메뉴 건너뛰기




Volumn , Issue , 2009, Pages 299-320

Surface-Enhanced Laser Desorption/Ionization for Urinary Proteome Analysis

Author keywords

Binding buffers; Biomarkers; Immunoglobulins; Isoelectric point; Laser pulses; SELDI

Indexed keywords


EID: 79955773679     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527628612.ch23     Document Type: Chapter
Times cited : (1)

References (55)
  • 1
    • 0141642224 scopus 로고    scopus 로고
    • The NIH Roadmap
    • Zerhouni, E. (2003) The NIH Roadmap. Science, 302, 63-65.
    • (2003) Science , vol.302 , pp. 63-65
    • Zerhouni, E.1
  • 2
    • 84990629710 scopus 로고
    • New desorption strategies for the mass spectrometric analysis of macromolecules
    • Hutchens, T.W. and Yip, T.T. (1993) New desorption strategies for the mass spectrometric analysis of macromolecules. Rapid Commun Mass Spectrom, 7, 576-580.
    • (1993) Rapid Commun Mass Spectrom , vol.7 , pp. 576-580
    • Hutchens, T.W.1    Yip, T.T.2
  • 3
    • 0038561093 scopus 로고    scopus 로고
    • SELDI ProteinChip array in oncoproteomic research
    • Yip, T.T. and Lomas, L. (2002) SELDI ProteinChip array in oncoproteomic research. Technol Cancer Res Treat, 1 (4), 273-280.
    • (2002) Technol Cancer Res Treat , vol.1 , Issue.4 , pp. 273-280
    • Yip, T.T.1    Lomas, L.2
  • 5
    • 3242674073 scopus 로고    scopus 로고
    • Detection of differentially expressed proteins in early-stage melanoma patients using SELDI-TOF mass spectrometry
    • Wilson, L.L., Tran, L., Morton, D.L., and Hoon, D.S. (2004) Detection of differentially expressed proteins in early-stage melanoma patients using SELDI-TOF mass spectrometry. Ann N Y Acad Sci, 1022, 317-322.
    • (2004) Ann N Y Acad Sci , vol.1022 , pp. 317-322
    • Wilson, L.L.1    Tran, L.2    Morton, D.L.3    Hoon, D.S.4
  • 9
    • 33644876659 scopus 로고    scopus 로고
    • SELDI-TOF-MS proteomics of breast cancer
    • Clarke, C.H., Buckley, J.A., and Fung, E. (2005) SELDI-TOF-MS proteomics of breast cancer. Clin Chem Lab Med, 43, 1314-1320.
    • (2005) Clin Chem Lab Med , vol.43 , pp. 1314-1320
    • Clarke, C.H.1    Buckley, J.A.2    Fung, E.3
  • 11
    • 0036322138 scopus 로고    scopus 로고
    • Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity
    • Beher, D., Wrigley, J., Owens, A.P., and Shearman, M.S. (2002) Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity. J Neurochem, 82, 563-575.
    • (2002) J Neurochem , vol.82 , pp. 563-575
    • Beher, D.1    Wrigley, J.2    Owens, A.P.3    Shearman, M.S.4
  • 13
    • 4444340188 scopus 로고    scopus 로고
    • Identification of pleiotrophin in conditioned medium secreted from neural stem cells
    • Furuta, M., Shiraishi, T., Okamoto, H., Mineta, T., Tabuchi, K., and Shiwa, M. (2004) Identification of pleiotrophin in conditioned medium secreted from neural stem cells. Dev Brain Res, 152, 189-197.
    • (2004) Dev Brain Res , vol.152 , pp. 189-197
    • Furuta, M.1    Shiraishi, T.2    Okamoto, H.3    Mineta, T.4    Tabuchi, K.5    Shiwa, M.6
  • 14
    • 0036021212 scopus 로고    scopus 로고
    • Profiling of acyl-CoA oxidase-deficient and peroxisome proliferator Wy14, 643-treated mouse liver
    • Chu, R., Zhang, W., Lim, H., Yeldandi, A.V., Herring, C., Brumfield, L., Reddy, J.K., and Davison, M. (2002) Profiling of acyl-CoA oxidase-deficient and peroxisome proliferator Wy14, 643-treated mouse liver. Gene Expr, 10, 165-177.
    • (2002) Gene Expr , vol.10 , pp. 165-177
    • Chu, R.1    Zhang, W.2    Lim, H.3    Yeldandi, A.V.4    Herring, C.5    Brumfield, L.6    Reddy, J.K.7    Davison, M.8
  • 16
    • 4644293667 scopus 로고    scopus 로고
    • Detection and analysis of the cyanobacterial peptide hepatotoxins microcystin and nodularin
    • Yuan, M. and Carmichael, W.W. (2004) Detection and analysis of the cyanobacterial peptide hepatotoxins microcystin and nodularin. Toxicon, 44, 561-570.
    • (2004) Toxicon , vol.44 , pp. 561-570
    • Yuan, M.1    Carmichael, W.W.2
  • 21
    • 13244271405 scopus 로고    scopus 로고
    • Proteomic biomarker analysis of amniotic fluid for identification of intra-amniotic inflammation
    • Buhimschi, I.A., Christner, R., and Buhimschi, C.S. (2005) Proteomic biomarker analysis of amniotic fluid for identification of intra-amniotic inflammation. Br J Obstet Gynaecol, 112, 173-181.
    • (2005) Br J Obstet Gynaecol , vol.112 , pp. 173-181
    • Buhimschi, I.A.1    Christner, R.2    Buhimschi, C.S.3
  • 22
    • 0346101481 scopus 로고    scopus 로고
    • Urine protein profiling with surface-enhanced laser-desorption/ionization time-of-flight mass spectrometry
    • Schaub, S., Wilkins, J., Weiler, T., Sangster, K., Rush, D., and Nickerson, P. (2004) Urine protein profiling with surface-enhanced laser-desorption/ionization time-of-flight mass spectrometry. Kidney Int, 65, 323-332.
    • (2004) Kidney Int , vol.65 , pp. 323-332
    • Schaub, S.1    Wilkins, J.2    Weiler, T.3    Sangster, K.4    Rush, D.5    Nickerson, P.6
  • 23
    • 23844449368 scopus 로고    scopus 로고
    • Early prediction of acute renal injury using urinary proteomics
    • Nguyen, M., Ross, G., Dent, C., and Devarajan, P. (2005) Early prediction of acute renal injury using urinary proteomics. Am J Nephrol, 25, 318-326.
    • (2005) Am J Nephrol , vol.25 , pp. 318-326
    • Nguyen, M.1    Ross, G.2    Dent, C.3    Devarajan, P.4
  • 24
    • 4043094133 scopus 로고    scopus 로고
    • Proteomics in nephrology: current status and future directions
    • Thongboonkerd, V. (2004) Proteomics in nephrology: current status and future directions. Am J Nephrol, 24, 360-378.
    • (2004) Am J Nephrol , vol.24 , pp. 360-378
    • Thongboonkerd, V.1
  • 25
    • 20544450846 scopus 로고    scopus 로고
    • Proteomic analysis of renal diseases: unraveling the pathophysiology and biomarker discovery
    • Thongboonkerd, V. (2005) Proteomic analysis of renal diseases: unraveling the pathophysiology and biomarker discovery. Expert Rev Proteomics, 2, 349-366.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 349-366
    • Thongboonkerd, V.1
  • 26
    • 27844532498 scopus 로고    scopus 로고
    • Towards the application of proteomics in renal disease diagnosis
    • Vidal, B.C., Bonventre, J.V., and Hsu, S.I.-H. (2005) Towards the application of proteomics in renal disease diagnosis. Clin Sci, 109, 421-430.
    • (2005) Clin Sci , vol.109 , pp. 421-430
    • Vidal, B.C.1    Bonventre, J.V.2    Hsu, S.I.-H.3
  • 28
    • 33746795859 scopus 로고    scopus 로고
    • Technology insight: renal proteomics - at the crossroads between promise and problems
    • O'Riordan, E., Gross, S.S., and Goligorsky, M.S. (2006) Technology insight: renal proteomics - at the crossroads between promise and problems. Nat Clin Pract Nephrol, 2, 445-458.
    • (2006) Nat Clin Pract Nephrol , vol.2 , pp. 445-458
    • O'Riordan, E.1    Gross, S.S.2    Goligorsky, M.S.3
  • 29
    • 33750626759 scopus 로고    scopus 로고
    • Developing a tool for noninvasive monitoring of renal allografts
    • Schaub, S., Wilkins, J.A., Rush, D., and Nickerson, P. (2006) Developing a tool for noninvasive monitoring of renal allografts. Expert Rev Proteomics, 3, 497-509.
    • (2006) Expert Rev Proteomics , vol.3 , pp. 497-509
    • Schaub, S.1    Wilkins, J.A.2    Rush, D.3    Nickerson, P.4
  • 30
    • 33947574141 scopus 로고    scopus 로고
    • Diagnostic potential for urinary proteomics
    • Hortin, G.L. and Sviridov, D. (2007) Diagnostic potential for urinary proteomics. Pharmacogenomics, 8, 237-255.
    • (2007) Pharmacogenomics , vol.8 , pp. 237-255
    • Hortin, G.L.1    Sviridov, D.2
  • 35
    • 20544478148 scopus 로고    scopus 로고
    • Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands
    • Thulasiraman, V., Lin, S., Gheorghiu, L., Lathrop, J., Lomas, L., Hammond, D., and Boschetti, E. (2005) Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands. Electrophoresis, 26, 3561-3571.
    • (2005) Electrophoresis , vol.26 , pp. 3561-3571
    • Thulasiraman, V.1    Lin, S.2    Gheorghiu, L.3    Lathrop, J.4    Lomas, L.5    Hammond, D.6    Boschetti, E.7
  • 38
    • 0036130648 scopus 로고    scopus 로고
    • ProteinChip clinical proteomics:computational challenges and solutions
    • Fung, E. and Enderwick, C. (2002) ProteinChip clinical proteomics:computational challenges and solutions. Comput Proteomics, 32, S34-S41.
    • (2002) Comput Proteomics , vol.32
    • Fung, E.1    Enderwick, C.2
  • 39
    • 0037176211 scopus 로고    scopus 로고
    • SELDI - a new method for rapid development of process chromatography conditions
    • Weinberger, S.R., Boschetti, E., Santambien, P., and Brenac, V. (2002) SELDI - a new method for rapid development of process chromatography conditions. J Chromatogr A, 782, 307-316.
    • (2002) J Chromatogr A , vol.782 , pp. 307-316
    • Weinberger, S.R.1    Boschetti, E.2    Santambien, P.3    Brenac, V.4
  • 40
    • 0037725182 scopus 로고    scopus 로고
    • Endostatin capture from Pichia pastoris culture in a fluidized bed from on-chip process optimization to application
    • Shiloach, J., Santambien, P., Trinh, L., Schapman, A., and Boschetti, E. (2003) Endostatin capture from Pichia pastoris culture in a fluidized bed from on-chip process optimization to application. J Chromatogr A, 790, 327-336.
    • (2003) J Chromatogr A , vol.790 , pp. 327-336
    • Shiloach, J.1    Santambien, P.2    Trinh, L.3    Schapman, A.4    Boschetti, E.5
  • 42
    • 0035131550 scopus 로고    scopus 로고
    • Detection and identification of virulence factors in Yersinia pestis using SELDI ProteinChip System
    • Thulasiraman, V., McCutchen-Maloney, S.L., Motin, V.L., and Garcia, E. (2001) Detection and identification of virulence factors in Yersinia pestis using SELDI ProteinChip System. BioTechniques, 30, 428-432.
    • (2001) BioTechniques , vol.30 , pp. 428-432
    • Thulasiraman, V.1    McCutchen-Maloney, S.L.2    Motin, V.L.3    Garcia, E.4
  • 43
    • 0012472421 scopus 로고    scopus 로고
    • Identification of prostate-specific membrane antigen (PMSA) as the target of monoclonal antibody 107-1A4
    • Wang, S., Diamond, D.L., Hass, G.M., Sokoloff, R., and Vessella, R.L. (2001) Identification of prostate-specific membrane antigen (PMSA) as the target of monoclonal antibody 107-1A4. Int J Cancer, 92, 871-876.
    • (2001) Int J Cancer , vol.92 , pp. 871-876
    • Wang, S.1    Diamond, D.L.2    Hass, G.M.3    Sokoloff, R.4    Vessella, R.L.5
  • 44
    • 0034013944 scopus 로고    scopus 로고
    • Recent advancements in surface-enhanced laser desorption-ionization-time of flight-mass spectrometry
    • Merchant, M. and Weinberger, S.R. (2000) Recent advancements in surface-enhanced laser desorption-ionization-time of flight-mass spectrometry. Electrophoresis, 21, 1164-1177.
    • (2000) Electrophoresis , vol.21 , pp. 1164-1177
    • Merchant, M.1    Weinberger, S.R.2
  • 46
    • 0037844820 scopus 로고    scopus 로고
    • Characterization of renal allograft rejection by urinary proteomic analysis
    • Clarke, W., Silverman, B.C., Zhang, Z., Chan, D.W., Klein, A.S., and Molmenti, E.P. (2003) Characterization of renal allograft rejection by urinary proteomic analysis. Ann Surg, 237, 660-665.
    • (2003) Ann Surg , vol.237 , pp. 660-665
    • Clarke, W.1    Silverman, B.C.2    Zhang, Z.3    Chan, D.W.4    Klein, A.S.5    Molmenti, E.P.6
  • 52
    • 33751412843 scopus 로고    scopus 로고
    • Urinary proteomic profiles distinguish between active and inactive lupus nephritis
    • Mosley, K., Tam, F.W.K., Edwards, R.J., Crozier, J., Pusey, C.D., and Lightstone, L. (2006) Urinary proteomic profiles distinguish between active and inactive lupus nephritis. Rheumatology, 45, 1497-1504.
    • (2006) Rheumatology , vol.45 , pp. 1497-1504
    • Mosley, K.1    Tam, F.W.K.2    Edwards, R.J.3    Crozier, J.4    Pusey, C.D.5    Lightstone, L.6
  • 53
    • 84889357180 scopus 로고    scopus 로고
    • Identification of signature urinary biomarker patterns in lupus nephritis sub-types
    • Suzuki, M., Ross, G., Brunner, H., and Devarajan, P. (2006) Identification of signature urinary biomarker patterns in lupus nephritis sub-types. J Am Soc Nephrol, 17, 437A.
    • (2006) J Am Soc Nephrol , vol.17
    • Suzuki, M.1    Ross, G.2    Brunner, H.3    Devarajan, P.4
  • 54
    • 23944510681 scopus 로고    scopus 로고
    • Analysis of Human Proteome Organization Plasma Proteome Project (HUPO PPP) reference specimens using surface enhanced laser desorption/ionization-time of flight (SELDI-TOF) mass spectrometry:multi-institution correlation of spectra and identification of biomarkers
    • Rai, A.J., Stemmer, P.M., Zhang, Z., Adam, B.L., Morgan, W.T., Caffrey, R.E., Podust, V.N., Patel, M., Lim, L.Y., Shipulina, N.V., Chan, D.W., Semmes, O.J., and Leung, H.C. (2005) Analysis of Human Proteome Organization Plasma Proteome Project (HUPO PPP) reference specimens using surface enhanced laser desorption/ionization-time of flight (SELDI-TOF) mass spectrometry:multi-institution correlation of spectra and identification of biomarkers. Proteomics, 5, 3467-3474.
    • (2005) Proteomics , vol.5 , pp. 3467-3474
    • Rai, A.J.1    Stemmer, P.M.2    Zhang, Z.3    Adam, B.L.4    Morgan, W.T.5    Caffrey, R.E.6    Podust, V.N.7    Patel, M.8    Lim, L.Y.9    Shipulina, N.V.10    Chan, D.W.11    Semmes, O.J.12    Leung, H.C.13


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.