메뉴 건너뛰기




Volumn 85, Issue 2, 2013, Pages 737-748

Mass-linked immuno-selective assays in targeted proteomics

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN; MASS SPECTROMETRY; PROTEOMICS; REVIEW;

EID: 84872510161     PISSN: 00032700     EISSN: 15206882     Source Type: Journal    
DOI: 10.1021/ac302071k     Document Type: Review
Times cited : (28)

References (159)
  • 16
    • 0029646014 scopus 로고
    • Probe-immobilized affinity chromatography/mass spectrometry
    • Brockman, A. H.; Orlando, R. Probe-immobilized affinity chromatography/mass spectrometry Anal. Chem. 1995, 67 (24) 4581-4585
    • (1995) Anal. Chem. , vol.67 , Issue.24 , pp. 4581-4585
    • Brockman, A.H.1    Orlando, R.2
  • 40
    • 84872580577 scopus 로고    scopus 로고
    • Proceedings μTAS 2001 Symposium, Monterey, CA, Oct 21-25, 2001; Ramsey, J. M. van den Berg, A. Kluwer Academic Publishers: Dordrecht, The Netherlands
    • Ekstrom, S.; Borrebaeck, C. A. K.; Malmborg Hager, A. C.; Nilsson, J.; Marko-Varga, G.; Laurell, T. In Micro Total Analysis Systems 2001, Proceedings μTAS 2001 Symposium, Monterey, CA, Oct 21-25, 2001; Ramsey, J. M.; van den Berg, A., Eds.; Kluwer Academic Publishers: Dordrecht, The Netherlands, 2001; 85-86.
    • (2001) Micro Total Analysis Systems 2001 , pp. 85-86
    • Ekstrom, S.1    Borrebaeck, C.A.K.2    Malmborg Hager, A.C.3    Nilsson, J.4    Marko-Varga, G.5    Laurell, T.6
  • 44
    • 15444367116 scopus 로고    scopus 로고
    • Affinity capture using Vancomycin-bound magnetic nanoparticles for the MALDI-MS analysis of bacteria
    • Lin, Y. S.; Tsai, P. J.; Weng, M. F.; Chen, Y. C. Affinity capture using Vancomycin-bound magnetic nanoparticles for the MALDI-MS analysis of bacteria Anal. Chem. 2005, 77, 1753-1760
    • (2005) Anal. Chem. , vol.77 , pp. 1753-1760
    • Lin, Y.S.1    Tsai, P.J.2    Weng, M.F.3    Chen, Y.C.4
  • 45
    • 0031260629 scopus 로고    scopus 로고
    • Surface plasmon resonance biomolecular interaction analysis mass spectrometry. 2. Fiber optic-based analysis
    • Nelson, R. W.; Krone, J. R.; Jansson, O. Surface plasmon resonance biomolecular interaction analysis mass spectrometry. 2. Fiber optic-based analysis Anal. Chem. 1997, 69 (21) 4369-4374
    • (1997) Anal. Chem. , vol.69 , Issue.21 , pp. 4369-4374
    • Nelson, R.W.1    Krone, J.R.2    Jansson, O.3
  • 46
    • 0034012952 scopus 로고    scopus 로고
    • Biosensor chip mass spectrometry: A chip-based proteomics approach
    • Nelson, R. W.; Nedelkov, D.; Tubbs, K. A. Biosensor chip mass spectrometry: A chip-based proteomics approach Electrophoresis 2000, 21 (6) 1155-1163
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1155-1163
    • Nelson, R.W.1    Nedelkov, D.2    Tubbs, K.A.3
  • 47
    • 0033920196 scopus 로고    scopus 로고
    • Practical Considerations in BIA/MS: Optimizing the biosensor-mass spectrometry interface
    • Nedelkov, D.; Nelson, R. W. Practical Considerations in BIA/MS: Optimizing the biosensor-mass spectrometry interface J. Mol. Recognit. 2000, 13 (3) 140-145
    • (2000) J. Mol. Recognit. , vol.13 , Issue.3 , pp. 140-145
    • Nedelkov, D.1    Nelson, R.W.2
  • 48
    • 0032113285 scopus 로고    scopus 로고
    • Combining MALDI mass spectrometry and biomolecular interaction analysis using a biomolecular interaction analysis instrument
    • Sönksen, C. P.; Nordhoff, E.; Jansson, O.; Malmqvist, M.; Roepstorff, P. Combining MALDI mass spectrometry and biomolecular interaction analysis using a biomolecular interaction analysis instrument Anal. Chem. 1998, 70 (13) 2731-2736
    • (1998) Anal. Chem. , vol.70 , Issue.13 , pp. 2731-2736
    • Sönksen, C.P.1    Nordhoff, E.2    Jansson, O.3    Malmqvist, M.4    Roepstorff, P.5
  • 49
    • 0032626631 scopus 로고    scopus 로고
    • Surface plasmon resonance sensors: Review
    • Homola, J.; Yee, S. S.; Gauglitz, G. Surface plasmon resonance sensors: Review Sens. Actuators 1999, B54 (1-2) 3-15
    • (1999) Sens. Actuators , vol.54 , Issue.1-2 , pp. 3-15
    • Homola, J.1    Yee, S.S.2    Gauglitz, G.3
  • 50
    • 0035605455 scopus 로고    scopus 로고
    • Capture and analysis of low molecular weight ligands by surface plasmon resonance combined with mass spectrometry
    • Sonksen, C. P.; Roepstorff, P.; Markgren, P. O. Capture and analysis of low molecular weight ligands by surface plasmon resonance combined with mass spectrometry Eur. J. Mass Spectrom. 2001, 7 (4-5) 385-391
    • (2001) Eur. J. Mass Spectrom. , vol.7 , Issue.4-5 , pp. 385-391
    • Sonksen, C.P.1    Roepstorff, P.2    Markgren, P.O.3
  • 51
    • 0037109027 scopus 로고    scopus 로고
    • Characterization and optimization of peptide arrays for the study of epitope-antibody interactions using surface plasmon resonance imaging
    • Wegner, G. J.; Lee, H. J.; Corn, R. M. Characterization and optimization of peptide arrays for the study of epitope-antibody interactions using surface plasmon resonance imaging Anal. Chem. 2002, 74 (20) 5161-5168
    • (2002) Anal. Chem. , vol.74 , Issue.20 , pp. 5161-5168
    • Wegner, G.J.1    Lee, H.J.2    Corn, R.M.3
  • 52
    • 0036558172 scopus 로고    scopus 로고
    • Mass spectrometry after capture and small-volume elution of analyte from a surface plasmon resonance biosensor
    • Gilligan, J. J.; Schuck, P.; Yergey, A. L. Mass spectrometry after capture and small-volume elution of analyte from a surface plasmon resonance biosensor Anal. Chem. 2002, 74 (9) 2041-2047
    • (2002) Anal. Chem. , vol.74 , Issue.9 , pp. 2041-2047
    • Gilligan, J.J.1    Schuck, P.2    Yergey, A.L.3
  • 53
    • 10644250946 scopus 로고    scopus 로고
    • Label-free reading of microarray-based immunoassays with surface plasmon resonance imaging
    • Kanda, V.; Kariuki, J. K.; Harrison, D. J.; McDermott, M. T. Label-free reading of microarray-based immunoassays with surface plasmon resonance imaging Anal. Chem. 2004, 76 (24) 7257-7262
    • (2004) Anal. Chem. , vol.76 , Issue.24 , pp. 7257-7262
    • Kanda, V.1    Kariuki, J.K.2    Harrison, D.J.3    Mcdermott, M.T.4
  • 54
    • 4043100606 scopus 로고    scopus 로고
    • Integration of surface plasmon resonance with mass spectrometry: Automated ligand fishing and sample preparation for MALDI-MS using a Biacore 3000 biosensor
    • Zhukov, A.; Schurenberg, M.; Jansson, O.; Areskoug, D.; Buijs, J. Integration of surface plasmon resonance with mass spectrometry: Automated ligand fishing and sample preparation for MALDI-MS using a Biacore 3000 biosensor J. Biomol. Tech. 2004, 15 (2) 112-119
    • (2004) J. Biomol. Tech. , vol.15 , Issue.2 , pp. 112-119
    • Zhukov, A.1    Schurenberg, M.2    Jansson, O.3    Areskoug, D.4    Buijs, J.5
  • 55
    • 4744363460 scopus 로고    scopus 로고
    • Real-time surface plasmon resonance imaging measurements for the multiplexed determination of protein adsorption/desorption kinetics and surface enzymatic reactions on peptide microarrays
    • Wegner, G. J.; Wark, A. W.; Lee, H. J. Real-time surface plasmon resonance imaging measurements for the multiplexed determination of protein adsorption/desorption kinetics and surface enzymatic reactions on peptide microarrays Anal. Chem. 2004, 76 (19) 5677-5684
    • (2004) Anal. Chem. , vol.76 , Issue.19 , pp. 5677-5684
    • Wegner, G.J.1    Wark, A.W.2    Lee, H.J.3
  • 56
    • 20644438243 scopus 로고    scopus 로고
    • A Novel Approach to Protein Expression Profiling Using Antibody Microarrays Combined with Surface Plasmon Resonance Technology
    • Usui-Aoki, K.; Shimada, K.; Nagano, M.; Kawai, M.; Koga, H. A Novel Approach to Protein Expression Profiling Using Antibody Microarrays Combined with Surface Plasmon Resonance Technology Proteomics 2005, 5 (9) 2396-2401
    • (2005) Proteomics , vol.5 , Issue.9 , pp. 2396-2401
    • Usui-Aoki, K.1    Shimada, K.2    Nagano, M.3    Kawai, M.4    Koga, H.5
  • 57
    • 27944501164 scopus 로고    scopus 로고
    • Label-free detection of proteins in crude cell lysate with antibody arrays by a surface plasmon resonance imaging technique
    • Kyo, M.; Usui-Aoki, K.; Koga, H. Label-free detection of proteins in crude cell lysate with antibody arrays by a surface plasmon resonance imaging technique Anal. Chem. 2005, 77 (22) 7115-7121
    • (2005) Anal. Chem. , vol.77 , Issue.22 , pp. 7115-7121
    • Kyo, M.1    Usui-Aoki, K.2    Koga, H.3
  • 58
    • 0031264322 scopus 로고    scopus 로고
    • Surface plasmon resonance biomolecular interaction analysis mass spectrometry. 1. Chip-based analysis
    • Nelson, R. W.; Krone, J. R.; Jansson, O. Surface plasmon resonance biomolecular interaction analysis mass spectrometry. 1. Chip-based analysis Anal. Chem. 1997, 69 (21) 4363-4368
    • (1997) Anal. Chem. , vol.69 , Issue.21 , pp. 4363-4368
    • Nelson, R.W.1    Krone, J.R.2    Jansson, O.3
  • 59
    • 0034775618 scopus 로고    scopus 로고
    • Analysis of native proteins from biological fluids by biomolecular interaction analysis mass spectrometry (BIA/MS): Exploring the limit of detection, identification of non- specific binding and detection of multi-protein complexes
    • Nedelkov, D.; Nelson, R. W. Analysis of native proteins from biological fluids by biomolecular interaction analysis mass spectrometry (BIA/MS): Exploring the limit of detection, identification of non- specific binding and detection of multi-protein complexes Biosens. Bioelectron. 2001, 16 (9-12) 1071-1078
    • (2001) Biosens. Bioelectron. , vol.16 , Issue.912 , pp. 1071-1078
    • Nedelkov, D.1    Nelson, R.W.2
  • 60
    • 0034874634 scopus 로고    scopus 로고
    • Analysis of human urine protein biomarkers via biomolecular interaction analysis mass spectrometry
    • Nedelkov, D.; Nelson, R. W. Analysis of human urine protein biomarkers via biomolecular interaction analysis mass spectrometry Am. J. Kidney Dis. 2001, 38 (3) 481-487
    • (2001) Am. J. Kidney Dis. , vol.38 , Issue.3 , pp. 481-487
    • Nedelkov, D.1    Nelson, R.W.2
  • 61
    • 0035524481 scopus 로고    scopus 로고
    • Delineation of in vivo assembled multiprotein complexes via biomolecular interaction analysis mass spectrometry
    • Nedelkov, D.; Nelson, R. W. Delineation of in vivo assembled multiprotein complexes via biomolecular interaction analysis mass spectrometry Proteomics 2001, 1 (11) 1441-1446
    • (2001) Proteomics , vol.1 , Issue.11 , pp. 1441-1446
    • Nedelkov, D.1    Nelson, R.W.2
  • 62
    • 0037271476 scopus 로고    scopus 로고
    • Design and use of multi-affinity surfaces in biomolecular interaction analysis-mass spectrometry (BIA/MS): A step toward the design of SPR/MS arrays
    • Nedelkov, D.; Nelson, R. W. Design and use of multi-affinity surfaces in biomolecular interaction analysis-mass spectrometry (BIA/MS): A step toward the design of SPR/MS arrays J. Mol. Recognit. 2003, 16 (1) 15-19
    • (2003) J. Mol. Recognit. , vol.16 , Issue.1 , pp. 15-19
    • Nedelkov, D.1    Nelson, R.W.2
  • 63
    • 33749454392 scopus 로고    scopus 로고
    • SPR-enabled mass spectrometry arrays
    • Nedelkov, D.; Tubbs, K. A.; Nelson, R. W. SPR-enabled mass spectrometry arrays Electrophoresis 2006, 27 (18) 3671-3675
    • (2006) Electrophoresis , vol.27 , Issue.18 , pp. 3671-3675
    • Nedelkov, D.1    Tubbs, K.A.2    Nelson, R.W.3
  • 64
    • 33748804979 scopus 로고    scopus 로고
    • SPR imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers
    • Lee, H. J.; Nedelkov, D.; Corn, R. M. SPR imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers Anal. Chem. 2006, 78 (18) 6504-6510
    • (2006) Anal. Chem. , vol.78 , Issue.18 , pp. 6504-6510
    • Lee, H.J.1    Nedelkov, D.2    Corn, R.M.3
  • 67
    • 0030468536 scopus 로고    scopus 로고
    • New immobilization chemistry for probe affinity mass spectrometry
    • Brockman, A. H.; Orlando, R. New immobilization chemistry for probe affinity mass spectrometry Rapid Commun. Mass Spectrom. 1996, 10 (13) 1688-1692
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , Issue.13 , pp. 1688-1692
    • Brockman, A.H.1    Orlando, R.2
  • 68
    • 0031991033 scopus 로고    scopus 로고
    • On-probe immunoaffinity extraction by matrix-assisted laser desorption/ionization mass spectrometry
    • Liang, X.; Lubman, D. M.; Rossi, D. T.; Nordblom, G. D.; Barksdale, C. M. On-probe immunoaffinity extraction by matrix-assisted laser desorption/ionization mass spectrometry Anal. Chem. 1998, 70 (3) 498-503
    • (1998) Anal. Chem. , vol.70 , Issue.3 , pp. 498-503
    • Liang, X.1    Lubman, D.M.2    Rossi, D.T.3    Nordblom, G.D.4    Barksdale, C.M.5
  • 70
    • 0031716772 scopus 로고    scopus 로고
    • Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry
    • Kuwata, H.; Yip, T.-T.; Yip, C. L.; Tomita, M.; Hutchens, T. W. Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry Adv. Exp. Med. Biol. 1998, 443, 23-32
    • (1998) Adv. Exp. Med. Biol. , vol.443 , pp. 23-32
    • Kuwata, H.1    Yip, T.-T.2    Yip, C.L.3    Tomita, M.4    Hutchens, T.W.5
  • 71
    • 84891494435 scopus 로고    scopus 로고
    • Clinical neuroproteomics of human body fluids: CSF and blood assays for early and differential diagnosis of dementia
    • Wiltfang, J.; Lewczuk, P. Clinical neuroproteomics of human body fluids: CSF and blood assays for early and differential diagnosis of dementia Methods Princ. Med. Chem. 2006, 28, 259-278
    • (2006) Methods Princ. Med. Chem. , vol.28 , pp. 259-278
    • Wiltfang, J.1    Lewczuk, P.2
  • 73
    • 84872553972 scopus 로고    scopus 로고
    • Cancer Biomarkers Discovery Using Mass Spectrometry
    • Sinise, G. A. Nova Science Publishers, Inc. Hauppauge, NY
    • Solassol, J.; Mange, A. Cancer Biomarkers Discovery Using Mass Spectrometry. In Tumor Markers Research Perspective; Sinise, G. A., Ed.; Nova Science Publishers, Inc.: Hauppauge, NY, 2007; pp 19-35.
    • (2007) Tumor Markers Research Perspective , pp. 19-35
    • Solassol, J.1    Mange, A.2
  • 74
    • 84871615520 scopus 로고    scopus 로고
    • Applications of proteomic techniques in cancer research
    • Roy, P.; Shukla, Y. Applications of proteomic techniques in cancer research Cancer Ther. 2008, 6, 841-856
    • (2008) Cancer Ther. , vol.6 , pp. 841-856
    • Roy, P.1    Shukla, Y.2
  • 75
    • 33645729811 scopus 로고    scopus 로고
    • Identification of serum proteins discriminating colorectal cancer patients and healthy controls using surface-enhanced laser desorption ionisation-time of flight mass spectrometry
    • Engwegen, J. Y. M. N.; Helgason, H. H.; Cats, A.; Harris, N.; Bonfrer, J. M. G.; Schellens, J. H. M.; Beijnen, J. H. Identification of serum proteins discriminating colorectal cancer patients and healthy controls using surface-enhanced laser desorption ionisation-time of flight mass spectrometry World J. Gastroenterol. 2006, 12 (10) 1536-1544
    • (2006) World J. Gastroenterol. , vol.12 , Issue.10 , pp. 1536-1544
    • Engwegen, J.Y.M.N.1    Helgason, H.H.2    Cats, A.3    Harris, N.4    Bonfrer, J.M.G.5    Schellens, J.H.M.6    Beijnen, J.H.7
  • 76
    • 79959585860 scopus 로고    scopus 로고
    • Cystatin C is released in association with exosomes: A new tool of neuronal communication which is unbalanced in Alzheimer's disease
    • Ghidoni, R.; Paterlini, A.; Albertini, V.; Glionna, M.; Monti, E.; Schiaffonati, L.; Benussi, L.; Levy, E.; Binetti, G. Cystatin C is released in association with exosomes: A new tool of neuronal communication which is unbalanced in Alzheimer's disease Neurobiol. Aging 2011, 32 (8) 1435-1442
    • (2011) Neurobiol. Aging , vol.32 , Issue.8 , pp. 1435-1442
    • Ghidoni, R.1    Paterlini, A.2    Albertini, V.3    Glionna, M.4    Monti, E.5    Schiaffonati, L.6    Benussi, L.7    Levy, E.8    Binetti, G.9
  • 77
    • 0031260629 scopus 로고    scopus 로고
    • Surface plasmon resonance biomolecular interaction analysis mass spectrometry. 2. Fiber optic-based analysis
    • Nelson, R. W.; Krone, J. R.; Jansson, O. Surface plasmon resonance biomolecular interaction analysis mass spectrometry. 2. Fiber optic-based analysis Anal. Chem. 1997, 69 (21) 4369-4374
    • (1997) Anal. Chem. , vol.69 , Issue.21 , pp. 4369-4374
    • Nelson, R.W.1    Krone, J.R.2    Jansson, O.3
  • 80
    • 4444381540 scopus 로고    scopus 로고
    • Quantitative mass spectrometric immunoasay of insulin like growth factor 1
    • Nelson, R. W.; Nedelkov, D.; Tubbs, K. A.; Kiernan, U. A. Quantitative mass spectrometric immunoasay of insulin like growth factor 1 J. Proteome Res. 2004, 3 (4) 851-855
    • (2004) J. Proteome Res. , vol.3 , Issue.4 , pp. 851-855
    • Nelson, R.W.1    Nedelkov, D.2    Tubbs, K.A.3    Kiernan, U.A.4
  • 81
    • 0035878164 scopus 로고    scopus 로고
    • Determination of [beta]-2 microglobulin levels in plasma using a high-throughput mass spectrometric immunoassay system
    • Niederkofler, E. E.; Tubbs, K. A.; Gruber, K.; Nedelkov, D.; Kiernan, U. A.; Williams, P.; Nelson, R. W. Determination of [beta]-2 microglobulin levels in plasma using a high-throughput mass spectrometric immunoassay system Anal. Chem. 2001, 73 (14) 3294-3299
    • (2001) Anal. Chem. , vol.73 , Issue.14 , pp. 3294-3299
    • Niederkofler, E.E.1    Tubbs, K.A.2    Gruber, K.3    Nedelkov, D.4    Kiernan, U.A.5    Williams, P.6    Nelson, R.W.7
  • 82
    • 8844233567 scopus 로고    scopus 로고
    • Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA)
    • Anderson, N. L.; Anderson, N. G.; Haines, L. R.; Hardie, D. B.; Olafson, R. W.; Pearson, T. W. Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA) J. Proteome Res. 2004, 3, 235-244
    • (2004) J. Proteome Res. , vol.3 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4    Olafson, R.W.5    Pearson, T.W.6
  • 83
    • 0021140937 scopus 로고
    • Peptide-elicited protein-reactive antibodies in molecular biology and medicine
    • Shinnick, T. M.; Sutcliffe, J. G.; Green, N.; Lerner, R. A. Peptide-elicited protein-reactive antibodies in molecular biology and medicine J. Invest. Dermatol. 1984, 83, 112-115
    • (1984) J. Invest. Dermatol. , vol.83 , pp. 112-115
    • Shinnick, T.M.1    Sutcliffe, J.G.2    Green, N.3    Lerner, R.A.4
  • 84
    • 0025630449 scopus 로고
    • Molecular epitope identification by limited proteolysis of an immobilized antigen-antibody complex and mass spectrometric peptide mapping
    • Suckau, D.; Kohl, J.; Karwath, G.; Schneider, K.; Casaretto, M.; Bitter-Suermann, D.; Michael, P. Molecular epitope identification by limited proteolysis of an immobilized antigen-antibody complex and mass spectrometric peptide mapping Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 9848-9852
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9848-9852
    • Suckau, D.1    Kohl, J.2    Karwath, G.3    Schneider, K.4    Casaretto, M.5    Bitter-Suermann, D.6    Michael, P.7
  • 85
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B.; Mann, M.; Meng, C. K.; Wong, S. F.; Whitehouse, C. M. Electrospray ionization for mass spectrometry of large biomolecules Science 1989, 246, 64-71
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 86
    • 0001331640 scopus 로고
    • Multiple reaction monitoring in mass specctrometry/mass spectrometry for direct analysis of complex mixtures
    • Kondrat, R. W.; McClusky, G. A.; Cooks, R. G. Multiple reaction monitoring in mass specctrometry/mass spectrometry for direct analysis of complex mixtures Anal. Chem. 1978, 50 (14) 2017-2021
    • (1978) Anal. Chem. , vol.50 , Issue.14 , pp. 2017-2021
    • Kondrat, R.W.1    Mcclusky, G.A.2    Cooks, R.G.3
  • 87
    • 33644643852 scopus 로고    scopus 로고
    • Targeted comparative proteomics by liquid chromatography/matrix-assisted laser desorption/ionization triple-quadrupole mass spectrometry
    • Melanson, J. E.; Chisholm, K. A.; Pinto, D. M. Targeted comparative proteomics by liquid chromatography/matrix-assisted laser desorption/ionization triple-quadrupole mass spectrometry Rapid Commun. Mass Spectrom. 2005, 20 (5) 904-910
    • (2005) Rapid Commun. Mass Spectrom. , vol.20 , Issue.5 , pp. 904-910
    • Melanson, J.E.1    Chisholm, K.A.2    Pinto, D.M.3
  • 88
    • 27644593240 scopus 로고    scopus 로고
    • Differential multisite phosphorylation of the trehalose-6-phosphate synthase gene family in Arabidopsis thaliana. A mass spectrometry-based process for multiparallel peptide library phosphorylation analysis
    • Glinski, M.; Weckwerth, W. Differential multisite phosphorylation of the trehalose-6-phosphate synthase gene family in Arabidopsis thaliana. A mass spectrometry-based process for multiparallel peptide library phosphorylation analysis Mol. Cell. Proteomics 2005, 4 (10) 1614-1625
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.10 , pp. 1614-1625
    • Glinski, M.1    Weckwerth, W.2
  • 89
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A.; Rush, J.; Stemman, O.; Kirschner, M. W.; Gygi, S. P. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 6940-6945
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 90
    • 0028004403 scopus 로고
    • Epitope mapping of the gastrin-releasing peptide/anti-bombesin monoclonal antibody complex by proteolysis followed by matrix-assisted laser desorption ionization mass spectrometry
    • Papac, D. I.; Hoyes, J.; Tomer, K. B. Epitope mapping of the gastrin-releasing peptide/anti-bombesin monoclonal antibody complex by proteolysis followed by matrix-assisted laser desorption ionization mass spectrometry Protein Sci. 1994, 3 (9) 1485-1492
    • (1994) Protein Sci. , vol.3 , Issue.9 , pp. 1485-1492
    • Papac, D.I.1    Hoyes, J.2    Tomer, K.B.3
  • 94
    • 33646083005 scopus 로고    scopus 로고
    • Effect of different hapten-carrier conjugation ratios and molecular orientations on antibody affinity against a peptide antigen
    • Maiken, K.; Pedersen, N. S.; Sorensen, P. M. H.; Heegaard, N.; Helena Beyer, L. B. Effect of different hapten-carrier conjugation ratios and molecular orientations on antibody affinity against a peptide antigen J. Immunol. Methods 2006, 311, 198-206
    • (2006) J. Immunol. Methods , vol.311 , pp. 198-206
    • Maiken, K.1    Pedersen, N.S.2    Sorensen, P.M.H.3    Heegaard, N.4    Helena Beyer, L.B.5
  • 95
    • 77649273179 scopus 로고    scopus 로고
    • Automated screening of monoclonal antibodies for SISCAPA assays using a magnetic bead processor and liquid chromatography-selected reaction monitoring-mass spectrometry
    • Schoenherr, R. M.; Zhao, L.; Whiteaker, J. R.; Feng, L.-C.; Li, L.; Liu, L.; Liu, X.; Paulovich, A. G. Automated screening of monoclonal antibodies for SISCAPA assays using a magnetic bead processor and liquid chromatography- selected reaction monitoring-mass spectrometry J. Immunol. Methods 2010, 353 (1-2) 49-61
    • (2010) J. Immunol. Methods , vol.353 , Issue.1-2 , pp. 49-61
    • Schoenherr, R.M.1    Zhao, L.2    Whiteaker, J.R.3    Feng, L.-C.4    Li, L.5    Liu, L.6    Liu, X.7    Paulovich, A.G.8
  • 96
    • 33644643852 scopus 로고    scopus 로고
    • Targeted comparative proteomics by liquid chromatography/matrix-assisted desorption/ionization triple-quadrupole mass sepectrometry
    • Melanson, J. E.; Chisholm, K. A.; Pinto, D. M. Targeted comparative proteomics by liquid chromatography/matrix-assisted desorption/ionization triple-quadrupole mass sepectrometry Rapid Commun. Mass Spectrom. 2006, 20 (5) 904-910
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , Issue.5 , pp. 904-910
    • Melanson, J.E.1    Chisholm, K.A.2    Pinto, D.M.3
  • 97
    • 8844233567 scopus 로고    scopus 로고
    • Mass spectrometric quantitation of peptides and proteins using stable isotope standards and capture by anti-peptide antibodies
    • Anderson, N. L.; Anderson, N. G.; Haines, L. R.; Hardie, D. B.; Olafson, R. W.; Pearson, T. W. Mass spectrometric quantitation of peptides and proteins using stable isotope standards and capture by anti-peptide antibodies J. Proteome Res. 2004, 3 (2) 235-244
    • (2004) J. Proteome Res. , vol.3 , Issue.2 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4    Olafson, R.W.5    Pearson, T.W.6
  • 100
    • 70349932824 scopus 로고    scopus 로고
    • Quantitative analysis of an aberrant glycoform of TIMP1 from colon cancer serum by L-PHA-enrichment and SISCAPA with MRM mass spectrometry
    • Ahn, Y. H.; Lee, J. Y.; Lee, J. Y.; Kim, Y.-S.; Ko, J. H.; Yoo, J. S. Quantitative analysis of an aberrant glycoform of TIMP1 from colon cancer serum by L-PHA-enrichment and SISCAPA with MRM mass spectrometry J. Proteome Res. 2009, 8, 4216-4224
    • (2009) J. Proteome Res. , vol.8 , pp. 4216-4224
    • Ahn, Y.H.1    Lee, J.Y.2    Lee, J.Y.3    Kim, Y.-S.4    Ko, J.H.5    Yoo, J.S.6
  • 101
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L.; Hunter, C. L. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins Mol. Cell. Proteomics 2006, 5 (4) 573-588
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.4 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 103
    • 76649109590 scopus 로고    scopus 로고
    • An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers
    • Whiteaker, J. R.; Zhao, L.; Anderson, L.; Paulovich, A. G. An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers Mol. Cell. Proteomics 2010, 9 (1) 184-196
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.1 , pp. 184-196
    • Whiteaker, J.R.1    Zhao, L.2    Anderson, L.3    Paulovich, A.G.4
  • 104
    • 0030078307 scopus 로고    scopus 로고
    • Automated analytical system for the examination of protein primary structure
    • Hsieh, F.; Wang, H. Q.; Elicone, C.; Mark, J.; Martin, S. A.; Regnier, F. Automated analytical system for the examination of protein primary structure Anal. Chem. 1996, 68 (3) 455-462
    • (1996) Anal. Chem. , vol.68 , Issue.3 , pp. 455-462
    • Hsieh, F.1    Wang, H.Q.2    Elicone, C.3    Mark, J.4    Martin, S.A.5    Regnier, F.6
  • 105
    • 84872587426 scopus 로고    scopus 로고
    • Automated Sample Preparation In Targeted Proteomics; Single Amino Acid Polymorphism
    • Presented, Denver, CO, June 5-9
    • Meyer, K.; Herold, N.; Regnier, F. E. Automated Sample Preparation In Targeted Proteomics; Single Amino Acid Polymorphism. Presented at 59th ASMS Meeting, Denver, CO, June 5-9, 2011.
    • (2011) 59th ASMS Meeting
    • Meyer, K.1    Herold, N.2    Regnier, F.E.3
  • 106
    • 61849161703 scopus 로고    scopus 로고
    • Glycoproteomics of Plasma Based on Narrow Selectivity Lectin Affinity Chromatography
    • Jung, K.; Cho, W.; Regnier, F. E. Glycoproteomics of Plasma Based on Narrow Selectivity Lectin Affinity Chromatography J. Proteome Res. 2009, 8 (2) 643-650
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 643-650
    • Jung, K.1    Cho, W.2    Regnier, F.E.3
  • 107
    • 49049112270 scopus 로고    scopus 로고
    • Use of glycan targeting antibodies to identify cancer-associated glycoproteins in plasma of breast cancer patients
    • Cho, W.; Jung, K.; Regnier, F. E. Use of glycan targeting antibodies to identify cancer-associated glycoproteins in plasma of breast cancer patients Anal. Chem. 2008, 80 (14) 5286-5292
    • (2008) Anal. Chem. , vol.80 , Issue.14 , pp. 5286-5292
    • Cho, W.1    Jung, K.2    Regnier, F.E.3
  • 108
    • 78149372472 scopus 로고    scopus 로고
    • Sialylated lewis-x antigen bearing glycoproteins in human plasma
    • Cho, W.; Jung, K.; Regnier, F. E. Sialylated lewis-x antigen bearing glycoproteins in human plasma J. Proteome Res. 2010, 9 (11) 5960-5968
    • (2010) J. Proteome Res. , vol.9 , Issue.11 , pp. 5960-5968
    • Cho, W.1    Jung, K.2    Regnier, F.E.3
  • 109
    • 79960138858 scopus 로고    scopus 로고
    • Protein expression and fucosylated glycans of the serum haptoglobin-β subunit in hepatitis B virus-based liver diseases
    • Shu, H.; Zhang, S.; Kang, X.; Li, S.; Qin, X.; Sun, C.; Lu, H.; Liu, Y. Protein expression and fucosylated glycans of the serum haptoglobin-β subunit in hepatitis B virus-based liver diseases Acta Biochim. Biophys. Sin. 2011, 43 (7) 528-534
    • (2011) Acta Biochim. Biophys. Sin. , vol.43 , Issue.7 , pp. 528-534
    • Shu, H.1    Zhang, S.2    Kang, X.3    Li, S.4    Qin, X.5    Sun, C.6    Lu, H.7    Liu, Y.8
  • 111
    • 0034666508 scopus 로고    scopus 로고
    • Multitoxin biosensor-mass spectrometry analysis: A new approach for rapid, real-time, sensitive analysis of Staphylococcal toxins in food
    • Nedelkov, D.; Rasooly, A.; Nelson, R. W. Multitoxin biosensor-mass spectrometry analysis: A new approach for rapid, real-time, sensitive analysis of Staphylococcal toxins in food Int. J. Food Microbiol. 2000, 60 (1) 1-13
    • (2000) Int. J. Food Microbiol. , vol.60 , Issue.1 , pp. 1-13
    • Nedelkov, D.1    Rasooly, A.2    Nelson, R.W.3
  • 112
    • 0034692462 scopus 로고    scopus 로고
    • Exploring the limit of detection in biomolecular interaction analysis mass spectrometry (BIA/MS): detection of attomole amounts of native proteins present in complex biological mixtures
    • Nedelkov, D.; Nelson, R. W. Exploring the limit of detection in biomolecular interaction analysis mass spectrometry (BIA/MS): detection of attomole amounts of native proteins present in complex biological mixtures Anal. Chim. Acta 2000, 423 (1) 1-7
    • (2000) Anal. Chim. Acta , vol.423 , Issue.1 , pp. 1-7
    • Nedelkov, D.1    Nelson, R.W.2
  • 113
    • 0036228649 scopus 로고    scopus 로고
    • Design of buffer exchange surfaces and sensor chips for biosensor chip mass spectrometry
    • Nedelkov, D.; Tubbs, K. A.; Nelson, R. W. Design of buffer exchange surfaces and sensor chips for biosensor chip mass spectrometry Proteomics 2002, 2 (4) 441-446
    • (2002) Proteomics , vol.2 , Issue.4 , pp. 441-446
    • Nedelkov, D.1    Tubbs, K.A.2    Nelson, R.W.3
  • 114
    • 0036398996 scopus 로고    scopus 로고
    • Comparative phenotypic analyses of human plasma and urinary retinol binding protein using mass spectrometric immunoassay
    • Kiernan, U. A.; Tubbs, K. A.; Nedelkov, D.; Niederkofler, E. E.; Nelson, R. W. Comparative phenotypic analyses of human plasma and urinary retinol binding protein using mass spectrometric immunoassay Biochem. Biophys. Res. Commun. 2002, 297 (2) 401-405
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , Issue.2 , pp. 401-405
    • Kiernan, U.A.1    Tubbs, K.A.2    Nedelkov, D.3    Niederkofler, E.E.4    Nelson, R.W.5
  • 115
    • 0042879976 scopus 로고    scopus 로고
    • Comparative urine protein phenotyping using mass spectrometric immunoassay
    • Kiernan, U. A.; Tubbs, K. A.; Nedelkov, D. Comparative urine protein phenotyping using mass spectrometric immunoassay J. Proteome Res. 2003, 2 (2) 191-197
    • (2003) J. Proteome Res. , vol.2 , Issue.2 , pp. 191-197
    • Kiernan, U.A.1    Tubbs, K.A.2    Nedelkov, D.3
  • 116
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid [beta] protein and variants by immunoprecipitation-mass spectrometry
    • Wang, R.; Sweeney, D.; Gandy, S. E.; Sisodia, S. S. The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid [beta] protein and variants by immunoprecipitation- mass spectrometry J. Biol. Chem. 1996, 271 (50) 31894-31902
    • (1996) J. Biol. Chem. , vol.271 , Issue.50 , pp. 31894-31902
    • Wang, R.1    Sweeney, D.2    Gandy, S.E.3    Sisodia, S.S.4
  • 117
    • 3042737683 scopus 로고    scopus 로고
    • Improving reproducibility and sensitivity in identifying human proteins by shotgun proteomics
    • Resing, K. A.; Meyer-Arendt, K.; Mendoza, A. M. Improving reproducibility and sensitivity in identifying human proteins by shotgun proteomics Anal. Chem. 2004, 76 (13) 3556-3568
    • (2004) Anal. Chem. , vol.76 , Issue.13 , pp. 3556-3568
    • Resing, K.A.1    Meyer-Arendt, K.2    Mendoza, A.M.3
  • 118
    • 12244300698 scopus 로고    scopus 로고
    • A dataset of human liver proteins identified by protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry
    • Yan, W.; Lee, H.; Deutsch, E. W. A dataset of human liver proteins identified by protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry Mol. Cell. Proteomics 2004, 3 (10) 1039-1041
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.10 , pp. 1039-1041
    • Yan, W.1    Lee, H.2    Deutsch, E.W.3
  • 119
    • 0038662530 scopus 로고    scopus 로고
    • Proteomic applications for the early detection of cancer
    • Wulfkuhle, J. D.; Liotta, L. A.; Petricoin, E. F. Proteomic applications for the early detection of cancer Nat. Rev. Cancer 2003, 3 (4) 267-275
    • (2003) Nat. Rev. Cancer , vol.3 , Issue.4 , pp. 267-275
    • Wulfkuhle, J.D.1    Liotta, L.A.2    Petricoin, E.F.3
  • 120
    • 0038281517 scopus 로고    scopus 로고
    • Novel mass spectrometric immunoassays for the rapid structural characterization of plasma apolipoproteins
    • Niederkofler, E. E.; Tubbs, K. A.; Kiernan, U. A.; Nedelkov, D.; Nelson, R. W. Novel mass spectrometric immunoassays for the rapid structural characterization of plasma apolipoproteins J. Lipid Res. 2003, 44 (3) 630-639
    • (2003) J. Lipid Res. , vol.44 , Issue.3 , pp. 630-639
    • Niederkofler, E.E.1    Tubbs, K.A.2    Kiernan, U.A.3    Nedelkov, D.4    Nelson, R.W.5
  • 121
    • 0037468458 scopus 로고    scopus 로고
    • Detection of novel truncated forms of human serum amyloid A protein in human plasma
    • Kiernan, U. A.; Tubbs, K. A.; Nedelkov, D.; Niederkofler, E. E.; Nelson, R. W. Detection of novel truncated forms of human serum amyloid A protein in human plasma FEBS Lett. 2003, 537 (1-3) 166-170
    • (2003) FEBS Lett. , vol.537 , Issue.13 , pp. 166-170
    • Kiernan, U.A.1    Tubbs, K.A.2    Nedelkov, D.3    Niederkofler, E.E.4    Nelson, R.W.5
  • 122
    • 20544478528 scopus 로고    scopus 로고
    • Selected expression profiling of full-length proteins and their variants in human plasma
    • Kiernan, U. A.; Nedelkov, D.; Tubbs, K. A.; Niederkofler, E. E.; Nelson, R. W. Selected expression profiling of full-length proteins and their variants in human plasma Clin. Proteomics 2004, 1 (1) 7-16
    • (2004) Clin. Proteomics , vol.1 , Issue.1 , pp. 7-16
    • Kiernan, U.A.1    Nedelkov, D.2    Tubbs, K.A.3    Niederkofler, E.E.4    Nelson, R.W.5
  • 123
    • 29544440590 scopus 로고    scopus 로고
    • High-throughput MS-based protein phenotyping: application to haptoglobin
    • Tubbs, K. A.; Kiernan, U. A.; Niederkofler, E. E.; Nelson, R. W. High-throughput MS-based protein phenotyping: application to haptoglobin Proteomics 2005, 5 (18) 5002-5007
    • (2005) Proteomics , vol.5 , Issue.18 , pp. 5002-5007
    • Tubbs, K.A.1    Kiernan, U.A.2    Niederkofler, E.E.3    Nelson, R.W.4
  • 124
    • 2942566253 scopus 로고    scopus 로고
    • Proteomic characterization of novel serum amyloid P component variants from human plasma and urine
    • Kiernan, U. A.; Nedelkov, D.; Tubbs, K. A.; Niederkofler, E. E.; Nelson, R. W. Proteomic characterization of novel serum amyloid P component variants from human plasma and urine Proteomics 2004, 4 (6) 1825-1829
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1825-1829
    • Kiernan, U.A.1    Nedelkov, D.2    Tubbs, K.A.3    Niederkofler, E.E.4    Nelson, R.W.5
  • 127
    • 33646537802 scopus 로고    scopus 로고
    • Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes
    • Fleischer, T. C.; Weaver, C. M.; McAfee, J. K.; Jennings, J. L.; Link, A. J. Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes Genes Dev. 2006, 20 (10) 1294-1307
    • (2006) Genes Dev. , vol.20 , Issue.10 , pp. 1294-1307
    • Fleischer, T.C.1    Weaver, C.M.2    Mcafee, J.K.3    Jennings, J.L.4    Link, A.J.5
  • 129
    • 46249129317 scopus 로고    scopus 로고
    • Isosilybin B causes androgen receptor degradation in human prostate carcinoma cells via P13K-Akt-Mdm2-mediated pathway
    • Deep, G.; Oberlies, N. H.; Kroll, D. J.; Agarwal, R. Isosilybin B causes androgen receptor degradation in human prostate carcinoma cells via P13K-Akt-Mdm2-mediated pathway Oncogene 2008, 27 (28) 3986-3998
    • (2008) Oncogene , vol.27 , Issue.28 , pp. 3986-3998
    • Deep, G.1    Oberlies, N.H.2    Kroll, D.J.3    Agarwal, R.4
  • 130
    • 33748747967 scopus 로고    scopus 로고
    • Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway
    • Cintron, N. S.; Toft, D. Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway J. Biol. Chem. 2006, 281 (36) 26235-26244
    • (2006) J. Biol. Chem. , vol.281 , Issue.36 , pp. 26235-26244
    • Cintron, N.S.1    Toft, D.2
  • 131
    • 37349111818 scopus 로고    scopus 로고
    • Toward chromatographic analysis of interacting protein networks
    • Liu, X.; Yang, W.-C.; Gao, Q.; Regnier, F. Toward chromatographic analysis of interacting protein networks J. Chromatogr., A 2008, 1178 (1-2) 24-32
    • (2008) J. Chromatogr., A , vol.1178 , Issue.1-2 , pp. 24-32
    • Liu, X.1    Yang, W.-C.2    Gao, Q.3    Regnier, F.4
  • 132
    • 70049106408 scopus 로고    scopus 로고
    • Geometric de-noising of protein-protein interaction networks
    • Kuchaiev, O.; Marija, R.; Higham, D. J.; Przulj, N. Geometric de-noising of protein-protein interaction networks PLoS Comput. Biol. 2009, 5 (8) e1000454
    • (2009) PLoS Comput. Biol. , vol.5 , Issue.8 , pp. 1000454
    • Kuchaiev, O.1    Marija, R.2    Higham, D.J.3    Przulj, N.4
  • 133
    • 33745620168 scopus 로고    scopus 로고
    • A statistical framework to discover true associations from multiprotein complex pull-down proteomics data
    • Shen, C.; Li, L.; Chen, J. Y. A statistical framework to discover true associations from multiprotein complex pull-down proteomics data Proteins: Struct., Funct., Bioinf. 2006, 64 (2) 436-443
    • (2006) Proteins: Struct., Funct., Bioinf. , vol.64 , Issue.2 , pp. 436-443
    • Shen, C.1    Li, L.2    Chen, J.Y.3
  • 134
    • 4444336740 scopus 로고    scopus 로고
    • New approach for analysis of the phosphotyrosine proteome and its application to the chicken B cell line, DT40
    • Zolodz, M. D.; Wood, K. V.; Regnier, F. E.; Geahlen, R. L. New approach for analysis of the phosphotyrosine proteome and its application to the chicken B cell line, DT40 J. Proteome Res. 2004, 3 (4) 743-750
    • (2004) J. Proteome Res. , vol.3 , Issue.4 , pp. 743-750
    • Zolodz, M.D.1    Wood, K.V.2    Regnier, F.E.3    Geahlen, R.L.4
  • 136
    • 79954454729 scopus 로고    scopus 로고
    • Optimization of immunoaffinity enrichment and detection: toward a comprehensive characterization of the phosphotyrosine proteome of K562 cells by liquid chromatography-mass spectrometry
    • Artemenko, K. A.; Lind, S. B.; Elfineh, L.; Mayrhofer, C.; Zubarev, R. A.; Bergquist, J.; Pettersson, U. Optimization of immunoaffinity enrichment and detection: toward a comprehensive characterization of the phosphotyrosine proteome of K562 cells by liquid chromatography-mass spectrometry Analyst 2011, 136 (9) 1971-1978
    • (2011) Analyst , vol.136 , Issue.9 , pp. 1971-1978
    • Artemenko, K.A.1    Lind, S.B.2    Elfineh, L.3    Mayrhofer, C.4    Zubarev, R.A.5    Bergquist, J.6    Pettersson, U.7
  • 138
    • 0038391227 scopus 로고    scopus 로고
    • Approaches to Define Antigen Receptor-induced Serine Kinase Signal Transduction Pathways
    • Astoul, E.; Laurence, A. D.; Totty, N.; Beer, S.; Alexander, D. R.; Cantrell, D. A. Approaches to Define Antigen Receptor-induced Serine Kinase Signal Transduction Pathways J. Biol. Chem. 2003, 278 (11) 9267-9275
    • (2003) J. Biol. Chem. , vol.278 , Issue.11 , pp. 9267-9275
    • Astoul, E.1    Laurence, A.D.2    Totty, N.3    Beer, S.4    Alexander, D.R.5    Cantrell, D.A.6
  • 141
    • 79959987745 scopus 로고    scopus 로고
    • In vivo protein tyrosine nitration in Arabidopsis thaliana
    • Lozano-Juste, J.; Colom-Moreno, R.; Leon, J. In vivo protein tyrosine nitration in Arabidopsis thaliana J. Exp. Bot. 2011, 62 (10) 3501-3517
    • (2011) J. Exp. Bot. , vol.62 , Issue.10 , pp. 3501-3517
    • Lozano-Juste, J.1    Colom-Moreno, R.2    Leon, J.3
  • 143
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S.-E.; Mittler, G.; Mann, M. Identifying and quantifying in vivo methylation sites by heavy methyl SILAC Nat. Methods 2004, 1 (2) 119-126
    • (2004) Nat. Methods , vol.1 , Issue.2 , pp. 119-126
    • Ong, S.-E.1    Mittler, G.2    Mann, M.3
  • 145
    • 77956315751 scopus 로고    scopus 로고
    • Acetylation of RNA processing proteins and cell cycle protein in mitosis
    • Chuang, C.; Lin, S.-H.; Huang, F.; Pan, J.; Josic, D.; Yu-Lee, L.-Y. Acetylation of RNA processing proteins and cell cycle protein in mitosis J. Proteome Res. 2010, 9 (9) 4554-4564
    • (2010) J. Proteome Res. , vol.9 , Issue.9 , pp. 4554-4564
    • Chuang, C.1    Lin, S.-H.2    Huang, F.3    Pan, J.4    Josic, D.5    Yu-Lee, L.-Y.6
  • 146
    • 56649114286 scopus 로고    scopus 로고
    • The diversity of lysine-acetylated proteins in Escherichia coli
    • Yu, B. J.; Kim, J. A.; Moon, J. H.; Ryu, S. E.; Pan, J.-G. The diversity of lysine-acetylated proteins in Escherichia coli J. Microbiol. Biotechnol. 2008, 18 (9) 1529-1536
    • (2008) J. Microbiol. Biotechnol. , vol.18 , Issue.9 , pp. 1529-1536
    • Yu, B.J.1    Kim, J.A.2    Moon, J.H.3    Ryu, S.E.4    Pan, J.-G.5
  • 147
    • 77952871097 scopus 로고    scopus 로고
    • Screening antibody and immunosorbent selectivity by two-dimensional liquid chromatography-MS/MS
    • Cho, W.; Jung, K.; Regnier, F. E. Screening antibody and immunosorbent selectivity by two-dimensional liquid chromatography-MS/MS J. Sep. Sci. 2010, 33 (10) 1438-1447
    • (2010) J. Sep. Sci. , vol.33 , Issue.10 , pp. 1438-1447
    • Cho, W.1    Jung, K.2    Regnier, F.E.3
  • 151
    • 15444378641 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis and western-blotting analyses with anti Ara h 3 Basic Subunit IgG evidence the cross-reacting polypeptides of Arachis hypogaea, Glycine max, and Lupinus albus seed proteomes
    • Magni, C.; Ballabio, C.; Restani, P.; Sironi, E.; Scarafoni, A.; Poiesi, C.; Duranti, M. Two-dimensional electrophoresis and western-blotting analyses with anti Ara h 3 Basic Subunit IgG evidence the cross-reacting polypeptides of Arachis hypogaea, Glycine max, and Lupinus albus seed proteomes J. Agric. Food Chem. 2005, 53 (6) 2275-2281
    • (2005) J. Agric. Food Chem. , vol.53 , Issue.6 , pp. 2275-2281
    • Magni, C.1    Ballabio, C.2    Restani, P.3    Sironi, E.4    Scarafoni, A.5    Poiesi, C.6    Duranti, M.7
  • 152
    • 0030174309 scopus 로고    scopus 로고
    • Mapping epitope structure and activity; from one dimensional prediction to four dimensional description of antigenic specificity
    • Van Regnemortel, M. H. V. Mapping epitope structure and activity; from one dimensional prediction to four dimensional description of antigenic specificity Methods 1996, 9, 465-472
    • (1996) Methods , vol.9 , pp. 465-472
    • Van Regnemortel, M.H.V.1
  • 153
    • 79960346115 scopus 로고    scopus 로고
    • Charting the peptide cross reactome between HIV-1 and the human proteome
    • Lucchese, G.; Stufano, A.; Calabro, M.; Kanduc, D. Charting the peptide cross reactome between HIV-1 and the human proteome Front. Biosci., Elite Ed. 2011, E3 (4) 1385-1400
    • (2011) Front. Biosci., Elite Ed. , vol.3 , Issue.4 , pp. 1385-1400
    • Lucchese, G.1    Stufano, A.2    Calabro, M.3    Kanduc, D.4
  • 154
    • 74449088287 scopus 로고    scopus 로고
    • Annexin A2 on lung epithelial cell surface is recognized by severe acute respiratory syndrome-associated coronavirus spike domain 2 antibodies
    • Fang, Y.-T.; Lin, C.-F.; Liao, P.-C.; Kuo, Y.-M.; Wang, S.; Yeh, T.-M.; Shieh, C.-C. K.; Su, I.-J.; Lei, H.-Y.; Lin, Y.-S. Annexin A2 on lung epithelial cell surface is recognized by severe acute respiratory syndrome-associated coronavirus spike domain 2 antibodies Mol. Immunol. 2010, 47 (5) 1000-1009
    • (2010) Mol. Immunol. , vol.47 , Issue.5 , pp. 1000-1009
    • Fang, Y.-T.1    Lin, C.-F.2    Liao, P.-C.3    Kuo, Y.-M.4    Wang, S.5    Yeh, T.-M.6    Shieh, C.-C.K.7    Su, I.-J.8    Lei, H.-Y.9    Lin, Y.-S.10
  • 155
    • 84872593790 scopus 로고    scopus 로고
    • This second designation was added by the authors of this review for clarification
    • This second designation was added by the authors of this review for clarification.
  • 157
    • 23044510003 scopus 로고    scopus 로고
    • Preparation of 20-μm-i.d. Silica-Based Monolithic Columns and Their Performance for Proteomics Analyses
    • Luo, Q.; Shen, Y.; Hixson, K. K.; Zhao, R.; Yang, F.; Moore, R. J.; Mottaz, H. M.; Smith, R. D. Preparation of 20-μm-i.d. Silica-Based Monolithic Columns and Their Performance for Proteomics Analyses Anal. Chem. 2005, 77 (15) 5028-5035
    • (2005) Anal. Chem. , vol.77 , Issue.15 , pp. 5028-5035
    • Luo, Q.1    Shen, Y.2    Hixson, K.K.3    Zhao, R.4    Yang, F.5    Moore, R.J.6    Mottaz, H.M.7    Smith, R.D.8
  • 159
    • 55349139657 scopus 로고    scopus 로고
    • Quantification of thyroglobulin, a low-abundance serum protein, by immunoaffinity peptide enrichment and tandem mass spectrometry
    • Hoofnagle, A. N.; Becker, J. O.; Wener, M. H.; Heinecke, J. W. Quantification of thyroglobulin, a low-abundance serum protein, by immunoaffinity peptide enrichment and tandem mass spectrometry Clin Chem. (Washington, DC, U.S.) 2008, 54, 1796-1804
    • (2008) Clin Chem. (Washington, DC, U.S.) , vol.54 , pp. 1796-1804
    • Hoofnagle, A.N.1    Becker, J.O.2    Wener, M.H.3    Heinecke, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.