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Volumn 100, Issue , 2014, Pages 79-91

Absolute proteomic quantification of the activity state of proteases and proteolytic cleavages using proteolytic signature peptides and isobaric tags

Author keywords

Degradomics; ITRAQ synthesis; MMPs; Protease; Proteolytic cleavages; Proteomics

Indexed keywords

CARBON 13; ENZYME PRECURSOR; GELATINASE A; INTERSTITIAL COLLAGENASE; NEUTROPHIL COLLAGENASE; PEPTIDE; PROTEINASE; PROTEOLYTIC SIGNATURE PEPTIDE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; UNCLASSIFIED DRUG; CARBON; MATRIX METALLOPROTEINASE; PEPTIDE HYDROLASE; TRYPSIN;

EID: 84897097267     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.09.006     Document Type: Article
Times cited : (26)

References (60)
  • 1
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: a new challenge for proteomics
    • Lopez-Otin C., Overall C.M. Protease degradomics: a new challenge for proteomics. Nat Rev Mol Cell Biol 2002, 3:509-519.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2
  • 2
    • 2442547741 scopus 로고    scopus 로고
    • Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies
    • Salvesen G.S., Abrams J.M. Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies. Oncogene 2004, 23:2774-2784.
    • (2004) Oncogene , vol.23 , pp. 2774-2784
    • Salvesen, G.S.1    Abrams, J.M.2
  • 3
    • 84881517471 scopus 로고    scopus 로고
    • Using proteomics to uncover extracellular matrix interactions during cardiac remodeling
    • Patterson N.L., Iyer R.P., Bras L.D., Li Y., Andrews T.G., Aune G.J., et al. Using proteomics to uncover extracellular matrix interactions during cardiac remodeling. Proteomics Clin Appl 2013, 7:516-527.
    • (2013) Proteomics Clin Appl , vol.7 , pp. 516-527
    • Patterson, N.L.1    Iyer, R.P.2    Bras, L.D.3    Li, Y.4    Andrews, T.G.5    Aune, G.J.6
  • 4
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: linking extracellular proteases to substrates
    • Overall C.M., Blobel C.P. In search of partners: linking extracellular proteases to substrates. Nat Rev Mol Cell Biol 2007, 8:245-257.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2
  • 5
    • 35648998466 scopus 로고    scopus 로고
    • Proteomics evaluation of chemically cleavable activity-based probes
    • Fonovic M., Verhelst S.H.L., Sorum M.T., Bogyo M. Proteomics evaluation of chemically cleavable activity-based probes. Mol Cell Proteomics 2007, 6:1761-1770.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1761-1770
    • Fonovic, M.1    Verhelst, S.H.L.2    Sorum, M.T.3    Bogyo, M.4
  • 6
    • 84875255239 scopus 로고    scopus 로고
    • Protein TAILS: when termini tell tales of proteolysis and function
    • Lange P.F., Overall C.M. Protein TAILS: when termini tell tales of proteolysis and function. Curr Opin Chem Biol 2013, 1:73-82.
    • (2013) Curr Opin Chem Biol , vol.1 , pp. 73-82
    • Lange, P.F.1    Overall, C.M.2
  • 7
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Ruth F.X. Structural aspects of the metzincin clan of metalloendopeptidases. Mol Biotechnol 2003, 24:157-202.
    • (2003) Mol Biotechnol , vol.24 , pp. 157-202
    • Gomis-Ruth, F.X.1
  • 8
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol Cell 2002, 9:459-470.
    • (2002) Mol Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 9
    • 0036144679 scopus 로고    scopus 로고
    • Caspase activation and disruption of mitochondrial membrane potential during UV radiation-induced apoptosis of human keratinocytes requires activation of protein kinase C
    • Denning M.F., Wang Y., Tibudan S., Alkan S., Nickoloff B.J., Qin J.Z. Caspase activation and disruption of mitochondrial membrane potential during UV radiation-induced apoptosis of human keratinocytes requires activation of protein kinase C. Cell Death Differ 2002, 9:40-52.
    • (2002) Cell Death Differ , vol.9 , pp. 40-52
    • Denning, M.F.1    Wang, Y.2    Tibudan, S.3    Alkan, S.4    Nickoloff, B.J.5    Qin, J.Z.6
  • 12
    • 33646576168 scopus 로고    scopus 로고
    • Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer
    • Overall C.M., Dean R.A. Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer. Cancer Metastasis Rev 2006, 25:69-75.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 69-75
    • Overall, C.M.1    Dean, R.A.2
  • 13
    • 84880017266 scopus 로고    scopus 로고
    • TNFα cleavage beyond TACE/ADAM17: matrix metalloproteinase 13 is a potential therapeutic target in sepsis and colitis
    • Becker-Pauly C., Rose-John S. TNFα cleavage beyond TACE/ADAM17: matrix metalloproteinase 13 is a potential therapeutic target in sepsis and colitis. EMBO Mol Med 2013, 5:970-972.
    • (2013) EMBO Mol Med , vol.5 , pp. 970-972
    • Becker-Pauly, C.1    Rose-John, S.2
  • 15
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick D.S., Gerber S.A., Gygi S.P. The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 2005, 35:265-273.
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 16
    • 84867026555 scopus 로고    scopus 로고
    • PSAQ standards for accurate MS-based quantification of proteins: from the concept to biomedical applications
    • Picard G., Lebert D., Louwagie M., Adrait A., Huillet C., Vandenesch F., et al. PSAQ standards for accurate MS-based quantification of proteins: from the concept to biomedical applications. J Mass Spectrom 2012, 47:1353-1363.
    • (2012) J Mass Spectrom , vol.47 , pp. 1353-1363
    • Picard, G.1    Lebert, D.2    Louwagie, M.3    Adrait, A.4    Huillet, C.5    Vandenesch, F.6
  • 17
    • 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
  • 18
    • 80053404377 scopus 로고    scopus 로고
    • Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates
    • Kleifeld O., Doucet A., Prudova A.,Keller U., Gioia M., Kizhakkedathu J.N., et al. Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates. Nat Protoc 2011, 6:1578-1611.
    • (2011) Nat Protoc , vol.6 , pp. 1578-1611
    • Kleifeld, O.1    Doucet, A.2    Prudova, A.3    Keller, U.4    Gioia, M.5    Kizhakkedathu, J.N.6
  • 19
    • 34247341829 scopus 로고    scopus 로고
    • Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome
    • Dean R.A., Overall C.M. Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome. Mol Cell Proteomics 2007, 6:611-623.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 611-623
    • Dean, R.A.1    Overall, C.M.2
  • 20
    • 49549113643 scopus 로고    scopus 로고
    • Global mapping of the topography and magnitude of proteolytic events in apoptosis
    • Dix M.M., Simon G.M., Cravatt B.F. Global mapping of the topography and magnitude of proteolytic events in apoptosis. Cell 2008, 134:679-691.
    • (2008) Cell , vol.134 , pp. 679-691
    • Dix, M.M.1    Simon, G.M.2    Cravatt, B.F.3
  • 21
    • 52649141086 scopus 로고    scopus 로고
    • Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini
    • Mahrus S., Trinidad J.C., Barkan D.T., Sali A., Burlingame A.L., Wells J.A. Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini. Cell 2008, 134:866-876.
    • (2008) Cell , vol.134 , pp. 866-876
    • Mahrus, S.1    Trinidad, J.C.2    Barkan, D.T.3    Sali, A.4    Burlingame, A.L.5    Wells, J.A.6
  • 23
    • 33846807650 scopus 로고    scopus 로고
    • Tagging and detection strategies for activity-based proteomics
    • Sadaghiani A.M., Verhelst S.H., Bogyo M. Tagging and detection strategies for activity-based proteomics. Curr Opin Chem Biol 2007, 11:20-28.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 20-28
    • Sadaghiani, A.M.1    Verhelst, S.H.2    Bogyo, M.3
  • 24
    • 84879378806 scopus 로고    scopus 로고
    • Relative quantification of proteasome activity by activity-based protein profiling and LC-MS/MS
    • Li N., Kuo C.L., Paniagua G., van den Elst H., Verdoes M., Willems L.I., et al. Relative quantification of proteasome activity by activity-based protein profiling and LC-MS/MS. Nat Protoc 2013, 8:1155-1168.
    • (2013) Nat Protoc , vol.8 , pp. 1155-1168
    • Li, N.1    Kuo, C.L.2    Paniagua, G.3    van den Elst, H.4    Verdoes, M.5    Willems, L.I.6
  • 25
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • Jeffery D.A., Bogyo M. Chemical proteomics and its application to drug discovery. Curr Opin Biotechnol 2003, 14:87-95.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 87-95
    • Jeffery, D.A.1    Bogyo, M.2
  • 26
    • 1042287130 scopus 로고    scopus 로고
    • The development and application of methods for activity-based protein profiling
    • Jessani N., Cravatt B.F. The development and application of methods for activity-based protein profiling. Curr Opin Chem Biol 2004, 8:54-59.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 54-59
    • Jessani, N.1    Cravatt, B.F.2
  • 28
    • 79960436501 scopus 로고    scopus 로고
    • Global absolute quantification of a proteome: challenges in the deployment of a QconCAT strategy
    • Brownridge P., Holman S.W., Gaskell S.J., Grant C.M., Harman V.M., Hubbard S.J., et al. Global absolute quantification of a proteome: challenges in the deployment of a QconCAT strategy. Proteomics 2011, 11:2957-2970.
    • (2011) Proteomics , vol.11 , pp. 2957-2970
    • Brownridge, P.1    Holman, S.W.2    Gaskell, S.J.3    Grant, C.M.4    Harman, V.M.5    Hubbard, S.J.6
  • 29
    • 0348014635 scopus 로고    scopus 로고
    • Stable-isotope dimethyl labeling for quantitative proteomics
    • Hsu J.L., Huang S.Y., Chow N.H., Chen S.H. Stable-isotope dimethyl labeling for quantitative proteomics. Anal Chem 2003, 75:6843-6852.
    • (2003) Anal Chem , vol.75 , pp. 6843-6852
    • Hsu, J.L.1    Huang, S.Y.2    Chow, N.H.3    Chen, S.H.4
  • 30
    • 0033915395 scopus 로고    scopus 로고
    • Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using (18)O-labeled internal standards
    • Mirgorodskaya O.A., Kozmin Y.P., Titov M.I., Korner R., Sonksen C.P., Roepstorff P. Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using (18)O-labeled internal standards. Rapid Commun Mass Spectrom 2000, 14:1226-1232.
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 1226-1232
    • Mirgorodskaya, O.A.1    Kozmin, Y.P.2    Titov, M.I.3    Korner, R.4    Sonksen, C.P.5    Roepstorff, P.6
  • 31
    • 84864117127 scopus 로고    scopus 로고
    • Absolute quantification of proteins using standard peptides and multiple reaction monitoring
    • Schmidt C., Urlaub H. Absolute quantification of proteins using standard peptides and multiple reaction monitoring. Methods Mol Biol 2012, 893:249-265.
    • (2012) Methods Mol Biol , vol.893 , pp. 249-265
    • Schmidt, C.1    Urlaub, H.2
  • 32
    • 84878446393 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade
    • Vandooren J., den Steen PE Van, Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade. Crit Rev Biochem Mol Biol 2013, 48:222-272.
    • (2013) Crit Rev Biochem Mol Biol , vol.48 , pp. 222-272
    • Vandooren, J.1    Steen, V.2    Opdenakker, G.3
  • 33
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • Mott J.D., Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol 2004, 16:558-564.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 35
    • 0035328844 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-4 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1-matrix metalloproteinase
    • Bigg H.F., Morrison C.J., Butler G.S., Bogoyevitch M.A.Wang Z., Soloway P.D., Overall C.M. Tissue inhibitor of metalloproteinases-4 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1-matrix metalloproteinase. Cancer Res 2001, 61:3610-3618.
    • (2001) Cancer Res , vol.61 , pp. 3610-3618
    • Bigg, H.F.1    Morrison, C.J.2    Butler, G.S.3    Bogoyevitch, M.A.W.Z.4    Soloway, P.D.5    Overall, C.M.6
  • 36
    • 33748748477 scopus 로고    scopus 로고
    • TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains
    • Morrison C.J., Overall C.M. TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains. J Biol Chem 2006, 281:26528-26539.
    • (2006) J Biol Chem , vol.281 , pp. 26528-26539
    • Morrison, C.J.1    Overall, C.M.2
  • 37
    • 66249146087 scopus 로고    scopus 로고
    • Chemical cross-linking with NHS esters: a systematic study on amino acid reactivities
    • Madler S., Bich C., Touboul D., Zenobi R. Chemical cross-linking with NHS esters: a systematic study on amino acid reactivities. J Mass Spectrom 2009, 44:694-706.
    • (2009) J Mass Spectrom , vol.44 , pp. 694-706
    • Madler, S.1    Bich, C.2    Touboul, D.3    Zenobi, R.4
  • 38
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban G.A., Gong J.H., Wong J.P., Wallace J.L., Clark-Lewis I., Overall C.M. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 2002, 100:1160-1167.
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1    Gong, J.H.2    Wong, J.P.3    Wallace, J.L.4    Clark-Lewis, I.5    Overall, C.M.6
  • 39
    • 0025096722 scopus 로고
    • Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation
    • Springman E.B., Angleton E.L., Birkedal-Hansen H., Van Wart H.E. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc Natl Acad Sci U S A 1990, 87:364-368.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 364-368
    • Springman, E.B.1    Angleton, E.L.2    Birkedal-Hansen, H.3    Van Wart, H.E.4
  • 40
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C., Dowdle E.B. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal Biochem 1980, 102:196-202.
    • (1980) Anal Biochem , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 41
    • 0028345645 scopus 로고
    • Quantitative zymography: detection of picogram quantities of gelatinases
    • Kleiner D.E., Stetler-Stevenson W.G. Quantitative zymography: detection of picogram quantities of gelatinases. Anal Biochem 1994, 218:325-329.
    • (1994) Anal Biochem , vol.218 , pp. 325-329
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 42
    • 33748550328 scopus 로고    scopus 로고
    • Combined determination of plasma MMP2, MMP9, and TIMP1 improves the non-invasive detection of transitional cell carcinoma of the bladder
    • Staack A., Badendieck S., Schnorr D., Loening S.A., Jung K. Combined determination of plasma MMP2, MMP9, and TIMP1 improves the non-invasive detection of transitional cell carcinoma of the bladder. BMC Urol 2006, 6:19.
    • (2006) BMC Urol , vol.6 , pp. 19
    • Staack, A.1    Badendieck, S.2    Schnorr, D.3    Loening, S.A.4    Jung, K.5
  • 43
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross P.L., Huang Y.N., Marchese J.N., Williamson B., Parker K., Hattan S., et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 2004, 3:1154-1169.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4    Parker, K.5    Hattan, S.6
  • 44
    • 33646439273 scopus 로고    scopus 로고
    • Matrix metalloproteinases/tissue inhibitors of metalloproteinases: relationship between changes in proteolytic determinants of matrix composition and structural, functional, and clinical manifestations of hypertensive heart disease
    • Ahmed S.H., Clark L.L., Pennington W.R., Webb C.S., Bonnema D.D., Leonardi A.H., et al. Matrix metalloproteinases/tissue inhibitors of metalloproteinases: relationship between changes in proteolytic determinants of matrix composition and structural, functional, and clinical manifestations of hypertensive heart disease. Circulation 2006, 113:2089-2096.
    • (2006) Circulation , vol.113 , pp. 2089-2096
    • Ahmed, S.H.1    Clark, L.L.2    Pennington, W.R.3    Webb, C.S.4    Bonnema, D.D.5    Leonardi, A.H.6
  • 45
    • 0842310469 scopus 로고    scopus 로고
    • Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS
    • Gehrig P.M., Hunziker P.E., Zahariev S., Pongor S. Fragmentation pathways of N(G)-methylated and unmodified arginine residues in peptides studied by ESI-MS/MS and MALDI-MS. J Am Soc Mass Spectrom 2004, 15:142-149.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 142-149
    • Gehrig, P.M.1    Hunziker, P.E.2    Zahariev, S.3    Pongor, S.4
  • 48
    • 84878644042 scopus 로고    scopus 로고
    • Targeted quantitation of proteins by mass spectrometry
    • Liebler D.C., Zimmerman L.J. Targeted quantitation of proteins by mass spectrometry. Biochemistry 2013, 52:3797-3806.
    • (2013) Biochemistry , vol.52 , pp. 3797-3806
    • Liebler, D.C.1    Zimmerman, L.J.2
  • 49
    • 84860856325 scopus 로고    scopus 로고
    • Range of protein detection by selected/multiple reaction monitoring mass spectrometry in an unfractionated human cell culture lysate
    • Ebhardt H.A., Sabido E., Huttenhain R., Collins B., Aebersold R. Range of protein detection by selected/multiple reaction monitoring mass spectrometry in an unfractionated human cell culture lysate. Proteomics 2012, 12:1185-1193.
    • (2012) Proteomics , vol.12 , pp. 1185-1193
    • Ebhardt, H.A.1    Sabido, E.2    Huttenhain, R.3    Collins, B.4    Aebersold, R.5
  • 51
    • 42349105213 scopus 로고    scopus 로고
    • Relative quantification of proteins in human cerebrospinal fluids by MS/MS using 6-plex isobaric tags
    • Dayon L., Hainard A., Licker V., Turck N., Kuhn K., Hochstrasser D.F., et al. Relative quantification of proteins in human cerebrospinal fluids by MS/MS using 6-plex isobaric tags. Anal Chem 2008, 80:2921-2931.
    • (2008) Anal Chem , vol.80 , pp. 2921-2931
    • Dayon, L.1    Hainard, A.2    Licker, V.3    Turck, N.4    Kuhn, K.5    Hochstrasser, D.F.6
  • 52
    • 33644669753 scopus 로고    scopus 로고
    • Automated comparative proteomics based on multiplex tandem mass spectrometry and stable isotope labeling
    • Zhang G., Neubert T.A. Automated comparative proteomics based on multiplex tandem mass spectrometry and stable isotope labeling. Mol Cell Proteomics 2006, 5:401-411.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 401-411
    • Zhang, G.1    Neubert, T.A.2
  • 53
    • 33645715370 scopus 로고    scopus 로고
    • Multiple reaction monitoring as a method for identifying protein posttranslational modifications
    • Cox D.M., Zhong F., Du M., Duchoslav E., Sakuma T., McDermott J.C. Multiple reaction monitoring as a method for identifying protein posttranslational modifications. J Biomol Tech 2005, 16:83-90.
    • (2005) J Biomol Tech , vol.16 , pp. 83-90
    • Cox, D.M.1    Zhong, F.2    Du, M.3    Duchoslav, E.4    Sakuma, T.5    McDermott, J.C.6
  • 55
    • 33748573295 scopus 로고    scopus 로고
    • Enhanced sequencing coverage of proteins in human cerebrospinal fluid using multiple enzymatic digestion and linear ion trap LC-MS/MS
    • Biringer R.G., Amato H., Harrington M.G., Fonteh A.N., Riggens J.N., Huhmer A.F. Enhanced sequencing coverage of proteins in human cerebrospinal fluid using multiple enzymatic digestion and linear ion trap LC-MS/MS. Brief Funct Genomic Proteomic 2006, 5:144-153.
    • (2006) Brief Funct Genomic Proteomic , vol.5 , pp. 144-153
    • Biringer, R.G.1    Amato, H.2    Harrington, M.G.3    Fonteh, A.N.4    Riggens, J.N.5    Huhmer, A.F.6
  • 56
    • 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. 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
  • 57
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 58
    • 55049133250 scopus 로고    scopus 로고
    • Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome
    • Doucet A., Butler G.S., Rodriguez D., Prudova A., Overall C.M. Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome. Mol Cell Proteomics 2008, 7:1925-1951.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1925-1951
    • Doucet, A.1    Butler, G.S.2    Rodriguez, D.3    Prudova, A.4    Overall, C.M.5
  • 59
    • 77951134556 scopus 로고    scopus 로고
    • Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics
    • Prudova A., Prudova A., auf dem Keller U., Butler G.S., Overall C.M. Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics. Mol Cell Proteomics 2010, 9:894-911.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 894-911
    • Prudova, A.1    Prudova, A.2    Keller, U.3    Butler, G.S.4    Overall, C.M.5
  • 60
    • 77749320923 scopus 로고    scopus 로고
    • Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products
    • Kleifeld O., Doucet A., auf dem Keller U., Prudova A., Schilling O., Kainthan R.K., et al. Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products. Nat Biotechnol 2010, 28:281-288.
    • (2010) Nat Biotechnol , vol.28 , pp. 281-288
    • Kleifeld, O.1    Doucet, A.2    Keller, U.3    Prudova, A.4    Schilling, O.5    Kainthan, R.K.6


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