메뉴 건너뛰기




Volumn 702, Issue , 2011, Pages 163-190

Gel-Based and Gel-Free Proteomic Technologies

Author keywords

Adipose derived stem cells; iTRAQ ; Liquid chromatography; Mass spectrometry; Proteomics; Two dimensional difference in gel electrophoresis

Indexed keywords

ADIPOSE DERIVED STEM CELL; CONTROLLED STUDY; HUMAN CELL; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEOMICS; TWO DIMENSIONAL DIFFERENCE GEL ELECTROPHORESIS; AMINO ACID SEQUENCE; ARTICLE; BIOASSAY; CELL FRACTIONATION; CHEMISTRY; HUMAN; ION EXCHANGE CHROMATOGRAPHY; ISOELECTRIC FOCUSING; ISOLATION AND PURIFICATION; ISOTOPE LABELING; METHODOLOGY; MOLECULAR GENETICS; PRECIPITATION; REVERSED PHASE LIQUID CHROMATOGRAPHY; STAINING; TWO DIMENSIONAL GEL ELECTROPHORESIS;

EID: 79952117255     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61737-960-4_13     Document Type: Chapter
Times cited : (48)

References (33)
  • 2
    • 0242552104 scopus 로고    scopus 로고
    • Adipose-derived adult stem cells: Isolation, characterization, and differentiation potential
    • Gimble, J. and Guilak, F. (2003) Adipose-derived adult stem cells: isolation, characterization, and differentiation potential. Cytotherapy 5, 362–9.
    • (2003) Cytotherapy , vol.5 , pp. 362-369
    • Gimble, J.1    Guilak, F.2
  • 6
    • 37349117349 scopus 로고    scopus 로고
    • Evidence supporting antioxidant action of adipose-derived stem cells: Protection of human dermal fibroblasts from oxidative stress
    • Kim, W. S., Park, B. S., Kim, H. K., Park, J. S., Kim, K. J., Choi, J. S., Chung, S. J., Kim, D. D., and Sung, J. H. (2008) Evidence supporting antioxidant action of adipose-derived stem cells: protection of human dermal fibroblasts from oxidative stress. J Dermatol Sci 49, 133–42.
    • (2008) J Dermatol Sci , vol.49 , pp. 133-142
    • Kim, W.S.1    Park, B.S.2    Kim, H.K.3    Park, J.S.4    Kim, K.J.5    Choi, J.S.6    Chung, S.J.7    Kim, D.D.8    Sung, J.H.9
  • 7
    • 40949099450 scopus 로고    scopus 로고
    • Cell specific differences between human adipose-derived and mesenchymal-stromal cells despite similar differentiation potentials
    • Noel, D., Caton, D., Roche, S., Bony, C., Lehmann, S., Casteilla, L., Jorgensen, C., and Cousin, B. (2008) Cell specific differences between human adipose-derived and mesenchymal-stromal cells despite similar differentiation potentials. Exp Cell Res 314, 1575–84.
    • (2008) Exp Cell Res , vol.314 , pp. 1575-1584
    • Noel, D.1    Caton, D.2    Roche, S.3    Bony, C.4    Lehmann, S.5    Casteilla, L.6    Jorgensen, C.7    Cousin, B.8
  • 10
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • Cravatt, B. F., Simon, G. M., and Yates, J. R., 3rd (2007) The biological impact of mass-spectrometry-based proteomics. Nature 450, 991–1000.
    • (2007) Nature , vol.450 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates, J.R.3
  • 11
    • 36549025838 scopus 로고    scopus 로고
    • Proteomics for biomarker discovery in acute kidney injury
    • Devarajan, P. (2007) Proteomics for biomarker discovery in acute kidney injury. Semin Nephrol 27, 637–51.
    • (2007) Semin Nephrol , vol.27 , pp. 637-651
    • Devarajan, P.1
  • 12
    • 36549001613 scopus 로고    scopus 로고
    • Proteomics and diabetic nephropathy
    • Merchant, M. L. and Klein, J. B. (2007) Proteomics and diabetic nephropathy. Semin Nephrol 27, 627–36.
    • (2007) Semin Nephrol , vol.27 , pp. 627-636
    • Merchant, M.L.1    Klein, J.B.2
  • 13
    • 53649087120 scopus 로고    scopus 로고
    • Proteomic approaches in biological and medical sciences: Principles and applications
    • Conrotto, P. and Souchelnytskyi, S. (2008) Proteomic approaches in biological and medical sciences: principles and applications. Exp Oncol 30, 171–80.
    • (2008) Exp Oncol , vol.30 , pp. 171-180
    • Conrotto, P.1    Souchelnytskyi, S.2
  • 14
    • 20544435982 scopus 로고    scopus 로고
    • Proteomics: From gel based to gel free
    • Lambert, J. P., Ethier, M., Smith, J. C., and Figeys, D. (2005) Proteomics: from gel based to gel free. Anal Chem 77, 3771–87.
    • (2005) Anal Chem , vol.77 , pp. 3771-3787
    • Lambert, J.P.1    Ethier, M.2    Smith, J.C.3    Figeys, D.4
  • 15
    • 67249117201 scopus 로고    scopus 로고
    • Proteomics: From technology developments to biological applications
    • Abu-Farha, M., Elisma, F., Zhou, H., Tian, R., Asmer, M. S., and Figeys, D. (2009) Proteomics: from technology developments to biological applications. Anal Chem 81, 4585–99.
    • (2009) Anal Chem , vol.81 , pp. 4585-4599
    • Abu-Farha, M.1    Elisma, F.2    Zhou, H.3    Tian, R.4    Asmer, M.S.5    Figeys, D.6
  • 16
    • 34548522775 scopus 로고    scopus 로고
    • Advances in proteomic workflows for systems biology
    • Malmstrom, J., Lee, H., and Aebersold, R. (2007) Advances in proteomic workflows for systems biology. Curr Opin Biotechnol 18, 378–84.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 378-384
    • Malmstrom, J.1    Lee, H.2    Aebersold, R.3
  • 17
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E. and Mann, M. (2005) Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol 1, 252–62.
    • (2005) Nat Chem Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 19
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O’Farrell, P. H. (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250, 4007–21.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O’Farrell, P.H.1
  • 20
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg, A., Weiss, W., and Dunn, M. J. (2004) Current two-dimensional electrophoresis technology for proteomics. Proteomics 4, 3665–85.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 21
    • 33748571491 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry
    • Wittmann-Liebold, B., Graack, H. R., and Pohl, T. (2006) Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry. Proteomics 6, 4688–703.
    • (2006) Proteomics , vol.6 , pp. 4688-4703
    • Wittmann-Liebold, B.1    Graack, H.R.2    Pohl, T.3
  • 22
    • 21244495253 scopus 로고    scopus 로고
    • The development of the DIGE system: 2D fluorescence difference gel analysis technology
    • Marouga, R., David, S., and Hawkins, E. (2005) The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal Bioanal Chem 382, 669–78.
    • (2005) Anal Bioanal Chem , vol.382 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 23
    • 77957255724 scopus 로고    scopus 로고
    • Regulation of insulin action by an extract of Artemisia dracunculus L. in primary human skeletal muscle culture – a proteomics approach
    • Kheterpal, I., Coleman, L., Ku, G., Wang, Z. Q., Ribnicky, D., and Cefalu, W. T. (2010) Regulation of insulin action by an extract of Artemisia dracunculus L. in primary human skeletal muscle culture – a proteomics approach. Phytother Res 24, 1278–84.
    • (2010) Phytother Res , vol.24 , pp. 1278-1284
    • Kheterpal, I.1    Coleman, L.2    Ku, G.3    Wang, Z.Q.4    Ribnicky, D.5    Cefalu, W.T.6
  • 24
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198–207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 25
    • 0036391454 scopus 로고    scopus 로고
    • Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Griffin, T. J., Eng, J., and Aebersold, R. (2002) Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags. J Proteome Res 1, 47–54.
    • (2002) J Proteome Res , vol.1 , pp. 47-54
    • Gygi, S.P.1    Rist, B.2    Griffin, T.J.3    Eng, J.4    Aebersold, R.5
  • 26
    • 33746255981 scopus 로고    scopus 로고
    • Identification of differentiating neural progenitor cell markers using shotgun isobaric tagging mass spectrometry
    • Salim, K., Kehoe, L., Minkoff, M. S., Bilsland, J. G., Munoz-Sanjuan, I., and Guest, P. C. (2006) Identification of differentiating neural progenitor cell markers using shotgun isobaric tagging mass spectrometry. Stem Cells Dev 15, 461–70.
    • (2006) Stem Cells Dev , vol.15 , pp. 461-470
    • Salim, K.1    Kehoe, L.2    Minkoff, M.S.3    Bilsland, J.G.4    Munoz-Sanjuan, I.5    Guest, P.C.6
  • 27
    • 35848931437 scopus 로고    scopus 로고
    • The use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia
    • Griffiths, S. D., Burthem, J., Unwin, R. D., Holyoake, T. L., Melo, J. V., Lucas, G. S., and Whetton, A. D. (2007) The use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia. Mol Biotechnol 36, 81–9.
    • (2007) Mol Biotechnol , vol.36 , pp. 81-89
    • Griffiths, S.D.1    Burthem, J.2    Unwin, R.D.3    Holyoake, T.L.4    Melo, J.V.5    Lucas, G.S.6    Whetton, A.D.7
  • 28
    • 33749630783 scopus 로고    scopus 로고
    • An integrated approach to mapping the proteome of the human bone marrow stromal cell
    • Seshi, B. (2006) An integrated approach to mapping the proteome of the human bone marrow stromal cell. Proteomics 6, 5169–82.
    • (2006) Proteomics , vol.6 , pp. 5169-5182
    • Seshi, B.1
  • 29
    • 39749195587 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of protein changes during platelet storage requires complementary proteomic approaches
    • Thon, J. N., Schubert, P., Duguay, M., Serrano, K., Lin, S., Kast, J., and Devine, D. V. (2008) Comprehensive proteomic analysis of protein changes during platelet storage requires complementary proteomic approaches. Transfusion 48, 425–35.
    • (2008) Transfusion , vol.48 , pp. 425-435
    • Thon, J.N.1    Schubert, P.2    Duguay, M.3    Serrano, K.4    Lin, S.5    Kast, J.6    Devine, D.V.7
  • 30
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel-or LC-MALDITOF/ TOF
    • Wu, W. W., Wang, G. H., Baek, S. J., and Shen, R. F. (2006) Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel-or LC-MALDITOF/ TOF. J Proteome Res 5, 651–58.
    • (2006) J Proteome Res , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.H.2    Baek, S.J.3    Shen, R.F.4
  • 31
    • 18844447205 scopus 로고    scopus 로고
    • Saturation labeling with cysteine-reactive cyanine fluorescent dyes provides increased sensitivity for protein expression profiling of laser-microdissected clinical specimens
    • Greengauz-Roberts, O., Stoppler, H., Nomura, S., Yamaguchi, H., Goldenring, J. R., Podolsky, R. H., Lee, J. R., and Dynan, W. S. (2005) Saturation labeling with cysteine-reactive cyanine fluorescent dyes provides increased sensitivity for protein expression profiling of laser-microdissected clinical specimens. Proteomics 5, 1746–57.
    • (2005) Proteomics , vol.5 , pp. 1746-1757
    • Greengauz-Roberts, O.1    Stoppler, H.2    Nomura, S.3    Yamaguchi, H.4    Goldenring, J.R.5    Podolsky, R.H.6    Lee, J.R.7    Dynan, W.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.