976, 48:807-809.
    • (1976) Anal. Chem. , vol.48 , pp. 807-809
    • Malcolm, S.L.1    Marten, T.R.2
  • 18
    • 0024789350 scopus 로고
    • Prenatal diagnosis of inherited metabolic disorders by stable isotope dilution GC-MS analysis of metabolites in amniotic fluid: review of four years experience
    • Jakobs C. Prenatal diagnosis of inherited metabolic disorders by stable isotope dilution GC-MS analysis of metabolites in amniotic fluid: review of four years experience. J. Inherit. Metab. Dis. 1989, 12(Suppl. 2):267-270.
    • (1989) J. Inherit. Metab. Dis. , vol.12 , pp. 267-270
    • Jakobs, C.1
  • 19
    • 0023053488 scopus 로고
    • Metabolic profiling with gas chromatography-mass spectrometry and its application to clinical medicine
    • Niwa T. Metabolic profiling with gas chromatography-mass spectrometry and its application to clinical medicine. J. Chromatogr. 1986, 379:313-345.
    • (1986) J. Chromatogr. , vol.379 , pp. 313-345
    • Niwa, T.1
  • 22
    • 84923112763 scopus 로고    scopus 로고
    • Bringing GC-MS profiling of steroids into clinical applications
    • Choi M.H., Chung B.C. Bringing GC-MS profiling of steroids into clinical applications. Mass Spectrom. Rev. 2014, 10.1002/mas.21436.
    • (2014) Mass Spectrom. Rev.
    • Choi, M.H.1    Chung, B.C.2
  • 23
    • 84903511605 scopus 로고    scopus 로고
    • GC-MS analysis of organic acids in human urine in clinical settings: a study of derivatization and other analytical parameters
    • Christou C., Gika H.G., Raikos N., Theodoridis G. GC-MS analysis of organic acids in human urine in clinical settings: a study of derivatization and other analytical parameters. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2014, 964:195-201.
    • (2014) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.964 , pp. 195-201
    • Christou, C.1    Gika, H.G.2    Raikos, N.3    Theodoridis, G.4
  • 24
    • 77955161078 scopus 로고    scopus 로고
    • Development of a quantitative metabolomic approach to study clinical human fecal water metabolome based on trimethylsilylation derivatization and GC/MS analysis
    • Gao X., Pujos-Guillot E., Sebedio J.L. Development of a quantitative metabolomic approach to study clinical human fecal water metabolome based on trimethylsilylation derivatization and GC/MS analysis. Anal. Chem. 2010, 82:6447-6456.
    • (2010) Anal. Chem. , vol.82 , pp. 6447-6456
    • Gao, X.1    Pujos-Guillot, E.2    Sebedio, J.L.3
  • 25
    • 0016710732 scopus 로고
    • GC-MS in clinical toxicological analyses
    • Bumler J., Jeger A. GC-MS in clinical toxicological analyses. Beitr. Gerichtl. Med. 1975, 33:177-181.
    • (1975) Beitr. Gerichtl. Med. , vol.33 , pp. 177-181
    • Bumler, J.1    Jeger, A.2
  • 26
    • 84860134406 scopus 로고    scopus 로고
    • Development and validation of a simple GC-MS method for the simultaneous determination of 11 anticholinesterase pesticides in blood-clinical and forensic toxicology applications
    • Papoutsis I., Mendonis M., Nikolaou P., Athanaselis S., Pistos C., Maravelias C., Spiliopoulou C. Development and validation of a simple GC-MS method for the simultaneous determination of 11 anticholinesterase pesticides in blood-clinical and forensic toxicology applications. J. Forensic Sci. 2012, 57:806-812.
    • (2012) J. Forensic Sci. , vol.57 , pp. 806-812
    • Papoutsis, I.1    Mendonis, M.2    Nikolaou, P.3    Athanaselis, S.4    Pistos, C.5    Maravelias, C.6    Spiliopoulou, C.7
  • 27
    • 33644974215 scopus 로고    scopus 로고
    • Comparison of an automated and point-of-care immunoassay to GC-MS for urine oxycodone testing in the clinical laboratory
    • Haller C.A., Stone J., Burke V., Branch J., Chen K., Gross S. Comparison of an automated and point-of-care immunoassay to GC-MS for urine oxycodone testing in the clinical laboratory. J. Anal. Toxicol. 2006, 30:106-111.
    • (2006) J. Anal. Toxicol. , vol.30 , pp. 106-111
    • Haller, C.A.1    Stone, J.2    Burke, V.3    Branch, J.4    Chen, K.5    Gross, S.6
  • 29
    • 77950368592 scopus 로고    scopus 로고
    • Maravelias, development and validation of an EI-GC-MS method for the determination of benzodiazepine drugs and their metabolites in blood: applications in clinical and forensic toxicology
    • Papoutsis S.A., Athanaselis P.D., Nikolaou C.M., Pistos C.A., Spiliopoulou C.P. Maravelias, development and validation of an EI-GC-MS method for the determination of benzodiazepine drugs and their metabolites in blood: applications in clinical and forensic toxicology. J. Pharm. Biomed. Anal. 2010, 52:609-614.
    • (2010) J. Pharm. Biomed. Anal. , vol.52 , pp. 609-614
    • Papoutsis, S.A.1    Athanaselis, P.D.2    Nikolaou, C.M.3    Pistos, C.A.4    Spiliopoulou, C.P.5
  • 30
    • 0034063415 scopus 로고    scopus 로고
    • GC-MS identification of sympathomimetic amine drugs in urine: rapid methodology applicable for emergency clinical toxicology
    • Valentine J.L., Middleton R. GC-MS identification of sympathomimetic amine drugs in urine: rapid methodology applicable for emergency clinical toxicology. J. Anal. Toxicol. 2000, 24:211-222.
    • (2000) J. Anal. Toxicol. , vol.24 , pp. 211-222
    • Valentine, J.L.1    Middleton, R.2
  • 31
    • 84880888372 scopus 로고    scopus 로고
    • Clinical validation of a highly sensitive GC-MS platform for routine urine drug screening and real-time reporting of up to 212 drugs
    • Nair H., Woo F., Hoofnagle A.N., Baird G.S. Clinical validation of a highly sensitive GC-MS platform for routine urine drug screening and real-time reporting of up to 212 drugs. J. Toxicol. 2013, 2013:1-7.
    • (2013) J. Toxicol. , vol.2013 , pp. 1-7
    • Nair, H.1    Woo, F.2    Hoofnagle, A.N.3    Baird, G.S.4
  • 32
    • 77949866490 scopus 로고    scopus 로고
    • Automated needle trap heart-cut GC/MS and needle trap comprehensive two-dimensional GC/TOF-MS for breath gas analysis in the clinical environment
    • Mieth M., Schubert J.K., Groger T., Sabel B., Kischkel S., Fuchs P., Hein D., Zimmermann R., Miekisch W. Automated needle trap heart-cut GC/MS and needle trap comprehensive two-dimensional GC/TOF-MS for breath gas analysis in the clinical environment. Anal. Chem. 2010, 82:2541-2551.
    • (2010) Anal. Chem. , vol.82 , pp. 2541-2551
    • Mieth, M.1    Schubert, J.K.2    Groger, T.3    Sabel, B.4    Kischkel, S.5    Fuchs, P.6    Hein, D.7    Zimmermann, R.8    Miekisch, W.9
  • 33
    • 84867373772 scopus 로고    scopus 로고
    • A workflow for the metabolomic/metabonomic investigation of exhaled breath using thermal desorption GC-MS
    • Guallar-Hoyas C., Turner M.A., Blackburn G.J., Wilson I.D., Thomas C.L. A workflow for the metabolomic/metabonomic investigation of exhaled breath using thermal desorption GC-MS. Bioanalysis 2012, 4:2227-2237.
    • (2012) Bioanalysis , vol.4 , pp. 2227-2237
    • Guallar-Hoyas, C.1    Turner, M.A.2    Blackburn, G.J.3    Wilson, I.D.4    Thomas, C.L.5
  • 34
    • 84867867754 scopus 로고    scopus 로고
    • Chemotherapy control by breath profile with application of SPME-GC/MS method
    • Ulanowska A., Trawinska E., Sawrycki P., Buszewski B. Chemotherapy control by breath profile with application of SPME-GC/MS method. J. Sep. Sci. 2012, 35:2908-2913.
    • (2012) J. Sep. Sci. , vol.35 , pp. 2908-2913
    • Ulanowska, A.1    Trawinska, E.2    Sawrycki, P.3    Buszewski, B.4
  • 35
    • 79951520246 scopus 로고    scopus 로고
    • Determination of volatile organic compounds in human breath for Helicobacter pylori detection by SPME-GC/MS
    • Ulanowska A., Kowalkowski T., Hrynkiewicz K., Jackowski M., Buszewski B. Determination of volatile organic compounds in human breath for Helicobacter pylori detection by SPME-GC/MS. Biomed. Chromatogr. 2011, 25:391-397.
    • (2011) Biomed. Chromatogr. , vol.25 , pp. 391-397
    • Ulanowska, A.1    Kowalkowski, T.2    Hrynkiewicz, K.3    Jackowski, M.4    Buszewski, B.5
  • 38
    • 0033552093 scopus 로고    scopus 로고
    • An optimized sampling and GC-MS analysis method for benzene in exhaled breath, as a biomarker for occupational exposure
    • Plebani C., Tranfo G., Salerno A., Panebianco A., Marcelloni A.M. An optimized sampling and GC-MS analysis method for benzene in exhaled breath, as a biomarker for occupational exposure. Talanta 1999, 50:409-412.
    • (1999) Talanta , vol.50 , pp. 409-412
    • Plebani, C.1    Tranfo, G.2    Salerno, A.3    Panebianco, A.4    Marcelloni, A.M.5
  • 40
    • 84890347130 scopus 로고    scopus 로고
    • Rapid diagnosis of TB using GC-MS and chemometrics
    • Dang N.A., Janssen H.G., Kolk A.H. Rapid diagnosis of TB using GC-MS and chemometrics. Bioanalysis 2013, 5:3079-3097.
    • (2013) Bioanalysis , vol.5 , pp. 3079-3097
    • Dang, N.A.1    Janssen, H.G.2    Kolk, A.H.3
  • 41
    • 48049103032 scopus 로고    scopus 로고
    • Dynamic liquid phase nanoextraction coupled to GC/MS for rapid analysis of methoxyacetophenone and anisaldehyde isomers in urine
    • Wu H.F., Yen J.H. Dynamic liquid phase nanoextraction coupled to GC/MS for rapid analysis of methoxyacetophenone and anisaldehyde isomers in urine. J. Sep. Sci. 2008, 31:2295-2302.
    • (2008) J. Sep. Sci. , vol.31 , pp. 2295-2302
    • Wu, H.F.1    Yen, J.H.2
  • 42
    • 85047682354 scopus 로고    scopus 로고
    • Analysis of 13C-mixed triacylglycerol in stool by bulk (EA-IRMS) and compound specific (GC/MS) methods
    • Slater C., Ling S.C., Preston T., Weaver L.T. Analysis of 13C-mixed triacylglycerol in stool by bulk (EA-IRMS) and compound specific (GC/MS) methods. Isotopes Environ. Health Stud. 2002, 38:79-86.
    • (2002) Isotopes Environ. Health Stud. , vol.38 , pp. 79-86
    • Slater, C.1    Ling, S.C.2    Preston, T.3    Weaver, L.T.4
  • 43
    • 84886808589 scopus 로고    scopus 로고
    • GC-MS analysis of ethanol and other volatile compounds in micro-volume blood samples-quantifying neonatal exposure
    • Cordell R.L., Pandya H., Hubbard M., Turner M.A., Monks P.S. GC-MS analysis of ethanol and other volatile compounds in micro-volume blood samples-quantifying neonatal exposure. Anal. Bioanal. Chem. 2013, 405:4139-4147.
    • (2013) Anal. Bioanal. Chem. , vol.405 , pp. 4139-4147
    • Cordell, R.L.1    Pandya, H.2    Hubbard, M.3    Turner, M.A.4    Monks, P.S.5
  • 44
    • 79951651945 scopus 로고    scopus 로고
    • GC/MS with post-column switching for large volume injection of headspace samples: sensitive determination of volatile organic compounds in human whole blood and urine
    • Watanabe K., Fujita H., Hasegawa K., Gonmori K., Suzuki O. GC/MS with post-column switching for large volume injection of headspace samples: sensitive determination of volatile organic compounds in human whole blood and urine. Anal. Chem. 2011, 83:1475-1479.
    • (2011) Anal. Chem. , vol.83 , pp. 1475-1479
    • Watanabe, K.1    Fujita, H.2    Hasegawa, K.3    Gonmori, K.4    Suzuki, O.5
  • 45
    • 84877633444 scopus 로고    scopus 로고
    • Implementation of liquid chromatography/mass spectrometry into the clinical laboratory
    • Wu A.H., French D. Implementation of liquid chromatography/mass spectrometry into the clinical laboratory. Clin. Chim. Acta 2013, 420:4-10.
    • (2013) Clin. Chim. Acta , vol.420 , pp. 4-10
    • Wu, A.H.1    French, D.2
  • 47
    • 80052539443 scopus 로고    scopus 로고
    • LC-MS/MS in the clinical laboratory-where to from here?
    • Grebe S.K., Singh R.J. LC-MS/MS in the clinical laboratory-where to from here?. Clin. Biochem. Rev. 2011, 32:5-31.
    • (2011) Clin. Biochem. Rev. , vol.32 , pp. 5-31
    • Grebe, S.K.1    Singh, R.J.2
  • 48
    • 84898035120 scopus 로고    scopus 로고
    • LC-MS/MS in the routine clinical laboratory: has its time come?
    • Leung K.S., Fong B.M. LC-MS/MS in the routine clinical laboratory: has its time come?. Anal. Bioanal. Chem. 2014, 406:2289-2301.
    • (2014) Anal. Bioanal. Chem. , vol.406 , pp. 2289-2301
    • Leung, K.S.1    Fong, B.M.2
  • 50
    • 84904356870 scopus 로고    scopus 로고
    • Multiplexing determination of small cell lung cancer biomarkers and their isovariants in serum by immunocapture LC-MS/MS
    • Torsetnes S.B., Levernaes M.S., Broughton M.N., Paus E., Halvorsen T.G., Reubsaet L. Multiplexing determination of small cell lung cancer biomarkers and their isovariants in serum by immunocapture LC-MS/MS. Anal. Chem. 2014, 86:6983-6992.
    • (2014) Anal. Chem. , vol.86 , pp. 6983-6992
    • Torsetnes, S.B.1    Levernaes, M.S.2    Broughton, M.N.3    Paus, E.4    Halvorsen, T.G.5    Reubsaet, L.6
  • 51
    • 34748879042 scopus 로고    scopus 로고
    • In vitro assessment of cytochrome P450 inhibition: strategies for increasing LC/MS-based assay throughput using a one-point IC(50) method and multiplexing high-performance liquid chromatography
    • Lin T., Pan K., Mordenti J., Pan L. In vitro assessment of cytochrome P450 inhibition: strategies for increasing LC/MS-based assay throughput using a one-point IC(50) method and multiplexing high-performance liquid chromatography. J. Pharm. Sci. 2007, 96:2485-2493.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 2485-2493
    • Lin, T.1    Pan, K.2    Mordenti, J.3    Pan, L.4
  • 53
    • 84899992538 scopus 로고    scopus 로고
    • Clinical applications of LC-MS sex steroid assays: evolution of methodologies in the 21st century
    • Ketha H., Kaur S., Grebe S.K., Singh R.J. Clinical applications of LC-MS sex steroid assays: evolution of methodologies in the 21st century. Curr. Opin. Endocrinol. 2014, 21:217-226.
    • (2014) Curr. Opin. Endocrinol. , vol.21 , pp. 217-226
    • Ketha, H.1    Kaur, S.2    Grebe, S.K.3    Singh, R.J.4
  • 54
    • 77955429127 scopus 로고    scopus 로고
    • Steroid measurement with LC-MS/MS. Application examples in pediatrics
    • Rauh M. Steroid measurement with LC-MS/MS. Application examples in pediatrics. J. Steroid Biochem. 2010, 121:520-527.
    • (2010) J. Steroid Biochem. , vol.121 , pp. 520-527
    • Rauh, M.1
  • 56
    • 78650883356 scopus 로고    scopus 로고
    • Current status and future developments of LC-MS/MS in clinical chemistry for quantification of biogenic amines
    • de Jong W.H., de Vries E.G., Kema I.P. Current status and future developments of LC-MS/MS in clinical chemistry for quantification of biogenic amines. Clin. Biochem. 2011, 44:95-103.
    • (2011) Clin. Biochem. , vol.44 , pp. 95-103
    • de Jong, W.H.1    de Vries, E.G.2    Kema, I.P.3
  • 57
    • 77951295305 scopus 로고    scopus 로고
    • LC-MS: a powerful tool in workplace drug testing
    • Gallardo E., Barroso M., Queiroz J.A. LC-MS: a powerful tool in workplace drug testing. Drug Test. Anal. 2009, 1:109-115.
    • (2009) Drug Test. Anal. , vol.1 , pp. 109-115
    • Gallardo, E.1    Barroso, M.2    Queiroz, J.A.3
  • 58
    • 16244422370 scopus 로고    scopus 로고
    • Effective use of liquid chromatography-mass spectrometry (LC/MS) in the routine clinical laboratory for monitoring sirolimus, tacrolimus, and cyclosporine
    • Poquette M.A., Lensmeyer G.L., Doran T.C. Effective use of liquid chromatography-mass spectrometry (LC/MS) in the routine clinical laboratory for monitoring sirolimus, tacrolimus, and cyclosporine. Ther. Drug Monit. 2005, 27:144-150.
    • (2005) Ther. Drug Monit. , vol.27 , pp. 144-150
    • Poquette, M.A.1    Lensmeyer, G.L.2    Doran, T.C.3
  • 60
    • 14844333118 scopus 로고    scopus 로고
    • Contemporary clinical usage of LC/MS: analysis of biologically important carboxylic acids
    • Johnson D.W. Contemporary clinical usage of LC/MS: analysis of biologically important carboxylic acids. Clin. Biochem. 2005, 38:351-361.
    • (2005) Clin. Biochem. , vol.38 , pp. 351-361
    • Johnson, D.W.1
  • 61
    • 82655178871 scopus 로고    scopus 로고
    • Analytical challenges: determination of tetrodotoxin in human urine and plasma by LC-MS/MS
    • Leung K.S., Fong B.M., Tsoi Y.K. Analytical challenges: determination of tetrodotoxin in human urine and plasma by LC-MS/MS. Mar. Drugs 2011, 9:2291-2303.
    • (2011) Mar. Drugs , vol.9 , pp. 2291-2303
    • Leung, K.S.1    Fong, B.M.2    Tsoi, Y.K.3
  • 62
    • 84881243291 scopus 로고    scopus 로고
    • Evaluation of two automated immunoassays for 25-OH vitamin D: comparison against LC-MS/MS
    • Hsu S.A., Soldo J., Gupta M. Evaluation of two automated immunoassays for 25-OH vitamin D: comparison against LC-MS/MS. J. Steroid Biochem. Mol. Biol. 2013, 136:139-145.
    • (2013) J. Steroid Biochem. Mol. Biol. , vol.136 , pp. 139-145
    • Hsu, S.A.1    Soldo, J.2    Gupta, M.3
  • 63
    • 85047687190 scopus 로고    scopus 로고
    • Simultaneous determination of vitamins D2 and D3 by LC-MS/MS in infant formula and adult nutritionals: First Action 2011.13
    • Gilliland D.L., Black C.K., Denison J.E., Seipelt C.T. Simultaneous determination of vitamins D2 and D3 by LC-MS/MS in infant formula and adult nutritionals: First Action 2011.13. J. AOAC Int. 2012, 95:583-587.
    • (2012) J. AOAC Int. , vol.95 , pp. 583-587
    • Gilliland, D.L.1    Black, C.K.2    Denison, J.E.3    Seipelt, C.T.4
  • 64
    • 34347377132 scopus 로고    scopus 로고
    • Compositional protein analysis of high density lipoproteins in hypercholesterolemia by shotgun LC-MS/MS and probabilistic peptide scoring
    • Heller M., Schlappritzi E., Stalder D., Nuoffer J.M., Haeberli A. Compositional protein analysis of high density lipoproteins in hypercholesterolemia by shotgun LC-MS/MS and probabilistic peptide scoring. Mol. Cell. Proteomics 2007, 6:1059-1072.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1059-1072
    • Heller, M.1    Schlappritzi, E.2    Stalder, D.3    Nuoffer, J.M.4    Haeberli, A.5
  • 65
    • 71649108493 scopus 로고    scopus 로고
    • Isotope coded protein label quantification of serum proteins-comparison with the label-free LC-MS and validation using the MRM approach
    • Turtoi A., Mazzucchelli G.D., De Pauw E. Isotope coded protein label quantification of serum proteins-comparison with the label-free LC-MS and validation using the MRM approach. Talanta 2010, 80:1487-1495.
    • (2010) Talanta , vol.80 , pp. 1487-1495
    • Turtoi, A.1    Mazzucchelli, G.D.2    De Pauw, E.3
  • 66
    • 84878051310 scopus 로고    scopus 로고
    • Statistical protein quantification and significance analysis in label-free LC-MS experiments with complex designs
    • Clough T., Thaminy S., Ragg S., Aebersold R., Vitek O. Statistical protein quantification and significance analysis in label-free LC-MS experiments with complex designs. BMC Bioinformatics 2012, 13(Suppl. 16):S6.
    • (2012) BMC Bioinformatics , vol.13 , pp. S6
    • Clough, T.1    Thaminy, S.2    Ragg, S.3    Aebersold, R.4    Vitek, O.5
  • 67
    • 84877796440 scopus 로고    scopus 로고
    • ComplexQuant: high-throughput computational pipeline for the global quantitative analysis of endogenous soluble protein complexes using high resolution protein HPLC and precision label-free LC/MS/MS
    • Wan C., Liu J., Fong V., Lugowski A., Stoilova S., Bethune-Waddell D., Borgeson B., Havugimana P.C., Marcotte E.M., Emili A. ComplexQuant: high-throughput computational pipeline for the global quantitative analysis of endogenous soluble protein complexes using high resolution protein HPLC and precision label-free LC/MS/MS. J. Proteomics 2013, 81:102-111.
    • (2013) J. Proteomics , vol.81 , pp. 102-111
    • Wan, C.1    Liu, J.2    Fong, V.3    Lugowski, A.4    Stoilova, S.5    Bethune-Waddell, D.6    Borgeson, B.7    Havugimana, P.C.8    Marcotte, E.M.9    Emili, A.10
  • 68
    • 34848862125 scopus 로고    scopus 로고
    • Label-free LC-MS/MS quantitative proteomics for large-scale biomarker discovery in complex samples
    • Levin Y., Schwarz E., Wang L., Leweke F.M., Bahn S. Label-free LC-MS/MS quantitative proteomics for large-scale biomarker discovery in complex samples. J. Sep. Sci. 2007, 30:2198-2203.
    • (2007) J. Sep. Sci. , vol.30 , pp. 2198-2203
    • Levin, Y.1    Schwarz, E.2    Wang, L.3    Leweke, F.M.4    Bahn, S.5
  • 69
    • 84862978357 scopus 로고    scopus 로고
    • Use of MDLC-DIGE and LC-MS/MS to identify serum biomarkers for complete remission in patients with acute myeloid leukemia
    • Lee S.W., Kim I.J., Jeong B.Y., Choi M.H., Kim J.Y., Kwon K.H., Lee J.W., Yu A., Shin M.G. Use of MDLC-DIGE and LC-MS/MS to identify serum biomarkers for complete remission in patients with acute myeloid leukemia. Electrophoresis 2012, 33:1863-1872.
    • (2012) Electrophoresis , vol.33 , pp. 1863-1872
    • Lee, S.W.1    Kim, I.J.2    Jeong, B.Y.3    Choi, M.H.4    Kim, J.Y.5    Kwon, K.H.6    Lee, J.W.7    Yu, A.8    Shin, M.G.9
  • 71
    • 84862978357 scopus 로고    scopus 로고
    • Use of MDLC-DIGE and LC-MS/MS to identify serum biomarkers for complete remission in patients with acute myeloid leukemia
    • Lee S.W., Kim I.J., Jeong B.Y., Choi M.H., Kim J.Y., Kwon K.H., Lee J.W., Yu A., Shin M.G. Use of MDLC-DIGE and LC-MS/MS to identify serum biomarkers for complete remission in patients with acute myeloid leukemia. Electrophoresis 2012, 33:1863-1872.
    • (2012) Electrophoresis , vol.33 , pp. 1863-1872
    • Lee, S.W.1    Kim, I.J.2    Jeong, B.Y.3    Choi, M.H.4    Kim, J.Y.5    Kwon, K.H.6    Lee, J.W.7    Yu, A.8    Shin, M.G.9
  • 75
    • 84920745938 scopus 로고    scopus 로고
    • LC-MS candidate reference methods for the harmonisation of parathyroid hormone (PTH) measurement: a review of recent developments and future considerations
    • Couchman L., Taylor D.R., Krastins B., Lopez M.F., Moniz C.F. LC-MS candidate reference methods for the harmonisation of parathyroid hormone (PTH) measurement: a review of recent developments and future considerations. Clin. Chem. Lab. Med. 2014, 52:1251-1263.
    • (2014) Clin. Chem. Lab. Med. , vol.52 , pp. 1251-1263
    • Couchman, L.1    Taylor, D.R.2    Krastins, B.3    Lopez, M.F.4    Moniz, C.F.5
  • 76
    • 84878208989 scopus 로고    scopus 로고
    • Hepcidin-25: measurement by LC-MS/MS in serum and urine, reference ranges and urinary fractional excretion
    • Wolff F., Deleers M., Melot C., Gulbis B., Cotton F. Hepcidin-25: measurement by LC-MS/MS in serum and urine, reference ranges and urinary fractional excretion. Clin. Chim. Acta 2013, 423:99-104.
    • (2013) Clin. Chim. Acta , vol.423 , pp. 99-104
    • Wolff, F.1    Deleers, M.2    Melot, C.3    Gulbis, B.4    Cotton, F.5
  • 77
    • 67349229546 scopus 로고    scopus 로고
    • Development of a method for the sensitive and quantitative determination of hepcidin in human serum using LC-MS/MS
    • Li H., Rose M.J., Tran L., Zhang J., Miranda L.P., James C.A., Sasu B.J. Development of a method for the sensitive and quantitative determination of hepcidin in human serum using LC-MS/MS. J. Pharmacol. Toxicol. Methods 2009, 59:171-180.
    • (2009) J. Pharmacol. Toxicol. Methods , vol.59 , pp. 171-180
    • Li, H.1    Rose, M.J.2    Tran, L.3    Zhang, J.4    Miranda, L.P.5    James, C.A.6    Sasu, B.J.7
  • 78
    • 84899508969 scopus 로고    scopus 로고
    • A simple and accurate HPLC method for fecal bile acid profile in healthy and cirrhotic subjects: validation by GC-MS and LC-MS
    • Kakiyama G., Muto A., Takei H., Nittono H., Murai T., Kurosawa T., Hofmann A.F., Pandak W.M., Bajaj J.S. A simple and accurate HPLC method for fecal bile acid profile in healthy and cirrhotic subjects: validation by GC-MS and LC-MS. J. Lipid Res. 2014, 55:978-990.
    • (2014) J. Lipid Res. , vol.55 , pp. 978-990
    • Kakiyama, G.1    Muto, A.2    Takei, H.3    Nittono, H.4    Murai, T.5    Kurosawa, T.6    Hofmann, A.F.7    Pandak, W.M.8    Bajaj, J.S.9
  • 80
    • 84877278993 scopus 로고    scopus 로고
    • Development and validation of an ultra-sensitive method for the measurement of plasma renin activity in human plasma via LC-MS/MS
    • Chappell D.L., McAvoy T., Weiss B., Weiner R., Laterza O.F. Development and validation of an ultra-sensitive method for the measurement of plasma renin activity in human plasma via LC-MS/MS. Bioanalysis 2012, 4:2843-2850.
    • (2012) Bioanalysis , vol.4 , pp. 2843-2850
    • Chappell, D.L.1    McAvoy, T.2    Weiss, B.3    Weiner, R.4    Laterza, O.F.5
  • 81
    • 27644598142 scopus 로고    scopus 로고
    • Ambient mass spectrometry using desorption electrospray ionization (DESI): instrumentation, mechanisms and applications in forensics, chemistry, and biology
    • Takats Z., Wiseman J.M., Cooks R.G. Ambient mass spectrometry using desorption electrospray ionization (DESI): instrumentation, mechanisms and applications in forensics, chemistry, and biology. J. Mass Spectrom. 2005, 40:1261-1275.
    • (2005) J. Mass Spectrom. , vol.40 , pp. 1261-1275
    • Takats, Z.1    Wiseman, J.M.2    Cooks, R.G.3
  • 82
    • 33645075709 scopus 로고    scopus 로고
    • Detection technologies. Ambient mass spectrometry
    • Cooks R.G., Ouyang Z., Takats Z., Wiseman J.M. Detection technologies. Ambient mass spectrometry. Science 2006, 311:1566-1570.
    • (2006) Science , vol.311 , pp. 1566-1570
    • Cooks, R.G.1    Ouyang, Z.2    Takats, Z.3    Wiseman, J.M.4
  • 85
    • 77949863848 scopus 로고    scopus 로고
    • Ambient ionization mass spectrometry: current understanding of mechanistic theory; analytical performance and application areas
    • Weston D.J. Ambient ionization mass spectrometry: current understanding of mechanistic theory; analytical performance and application areas. Analyst 2010, 135:661-668.
    • (2010) Analyst , vol.135 , pp. 661-668
    • Weston, D.J.1
  • 87
    • 84862552533 scopus 로고    scopus 로고
    • Characterization of proteins by ambient mass spectrometry
    • Yao Z.P. Characterization of proteins by ambient mass spectrometry. Mass Spectrom. Rev. 2012, 31:437-447.
    • (2012) Mass Spectrom. Rev. , vol.31 , pp. 437-447
    • Yao, Z.P.1
  • 88
    • 84877677478 scopus 로고    scopus 로고
    • Applications of ambient mass spectrometry in high-throughput screening
    • Li L.P., Feng B.S., Yang J.W., Chang C.L., Bai Y., Liu H.W. Applications of ambient mass spectrometry in high-throughput screening. Analyst 2013, 138:3097-3103.
    • (2013) Analyst , vol.138 , pp. 3097-3103
    • Li, L.P.1    Feng, B.S.2    Yang, J.W.3    Chang, C.L.4    Bai, Y.5    Liu, H.W.6
  • 89
    • 46849105446 scopus 로고    scopus 로고
    • Detection of native protein ions in aqueous solution under ambient conditions by electrospray laser desorption/ionization mass spectrometry
    • Shiea J., Yuan C.H., Huang M.Z., Cheng S.C., Ma Y.L., Tseng W.L., Chang H.C., Hung W.C. Detection of native protein ions in aqueous solution under ambient conditions by electrospray laser desorption/ionization mass spectrometry. Anal. Chem. 2008, 80:4845-4852.
    • (2008) Anal. Chem. , vol.80 , pp. 4845-4852
    • Shiea, J.1    Yuan, C.H.2    Huang, M.Z.3    Cheng, S.C.4    Ma, Y.L.5    Tseng, W.L.6    Chang, H.C.7    Hung, W.C.8
  • 90
    • 79952529218 scopus 로고    scopus 로고
    • A powerful couple in the future of clinical biochemistry: in situ analysis of dried blood spots by ambient mass spectrometry
    • Corso G., D'Apolito O., Gelzo M., Paglia G., Dello Russo A. A powerful couple in the future of clinical biochemistry: in situ analysis of dried blood spots by ambient mass spectrometry. Bioanalysis 2010, 2:1883-1891.
    • (2010) Bioanalysis , vol.2 , pp. 1883-1891
    • Corso, G.1    D'Apolito, O.2    Gelzo, M.3    Paglia, G.4    Dello Russo, A.5
  • 91
    • 36849053842 scopus 로고    scopus 로고
    • Neutral loss analysis of amino acids by desorption electrospray ionization using an unmodified tandem quadrupole mass spectrometer
    • Corso G., Paglia G., Garofalo D., D'Apolito O. Neutral loss analysis of amino acids by desorption electrospray ionization using an unmodified tandem quadrupole mass spectrometer. Rapid Commun. Mass Spectrom. 2007, 21:3777-3784.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3777-3784
    • Corso, G.1    Paglia, G.2    Garofalo, D.3    D'Apolito, O.4
  • 92
    • 77949803629 scopus 로고    scopus 로고
    • Direct analysis of dried blood spots utilizing desorption electrospray ionization (DESI) mass spectrometry
    • Wiseman J.M., Evans C.A., Bowen C.L., Kennedy J.H. Direct analysis of dried blood spots utilizing desorption electrospray ionization (DESI) mass spectrometry. Analyst 2010, 135:720-725.
    • (2010) Analyst , vol.135 , pp. 720-725
    • Wiseman, J.M.1    Evans, C.A.2    Bowen, C.L.3    Kennedy, J.H.4
  • 93
    • 79958708793 scopus 로고    scopus 로고
    • Direct analysis in real time coupled with dried spot sampling for bioanalysis in a drug-discovery setting
    • Crawford E., Gordon J., Wu J.T., Musselman B., Liu R., Yu S. Direct analysis in real time coupled with dried spot sampling for bioanalysis in a drug-discovery setting. Bioanalysis 2011, 3:1217-1226.
    • (2011) Bioanalysis , vol.3 , pp. 1217-1226
    • Crawford, E.1    Gordon, J.2    Wu, J.T.3    Musselman, B.4    Liu, R.5    Yu, S.6
  • 94
    • 84880407426 scopus 로고    scopus 로고
    • Quantitative paper spray mass spectrometry analysis of drugs of abuse
    • Su Y., Wang H., Liu J.J., Wei P., Cooks R.G., Ouyang Z. Quantitative paper spray mass spectrometry analysis of drugs of abuse. Analyst 2013, 138:4443-4447.
    • (2013) Analyst , vol.138 , pp. 4443-4447
    • Su, Y.1    Wang, H.2    Liu, J.J.3    Wei, P.4    Cooks, R.G.5    Ouyang, Z.6
  • 95
    • 84862963425 scopus 로고    scopus 로고
    • Silica coated paper substrate for paper-spray analysis of therapeutic drugs in dried blood spots
    • Zhang Z.P., Xu W., Manicke N.E., Cooks R.G., Ouyang Z. Silica coated paper substrate for paper-spray analysis of therapeutic drugs in dried blood spots. Anal. Chem. 2012, 84:931-938.
    • (2012) Anal. Chem. , vol.84 , pp. 931-938
    • Zhang, Z.P.1    Xu, W.2    Manicke, N.E.3    Cooks, R.G.4    Ouyang, Z.5
  • 96
    • 84880787578 scopus 로고    scopus 로고
    • Data-independent microbial metabolomics with ambient ionization mass spectrometry
    • Rath C.M., Yang J.Y., Alexandrov T., Dorrestein P.C. Data-independent microbial metabolomics with ambient ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 2013, 24:1167-1176.
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 1167-1176
    • Rath, C.M.1    Yang, J.Y.2    Alexandrov, T.3    Dorrestein, P.C.4
  • 98
    • 84864265204 scopus 로고    scopus 로고
    • Interactive hyperspectral approach for exploring and interpreting DESI-MS images of cancerous and normal tissue sections
    • Pirro V., Eberlin L.S., Oliveri P., Cooks R.G. Interactive hyperspectral approach for exploring and interpreting DESI-MS images of cancerous and normal tissue sections. Analyst 2012, 137:2374-2380.
    • (2012) Analyst , vol.137 , pp. 2374-2380
    • Pirro, V.1    Eberlin, L.S.2    Oliveri, P.3    Cooks, R.G.4
  • 99
    • 78651322735 scopus 로고    scopus 로고
    • New ionization methods and miniature mass spectrometers for biomedicine: DESI imaging for cancer diagnostics and paper spray ionization for therapeutic drug monitoring
    • Cooks R.G., Manicke N.E., Dill A.L., Ifa D.R., Eberlin L.S., Costa A.B., Wang H., Huang G.M., Zheng O.Y. New ionization methods and miniature mass spectrometers for biomedicine: DESI imaging for cancer diagnostics and paper spray ionization for therapeutic drug monitoring. Faraday Discuss. 2011, 149:247-267.
    • (2011) Faraday Discuss. , vol.149 , pp. 247-267
    • Cooks, R.G.1    Manicke, N.E.2    Dill, A.L.3    Ifa, D.R.4    Eberlin, L.S.5    Costa, A.B.6    Wang, H.7    Huang, G.M.8    Zheng, O.Y.9
  • 101
    • 84922562131 scopus 로고    scopus 로고
    • Through a glass darkly: glimpses into the future of mass spectrometry
    • Cooks R.G., Mueller T. Through a glass darkly: glimpses into the future of mass spectrometry. Mass Spectrom. 2013, 2:S0001.
    • (2013) Mass Spectrom. , vol.2 , pp. S0001
    • Cooks, R.G.1    Mueller, T.2
  • 102
    • 84945449217 scopus 로고    scopus 로고
    • Mass spectrometric methods and mass spectrometer for analyzing a vaporized sample
    • US patent
    • J. Shiea, Mass spectrometric methods and mass spectrometer for analyzing a vaporized sample, US patent 2010, US7,750,291 B2.
    • (2010)
    • Shiea, J.1
  • 103
    • 80054766993 scopus 로고    scopus 로고
    • Contribution of liquid-phase and gas-phase ionization in extractive electrospray ionization mass spectrometry of primary amines
    • Meier L., Schmid S., Berchtold C., Zenobi R. Contribution of liquid-phase and gas-phase ionization in extractive electrospray ionization mass spectrometry of primary amines. Eur. J. Mass Spectrom. 2011, 17:345-351.
    • (2011) Eur. J. Mass Spectrom. , vol.17 , pp. 345-351
    • Meier, L.1    Schmid, S.2    Berchtold, C.3    Zenobi, R.4
  • 104
    • 84863727473 scopus 로고    scopus 로고
    • Direct analysis of biological samples using extractive electrospray ionization mass spectrometry (EESI-MS)
    • Gu H., Xu N., Chen H. Direct analysis of biological samples using extractive electrospray ionization mass spectrometry (EESI-MS). Anal. Bioanal. Chem. 2012, 403:2145-2153.
    • (2012) Anal. Bioanal. Chem. , vol.403 , pp. 2145-2153
    • Gu, H.1    Xu, N.2    Chen, H.3
  • 105
    • 70349334667 scopus 로고    scopus 로고
    • Development of extractive electrospray ionization ion trap mass spectrometry for in vivo breath analysis
    • Ding J., Yang S., Liang D., Chen H., Wu Z., Zhang L., Ren Y. Development of extractive electrospray ionization ion trap mass spectrometry for in vivo breath analysis. Analyst 2009, 134:2040-2050.
    • (2009) Analyst , vol.134 , pp. 2040-2050
    • Ding, J.1    Yang, S.2    Liang, D.3    Chen, H.4    Wu, Z.5    Zhang, L.6    Ren, Y.7
  • 106
    • 84884161403 scopus 로고    scopus 로고
    • Robust detection of P. aeruginosa and S. aureus acute lung infections by secondary electrospray ionization-mass spectrometry (SESI-MS) breathprinting: from initial infection to clearance
    • Zhu J., Jimenez-Diaz J., Bean H.D., Daphtary N.A., Aliyeva M.I., Lundblad L.K., Hill J.E. Robust detection of P. aeruginosa and S. aureus acute lung infections by secondary electrospray ionization-mass spectrometry (SESI-MS) breathprinting: from initial infection to clearance. J. Breath Res. 2013, 7:037106.
    • (2013) J. Breath Res. , vol.7 , pp. 037106
    • Zhu, J.1    Jimenez-Diaz, J.2    Bean, H.D.3    Daphtary, N.A.4    Aliyeva, M.I.5    Lundblad, L.K.6    Hill, J.E.7
  • 107
    • 84878531072 scopus 로고    scopus 로고
    • Secondary electrospray ionization-mass spectrometry (SESI-MS) breathprinting of multiple bacterial lung pathogens, a mouse model study
    • Zhu J., Bean H.D., Jimenez-Diaz J., Hill J.E. Secondary electrospray ionization-mass spectrometry (SESI-MS) breathprinting of multiple bacterial lung pathogens, a mouse model study. J. Appl. Physiol. 2013, 114:1544-1549.
    • (2013) J. Appl. Physiol. , vol.114 , pp. 1544-1549
    • Zhu, J.1    Bean, H.D.2    Jimenez-Diaz, J.3    Hill, J.E.4
  • 108
    • 84874861549 scopus 로고    scopus 로고
    • Detecting bacterial lung infections: in vivo evaluation of in vitro volatile fingerprints
    • Zhu J., Bean H.D., Wargo M.J., Leclair L.W., Hill J.E. Detecting bacterial lung infections: in vivo evaluation of in vitro volatile fingerprints. J. Breath Res. 2013, 7:016003.
    • (2013) J. Breath Res. , vol.7 , pp. 016003
    • Zhu, J.1    Bean, H.D.2    Wargo, M.J.3    Leclair, L.W.4    Hill, J.E.5
  • 109
    • 84871770767 scopus 로고    scopus 로고
    • Monitoring diurnal changes in exhaled human breath
    • Sinues P.M., Kohler M., Zenobi R. Monitoring diurnal changes in exhaled human breath. Anal. Chem. 2013, 85:369-373.
    • (2013) Anal. Chem. , vol.85 , pp. 369-373
    • Sinues, P.M.1    Kohler, M.2    Zenobi, R.3
  • 110
    • 80355135222 scopus 로고    scopus 로고
    • Characterizing bacterial volatiles using secondary electrospray ionization mass spectrometry (SESI-MS)
    • Bean H.D., Zhu J., Hill J.E. Characterizing bacterial volatiles using secondary electrospray ionization mass spectrometry (SESI-MS). J. Vis. Exp. 2011, 52:e2664.
    • (2011) J. Vis. Exp. , vol.52 , pp. e2664
    • Bean, H.D.1    Zhu, J.2    Hill, J.E.3
  • 111
    • 79952550444 scopus 로고    scopus 로고
    • Secondary electrospray ionization-mass spectrometry: breath study on a control group
    • Martinez-Lozano P., Zingaro L., Finiguerra A., Cristoni S. Secondary electrospray ionization-mass spectrometry: breath study on a control group. J. Breath Res. 2011, 5:016002.
    • (2011) J. Breath Res. , vol.5 , pp. 016002
    • Martinez-Lozano, P.1    Zingaro, L.2    Finiguerra, A.3    Cristoni, S.4
  • 114
    • 0025677738 scopus 로고
    • Mass-spectrometry of peptides and proteins by matrix-assisted ultraviolet-laser desorption ionization
    • Hillenkamp F., Karas M. Mass-spectrometry of peptides and proteins by matrix-assisted ultraviolet-laser desorption ionization. Methods Enzymol. 1990, 193:280-295.
    • (1990) Methods Enzymol. , vol.193 , pp. 280-295
    • Hillenkamp, F.1    Karas, M.2
  • 115
    • 0028484542 scopus 로고
    • Mass determination of human-immunoglobulin IgM using matrix-assisted laser-desorption ionization time-of-flight mass-spectrometry
    • Nelson R.W., Dogruel D., Williams P. Mass determination of human-immunoglobulin IgM using matrix-assisted laser-desorption ionization time-of-flight mass-spectrometry. Rapid Commun. Mass Spectrom. 1994, 8:627-631.
    • (1994) Rapid Commun. Mass Spectrom. , vol.8 , pp. 627-631
    • Nelson, R.W.1    Dogruel, D.2    Williams, P.3
  • 116
    • 20544468239 scopus 로고    scopus 로고
    • High-throughput proteomics using matrix-assisted laser desorption/ionization mass spectrometry
    • Cramer R., Gobom J., Nordhoff E. High-throughput proteomics using matrix-assisted laser desorption/ionization mass spectrometry. Expert Rev. Proteomics 2005, 2:407-420.
    • (2005) Expert Rev. Proteomics , vol.2 , pp. 407-420
    • Cramer, R.1    Gobom, J.2    Nordhoff, E.3
  • 117
    • 0029146356 scopus 로고
    • Matrix-assisted laser-desorption ionization (MALDI) mass-spectrometry-a novel analytical tool in molecular-biology and biotechnology
    • Kaufmann R. Matrix-assisted laser-desorption ionization (MALDI) mass-spectrometry-a novel analytical tool in molecular-biology and biotechnology. J. Biotechnol. 1995, 41:155-175.
    • (1995) J. Biotechnol. , vol.41 , pp. 155-175
    • Kaufmann, R.1
  • 118
    • 3242890699 scopus 로고    scopus 로고
    • MALDI: more than peptide mass fingerprints
    • Stuhler K., Meyer H.E. MALDI: more than peptide mass fingerprints. Curr. Opin. Mol. Ther. 2004, 6:239-248.
    • (2004) Curr. Opin. Mol. Ther. , vol.6 , pp. 239-248
    • Stuhler, K.1    Meyer, H.E.2
  • 119
    • 77957755377 scopus 로고    scopus 로고
    • Effects of humidity on the dried-droplet sample preparation for MALDI-TOF MS peptide profiling
    • Umemura H., Kodera Y., Nomura F. Effects of humidity on the dried-droplet sample preparation for MALDI-TOF MS peptide profiling. Clin. Chim. Acta 2010, 411:2109-2111.
    • (2010) Clin. Chim. Acta , vol.411 , pp. 2109-2111
    • Umemura, H.1    Kodera, Y.2    Nomura, F.3
  • 120
    • 65549105934 scopus 로고    scopus 로고
    • Comparison between vacuum sublimed matrices and conventional dried droplet preparation in MALDI-TOF mass spectrometry
    • Jaskolla T.W., Karas M., Roth U., Steinert K., Menzel C., Reihs K. Comparison between vacuum sublimed matrices and conventional dried droplet preparation in MALDI-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 2009, 20:1104-1114.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1104-1114
    • Jaskolla, T.W.1    Karas, M.2    Roth, U.3    Steinert, K.4    Menzel, C.5    Reihs, K.6
  • 121
    • 47249106077 scopus 로고    scopus 로고
    • Matrix layer sample preparation: an improved MALDI-MS peptide analysis method for proteomic studies
    • Garaguso I., Borlak J. Matrix layer sample preparation: an improved MALDI-MS peptide analysis method for proteomic studies. Proteomics 2008, 8:2583-2595.
    • (2008) Proteomics , vol.8 , pp. 2583-2595
    • Garaguso, I.1    Borlak, J.2
  • 122
    • 33646429751 scopus 로고    scopus 로고
    • Three-layer matrix/sample preparation method for MALDI MS analysis of low nanomolar protein samples
    • Keller B.O., Li L. Three-layer matrix/sample preparation method for MALDI MS analysis of low nanomolar protein samples. J. Am. Soc. Mass Spectrom. 2006, 17:780-785.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 780-785
    • Keller, B.O.1    Li, L.2
  • 123
    • 26844536197 scopus 로고    scopus 로고
    • Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides
    • Zheng J., Li N., Ridyard M., Dai H., Robbins S.M., Li L. Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides. J. Proteome Res. 2005, 4:1709-1716.
    • (2005) J. Proteome Res. , vol.4 , pp. 1709-1716
    • Zheng, J.1    Li, N.2    Ridyard, M.3    Dai, H.4    Robbins, S.M.5    Li, L.6
  • 124
    • 0031264076 scopus 로고    scopus 로고
    • MALDI MS and strategies for protein analysis
    • Fenselau C. MALDI MS and strategies for protein analysis. Anal. Chem. 1997, 69:A661-A665.
    • (1997) Anal. Chem. , vol.69 , pp. A661-A665
    • Fenselau, C.1
  • 125
    • 0035139370 scopus 로고    scopus 로고
    • MALDI-TOF-MS analysis of protein and DNA
    • Bonk T., Humeny A. MALDI-TOF-MS analysis of protein and DNA. Neuroscientist 2001, 7:6-12.
    • (2001) Neuroscientist , vol.7 , pp. 6-12
    • Bonk, T.1    Humeny, A.2
  • 126
    • 84857118726 scopus 로고    scopus 로고
    • Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2007-2008
    • Harvey D.J. Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2007-2008. Mass Spectrom. Rev. 2012, 31:183-311.
    • (2012) Mass Spectrom. Rev. , vol.31 , pp. 183-311
    • Harvey, D.J.1
  • 129
    • 55249096201 scopus 로고    scopus 로고
    • Clinical proteomics in cancer research-promises and limitations of current two-dimensional gel electrophoresis
    • Iwadate Y. Clinical proteomics in cancer research-promises and limitations of current two-dimensional gel electrophoresis. Curr. Med. Chem. 2008, 15:2393-2400.
    • (2008) Curr. Med. Chem. , vol.15 , pp. 2393-2400
    • Iwadate, Y.1
  • 130
    • 22944438393 scopus 로고    scopus 로고
    • Application of MALDI-TOF mass spectrometry in screening and diagnostic research
    • Pusch W., Kostrzewa M. Application of MALDI-TOF mass spectrometry in screening and diagnostic research. Curr. Pharm. Des. 2005, 11:2577-2591.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 2577-2591
    • Pusch, W.1    Kostrzewa, M.2
  • 131
    • 0142227011 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in clinical chemistry
    • Marvin L.F., Roberts M.A., Fay L.B. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in clinical chemistry. Clin. Chim. Acta 2003, 337:11-21.
    • (2003) Clin. Chim. Acta , vol.337 , pp. 11-21
    • Marvin, L.F.1    Roberts, M.A.2    Fay, L.B.3
  • 132
    • 84856763848 scopus 로고    scopus 로고
    • Applications of MALDI-TOF mass spectrometry in clinical diagnostic microbiology
    • Croxatto A., Prod'hom G., Greub G. Applications of MALDI-TOF mass spectrometry in clinical diagnostic microbiology. FEMS Microbiol. Rev. 2012, 36:380-407.
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 380-407
    • Croxatto, A.1    Prod'hom, G.2    Greub, G.3
  • 133
    • 0033967208 scopus 로고    scopus 로고
    • Single-nucleotide polymorphism analysis by MALDI-TOF mass spectrometry
    • Griffin T.J., Smith L.M. Single-nucleotide polymorphism analysis by MALDI-TOF mass spectrometry. Trends Biotechnol. 2000, 18:77-84.
    • (2000) Trends Biotechnol. , vol.18 , pp. 77-84
    • Griffin, T.J.1    Smith, L.M.2
  • 134
    • 78349308405 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry-painting molecular pictures
    • Schwamborn K., Caprioli R.M. MALDI imaging mass spectrometry-painting molecular pictures. Mol. Oncol. 2010, 4:529-538.
    • (2010) Mol. Oncol. , vol.4 , pp. 529-538
    • Schwamborn, K.1    Caprioli, R.M.2
  • 135
    • 84870374901 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization/time-of-flight mass spectrometry for clinical diagnosis
    • Cho Y.T., Su H., Huang T.L., Chen H.C., Wu W.J., Wu P.C., Wu D.C., Shiea J. Matrix-assisted laser desorption ionization/time-of-flight mass spectrometry for clinical diagnosis. Clin. Chim. Acta 2013, 415:266-275.
    • (2013) Clin. Chim. Acta , vol.415 , pp. 266-275
    • Cho, Y.T.1    Su, H.2    Huang, T.L.3    Chen, H.C.4    Wu, W.J.5    Wu, P.C.6    Wu, D.C.7    Shiea, J.8
  • 137
    • 73949146997 scopus 로고    scopus 로고
    • Mass spectrometry tools for the classification and identification of bacteria
    • Sauer S., Kliem M. Mass spectrometry tools for the classification and identification of bacteria. Nat. Rev. Microbiol. 2010, 8:74-82.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 74-82
    • Sauer, S.1    Kliem, M.2
  • 138
    • 84856392317 scopus 로고    scopus 로고
    • MALDI-TOF MS in microbiological diagnostics-identification of microorganisms and beyond (mini review)
    • Wieser A., Schneider L., Jung J., Schubert S. MALDI-TOF MS in microbiological diagnostics-identification of microorganisms and beyond (mini review). Appl. Microbiol. Biotechnol. 2012, 93:965-974.
    • (2012) Appl. Microbiol. Biotechnol. , vol.93 , pp. 965-974
    • Wieser, A.1    Schneider, L.2    Jung, J.3    Schubert, S.4
  • 140
    • 84879779075 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization-time of flight mass spectrometry: a fundamental shift in the routine practice of clinical microbiology
    • Clark A.E., Kaleta E.J., Arora A., Wolk D.M. Matrix-assisted laser desorption ionization-time of flight mass spectrometry: a fundamental shift in the routine practice of clinical microbiology. Clin. Microbiol. Rev. 2013, 26:547-603.
    • (2013) Clin. Microbiol. Rev. , vol.26 , pp. 547-603
    • Clark, A.E.1    Kaleta, E.J.2    Arora, A.3    Wolk, D.M.4
  • 141
    • 82955233601 scopus 로고    scopus 로고
    • Advances in mass spectrometry for the identification of pathogens
    • Ho Y.P., Reddy P.M. Advances in mass spectrometry for the identification of pathogens. Mass Spectrom. Rev. 2011, 30:1203-1224.
    • (2011) Mass Spectrom. Rev. , vol.30 , pp. 1203-1224
    • Ho, Y.P.1    Reddy, P.M.2
  • 143
    • 85056039235 scopus 로고    scopus 로고
    • Application of MALDI-TOF mass spectrometry in clinical virology: a review
    • Cobo F. Application of MALDI-TOF mass spectrometry in clinical virology: a review. Open Virol. J. 2013, 7:84-90.
    • (2013) Open Virol. J. , vol.7 , pp. 84-90
    • Cobo, F.1
  • 144
    • 0035385154 scopus 로고    scopus 로고
    • Characterization of intact microorganisms by MALDI mass spectrometry
    • Fenselau C., Demirev P.A. Characterization of intact microorganisms by MALDI mass spectrometry. Mass Spectrom. Rev. 2001, 20:157-171.
    • (2001) Mass Spectrom. Rev. , vol.20 , pp. 157-171
    • Fenselau, C.1    Demirev, P.A.2
  • 145
    • 84875881008 scopus 로고    scopus 로고
    • MALDI mass spectrometry for nucleic acid analysis
    • Gao X., Tan B.H., Sugrue R.J., Tang K. MALDI mass spectrometry for nucleic acid analysis. Top. Curr. Chem. 2013, 331:55-77.
    • (2013) Top. Curr. Chem. , vol.331 , pp. 55-77
    • Gao, X.1    Tan, B.H.2    Sugrue, R.J.3    Tang, K.4
  • 146
    • 28544451371 scopus 로고    scopus 로고
    • Typing of single nucleotide polymorphisms by MALDI mass spectrometry: principles and diagnostic applications
    • Sauer S. Typing of single nucleotide polymorphisms by MALDI mass spectrometry: principles and diagnostic applications. Clin. Chim. Acta 2006, 363:95-105.
    • (2006) Clin. Chim. Acta , vol.363 , pp. 95-105
    • Sauer, S.1
  • 147
    • 14844303718 scopus 로고    scopus 로고
    • Genotyping single nucleotide polymorphisms by MALDI mass spectrometry in clinical applications
    • Tost J., Gut I.G. Genotyping single nucleotide polymorphisms by MALDI mass spectrometry in clinical applications. Clin. Biochem. 2005, 38:335-350.
    • (2005) Clin. Biochem. , vol.38 , pp. 335-350
    • Tost, J.1    Gut, I.G.2
  • 149
    • 0035557687 scopus 로고    scopus 로고
    • MALDI TOF mass spectrometry: an emerging platform for genomics and diagnostics
    • Leushner J. MALDI TOF mass spectrometry: an emerging platform for genomics and diagnostics. Expert Rev. Mol. Diagn. 2001, 1:11-18.
    • (2001) Expert Rev. Mol. Diagn. , vol.1 , pp. 11-18
    • Leushner, J.1
  • 151
    • 4344718528 scopus 로고    scopus 로고
    • MALDI-TOF mass spectrometry: a versatile tool for high-performance DNA analysis
    • Jurinke C., Oeth P., van den Boom D. MALDI-TOF mass spectrometry: a versatile tool for high-performance DNA analysis. Mol. Biotechnol. 2004, 26:147-164.
    • (2004) Mol. Biotechnol. , vol.26 , pp. 147-164
    • Jurinke, C.1    Oeth, P.2    van den Boom, D.3
  • 152
    • 33751001298 scopus 로고    scopus 로고
    • New developments in profiling and imaging of proteins from tissue sections by MALDI mass spectrometry
    • Chaurand P., Norris J.L., Cornett D.S., Mobley J.A., Caprioli R.M. New developments in profiling and imaging of proteins from tissue sections by MALDI mass spectrometry. J. Proteome Res. 2006, 5:2889-2900.
    • (2006) J. Proteome Res. , vol.5 , pp. 2889-2900
    • Chaurand, P.1    Norris, J.L.2    Cornett, D.S.3    Mobley, J.A.4    Caprioli, R.M.5
  • 153
    • 35848970035 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry: molecular snapshots of biochemical systems
    • Cornett D.S., Reyzer M.L., Chaurand P., Caprioli R.M. MALDI imaging mass spectrometry: molecular snapshots of biochemical systems. Nat. Methods 2007, 4:828-833.
    • (2007) Nat. Methods , vol.4 , pp. 828-833
    • Cornett, D.S.1    Reyzer, M.L.2    Chaurand, P.3    Caprioli, R.M.4
  • 154
    • 53549134461 scopus 로고    scopus 로고
    • Protein and peptides in pictures: imaging with MALDI mass spectrometry
    • Goodwin R.J., Pennington S.R., Pitt A.R. Protein and peptides in pictures: imaging with MALDI mass spectrometry. Proteomics 2008, 8:3785-3800.
    • (2008) Proteomics , vol.8 , pp. 3785-3800
    • Goodwin, R.J.1    Pennington, S.R.2    Pitt, A.R.3
  • 155
    • 51949104682 scopus 로고    scopus 로고
    • Peptides in the brain: mass spectrometry-based measurement approaches and challenges
    • Li L., Sweedler J.V. Peptides in the brain: mass spectrometry-based measurement approaches and challenges. Annu. Rev. Anal. Chem. 2008, 1:451-483.
    • (2008) Annu. Rev. Anal. Chem. , vol.1 , pp. 451-483
    • Li, L.1    Sweedler, J.V.2
  • 156
    • 50249147732 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry for direct tissue analysis: a new frontier for molecular histology
    • Walch A., Rauser S., Deininger S.O., Hofler H. MALDI imaging mass spectrometry for direct tissue analysis: a new frontier for molecular histology. Histochem. Cell Biol. 2008, 130:421-434.
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 421-434
    • Walch, A.1    Rauser, S.2    Deininger, S.O.3    Hofler, H.4
  • 158
    • 80052441199 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry for direct tissue analysis: technological advancements and recent applications
    • Balluff B., Schone C., Hofler H., Walch A. MALDI imaging mass spectrometry for direct tissue analysis: technological advancements and recent applications. Histochem. Cell Biol. 2011, 136:227-244.
    • (2011) Histochem. Cell Biol. , vol.136 , pp. 227-244
    • Balluff, B.1    Schone, C.2    Hofler, H.3    Walch, A.4
  • 160
    • 81055144381 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry: bridging biology and chemistry in drug development
    • Castellino S., Groseclose M.R., Wagner D. MALDI imaging mass spectrometry: bridging biology and chemistry in drug development. Bioanalysis 2011, 3:2427-2441.
    • (2011) Bioanalysis , vol.3 , pp. 2427-2441
    • Castellino, S.1    Groseclose, M.R.2    Wagner, D.3
  • 161
    • 79953186946 scopus 로고    scopus 로고
    • From whole-body sections down to cellular level, multiscale imaging of phospholipids by MALDI mass spectrometry
    • O110.004259
    • Chaurand P., Cornett D.S., Angel P.M., Caprioli R.M. From whole-body sections down to cellular level, multiscale imaging of phospholipids by MALDI mass spectrometry. Mol. Cell Proteomic. 2011, 10. O110.004259.
    • (2011) Mol. Cell Proteomic. , vol.10
    • Chaurand, P.1    Cornett, D.S.2    Angel, P.M.3    Caprioli, R.M.4
  • 162
    • 80053106303 scopus 로고    scopus 로고
    • MALDI mass spectrometry imaging in oncology (review)
    • Gemoll T., Roblick U.J., Habermann J.K. MALDI mass spectrometry imaging in oncology (review). Mol. Med. Rep. 2011, 4:1045-1051.
    • (2011) Mol. Med. Rep. , vol.4 , pp. 1045-1051
    • Gemoll, T.1    Roblick, U.J.2    Habermann, J.K.3
  • 163
    • 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
  • 165
    • 79251606950 scopus 로고    scopus 로고
    • MALDI Imaging Mass Spectrometry (MALDI-IMS)-application of spatial proteomics for ovarian cancer classification and diagnosis
    • Gustafsson J.O., Oehler M.K., Ruszkiewicz A., McColl S.R., Hoffmann P. MALDI Imaging Mass Spectrometry (MALDI-IMS)-application of spatial proteomics for ovarian cancer classification and diagnosis. Int. J. Mol. Sci. 2011, 12:773-794.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 773-794
    • Gustafsson, J.O.1    Oehler, M.K.2    Ruszkiewicz, A.3    McColl, S.R.4    Hoffmann, P.5
  • 166
    • 79951673520 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry of human tissue: method challenges and clinical perspectives
    • Seeley E.H., Caprioli R.M. MALDI imaging mass spectrometry of human tissue: method challenges and clinical perspectives. Trends Biotechnol. 2011, 29:136-143.
    • (2011) Trends Biotechnol. , vol.29 , pp. 136-143
    • Seeley, E.H.1    Caprioli, R.M.2
  • 167
    • 84865499147 scopus 로고    scopus 로고
    • Direct molecular tissue analysis by MALDI imaging mass spectrometry in the field of gastrointestinal disease
    • Balluff B., Rauser S., Ebert M.P., Siveke J.T., Hofler H., Walch A. Direct molecular tissue analysis by MALDI imaging mass spectrometry in the field of gastrointestinal disease. Gastroenterology 2012, 143:544-549.
    • (2012) Gastroenterology , vol.143 , pp. 544-549
    • Balluff, B.1    Rauser, S.2    Ebert, M.P.3    Siveke, J.T.4    Hofler, H.5    Walch, A.6
  • 168
    • 84894101339 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry and analysis of endogenous peptides
    • Chatterji B., Pich A. MALDI imaging mass spectrometry and analysis of endogenous peptides. Expert Rev. Proteomics 2013, 10:381-388.
    • (2013) Expert Rev. Proteomics , vol.10 , pp. 381-388
    • Chatterji, B.1    Pich, A.2
  • 169
    • 84879341172 scopus 로고    scopus 로고
    • Current frontiers in clinical research application of MALDI imaging mass spectrometry
    • Neubert P., Walch A. Current frontiers in clinical research application of MALDI imaging mass spectrometry. Expert Rev. Proteomics 2013, 10:259-273.
    • (2013) Expert Rev. Proteomics , vol.10 , pp. 259-273
    • Neubert, P.1    Walch, A.2
  • 170
    • 84891693836 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry in cancer research: combining proteomic profiling and histological evaluation
    • Schone C., Hofler H., Walch A. MALDI imaging mass spectrometry in cancer research: combining proteomic profiling and histological evaluation. Clin. Biochem. 2013, 46:539-545.
    • (2013) Clin. Biochem. , vol.46 , pp. 539-545
    • Schone, C.1    Hofler, H.2    Walch, A.3
  • 171
    • 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
  • 172
    • 84920363781 scopus 로고    scopus 로고
    • MALDI mass spectrometry imaging of formalin-fixed paraffin-embedded tissues in clinical research
    • Gorzolka K., Walch A. MALDI mass spectrometry imaging of formalin-fixed paraffin-embedded tissues in clinical research. Histol. Histopathol. 2014, 29:1365-1376.
    • (2014) Histol. Histopathol. , vol.29 , pp. 1365-1376
    • Gorzolka, K.1    Walch, A.2
  • 174
    • 34248334942 scopus 로고    scopus 로고
    • Reproducibility in protein profiling by MALDI-TOF mass spectrometry
    • Albrethsen J. Reproducibility in protein profiling by MALDI-TOF mass spectrometry. Clin. Chem. 2007, 53:852-858.
    • (2007) Clin. Chem. , vol.53 , pp. 852-858
    • Albrethsen, J.1
  • 176
    • 79955842913 scopus 로고    scopus 로고
    • Production of reliable MALDI spectra with quality threshold clustering of replicates
    • Olson M.T., Epstein J.A., Sackett D.L., Yergey A.L. Production of reliable MALDI spectra with quality threshold clustering of replicates. J. Am. Soc. Mass Spectrom. 2011, 22:969-975.
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 969-975
    • Olson, M.T.1    Epstein, J.A.2    Sackett, D.L.3    Yergey, A.L.4
  • 179
    • 33748417283 scopus 로고    scopus 로고
    • Proteomic profiling in musculoskeletal oncology by MALDI mass spectrometry
    • Holt G.E., Schwartz H.S., Caldwell R.L. Proteomic profiling in musculoskeletal oncology by MALDI mass spectrometry. Clin. Orthop. Relat. Res. 2006, 450:105-110.
    • (2006) Clin. Orthop. Relat. Res. , vol.450 , pp. 105-110
    • Holt, G.E.1    Schwartz, H.S.2    Caldwell, R.L.3
  • 180
    • 84934440900 scopus 로고    scopus 로고
    • A novel approach using MALDI-TOF/TOF mass spectrometry and prestructured sample supports (AnchorChip Technology) for proteomic profiling and protein identification
    • Leung S.M., Pitts R.L. A novel approach using MALDI-TOF/TOF mass spectrometry and prestructured sample supports (AnchorChip Technology) for proteomic profiling and protein identification. Methods Mol. Biol. 2008, 441:57-70.
    • (2008) Methods Mol. Biol. , vol.441 , pp. 57-70
    • Leung, S.M.1    Pitts, R.L.2
  • 182
    • 70349921496 scopus 로고    scopus 로고
    • Proteomic expression profiling and identification of serum proteins using immobilized trypsin beads with MALDI-TOF/TOF
    • Karbassi I.D., Nyalwidhe J.O., Wilkins C.E., Cazares L.H., Lance R.S., Semmes O.J., Drake R.R. Proteomic expression profiling and identification of serum proteins using immobilized trypsin beads with MALDI-TOF/TOF. J. Proteome Res. 2009, 8:4182-4192.
    • (2009) J. Proteome Res. , vol.8 , pp. 4182-4192
    • Karbassi, I.D.1    Nyalwidhe, J.O.2    Wilkins, C.E.3    Cazares, L.H.4    Lance, R.S.5    Semmes, O.J.6    Drake, R.R.7
  • 183
    • 77958164420 scopus 로고    scopus 로고
    • Proteomic profiling of uremia in serum using magnetic bead-based sample fractionation and MALDI-TOF MS
    • Sui W., Dai Y., Zhang Y., Chen J., Liu H., Huang H. Proteomic profiling of uremia in serum using magnetic bead-based sample fractionation and MALDI-TOF MS. Ren. Fail. 2010, 32:1153-1159.
    • (2010) Ren. Fail. , vol.32 , pp. 1153-1159
    • Sui, W.1    Dai, Y.2    Zhang, Y.3    Chen, J.4    Liu, H.5    Huang, H.6
  • 184
    • 78049331682 scopus 로고    scopus 로고
    • Proteomic profiling of renal allograft rejection in serum using magnetic bead-based sample fractionation and MALDI-TOF MS
    • Sui W., Huang L., Dai Y., Chen J., Yan Q., Huang H. Proteomic profiling of renal allograft rejection in serum using magnetic bead-based sample fractionation and MALDI-TOF MS. Clin. Exp. Med. 2010, 10:259-268.
    • (2010) Clin. Exp. Med. , vol.10 , pp. 259-268
    • Sui, W.1    Huang, L.2    Dai, Y.3    Chen, J.4    Yan, Q.5    Huang, H.6
  • 185
    • 84860374289 scopus 로고    scopus 로고
    • Proteomic profiling of nephrotic syndrome in serum using magnetic bead based sample fractionation & MALDI-TOF MS
    • Sui W., Dai Y., Zhang Y., Chen J., Liu H., Huang H. Proteomic profiling of nephrotic syndrome in serum using magnetic bead based sample fractionation & MALDI-TOF MS. Indian J. Med. Res. 2012, 135:305-311.
    • (2012) Indian J. Med. Res. , vol.135 , pp. 305-311
    • Sui, W.1    Dai, Y.2    Zhang, Y.3    Chen, J.4    Liu, H.5    Huang, H.6
  • 186
    • 84892712389 scopus 로고    scopus 로고
    • Classical MALDI-MS versus CE-based ESI-MS proteomic profiling in urine for clinical applications
    • Albalat A., Husi H., Stalmach A., Schanstra J.P., Mischak H. Classical MALDI-MS versus CE-based ESI-MS proteomic profiling in urine for clinical applications. Bioanalysis 2014, 6:247-266.
    • (2014) Bioanalysis , vol.6 , pp. 247-266
    • Albalat, A.1    Husi, H.2    Stalmach, A.3    Schanstra, J.P.4    Mischak, H.5
  • 187
    • 79955462941 scopus 로고    scopus 로고
    • The first decade of MALDI protein profiling: a lesson in translational biomarker research
    • Albrethsen J. The first decade of MALDI protein profiling: a lesson in translational biomarker research. J. Proteomics 2011, 74:765-773.
    • (2011) J. Proteomics , vol.74 , pp. 765-773
    • Albrethsen, J.1
  • 188
    • 84866242689 scopus 로고    scopus 로고
    • Liquid chromatography tandem mass spectrometry determination of chemical markers and principal component analysis of Vitex agnus-castus L. fruits (Verbenaceae) and derived food supplements
    • Mari A., Montoro P., Pizza C., Piacente S. Liquid chromatography tandem mass spectrometry determination of chemical markers and principal component analysis of Vitex agnus-castus L. fruits (Verbenaceae) and derived food supplements. J. Pharm. Biomed. Anal. 2012, 70:224-230.
    • (2012) J. Pharm. Biomed. Anal. , vol.70 , pp. 224-230
    • Mari, A.1    Montoro, P.2    Pizza, C.3    Piacente, S.4
  • 189
    • 77955103205 scopus 로고    scopus 로고
    • Analysis of triglycerides in food items by desorption electrospray ionization mass spectrometry
    • Gerbig S., Takats Z. Analysis of triglycerides in food items by desorption electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom. 2010, 24:2186-2192.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 2186-2192
    • Gerbig, S.1    Takats, Z.2
  • 191
    • 84872619025 scopus 로고    scopus 로고
    • The use of principal component analysis in MALDI-TOF MS: a powerful tool for establishing a mini-optimized proteomic profile
    • Shao C., Tian Y., Dong Z., Gao J., Gao Y., Jia X., Guo G., Wen X., Jiang C., Zhang X. The use of principal component analysis in MALDI-TOF MS: a powerful tool for establishing a mini-optimized proteomic profile. Am. J. Biomed. Sci. 2012, 4:85-101.
    • (2012) Am. J. Biomed. Sci. , vol.4 , pp. 85-101
    • Shao, C.1    Tian, Y.2    Dong, Z.3    Gao, J.4    Gao, Y.5    Jia, X.6    Guo, G.7    Wen, X.8    Jiang, C.9    Zhang, X.10
  • 194
    • 61349147183 scopus 로고    scopus 로고
    • MALDI imaging combined with hierarchical clustering as a new tool for the interpretation of complex human cancers
    • Deininger S.O., Ebert M.P., Futterer A., Gerhard M., Rocken C. MALDI imaging combined with hierarchical clustering as a new tool for the interpretation of complex human cancers. J. Proteome Res. 2008, 7:5230-5236.
    • (2008) J. Proteome Res. , vol.7 , pp. 5230-5236
    • Deininger, S.O.1    Ebert, M.P.2    Futterer, A.3    Gerhard, M.4    Rocken, C.5
  • 197
    • 84944178665 scopus 로고
    • Hierarchical grouping to optimize an objective function
    • Ward J.H. Hierarchical grouping to optimize an objective function. J. Am. Stat. Assoc. 1963, 58:236-244.
    • (1963) J. Am. Stat. Assoc. , vol.58 , pp. 236-244
    • Ward, J.H.1
  • 200
  • 201
    • 84862819546 scopus 로고    scopus 로고
    • The study of interferences for diagnosing albuminuria by matrix-assisted laser desorption ionization/time-of-flight mass spectrometry
    • Cho Y.T., Chen Y.S., Hu J.L., Shiea J., Yeh S.M., Chen H.C., Lee Y.C., Wu D.C. The study of interferences for diagnosing albuminuria by matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. Clin. Chim. Acta 2012, 413:875-882.
    • (2012) Clin. Chim. Acta , vol.413 , pp. 875-882
    • Cho, Y.T.1    Chen, Y.S.2    Hu, J.L.3    Shiea, J.4    Yeh, S.M.5    Chen, H.C.6    Lee, Y.C.7    Wu, D.C.8
  • 202
    • 24044530723 scopus 로고    scopus 로고
    • Lysosomal metabolism of glycoproteins
    • Winchester B. Lysosomal metabolism of glycoproteins. Glycobiology 2005, 15:1R-15R.
    • (2005) Glycobiology , vol.15 , pp. 1R-15R
    • Winchester, B.1
  • 204
    • 84883314366 scopus 로고    scopus 로고
    • Oligosaccharide analysis in urine by MALDI-TOF mass spectrometry for the diagnosis of lysosomal storage diseases
    • Xia B., Asif G., Arthur L., Pervaiz M.A., Li X., Liu R., Cummings R.D., He M. Oligosaccharide analysis in urine by MALDI-TOF mass spectrometry for the diagnosis of lysosomal storage diseases. Clin. Chem. 2013, 59:1357-1368.
    • (2013) Clin. Chem. , vol.59 , pp. 1357-1368
    • Xia, B.1    Asif, G.2    Arthur, L.3    Pervaiz, M.A.4    Li, X.5    Liu, R.6    Cummings, R.D.7    He, M.8
  • 205
    • 0029768014 scopus 로고    scopus 로고
    • The in vivo glyco-oxidation of alpha- and beta-globins investigated by matrix-assisted laser desorption/ionization mass spectrometry
    • Lapolla A., Fedele D., Aronica R., Garbeglio M., D'Alpaos M., Seraglia R., Traldi P. The in vivo glyco-oxidation of alpha- and beta-globins investigated by matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 1996, 10:1133-1135.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1133-1135
    • Lapolla, A.1    Fedele, D.2    Aronica, R.3    Garbeglio, M.4    D'Alpaos, M.5    Seraglia, R.6    Traldi, P.7
  • 207
    • 0005176020 scopus 로고    scopus 로고
    • Further considerations on the use of matrix-assisted laser desorption/ionization mass spectrometry in the analysis of glycated globins
    • Resemann A., Mayer-Posner F.J., Lapolla A., Fedele D., D'Alpaos M., Traldi P. Further considerations on the use of matrix-assisted laser desorption/ionization mass spectrometry in the analysis of glycated globins. Rapid Commun. Mass Spectrom. 1998, 12:805-807.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 805-807
    • Resemann, A.1    Mayer-Posner, F.J.2    Lapolla, A.3    Fedele, D.4    D'Alpaos, M.5    Traldi, P.6
  • 210
    • 0034582197 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry, enzymatic digestion, and molecular modeling in the study of nonenzymatic glycation of IgG
    • Lapolla A., Fedele D., Garbeglio M., Martano L., Tonani R., Seraglia R., Favretto D., Fedrigo M.A., Traldi P. Matrix-assisted laser desorption/ionization mass spectrometry, enzymatic digestion, and molecular modeling in the study of nonenzymatic glycation of IgG. J. Am. Soc. Mass Spectrom. 2000, 11:153-159.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 153-159
    • Lapolla, A.1    Fedele, D.2    Garbeglio, M.3    Martano, L.4    Tonani, R.5    Seraglia, R.6    Favretto, D.7    Fedrigo, M.A.8    Traldi, P.9
  • 213
    • 34248577404 scopus 로고    scopus 로고
    • Multivariate analysis of matrix-assisted laser desorption/ionization mass spectrometric data related to glycoxidation products of human globins in nephropathic patients
    • Lapolla A., Ragazzi E., Andretta B., Fedele D., Tubaro M., Seraglia R., Molin L., Traldi P. Multivariate analysis of matrix-assisted laser desorption/ionization mass spectrometric data related to glycoxidation products of human globins in nephropathic patients. J. Am. Soc. Mass Spectrom. 2007, 18:1018-1023.
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1018-1023
    • Lapolla, A.1    Ragazzi, E.2    Andretta, B.3    Fedele, D.4    Tubaro, M.5    Seraglia, R.6    Molin, L.7    Traldi, P.8
  • 214
    • 65749103187 scopus 로고    scopus 로고
    • Serum free hemoglobin as a novel potential biomarker for acute ischemic stroke
    • Huang P.Y., Lo L.H., Chen Y.C., Lin R.T., Shiea J., Liu C.K. Serum free hemoglobin as a novel potential biomarker for acute ischemic stroke. J. Neurol. 2009, 256:625-631.
    • (2009) J. Neurol. , vol.256 , pp. 625-631
    • Huang, P.Y.1    Lo, L.H.2    Chen, Y.C.3    Lin, R.T.4    Shiea, J.5    Liu, C.K.6
  • 216
    • 33745141905 scopus 로고    scopus 로고
    • Regular transfusion lowers plasma free hemoglobin in children with sickle-cell disease at risk for stroke
    • Lezcano N.E., Odo N., Kutlar A., Brambilla D., Adams R.J. Regular transfusion lowers plasma free hemoglobin in children with sickle-cell disease at risk for stroke. Stroke 2006, 37:1424-1426.
    • (2006) Stroke , vol.37 , pp. 1424-1426
    • Lezcano, N.E.1    Odo, N.2    Kutlar, A.3    Brambilla, D.4    Adams, R.J.5
  • 218
    • 15944398355 scopus 로고    scopus 로고
    • The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease
    • Rother R.P., Bell L., Hillmen P., Gladwin M.T. The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease. JAMA 2005, 293:1653-1662.
    • (2005) JAMA , vol.293 , pp. 1653-1662
    • Rother, R.P.1    Bell, L.2    Hillmen, P.3    Gladwin, M.T.4
  • 219
    • 24144452810 scopus 로고    scopus 로고
    • Serum free hemoglobin concentrations in healthy individuals are related to haptoglobin type
    • Na N., Ouyang J., Taes Y.E., Delanghe J.R. Serum free hemoglobin concentrations in healthy individuals are related to haptoglobin type. Clin. Chem. 2005, 51:1754-1755.
    • (2005) Clin. Chem. , vol.51 , pp. 1754-1755
    • Na, N.1    Ouyang, J.2    Taes, Y.E.3    Delanghe, J.R.4
  • 220
    • 78650381240 scopus 로고    scopus 로고
    • Characterization of human neutrophil peptides (alpha-Defensins) in the tears of dry eye patients
    • Lo L.H., Wu P.C., Wu Y.C., Shiea J. Characterization of human neutrophil peptides (alpha-Defensins) in the tears of dry eye patients. Anal. Methods 2010, 2:1934-1940.
    • (2010) Anal. Methods , vol.2 , pp. 1934-1940
    • Lo, L.H.1    Wu, P.C.2    Wu, Y.C.3    Shiea, J.4
  • 223
    • 21244439383 scopus 로고    scopus 로고
    • Glyco-oxidation in diabetes and related diseases
    • Lapolla A., Fedele D., Traldi P. Glyco-oxidation in diabetes and related diseases. Clin. Chim. Acta 2005, 357:236-250.
    • (2005) Clin. Chim. Acta , vol.357 , pp. 236-250
    • Lapolla, A.1    Fedele, D.2    Traldi, P.3
  • 224
    • 62149085888 scopus 로고    scopus 로고
    • Low molecular weight proteins in urines from healthy subjects as well as diabetic, nephropathic and diabetic-nephropathic patients: a MALDI study
    • Lapolla A., Seraglia R., Molin L., Williams K., Cosma C., Reitano R., Sechi A., Ragazzi E., Traldi P. Low molecular weight proteins in urines from healthy subjects as well as diabetic, nephropathic and diabetic-nephropathic patients: a MALDI study. J. Mass Spectrom. 2009, 44:419-425.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 419-425
    • Lapolla, A.1    Seraglia, R.2    Molin, L.3    Williams, K.4    Cosma, C.5    Reitano, R.6    Sechi, A.7    Ragazzi, E.8    Traldi, P.9
  • 225
    • 80051721110 scopus 로고    scopus 로고
    • Urinary peptides as a diagnostic tool for renal failure detected by matrix-assisted laser desorption/ionisation mass spectrometry: an evaluation of their clinical significance
    • Lapolla A., Molin L., Seraglia R., Sechi A., Cosma C., Bonfante L., Chilelli N.C., Ragazzi E., Traldi P. Urinary peptides as a diagnostic tool for renal failure detected by matrix-assisted laser desorption/ionisation mass spectrometry: an evaluation of their clinical significance. Eur. J. Mass Spectrom. 2011, 17:245-253.
    • (2011) Eur. J. Mass Spectrom. , vol.17 , pp. 245-253
    • Lapolla, A.1    Molin, L.2    Seraglia, R.3    Sechi, A.4    Cosma, C.5    Bonfante, L.6    Chilelli, N.C.7    Ragazzi, E.8    Traldi, P.9
  • 226
    • 34250025453 scopus 로고    scopus 로고
    • Sample preparation and bioinformatics in MALDI profiling of urinary proteins
    • Zerefos P., Prados J., Kossida S., Kalousis A., Vlahou A. Sample preparation and bioinformatics in MALDI profiling of urinary proteins. J. Chromatogr. B 2007, 853:20-30.
    • (2007) J. Chromatogr. B , vol.853 , pp. 20-30
    • Zerefos, P.1    Prados, J.2    Kossida, S.3    Kalousis, A.4    Vlahou, A.5
  • 227
    • 84892486633 scopus 로고    scopus 로고
    • Micro extraction to quantitate spermidine and spermine in human urine and blood by matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • Lu C.Y., Su H.H., Chen Y.L., Tseng W.L. Micro extraction to quantitate spermidine and spermine in human urine and blood by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. J. Chromatogr. A 2014, 1326:1-6.
    • (2014) J. Chromatogr. A , vol.1326 , pp. 1-6
    • Lu, C.Y.1    Su, H.H.2    Chen, Y.L.3    Tseng, W.L.4
  • 228
    • 35348975693 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for the detection of hemoglobins as the protein biomarkers for fecal occult blood
    • Lin S.Y., Shih S.H., Wu D.C., Lee Y.C., Wu C.I., Lo L.H., Shiea J. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for the detection of hemoglobins as the protein biomarkers for fecal occult blood. Rapid Commun. Mass Spectrom. 2007, 21:3311-3316.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3311-3316
    • Lin, S.Y.1    Shih, S.H.2    Wu, D.C.3    Lee, Y.C.4    Wu, C.I.5    Lo, L.H.6    Shiea, J.7
  • 229
    • 34547896271 scopus 로고    scopus 로고
    • Diagnosis of occult blood in human feces using matrix-assisted laser desorption ionization/time-of-flight mass spectrometry
    • Wu C.I., Tsai C.C., Lu C.C., Wu P.C., Wu D.C., Lin S.Y., Shiea J. Diagnosis of occult blood in human feces using matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. Clin. Chim. Acta 2007, 384:86-92.
    • (2007) Clin. Chim. Acta , vol.384 , pp. 86-92
    • Wu, C.I.1    Tsai, C.C.2    Lu, C.C.3    Wu, P.C.4    Wu, D.C.5    Lin, S.Y.6    Shiea, J.7
  • 230
    • 84870335965 scopus 로고    scopus 로고
    • Occult blood detection in biological samples by laser desorption and matrix-assisted laser desorption/ionization mass spectrometry for biomedical applications
    • US patent
    • P.F. Scholl, P. Demirev, A.B. Feldman, Occult blood detection in biological samples by laser desorption and matrix-assisted laser desorption/ionization mass spectrometry for biomedical applications, US patent 2006, US7,109,038 B2.
    • (2006)
    • Scholl, P.F.1    Demirev, P.2    Feldman, A.B.3
  • 231
    • 58149383790 scopus 로고    scopus 로고
    • Quantitative matrix-assisted laser desorption/ionization mass spectrometry
    • Duncan M.W., Roder H., Hunsucker S.W. Quantitative matrix-assisted laser desorption/ionization mass spectrometry. Brief. Funct. Genomic. Proteomic. 2008, 7:355-370.
    • (2008) Brief. Funct. Genomic. Proteomic. , vol.7 , pp. 355-370
    • Duncan, M.W.1    Roder, H.2    Hunsucker, S.W.3
  • 232
    • 47249166413 scopus 로고    scopus 로고
    • Quantitative evaluation of sphingomyelin and glucosylceramide using matrix-assisted laser desorption ionization time-of-flight mass spectrometry with sphingosylphosphorylcholine as an internal standard practical application to tissues from patients with Niemann-Pick disease types A and C, and Gaucher disease
    • Fujiwaki T., Tasaka M., Yamaguchi S. Quantitative evaluation of sphingomyelin and glucosylceramide using matrix-assisted laser desorption ionization time-of-flight mass spectrometry with sphingosylphosphorylcholine as an internal standard practical application to tissues from patients with Niemann-Pick disease types A and C, and Gaucher disease. J. Chromatogr. B 2008, 870:170-176.
    • (2008) J. Chromatogr. B , vol.870 , pp. 170-176
    • Fujiwaki, T.1    Tasaka, M.2    Yamaguchi, S.3
  • 233
    • 32244433826 scopus 로고    scopus 로고
    • Quantitative evaluation of sphingolipids using delayed extraction matrix-assisted laser desorption ionization time-of-flight mass spectrometry with sphingosylphosphorylcholine as an internal standard-practical application to cardiac valves from a patient with Fabry disease
    • Fujiwaki T., Tasaka M., Takahashi N., Kobayashi H., Murakami Y., Shimada T., Yamaguchi S. Quantitative evaluation of sphingolipids using delayed extraction matrix-assisted laser desorption ionization time-of-flight mass spectrometry with sphingosylphosphorylcholine as an internal standard-practical application to cardiac valves from a patient with Fabry disease. J. Chromatogr. B 2006, 832:97-102.
    • (2006) J. Chromatogr. B , vol.832 , pp. 97-102
    • Fujiwaki, T.1    Tasaka, M.2    Takahashi, N.3    Kobayashi, H.4    Murakami, Y.5    Shimada, T.6    Yamaguchi, S.7
  • 234
    • 0037365165 scopus 로고    scopus 로고
    • Quantification of bile acids directly from urine by MALDI-TOF-MS
    • Mims D., Hercules D. Quantification of bile acids directly from urine by MALDI-TOF-MS. Anal. Bioanal. Chem. 2003, 375:609-616.
    • (2003) Anal. Bioanal. Chem. , vol.375 , pp. 609-616
    • Mims, D.1    Hercules, D.2
  • 235
    • 16244390349 scopus 로고    scopus 로고
    • Quantification of bile acids directly from plasma by MALDI-TOF-MS
    • Mims D., Hercules D. Quantification of bile acids directly from plasma by MALDI-TOF-MS. Anal. Bioanal. Chem. 2004, 378:1322-1326.
    • (2004) Anal. Bioanal. Chem. , vol.378 , pp. 1322-1326
    • Mims, D.1    Hercules, D.2
  • 237
    • 84878663507 scopus 로고    scopus 로고
    • Screening analysis of 10 adrenal steroids by matrix-assisted laser desorption ionization-tandem mass spectrometry
    • Kim S.J., Jung H.J., Chung B.C., Choi M.H. Screening analysis of 10 adrenal steroids by matrix-assisted laser desorption ionization-tandem mass spectrometry. Mass Spectrom. Lett. 2011, 2:69-72.
    • (2011) Mass Spectrom. Lett. , vol.2 , pp. 69-72
    • Kim, S.J.1    Jung, H.J.2    Chung, B.C.3    Choi, M.H.4
  • 238
    • 84890118862 scopus 로고    scopus 로고
    • MALDI MS profiling of post-DRE urine samples highlights the potential of beta-microseminoprotein as a marker for prostatic diseases
    • Flatley B., Wilmott K.G., Malone P., Cramer R. MALDI MS profiling of post-DRE urine samples highlights the potential of beta-microseminoprotein as a marker for prostatic diseases. Prostate 2014, 74:103-111.
    • (2014) Prostate , vol.74 , pp. 103-111
    • Flatley, B.1    Wilmott, K.G.2    Malone, P.3    Cramer, R.4
  • 240
    • 38149042878 scopus 로고    scopus 로고
    • An investigation on the nature of the peptide at m/z 904, overexpressed in plasma of patients with colorectal cancer and familial adenomatous polyposis
    • Seraglia R., Molin L., Tonidandel L., Pucciarelli S., Agostini M., Urso E.D., Bedin C., Quaia M., Nitti D., Traldi P. An investigation on the nature of the peptide at m/z 904, overexpressed in plasma of patients with colorectal cancer and familial adenomatous polyposis. J. Mass Spectrom. 2007, 42:1606-1612.
    • (2007) J. Mass Spectrom. , vol.42 , pp. 1606-1612
    • Seraglia, R.1    Molin, L.2    Tonidandel, L.3    Pucciarelli, S.4    Agostini, M.5    Urso, E.D.6    Bedin, C.7    Quaia, M.8    Nitti, D.9    Traldi, P.10
  • 241
    • 84900451800 scopus 로고    scopus 로고
    • Urinary peptide profiling to differentiate between minimal change disease and focal segmental glomerulosclerosis
    • e87731
    • Perez V., Ibernon M., Lopez D., Pastor M.C., Navarro M., Navarro-Munoz M., Bonet J., Romero R. Urinary peptide profiling to differentiate between minimal change disease and focal segmental glomerulosclerosis. PLoS One 2014, 9. e87731.
    • (2014) PLoS One , vol.9
    • Perez, V.1    Ibernon, M.2    Lopez, D.3    Pastor, M.C.4    Navarro, M.5    Navarro-Munoz, M.6    Bonet, J.7    Romero, R.8
  • 242
    • 84881224625 scopus 로고    scopus 로고
    • Identification of urinary biomarkers for type 2 diabetes using bead-based proteomic approach
    • Chu L., Fu G.Z., Meng Q., Zhou H., Zhang M. Identification of urinary biomarkers for type 2 diabetes using bead-based proteomic approach. Diabetes Res. Clin. Pract. 2013, 101:187-193.
    • (2013) Diabetes Res. Clin. Pract. , vol.101 , pp. 187-193
    • Chu, L.1    Fu, G.Z.2    Meng, Q.3    Zhou, H.4    Zhang, M.5
  • 245
    • 84882726332 scopus 로고    scopus 로고
    • Serum peptidome patterns of hepatocellular carcinoma based on magnetic bead separation and mass spectrometry analysis
    • Ying X., Han S.X., Wang J.L., Zhou X., Jin G.H., Jin L., Wang H., Wu L., Zhang J.Y., Zhu Q. Serum peptidome patterns of hepatocellular carcinoma based on magnetic bead separation and mass spectrometry analysis. Diagn. Pathol. 2013, 8:130.
    • (2013) Diagn. Pathol. , vol.8 , pp. 130
    • Ying, X.1    Han, S.X.2    Wang, J.L.3    Zhou, X.4    Jin, G.H.5    Jin, L.6    Wang, H.7    Wu, L.8    Zhang, J.Y.9    Zhu, Q.10
  • 247
    • 84898606532 scopus 로고    scopus 로고
    • Mass spectrum analysis of serum biomarker proteins from patients with schizophrenia
    • Zhou N., Wang J., Yu Y.Q., Shi J.P., Li X.K., Xu B., Yu Q. Mass spectrum analysis of serum biomarker proteins from patients with schizophrenia. Biomed. Chromatogr. 2014, 28:654-659.
    • (2014) Biomed. Chromatogr. , vol.28 , pp. 654-659
    • Zhou, N.1    Wang, J.2    Yu, Y.Q.3    Shi, J.P.4    Li, X.K.5    Xu, B.6    Yu, Q.7
  • 250
    • 37649017918 scopus 로고    scopus 로고
    • Serum protein profiling in patients with inflammatory bowel diseases using selective solid-phase bulk extraction, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and chemometric data analysis
    • Nanni P., Parisi D., Roda G., Casale M., Belluzzi A., Roda E., Mayer L., Roda A. Serum protein profiling in patients with inflammatory bowel diseases using selective solid-phase bulk extraction, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and chemometric data analysis. Rapid Commun. Mass Spectrom. 2007, 21:4142-4148.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 4142-4148
    • Nanni, P.1    Parisi, D.2    Roda, G.3    Casale, M.4    Belluzzi, A.5    Roda, E.6    Mayer, L.7    Roda, A.8
  • 251
    • 84880399884 scopus 로고    scopus 로고
    • Diagnostic model of saliva peptide finger print analysis of primary Sjogren's syndrome patients by using weak cation exchange magnetic beads
    • Wei P., Kuo W.P., Chen F., Hua H. Diagnostic model of saliva peptide finger print analysis of primary Sjogren's syndrome patients by using weak cation exchange magnetic beads. Biosci. Rep. 2013, 33:567-573.
    • (2013) Biosci. Rep. , vol.33 , pp. 567-573
    • Wei, P.1    Kuo, W.P.2    Chen, F.3    Hua, H.4
  • 252
    • 84901197792 scopus 로고    scopus 로고
    • Urine peptide patterns for non-invasive diagnosis of endometriosis: a preliminary prospective study
    • Wang L., Liu H.Y., Shi H.H., Lang J.H., Sun W. Urine peptide patterns for non-invasive diagnosis of endometriosis: a preliminary prospective study. Eur. J. Obstet. Gynecol. Reprod. Biol. 2014, 177:23-28.
    • (2014) Eur. J. Obstet. Gynecol. Reprod. Biol. , vol.177 , pp. 23-28
    • Wang, L.1    Liu, H.Y.2    Shi, H.H.3    Lang, J.H.4    Sun, W.5
  • 254
    • 77956878144 scopus 로고    scopus 로고
    • Towards the development of an immuno MALDI (iMALDI) mass spectrometry assay for the diagnosis of hypertension
    • Reid J.D., Holmes D.T., Mason D.R., Shah B., Borchers C.H. Towards the development of an immuno MALDI (iMALDI) mass spectrometry assay for the diagnosis of hypertension. J. Am. Soc. Mass Spectrom. 2010, 21:1680-1686.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1680-1686
    • Reid, J.D.1    Holmes, D.T.2    Mason, D.R.3    Shah, B.4    Borchers, C.H.5
  • 255
    • 84902384049 scopus 로고    scopus 로고
    • Development and evaluation of an immuno-MALDI (iMALDI) assay for angiotensin I and the diagnosis of secondary hypertension
    • Camenzind A.G., van der Gugten J.G., Popp R., Holmes D.T., Borchers C.H. Development and evaluation of an immuno-MALDI (iMALDI) assay for angiotensin I and the diagnosis of secondary hypertension. Clin. Proteomics 2013, 10:20.
    • (2013) Clin. Proteomics , vol.10 , pp. 20
    • Camenzind, A.G.1    van der Gugten, J.G.2    Popp, R.3    Holmes, D.T.4    Borchers, C.H.5
  • 256
    • 81555226883 scopus 로고    scopus 로고
    • Direct antigen detection from immunoprecipitated beads using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; a new method for immunobeads-mass spectrometry (iMS)
    • Shimada T., Toyama A., Aoki C., Aoki Y., Tanaka K., Sato T.A. Direct antigen detection from immunoprecipitated beads using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; a new method for immunobeads-mass spectrometry (iMS). Rapid Commun. Mass Spectrom. 2011, 25:3521-3526.
    • (2011) Rapid Commun. Mass Spectrom. , vol.25 , pp. 3521-3526
    • Shimada, T.1    Toyama, A.2    Aoki, C.3    Aoki, Y.4    Tanaka, K.5    Sato, T.A.6
  • 257
    • 84896836139 scopus 로고    scopus 로고
    • Identification and quantification of amyloid beta-related peptides in human plasma using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Kaneko N., Yamamoto R., Sato T.A., Tanaka K. Identification and quantification of amyloid beta-related peptides in human plasma using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 2014, 90:104-117.
    • (2014) Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. , vol.90 , pp. 104-117
    • Kaneko, N.1    Yamamoto, R.2    Sato, T.A.3    Tanaka, K.4
  • 258
    • 78650572412 scopus 로고    scopus 로고
    • Nanomaterial-assisted laser desorption ionization for mass spectrometry-based biomedical analysis
    • Qiao L., Liu B., Girault H.H. Nanomaterial-assisted laser desorption ionization for mass spectrometry-based biomedical analysis. Nanomedicine 2010, 5:1641-1652.
    • (2010) Nanomedicine , vol.5 , pp. 1641-1652
    • Qiao, L.1    Liu, B.2    Girault, H.H.3
  • 261
    • 84873334311 scopus 로고    scopus 로고
    • Capture, enrichment, and mass spectrometric detection of low-molecular-weight biomarkers with nanoporous silicon microparticles
    • Tan J., Zhao W.J., Yu J.K., Ma S., Sailor M.J., Wu J.M. Capture, enrichment, and mass spectrometric detection of low-molecular-weight biomarkers with nanoporous silicon microparticles. Adv. Healthc. Mater. 2012, 1:742-750.
    • (2012) Adv. Healthc. Mater. , vol.1 , pp. 742-750
    • Tan, J.1    Zhao, W.J.2    Yu, J.K.3    Ma, S.4    Sailor, M.J.5    Wu, J.M.6
  • 262
    • 38049060252 scopus 로고    scopus 로고
    • Specific on-plate enrichment of phosphorylated peptides for direct MALDI-TOF MS analysis
    • Qiao L., Roussel C., Wan J., Yang P., Girault H.H., Liu B. Specific on-plate enrichment of phosphorylated peptides for direct MALDI-TOF MS analysis. J. Proteome Res. 2007, 6:4763-4769.
    • (2007) J. Proteome Res. , vol.6 , pp. 4763-4769
    • Qiao, L.1    Roussel, C.2    Wan, J.3    Yang, P.4    Girault, H.H.5    Liu, B.6
  • 263
    • 84891460472 scopus 로고    scopus 로고
    • Synthesis of polydopamine-coated magnetic graphene for Cu(2+) immobilization and application to the enrichment of low-concentration peptides for mass spectrometry analysis
    • Zhao M., Deng C., Zhang X. Synthesis of polydopamine-coated magnetic graphene for Cu(2+) immobilization and application to the enrichment of low-concentration peptides for mass spectrometry analysis. ACS Appl. Mater. Interfaces 2013, 5:13104-13112.
    • (2013) ACS Appl. Mater. Interfaces , vol.5 , pp. 13104-13112
    • Zhao, M.1    Deng, C.2    Zhang, X.3
  • 264
    • 34248190291 scopus 로고    scopus 로고
    • Functionalized magnetic nanoparticles for small-molecule isolation, identification, and quantification
    • Lin P.C., Tseng M.C., Su A.K., Chen Y.J., Lin C.C. Functionalized magnetic nanoparticles for small-molecule isolation, identification, and quantification. Anal. Chem. 2007, 79:3401-3408.
    • (2007) Anal. Chem. , vol.79 , pp. 3401-3408
    • Lin, P.C.1    Tseng, M.C.2    Su, A.K.3    Chen, Y.J.4    Lin, C.C.5
  • 265
    • 84872864398 scopus 로고    scopus 로고
    • A rapid and simple separation and direct detection of glutathione by gold nanoparticles and graphene-based MALDI-TOF-MS
    • Wan D., Gao M., Wang Y., Zhang P., Zhang X. A rapid and simple separation and direct detection of glutathione by gold nanoparticles and graphene-based MALDI-TOF-MS. J. Sep. Sci. 2013, 36:629-635.
    • (2013) J. Sep. Sci. , vol.36 , pp. 629-635
    • Wan, D.1    Gao, M.2    Wang, Y.3    Zhang, P.4    Zhang, X.5
  • 266
    • 38949105850 scopus 로고    scopus 로고
    • Highly selective and rapid enrichment of phosphorylated peptides using gallium oxide-coated magnetic microspheres for MALDI-TOF-MS and nano-LC-ESI-MS/MS/MS analysis
    • Li Y., Lin H., Deng C., Yang P., Zhang X. Highly selective and rapid enrichment of phosphorylated peptides using gallium oxide-coated magnetic microspheres for MALDI-TOF-MS and nano-LC-ESI-MS/MS/MS analysis. Proteomics 2008, 8:238-249.
    • (2008) Proteomics , vol.8 , pp. 238-249
    • Li, Y.1    Lin, H.2    Deng, C.3    Yang, P.4    Zhang, X.5
  • 267
    • 84855936639 scopus 로고    scopus 로고
    • Highly sensitive thrombin detection by matrix assisted laser desorption ionization-time of flight mass spectrometry with aptamer functionalized core-shell Fe(3)O(4)@C@Au magnetic microspheres
    • Zhang X., Zhu S., Deng C., Zhang X. Highly sensitive thrombin detection by matrix assisted laser desorption ionization-time of flight mass spectrometry with aptamer functionalized core-shell Fe(3)O(4)@C@Au magnetic microspheres. Talanta 2012, 88:295-302.
    • (2012) Talanta , vol.88 , pp. 295-302
    • Zhang, X.1    Zhu, S.2    Deng, C.3    Zhang, X.4
  • 268
    • 80052560146 scopus 로고    scopus 로고
    • Highly specific capture and direct MALDI-MS analysis of phosphorylated peptides using novel multifunctional chitosan-GMA-IDA-Fe (III) nanosphere
    • Zou X., Liu D., Zhong L., Yang B., Lou Y., Hu B., Yin Y. Highly specific capture and direct MALDI-MS analysis of phosphorylated peptides using novel multifunctional chitosan-GMA-IDA-Fe (III) nanosphere. Anal. Bioanal. Chem. 2011, 401:1251-1261.
    • (2011) Anal. Bioanal. Chem. , vol.401 , pp. 1251-1261
    • Zou, X.1    Liu, D.2    Zhong, L.3    Yang, B.4    Lou, Y.5    Hu, B.6    Yin, Y.7
  • 269
    • 80052813106 scopus 로고    scopus 로고
    • Synthesis and optimization of lectin functionalized nanoprobes for the selective recovery of glycoproteins from human body fluids
    • Ferreira J.A., Daniel-da-Silva A.L., Alves R.M., Duarte D., Vieira I., Santos L.L., Vitorino R., Amado F. Synthesis and optimization of lectin functionalized nanoprobes for the selective recovery of glycoproteins from human body fluids. Anal. Chem. 2011, 83:7035-7043.
    • (2011) Anal. Chem. , vol.83 , pp. 7035-7043
    • Ferreira, J.A.1    Daniel-da-Silva, A.L.2    Alves, R.M.3    Duarte, D.4    Vieira, I.5    Santos, L.L.6    Vitorino, R.7    Amado, F.8
  • 270
    • 84883474521 scopus 로고    scopus 로고
    • Gold nanoparticle-conjugated anti-oxidized low-density lipoprotein antibodies for targeted lipidomics of oxidative stress biomarkers
    • Hinterwirth H., Stubiger G., Lindner W., Lammerhofer M. Gold nanoparticle-conjugated anti-oxidized low-density lipoprotein antibodies for targeted lipidomics of oxidative stress biomarkers. Anal. Chem. 2013, 85:8376-8384.
    • (2013) Anal. Chem. , vol.85 , pp. 8376-8384
    • Hinterwirth, H.1    Stubiger, G.2    Lindner, W.3    Lammerhofer, M.4
  • 271
    • 84922652131 scopus 로고    scopus 로고
    • Development of aptamer-conjugated magnetic graphene/gold nanoparticle hybrid nanocomposites for specific enrichment and rapid analysis of thrombin by MALDI-TOF MS
    • Xiong Y., Deng C., Zhang X. Development of aptamer-conjugated magnetic graphene/gold nanoparticle hybrid nanocomposites for specific enrichment and rapid analysis of thrombin by MALDI-TOF MS. Talanta 2014, 129:282-289.
    • (2014) Talanta , vol.129 , pp. 282-289
    • Xiong, Y.1    Deng, C.2    Zhang, X.3
  • 273
    • 0036529538 scopus 로고    scopus 로고
    • Letsinger, multiple thiol-anchor capped DNA-gold nanoparticle conjugates
    • Li R., Jin C.A., Mirkin R.L. Letsinger, multiple thiol-anchor capped DNA-gold nanoparticle conjugates. Nucleic Acids Res. 2002, 30:1558-1562.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1558-1562
    • Li, R.1    Jin, C.A.2    Mirkin, R.L.3
  • 274
    • 49849095249 scopus 로고    scopus 로고
    • Monolayer-barcoded nanoparticles for on-chip DNA hybridization assay
    • Qiu F., Jiang D., Ding Y., Zhu J., Huang L.L. Monolayer-barcoded nanoparticles for on-chip DNA hybridization assay. Angew. Chem. 2008, 47:5009-5012.
    • (2008) Angew. Chem. , vol.47 , pp. 5009-5012
    • Qiu, F.1    Jiang, D.2    Ding, Y.3    Zhu, J.4    Huang, L.L.5
  • 275
    • 81055127548 scopus 로고    scopus 로고
    • Rapid and specific influenza virus detection by functionalized magnetic nanoparticles and mass spectrometry
    • Chou T.C., Hsu W., Wang C.H., Chen Y.J., Fang J.M. Rapid and specific influenza virus detection by functionalized magnetic nanoparticles and mass spectrometry. J. Nanobiotechnol. 2011, 9:52.
    • (2011) J. Nanobiotechnol. , vol.9 , pp. 52
    • Chou, T.C.1    Hsu, W.2    Wang, C.H.3    Chen, Y.J.4    Fang, J.M.5
  • 276
    • 3543044990 scopus 로고    scopus 로고
    • Gold nanoparticles as selective and concentrating probes for samples in MALDI MS analysis
    • Teng C.H., Ho K.C., Lin Y.S., Chen Y.C. Gold nanoparticles as selective and concentrating probes for samples in MALDI MS analysis. Anal. Chem. 2004, 76:4337-4342.
    • (2004) Anal. Chem. , vol.76 , pp. 4337-4342
    • Teng, C.H.1    Ho, K.C.2    Lin, Y.S.3    Chen, Y.C.4
  • 277
    • 57249108243 scopus 로고    scopus 로고
    • In-source photocatalytic reduction of disulfide bonds during laser desorption ionization
    • Qiao L., Bi H., Busnel J.M., Liu B., Girault H.H. In-source photocatalytic reduction of disulfide bonds during laser desorption ionization. Chem. Commun. 2008, 6357-6359.
    • (2008) Chem. Commun. , pp. 6357-6359
    • Qiao, L.1    Bi, H.2    Busnel, J.M.3    Liu, B.4    Girault, H.H.5
  • 278
  • 281
    • 78649983210 scopus 로고    scopus 로고
    • Surface modified silver selinide nanoparticles as extracting probes to improve peptide/protein detection via nanoparticles-based liquid phase microextraction coupled with MALDI mass spectrometry
    • Kailasa S.K., Wu H.F. Surface modified silver selinide nanoparticles as extracting probes to improve peptide/protein detection via nanoparticles-based liquid phase microextraction coupled with MALDI mass spectrometry. Talanta 2010, 83:527-534.
    • (2010) Talanta , vol.83 , pp. 527-534
    • Kailasa, S.K.1    Wu, H.F.2
  • 282
    • 77952103355 scopus 로고    scopus 로고
    • Nanoparticle-single drop microextraction as multifunctional and sensitive nanoprobes: binary matrix approach for gold nanoparticles modified with (4-mercaptophenyliminomethyl)-2-methoxyphenol for peptide and protein analysis in MALDI-TOF MS
    • Shastri L., Kailasa S.K., Wu H.F. Nanoparticle-single drop microextraction as multifunctional and sensitive nanoprobes: binary matrix approach for gold nanoparticles modified with (4-mercaptophenyliminomethyl)-2-methoxyphenol for peptide and protein analysis in MALDI-TOF MS. Talanta 2010, 81:1176-1182.
    • (2010) Talanta , vol.81 , pp. 1176-1182
    • Shastri, L.1    Kailasa, S.K.2    Wu, H.F.3
  • 283
    • 0038442825 scopus 로고    scopus 로고
    • Characterization of transcription factors by mass spectrometry and the role of SELDI-MS
    • Forde C.E., McCutchen-Maloney S.L. Characterization of transcription factors by mass spectrometry and the role of SELDI-MS. Mass Spectrom. Rev. 2002, 21:419-439.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 419-439
    • Forde, C.E.1    McCutchen-Maloney, S.L.2
  • 285
    • 0036855519 scopus 로고    scopus 로고
    • SELDI proteinchip MS: a platform for biomarker discovery and cancer diagnosis
    • Wright G.L. SELDI proteinchip MS: a platform for biomarker discovery and cancer diagnosis. Expert Rev. Mol. Diagn. 2002, 2:549-563.
    • (2002) Expert Rev. Mol. Diagn. , vol.2 , pp. 549-563
    • Wright, G.L.1
  • 286
    • 0038561093 scopus 로고    scopus 로고
    • SELDI ProteinChip (R) array in oncoproteomic research
    • Yip T.T., Lomas L. SELDI ProteinChip (R) array in oncoproteomic research. Technol. Cancer Res. Treat. 2002, 1:273-279.
    • (2002) Technol. Cancer Res. Treat. , vol.1 , pp. 273-279
    • Yip, T.T.1    Lomas, L.2
  • 287
    • 1642434579 scopus 로고    scopus 로고
    • Modern tumor marker discovery in urology: surface enhanced laser desorption and ionization (SELDI)
    • Gretzer M.B., Partin A.W., Chan D.W., Veltri R.W. Modern tumor marker discovery in urology: surface enhanced laser desorption and ionization (SELDI). Rev. Urol. 2003, 5:81-89.
    • (2003) Rev. Urol. , vol.5 , pp. 81-89
    • Gretzer, M.B.1    Partin, A.W.2    Chan, D.W.3    Veltri, R.W.4
  • 291
    • 0042232784 scopus 로고    scopus 로고
    • The use of SELDI ProteinChip array technology in renal disease research
    • Fung E., Diamond D., Simonsesn A.H., Weinberger S.R. The use of SELDI ProteinChip array technology in renal disease research. Methods Mol. Med. 2003, 86:295-312.
    • (2003) Methods Mol. Med. , vol.86 , pp. 295-312
    • Fung, E.1    Diamond, D.2    Simonsesn, A.H.3    Weinberger, S.R.4
  • 292
    • 80052669443 scopus 로고    scopus 로고
    • The application of SELDI-TOF-MS in clinical diagnosis of cancers
    • Liu C.B. The application of SELDI-TOF-MS in clinical diagnosis of cancers. J. Biomed. Biotechnol. 2011, 2011:245821.
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 245821
    • Liu, C.B.1
  • 293
    • 19444387632 scopus 로고    scopus 로고
    • Advances in clinical cancer proteomics: SELDI-ToF-mass spectrometry and biomarker discovery
    • Seibert V., Ebert M.P., Buschmann T. Advances in clinical cancer proteomics: SELDI-ToF-mass spectrometry and biomarker discovery. Brief. Funct. Genomic. Proteomic. 2005, 4:16-26.
    • (2005) Brief. Funct. Genomic. Proteomic. , vol.4 , pp. 16-26
    • Seibert, V.1    Ebert, M.P.2    Buschmann, T.3
  • 294
    • 74149084375 scopus 로고    scopus 로고
    • Identification of a truncated cystatin SA-I as a saliva biomarker for oral squamous cell carcinoma using the SELDI ProteinChip platform
    • Shintani S., Hamakawa H., Ueyama Y., Hatori M., Toyoshima T. Identification of a truncated cystatin SA-I as a saliva biomarker for oral squamous cell carcinoma using the SELDI ProteinChip platform. Int. J. Oral Maxillofac. Surg. 2010, 39:68-74.
    • (2010) Int. J. Oral Maxillofac. Surg. , vol.39 , pp. 68-74
    • Shintani, S.1    Hamakawa, H.2    Ueyama, Y.3    Hatori, M.4    Toyoshima, T.5
  • 295
    • 33846871854 scopus 로고    scopus 로고
    • Detection of breast cancer biomarkers in nipple aspirate fluid by SELDI-TOF and their identification by combined liquid chromatography-tandem mass spectrometry
    • He J.B., Gornbein J., Shen D., Lu M., Rovai L.E., Shau H., Katz J., Whitelegge J.P., Faull K.F., Chang H.R. Detection of breast cancer biomarkers in nipple aspirate fluid by SELDI-TOF and their identification by combined liquid chromatography-tandem mass spectrometry. Int. J. Oncol. 2007, 30:145-154.
    • (2007) Int. J. Oncol. , vol.30 , pp. 145-154
    • He, J.B.1    Gornbein, J.2    Shen, D.3    Lu, M.4    Rovai, L.E.5    Shau, H.6    Katz, J.7    Whitelegge, J.P.8    Faull, K.F.9    Chang, H.R.10
  • 296
    • 33846934658 scopus 로고    scopus 로고
    • Opportunities and limitations of SELDI-TOF-MS in biomedical research: practical advices
    • Poon T.C.W. Opportunities and limitations of SELDI-TOF-MS in biomedical research: practical advices. Expert Rev. Proteomics 2007, 4:51-65.
    • (2007) Expert Rev. Proteomics , vol.4 , pp. 51-65
    • Poon, T.C.W.1
  • 297
    • 67649359725 scopus 로고    scopus 로고
    • SELDI protein chip technology for the detection of serum biomarkers for liver disease
    • Chen L., Fatima S., Peng J.R., Leng X.S. SELDI protein chip technology for the detection of serum biomarkers for liver disease. Protein Pept. Lett. 2009, 16:467-472.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 467-472
    • Chen, L.1    Fatima, S.2    Peng, J.R.3    Leng, X.S.4
  • 298
  • 303
    • 84904709134 scopus 로고    scopus 로고
    • SELDI-TOF-MS proteomic profiling of serum, urine, and amniotic fluid in neural tube defects
    • Liu Z., Yuan Z., Zhao Q. SELDI-TOF-MS proteomic profiling of serum, urine, and amniotic fluid in neural tube defects. PLoS One 2014, 9:e103276.
    • (2014) PLoS One , vol.9 , pp. e103276
    • Liu, Z.1    Yuan, Z.2    Zhao, Q.3
  • 304
    • 77953292515 scopus 로고    scopus 로고
    • Effects of pretreatment protocols on human amniotic fluid protein profiling with SELDI-TOF MS using protein chips and magnetic beads
    • Deng B.P., Dong Z.G., Liu Y.G., Wang C.N., Liu J., Wang C.X., Qu X. Effects of pretreatment protocols on human amniotic fluid protein profiling with SELDI-TOF MS using protein chips and magnetic beads. Clin. Chim. Acta 2010, 411:1051-1057.
    • (2010) Clin. Chim. Acta , vol.411 , pp. 1051-1057
    • Deng, B.P.1    Dong, Z.G.2    Liu, Y.G.3    Wang, C.N.4    Liu, J.5    Wang, C.X.6    Qu, X.7
  • 309
    • 84863055814 scopus 로고    scopus 로고
    • Identification of low-abundance cancer biomarker candidate TIMP1 from serum with lectin fractionation and peptide affinity enrichment by ultrahigh-resolution mass spectrometry
    • Ahn Y.H., Kim K.H., Shin P.M., Ji E.S., Kim H., Yoo J.S. Identification of low-abundance cancer biomarker candidate TIMP1 from serum with lectin fractionation and peptide affinity enrichment by ultrahigh-resolution mass spectrometry. Anal. Chem. 2012, 84:1425-1431.
    • (2012) Anal. Chem. , vol.84 , pp. 1425-1431
    • Ahn, Y.H.1    Kim, K.H.2    Shin, P.M.3    Ji, E.S.4    Kim, H.5    Yoo, J.S.6
  • 310
    • 14644418981 scopus 로고    scopus 로고
    • Proteolytic peptide patterns as indicators for fungal infections and nonfungal affections of human nails measured by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Hollemeyer K., Jager S., Altmeyer W., Heinzle E. Proteolytic peptide patterns as indicators for fungal infections and nonfungal affections of human nails measured by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Biochem. 2005, 338:326-331.
    • (2005) Anal. Biochem. , vol.338 , pp. 326-331
    • Hollemeyer, K.1    Jager, S.2    Altmeyer, W.3    Heinzle, E.4
  • 311
    • 84877628551 scopus 로고    scopus 로고
    • Diagnosis of albuminuria by tryptic digestion and matrix-assisted laser desorption ionization/time-of-flight mass spectrometry
    • Cho Y.T., Chen C.W., Chen M.P., Hu J.L., Su H., Shiea J., Wu W.J., Wu D.C. Diagnosis of albuminuria by tryptic digestion and matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. Clin. Chim. Acta 2013, 420:76-81.
    • (2013) Clin. Chim. Acta , vol.420 , pp. 76-81
    • Cho, Y.T.1    Chen, C.W.2    Chen, M.P.3    Hu, J.L.4    Su, H.5    Shiea, J.6    Wu, W.J.7    Wu, D.C.8
  • 313
    • 62549139249 scopus 로고    scopus 로고
    • Acid hydrolysis followed by matrix-assisted laser desorption/ionization mass spectrometry for the rapid diagnosis of serum protein biomarkers in patients with major depression
    • Lo L.H., Huang T.L., Shiea J. Acid hydrolysis followed by matrix-assisted laser desorption/ionization mass spectrometry for the rapid diagnosis of serum protein biomarkers in patients with major depression. Rapid Commun. Mass Spectrom. 2009, 23:589-598.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 589-598
    • Lo, L.H.1    Huang, T.L.2    Shiea, J.3
  • 315
    • 25144468506 scopus 로고    scopus 로고
    • Characterization of oligosaccharide moieties of intact glycoproteins by microwave-assisted partial acid hydrolysis and mass spectrometry
    • Lee B.S., Krishnanchettiar S., Lateef S.S., Lateef N.S., Gupta S. Characterization of oligosaccharide moieties of intact glycoproteins by microwave-assisted partial acid hydrolysis and mass spectrometry. Rapid Commun. Mass Spectrom. 2005, 19:2629-2635.
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 2629-2635
    • Lee, B.S.1    Krishnanchettiar, S.2    Lateef, S.S.3    Lateef, N.S.4    Gupta, S.5
  • 316
    • 20444403015 scopus 로고    scopus 로고
    • Characterization of oligosaccharide moieties of glycopeptides by microwave-assisted partial acid hydrolysis and mass spectrometry
    • Lee B.S., Krishnanchettiar S., Lateef S.S., Gupta S. Characterization of oligosaccharide moieties of glycopeptides by microwave-assisted partial acid hydrolysis and mass spectrometry. Rapid Commun. Mass Spectrom. 2005, 19:1545-1550.
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 1545-1550
    • Lee, B.S.1    Krishnanchettiar, S.2    Lateef, S.S.3    Gupta, S.4
  • 317
    • 3042742112 scopus 로고    scopus 로고
    • Absolute quantitation of proteins by a combination of acid hydrolysis and matrix-assisted laser desorption/ionization mass spectrometry
    • Mirgorodskaya O.A., Korner R., Novikov A., Roepstorff P. Absolute quantitation of proteins by a combination of acid hydrolysis and matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 2004, 76:3569-3575.
    • (2004) Anal. Chem. , vol.76 , pp. 3569-3575
    • Mirgorodskaya, O.A.1    Korner, R.2    Novikov, A.3    Roepstorff, P.4
  • 318
    • 0028170485 scopus 로고
    • Peptide sequence information derived by partial acid hydrolysis and matrix-assisted laser desorption/ionization mass spectrometry
    • Vorm O., Roepstorff P. Peptide sequence information derived by partial acid hydrolysis and matrix-assisted laser desorption/ionization mass spectrometry. Biol. Mass Spectrom. 1994, 23:734-740.
    • (1994) Biol. Mass Spectrom. , vol.23 , pp. 734-740
    • Vorm, O.1    Roepstorff, P.2
  • 319
    • 0028723240 scopus 로고
    • Peptide fingerprints after partial acid hydrolysis: analysis by matrix-assisted laser desorption/ionization mass spectrometry
    • Knierman M.D., Coligan J.E., Parker K.C. Peptide fingerprints after partial acid hydrolysis: analysis by matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 1994, 8:1007-1010.
    • (1994) Rapid Commun. Mass Spectrom. , vol.8 , pp. 1007-1010
    • Knierman, M.D.1    Coligan, J.E.2    Parker, K.C.3
  • 320
    • 57749121406 scopus 로고    scopus 로고
    • MALDI-TOF MS/microwave-assisted acid hydrolysis identification of HbG Coushatta
    • Guo N., Higgins T.N. MALDI-TOF MS/microwave-assisted acid hydrolysis identification of HbG Coushatta. Clin. Biochem. 2009, 42:99-107.
    • (2009) Clin. Biochem. , vol.42 , pp. 99-107
    • Guo, N.1    Higgins, T.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.