메뉴 건너뛰기




Volumn 10, Issue 2, 2011, Pages

Pressurized pepsin digestion in proteomics: An automatable alternative to trypsin for integrated top-down bottom-up proteomics

Author keywords

[No Author keywords available]

Indexed keywords

PEPSIN A; TRYPSIN; BACTERIAL PROTEIN; PEPTIDE; PROTEIN; PROTEOME;

EID: 78149422253     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.001479     Document Type: Article
Times cited : (47)

References (48)
  • 1
    • 0032455894 scopus 로고    scopus 로고
    • Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry
    • Kelleher, N. L., Taylor, S. V., Grannis, D., Kinsland, C., Chiu, H. J., Begley, T. P., and McLafferty, F. W. (1998) Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry. Protein Sci. 7, 1796-1801
    • (1998) Protein Sci. , vol.7 , pp. 1796-1801
    • Kelleher, N.L.1    Taylor, S.V.2    Grannis, D.3    Kinsland, C.4    Chiu, H.J.5    Begley, T.P.6    McLafferty, F.W.7
  • 3
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., and Yates, J. R., 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 4
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert, K., Goethals, M., Martens, L., Van Damme, J., Staes, A., Thomas, G. R., and Vandekerckhove, J. (2003) Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 21, 566-569
    • (2003) Nat. Biotechnol. , vol.21 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 5
  • 8
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A., Washburn, M. P., and Yates, J. R., 3rd (2001) An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73, 5683-5690
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 11
    • 0038070646 scopus 로고    scopus 로고
    • On-column digestion of proteins in aqueous-organic solvents
    • Slysz, G. W., and Schriemer, D. C. (2003) On-column digestion of proteins in aqueous-organic solvents. Rapid Commun. Mass Spectrom. 17, 1044-1050
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1044-1050
    • Slysz, G.W.1    Schriemer, D.C.2
  • 12
    • 15444379768 scopus 로고    scopus 로고
    • Blending protein separation and peptide analysis through real-time proteolytic digestion
    • Slysz, G. W., and Schriemer, D. C. (2005) Blending protein separation and peptide analysis through real-time proteolytic digestion. Anal. Chem. 77, 1572-1579
    • (2005) Anal. Chem. , vol.77 , pp. 1572-1579
    • Slysz, G.W.1    Schriemer, D.C.2
  • 14
    • 60649094922 scopus 로고    scopus 로고
    • Fast reversed-phase liquid chromatography to reduce back exchange and increase throughput in H/D exchange monitored by FT-ICR mass spectrometry
    • Zhang, H. M., Bou-Assaf, G. M., Emmett, M. R., and Marshall, A. G. (2009) Fast reversed-phase liquid chromatography to reduce back exchange and increase throughput in H/D exchange monitored by FT-ICR mass spectrometry. J. Am. Soc. Mass Spectrom. 20, 520-524
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 520-524
    • Zhang, H.M.1    Bou-Assaf, G.M.2    Emmett, M.R.3    Marshall, A.G.4
  • 15
    • 57449107282 scopus 로고    scopus 로고
    • Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry
    • Zhang, H. M., Kazazić, S., Schaub, T. M., Tipton, J. D., Emmett, M. R., and Marshall, A. G. (2008) Enhanced digestion efficiency, peptide ionization efficiency, and sequence resolution for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 80, 9034-9041
    • (2008) Anal. Chem. , vol.80 , pp. 9034-9041
    • Zhang, H.M.1    Kazazić, S.2    Schaub, T.M.3    Tipton, J.D.4    Emmett, M.R.5    Marshall, A.G.6
  • 16
    • 0034800836 scopus 로고    scopus 로고
    • Use of nitrocellulose films for affinity-directed mass spectrometry for the analysis of antibody/antigen interactions
    • Sun, S., Mo, W., Ji, Y., and Liu, S. (2001) Use of nitrocellulose films for affinity-directed mass spectrometry for the analysis of antibody/antigen interactions. Rapid Commun. Mass Spectrom. 15, 1743-1746
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1743-1746
    • Sun, S.1    Mo, W.2    Ji, Y.3    Liu, S.4
  • 17
    • 0035004248 scopus 로고    scopus 로고
    • Preparation and mass spectrometric study of egg yolk antibody (IgY) against rabies virus
    • Sun, S., Mo, W., Ji, Y., and Liu, S. (2001) Preparation and mass spectrometric study of egg yolk antibody (IgY) against rabies virus. Rapid Commun. Mass Spectrom. 15, 708-712
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 708-712
    • Sun, S.1    Mo, W.2    Ji, Y.3    Liu, S.4
  • 18
    • 33846458989 scopus 로고    scopus 로고
    • A triaxial probe for on-line proteolysis coupled with hydrogen/deuterium exchange-electrospray mass spectrometry
    • Chen, M., Cook, K. D., Kheterpal, I., and Wetzel, R. (2007) A triaxial probe for on-line proteolysis coupled with hydrogen/deuterium exchange-electrospray mass spectrometry. J. Am. Soc. Mass Spectrom. 18, 208-217
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 208-217
    • Chen, M.1    Cook, K.D.2    Kheterpal, I.3    Wetzel, R.4
  • 19
    • 0035797795 scopus 로고    scopus 로고
    • Structural features of the Abeta amyloid fibril elucidated by limited proteolysis
    • DOI 10.1021/bi010805z
    • Kheterpal, I., Williams, A., Murphy, C., Bledsoe, B., and Wetzel, R. (2001) Structural features of the Abeta amyloid fibril elucidated by limited proteolysis. Biochemistry 40, 11757-11767 (Pubitemid 32906037)
    • (2001) Biochemistry , vol.40 , Issue.39 , pp. 11757-11767
    • Kheterpal, I.1    Williams, A.2    Murphy, C.3    Bledsoe, B.4    Wetzel, R.5
  • 20
    • 26844475051 scopus 로고    scopus 로고
    • Ultra fast trypsin digestion of proteins by high intensity focused ultrasound
    • López-Ferrer, D., Capelo, J. L., and Vázquez, J. (2005) Ultra fast trypsin digestion of proteins by high intensity focused ultrasound. J. Proteome Res. 4, 1569-1574
    • (2005) J. Proteome Res. , vol.4 , pp. 1569-1574
    • López-Ferrer, D.1    Capelo, J.L.2    Vázquez, J.3
  • 21
    • 0037444512 scopus 로고    scopus 로고
    • Fast-response proteomics by accelerated in-gel digestion of proteins
    • Havlis, J., Thomas, H., Sebela, M., and Shevchenko, A. (2003) Fast-response proteomics by accelerated in-gel digestion of proteins. Anal. Chem. 75, 1300-1306
    • (2003) Anal. Chem. , vol.75 , pp. 1300-1306
    • Havlis, J.1    Thomas, H.2    Sebela, M.3    Shevchenko, A.4
  • 28
    • 34147152859 scopus 로고    scopus 로고
    • Ultrahigh-pressure dual online solid phase extraction/capillary reverse-phase liquid chromatography/tandem mass spectrometry (DO-SPE/cRPLC/MS/MS): A versatile separation platform for high-throughput and highly sensitive proteomic analyses
    • Min, H. K., Hyung, S. W., Shin, J. W., Nam, H. S., Ahn, S. H., Jung, H. J., and Lee, S. W. (2007) Ultrahigh-pressure dual online solid phase extraction/capillary reverse-phase liquid chromatography/tandem mass spectrometry (DO-SPE/cRPLC/MS/MS): a versatile separation platform for high-throughput and highly sensitive proteomic analyses. Electrophoresis 28, 1012-1021
    • (2007) Electrophoresis , vol.28 , pp. 1012-1021
    • Min, H.K.1    Hyung, S.W.2    Shin, J.W.3    Nam, H.S.4    Ahn, S.H.5    Jung, H.J.6    Lee, S.W.7
  • 30
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R., 3rd (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 33
    • 62149121444 scopus 로고    scopus 로고
    • Decon2LS: An open-source software package for automated processing and visualization of high resolution mass spectrometry data
    • Jaitly, N., Mayampurath, A., Littlefield, K., Adkins, J. N., Anderson, G. A., and Smith, R. D. (2009) Decon2LS: an open-source software package for automated processing and visualization of high resolution mass spectrometry data. BMC Bioinformatics 10, 87
    • (2009) BMC Bioinformatics , vol.10 , pp. 87
    • Jaitly, N.1    Mayampurath, A.2    Littlefield, K.3    Adkins, J.N.4    Anderson, G.A.5    Smith, R.D.6
  • 34
    • 54349083037 scopus 로고    scopus 로고
    • De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins
    • Shen, Y., Tolić, N., Hixson, K. K., Purvine, S. O., Anderson, G. A., and Smith, R. D. (2008) De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins. Anal. Chem. 80, 7742-7754
    • (2008) Anal. Chem. , vol.80 , pp. 7742-7754
    • Shen, Y.1    Tolić, N.2    Hixson, K.K.3    Purvine, S.O.4    Anderson, G.A.5    Smith, R.D.6
  • 35
    • 41449112363 scopus 로고    scopus 로고
    • Proteome-wide identification of proteins and their modifications with decreased ambiguities and improved false discovery rates using unique sequence tags
    • Shen, Y., Tolić, N., Hixson, K. K., Purvine, S. O., Pasa-Toliæ, L., Qian, W. J., Adkins, J. N., Moore, R. J., and Smith, R. D. (2008) Proteome-wide identification of proteins and their modifications with decreased ambiguities and improved false discovery rates using unique sequence tags. Anal. Chem. 80, 1871-1882
    • (2008) Anal. Chem. , vol.80 , pp. 1871-1882
    • Shen, Y.1    Tolić, N.2    Hixson, K.K.3    Purvine, S.O.4    Pasa-Toliæ, L.5    Qian, W.J.6    Adkins, J.N.7    Moore, R.J.8    Smith, R.D.9
  • 36
    • 52949098360 scopus 로고    scopus 로고
    • Protein meta-functional signatures from combining sequence, structure, evolution, and amino acid property information
    • Wang, K., Horst, J. A., Cheng, G., Nickle, D. C., and Samudrala, R. (2008) Protein meta-functional signatures from combining sequence, structure, evolution, and amino acid property information. PLoS Comput. Biol. 4, e1000181
    • (2008) PLoS Comput. Biol. , vol.4
    • Wang, K.1    Horst, J.A.2    Cheng, G.3    Nickle, D.C.4    Samudrala, R.5
  • 38
    • 77949786295 scopus 로고    scopus 로고
    • Value of using multiple proteases for large-scale mass spectrometry-based proteomics
    • Swaney, D. L., Wenger, C. D., and Coon, J. J. (2010) Value of using multiple proteases for large-scale mass spectrometry-based proteomics. J. Proteome Res. 9, 1323-1329
    • (2010) J. Proteome Res. , vol.9 , pp. 1323-1329
    • Swaney, D.L.1    Wenger, C.D.2    Coon, J.J.3
  • 42
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 44
    • 76849100851 scopus 로고    scopus 로고
    • Online, high-pressure digestion system for protein characterization by hydrogen/deuterium exchange and mass spectrometry
    • Jones, L. M., Zhang, H., Vidavsky, I., and Gross, M. L. (2010) Online, high-pressure digestion system for protein characterization by hydrogen/deuterium exchange and mass spectrometry. Anal. Chem. 82, 1171-1174
    • (2010) Anal. Chem. , vol.82 , pp. 1171-1174
    • Jones, L.M.1    Zhang, H.2    Vidavsky, I.3    Gross, M.L.4
  • 45
    • 33746224344 scopus 로고    scopus 로고
    • Nanopore-based proteolytic reactor for sensitive and comprehensive proteomic analyses
    • DOI 10.1021/ac060116z
    • Shui, W., Fan, J., Yang, P., Liu, C., Zhai, J., Lei, J., Yan, Y., Zhao, D., and Chen, X. (2006) Nanopore-based proteolytic reactor for sensitive and comprehensive proteomic analyses. Anal. Chem. 78, 4811-4819 (Pubitemid 44100614)
    • (2006) Analytical Chemistry , vol.78 , Issue.14 , pp. 4811-4819
    • Shui, W.1    Fan, J.2    Yang, P.3    Liu, C.4    Zhai, J.5    Lei, J.6    Yan, Y.7    Zhao, D.8    Chen, X.9
  • 46
    • 33747202736 scopus 로고    scopus 로고
    • Detection and identification of sub-nanogram levels of protein in a nanoLC-trypsin-MS system
    • Slysz, G. W., Lewis, D. F., and Schriemer, D. C. (2006) Detection and identification of sub-nanogram levels of protein in a nanoLC-trypsin-MS system. J. Proteome Res. 5, 1959-1966
    • (2006) J. Proteome Res. , vol.5 , pp. 1959-1966
    • Slysz, G.W.1    Lewis, D.F.2    Schriemer, D.C.3
  • 47
    • 70549103114 scopus 로고    scopus 로고
    • Rheostatic control of tryptic digestion in a microscale fluidic system
    • Percy, A. J., and Schriemer, D. C. (2010) Rheostatic control of tryptic digestion in a microscale fluidic system. Anal. Chim. Acta 657, 53-59
    • (2010) Anal. Chim. Acta , vol.657 , pp. 53-59
    • Percy, A.J.1    Schriemer, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.