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Volumn 23, Issue 10, 2012, Pages 1750-1756

Electron transfer dissociation mass spectrometry of hemoglobin on clinical samples

Author keywords

Clinical proteomics; Electron transfer dissociation; Hemoglobin; Single reaction monitoring; Top down mass spectrometry

Indexed keywords

CLINICAL SAMPLES; DIAGNOSTIC APPLICATIONS; ELECTRON TRANSFER DISSOCIATION; GLOBIN SEQUENCES; ION ACTIVATION; ION TRAP MASS SPECTROMETER; MASS ACCURACY; MASS SHIFT; MASS SPECTROMETRY ANALYSIS; PROTEOLYTIC CLEAVAGE; PROTEOMICS; RAPID IDENTIFICATION; REACTION MONITORING; SELECTED REACTION MONITORING; TOPDOWN; WHOLE BLOOD;

EID: 84868251662     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-012-0446-3     Document Type: Article
Times cited : (24)

References (17)
  • 1
    • 44949128064 scopus 로고    scopus 로고
    • Global epidemiology of hemoglobin disorders and derived service indicators
    • Modell, B., Darlison, M.: Global epidemiology of hemoglobin disorders and derived service indicators. Bull. World Health Org. 86, 480-487 (2008)
    • (2008) Bull. World Health Org. , vol.86 , pp. 480-487
    • Modell, B.1    Darlison, M.2
  • 2
    • 77953952024 scopus 로고    scopus 로고
    • The inherited diseases of hemoglobin are an emerging global health burden
    • Weatherall, D.J.: The inherited diseases of hemoglobin are an emerging global health burden. Blood 115, 4331-4336 (2010)
    • (2010) Blood , vol.115 , pp. 4331-4336
    • Weatherall, D.J.1
  • 3
    • 0037365343 scopus 로고    scopus 로고
    • Screening and genetic diagnosis of hemoglobin disorders
    • Old, J.M.: Screening and genetic diagnosis of hemoglobin disorders. Blood Rev. 17, 43-53 (2003)
    • (2003) Blood Rev. , vol.17 , pp. 43-53
    • Old, J.M.1
  • 4
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • Lange, V., Picotti, P., Domon, B., Aebersold, R.: Selected reaction monitoring for quantitative proteomics: a tutorial. Mol. Syst. Biol. 4, 1-14 (2008)
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 1-14
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 5
    • 24944506479 scopus 로고    scopus 로고
    • Rapid and specific detection of clinically significant hemoglobinopathies using electrospray mass spectrometry-mass spectrometry
    • Daniel, Y.A., Turner, C., Haynes, R.M., Hunt, B.J., Dalton, R.N.: Rapid and specific detection of clinically significant hemoglobinopathies using electrospray mass spectrometry-mass spectrometry. Br. J. Haematol 130, 635-643 (2005)
    • (2005) Br. J. Haematol , vol.130 , pp. 635-643
    • Daniel, Y.A.1    Turner, C.2    Haynes, R.M.3    Hunt, B.J.4    Dalton, R.N.5
  • 7
    • 75749100667 scopus 로고    scopus 로고
    • Quantitative clinical proteomics by liquid chromatography-tandem mass spectrometry: Assessing the platform
    • Hoofnagle, A.N.: Quantitative clinical proteomics by liquid chromatography-tandem mass spectrometry: assessing the platform. Clin. Chem. 56, 161-164 (2010)
    • (2010) Clin. Chem. , vol.56 , pp. 161-164
    • Hoofnagle, A.N.1
  • 8
    • 0027551614 scopus 로고
    • Collisionally activated dissociation and tandem mass spectrometry of intact hemoglobin beta-chain variant proteins with electrospray ionization
    • Light-Wahl, K.J., Loo, J.A., Edmonds, C.G., Smith, R.D., Witkowska, H.E., Shackleton, C.H., Wu, C.S.: Collisionally activated dissociation and tandem mass spectrometry of intact hemoglobin beta-chain variant proteins with electrospray ionization. Biol. Mass Spectrom. 22, 112-120 (1993)
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 112-120
    • Light-Wahl, K.J.1    Loo, J.A.2    Edmonds, C.G.3    Smith, R.D.4    Witkowska, H.E.5    Shackleton, C.H.6    Wu, C.S.7
  • 9
    • 79954624236 scopus 로고    scopus 로고
    • Hemoglobin variant analysis via direct surface sampling of dried blood spots coupled with high-resolution mass spectrometry
    • Edwards, R.L., Creese, A.J., Baumert, M., Griffiths, P., Bunch, J., Cooper, H.J.: Hemoglobin variant analysis via direct surface sampling of dried blood spots coupled with high-resolution mass spectrometry. Anal. Chem. 83, 2265-2270 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 2265-2270
    • Edwards, R.L.1    Creese, A.J.2    Baumert, M.3    Griffiths, P.4    Bunch, J.5    Cooper, H.J.6
  • 10
    • 79952759679 scopus 로고    scopus 로고
    • Top down analysis of small plasma proteins using an LTQ-orbitrap. Potential for mass spectrometry-based clinical assays for transthyretin and hemoglobin
    • Theberge, R., Infusini, G., Tong, W.W., McComb, M.E., Costello, C.E.: Top down analysis of small plasma proteins using an LTQ-Orbitrap. Potential for mass spectrometry-based clinical assays for transthyretin and hemoglobin. Int. J. Mass Spectrom. 300, 130-142 (2011)
    • (2011) Int. J. Mass Spectrom. , vol.300 , pp. 130-142
    • Theberge, R.1    Infusini, G.2    Tong, W.W.3    McComb, M.E.4    Costello, C.E.5
  • 12
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J.E.P., Coon, J.J., Schroeder, M.J., Shabanowitz, J., Hunt, D.F.: Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 101, 9528-9533 (2004)
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9528-9533
    • Syka, J.E.P.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 13
    • 82555170557 scopus 로고    scopus 로고
    • Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry
    • Tsybin, Y.O., Fornelli, L., Stoermer, C., Luebeck, M., Parra, J., Nallet, S., Wurm, F.M., Hartmer, R.: Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry. Anal. Chem. 83, 8919-8927 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 8919-8927
    • Tsybin, Y.O.1    Fornelli, L.2    Stoermer, C.3    Luebeck, M.4    Parra, J.5    Nallet, S.6    Wurm, F.M.7    Hartmer, R.8
  • 14
    • 39449111536 scopus 로고    scopus 로고
    • Genome-specific gas-phase fractionation strategy for improved shotgun proteomic profiling of proteotypic peptides
    • Scherl, A., Shaffer, S.A., Taylor, G.K., Kulasekara, H.D., Miller, S.I., Goodlett, D.R.: Genome-specific gas-phase fractionation strategy for improved shotgun proteomic profiling of proteotypic peptides. Anal. Chem. 80, 1182-1191 (2008)
    • (2008) Anal. Chem. , vol.80 , pp. 1182-1191
    • Scherl, A.1    Shaffer, S.A.2    Taylor, G.K.3    Kulasekara, H.D.4    Miller, S.I.5    Goodlett, D.R.6
  • 15
    • 85033190528 scopus 로고    scopus 로고
    • Label-free protein quantification on tandem mass spectra acquired in a data-independent mode provides accurate measurements over five orders of concentration magnitude in complex matrices
    • Pak, H., Pasquarello, C., Scherl, A.: Label-free protein quantification on tandem mass spectra acquired in a data-independent mode provides accurate measurements over five orders of concentration magnitude in complex matrices. J. Int. Omics 1, 211-215 (2011)
    • (2011) J. Int. Omics , vol.1 , pp. 211-215
    • Pak, H.1    Pasquarello, C.2    Scherl, A.3
  • 16
    • 77957667141 scopus 로고    scopus 로고
    • A novel approach for quantitative peptides analysis by selected electron transfer reaction monitoring
    • Wei, B.Y., Juang, Y.M., Lai, C.C.: A novel approach for quantitative peptides analysis by selected electron transfer reaction monitoring. J. Chromatogr. A 1217, 6927-6931 (2010)
    • (2010) J. Chromatogr. A , vol.1217 , pp. 6927-6931
    • Wei, B.Y.1    Juang, Y.M.2    Lai, C.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.