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Volumn 806, Issue , 2014, Pages 1-32

Mass spectrometry for proteomics-based investigation

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ELECTROSPRAY MASS SPECTROMETRY; GEL PERMEATION CHROMATOGRAPHY; HUMAN; ION CYCLOTRON RESONANCE MASS SPECTROMETRY; ION EXCHANGE CHROMATOGRAPHY; LIMIT OF QUANTITATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETER; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PHYSICAL CHEMISTRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DATABASE; PROTEIN GLYCOSYLATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEOMICS; TANDEM MASS SPECTROMETRY; TIME OF FLIGHT MASS SPECTROMETRY; METHODOLOGY; REVIEW;

EID: 84937978311     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-3-319-06068-2_1     Document Type: Article
Times cited : (15)

References (163)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M (2003) Mass spectrometry-based proteomics. Nature 422:198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 33745055719 scopus 로고    scopus 로고
    • High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of cytoplasmatic protein complexes from Chlorobium tepidum
    • Aivaliotis M, Karas M, Tsiotis G (2006) High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of cytoplasmatic protein complexes from Chlorobium tepidum. Photosynth Res 88:143-157
    • (2006) Photosynth Res , vol.88 , pp. 143-157
    • Aivaliotis, M.1    Karas, M.2    Tsiotis, G.3
  • 3
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B, Kratchmarova I, Ong SE, Nielsen M, Foster LJ, Mann M (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 21:315-318
    • (2003) Nat Biotechnol , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 4
    • 2642529334 scopus 로고    scopus 로고
    • Twodimensional Blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: A proteomics approach
    • Camacho-Carvajal MM, Wollscheid B, Aebersold R, Steimle V, Schamel WW (2004) Twodimensional Blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: a proteomics approach. Mol Cell Proteomics 3:176-182
    • (2004) Mol Cell Proteomics , vol.3 , pp. 176-182
    • Camacho-Carvajal, M.M.1    Wollscheid, B.2    Aebersold, R.3    Steimle, V.4    Schamel, W.W.5
  • 6
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong SE, Foster LJ, Mann M (2003) Mass spectrometric-based approaches in quantitative proteomics. Methods 29:124-130
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 7
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68:850-858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 8
    • 33644836196 scopus 로고    scopus 로고
    • Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)
    • Zhang G, Spellman DS, Skolnik EY, Neubert TA (2006) Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC). J Proteome Res 5:581-588
    • (2006) J Proteome Res , vol.5 , pp. 581-588
    • Zhang, G.1    Spellman, D.S.2    Skolnik, E.Y.3    Neubert, T.A.4
  • 9
    • 84938222518 scopus 로고    scopus 로고
    • Mass spectrometry and proteomics: Principle, workflow, challenges and perspectives
    • Darie C (2013) Mass spectrometry and proteomics: principle, workflow, challenges and perspectives. Mod Chem Appl 1:e105
    • (2013) Mod Chem Appl , vol.1
    • Darie, C.1
  • 10
    • 84881102738 scopus 로고    scopus 로고
    • Mass spectrometry and its application in life sciences
    • Darie CC (2013) Mass spectrometry and its application in life sciences. Aust J Chem 66:1-2
    • (2013) Aust J Chem , vol.66 , pp. 1-2
    • Darie, C.C.1
  • 11
    • 84881105512 scopus 로고    scopus 로고
    • Identification of posttranslational modifications by mass spectrometry
    • Ngounou Wetie AG, Sokolowska I, Woods AG, Darie CC (2013) Identification of posttranslational modifications by mass spectrometry. Aust J Chem 66:734-748
    • (2013) Aust J Chem , vol.66 , pp. 734-748
    • Ngounou Wetie, A.G.1    Sokolowska, I.2    Woods, A.G.3    Darie, C.C.4
  • 12
    • 84892802037 scopus 로고    scopus 로고
    • Protein-protein interactions: Switch from classical methods to proteomics and bioinformaticsbased approaches
    • Ngounou Wetie AG, Sokolowska I, Woods AG, Roy U, Deinhardt K, Darie CC (2014) Protein-protein interactions: switch from classical methods to proteomics and bioinformaticsbased approaches. Cell Mol Life Sci 71(2):205-228
    • (2014) Cell Mol Life Sci , vol.71 , Issue.2 , pp. 205-228
    • Ngounou Wetie, A.G.1    Sokolowska, I.2    Woods, A.G.3    Roy, U.4    Deinhardt, K.5    Darie, C.C.6
  • 14
    • 84882259886 scopus 로고    scopus 로고
    • Mass spectrometry investigation of glycosylation on the NXS/T sites in recombinant glycoproteins
    • Sokolowska I, Ngounou Wetie AG, Roy U, Woods AG, Darie CC (2013) Mass spectrometry investigation of glycosylation on the NXS/T sites in recombinant glycoproteins. Biochim Biophys Acta 1834:1474-1483
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1474-1483
    • Sokolowska, I.1    Ngounou Wetie, A.G.2    Roy, U.3    Woods, A.G.4    Darie, C.C.5
  • 18
    • 20444434349 scopus 로고    scopus 로고
    • Isolation and structural characterization of the Ndh complex from mesophyll and bundle sheath chloroplasts of Zea mays
    • Darie CC, Biniossek ML, Winter V, Mutschler B, Haehnel W (2005) Isolation and structural characterization of the Ndh complex from mesophyll and bundle sheath chloroplasts of Zea mays. Febs J 272:2705-2716
    • (2005) Febs J , vol.272 , pp. 2705-2716
    • Darie, C.C.1    Biniossek, M.L.2    Winter, V.3    Mutschler, B.4    Haehnel, W.5
  • 19
    • 38549147576 scopus 로고    scopus 로고
    • Purified trout egg vitelline envelope proteins VEbeta and VEgamma polymerize into homomeric fibrils from dimers in vitro
    • Darie CC, Janssen WG, Litscher ES, Wassarman PM (2008) Purified trout egg vitelline envelope proteins VEbeta and VEgamma polymerize into homomeric fibrils from dimers in vitro. Biochim Biophys Acta 1784:385-392
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 385-392
    • Darie, C.C.1    Janssen, W.G.2    Litscher, E.S.3    Wassarman, P.M.4
  • 20
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger H, Cramer WA, von Jagow G (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal Biochem 217:220-230
    • (1994) Anal Biochem , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 21
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H, von Jagow G (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199:223-231
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 22
    • 45749144385 scopus 로고    scopus 로고
    • Stable isotopic labeling by amino acids in cultured primary neurons: Application to brain-derived neurotrophic factordependent phosphotyrosine-associated signaling
    • Spellman DS, Deinhardt K, Darie CC, Chao MV, Neubert TA (2008) Stable isotopic labeling by amino acids in cultured primary neurons: application to brain-derived neurotrophic factordependent phosphotyrosine-associated signaling. Mol Cell Proteomics 7:1067-1076
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1067-1076
    • Spellman, D.S.1    Deinhardt, K.2    Darie, C.C.3    Chao, M.V.4    Neubert, T.A.5
  • 26
    • 2942588629 scopus 로고    scopus 로고
    • Structural characterization of fish egg vitelline envelope proteins by mass spectrometry
    • Darie CC, Biniossek ML, Jovine L, Litscher ES, Wassarman PM (2004) Structural characterization of fish egg vitelline envelope proteins by mass spectrometry. Biochemistry 43: 7459-7478
    • (2004) Biochemistry , vol.43 , pp. 7459-7478
    • Darie, C.C.1    Biniossek, M.L.2    Jovine, L.3    Litscher, E.S.4    Wassarman, P.M.5
  • 27
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schagger H (2006) Tricine-SDS-PAGE. Nat Protoc 1:16-22
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schagger, H.1
  • 28
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 30
    • 36849049826 scopus 로고    scopus 로고
    • Purified mouse egg zona pellucida glycoproteins polymerize into homomeric fibrils under non-denaturing conditions
    • Litscher ES, Janssen WG, Darie CC, Wassarman PM (2008) Purified mouse egg zona pellucida glycoproteins polymerize into homomeric fibrils under non-denaturing conditions. J Cell Physiol 214:153-157
    • (2008) J Cell Physiol , vol.214 , pp. 153-157
    • Litscher, E.S.1    Janssen, W.G.2    Darie, C.C.3    Wassarman, P.M.4
  • 32
    • 84938283945 scopus 로고    scopus 로고
    • Investigation of protein-protein interactions by blue native-PAGE & mass spectrometry
    • Darie C (2013) Investigation of protein-protein interactions by blue native-PAGE & mass spectrometry. Mod Chem Appl 1:e111
    • (2013) Mod Chem Appl , vol.1
    • Darie, C.1
  • 33
    • 84938222518 scopus 로고    scopus 로고
    • Post-translational modification (PTM) proteomics: Challenges and perspectives
    • Darie C (2013) Post-translational modification (PTM) proteomics: challenges and perspectives. Mod Chem appl 1:e114
    • (2013) Mod Chem appl , vol.1
    • Darie, C.1
  • 34
    • 84931582771 scopus 로고    scopus 로고
    • Blue native page and mass spectrometry as an approach for the investigation of stable and transient protein-protein interactions
    • Andreescu S, Hepel M (eds), American Chemical Society, Washington, DC
    • Woods AG, Sokolowska I, Yakubu R, Butkiewicz M, LaFleur M, Talbot C, Darie CC (2011) Blue native page and mass spectrometry as an approach for the investigation of stable and transient protein-protein interactions. In: Andreescu S, Hepel M (eds) Oxidative stress: diagnostics, prevention, and therapy. American Chemical Society, Washington, DC
    • (2011) Oxidative stress: Diagnostics, prevention, and therapy
    • Woods, A.G.1    Sokolowska, I.2    Yakubu, R.3    Butkiewicz, M.4    LaFleur, M.5    Talbot, C.6    Darie, C.C.7
  • 35
    • 0042164949 scopus 로고    scopus 로고
    • Redox proteomics: Identification of oxidatively modified proteins
    • Ghezzi P, Bonetto V (2003) Redox proteomics: identification of oxidatively modified proteins. Proteomics 3:1145-1153
    • (2003) Proteomics , vol.3 , pp. 1145-1153
    • Ghezzi, P.1    Bonetto, V.2
  • 36
    • 79955889171 scopus 로고    scopus 로고
    • Proteome analysis of differential protein expression in brain of rats with type 1 diabetes mellitus
    • Li X, Pan W, Yang GZ, Di YN, Zhao F, Zhu LY, Jiang ZH (2011) Proteome analysis of differential protein expression in brain of rats with type 1 diabetes mellitus. Exp Clin Endocrinol Diabetes 119:265-270
    • (2011) Exp Clin Endocrinol Diabetes , vol.119 , pp. 265-270
    • Li, X.1    Pan, W.2    Yang, G.Z.3    Di, Y.N.4    Zhao, F.5    Zhu, L.Y.6    Jiang, Z.H.7
  • 37
    • 77954203166 scopus 로고    scopus 로고
    • Application of proteomic profiling based on 2D-DIGE for classification of compounds according to the mechanism of action
    • Muroi M, Kazami S, Noda K, Kondo H, Takayama H, Kawatani M, Usui T, Osada H (2010) Application of proteomic profiling based on 2D-DIGE for classification of compounds according to the mechanism of action. Chem Biol 17:460-470
    • (2010) Chem Biol , vol.17 , pp. 460-470
    • Muroi, M.1    Kazami, S.2    Noda, K.3    Kondo, H.4    Takayama, H.5    Kawatani, M.6    Usui, T.7    Osada, H.8
  • 38
    • 80051817548 scopus 로고    scopus 로고
    • A 2-D gel reference map of the basic human heart proteome
    • Polden J, McManus CA, Remedios CD, Dunn MJ (2011) A 2-D gel reference map of the basic human heart proteome. Proteomics 11(17):3582-3586
    • (2011) Proteomics , vol.11 , Issue.17 , pp. 3582-3586
    • Polden, J.1    McManus, C.A.2    Remedios, C.D.3    Dunn, M.J.4
  • 40
    • 79961227218 scopus 로고    scopus 로고
    • Bacterial proteome of Streptococcus pneumoniae through multidimensional separations coupled with LC-MS/MS
    • Sun X, Jia HL, Xiao CL, Yin XF, Yang XY, Lu J, He X, Li N, Li H, He QY (2011) Bacterial proteome of Streptococcus pneumoniae through multidimensional separations coupled with LC-MS/MS. OMICS 15(7-8):477-482
    • (2011) OMICS , vol.15 , Issue.7 , pp. 477-482
    • Sun, X.1    Jia, H.L.2    Xiao, C.L.3    Yin, X.F.4    Yang, X.Y.5    Lu, J.6    He, X.7    Li, N.8    Li, H.9    He, Q.Y.10
  • 41
    • 33645795212 scopus 로고    scopus 로고
    • Proteomic analysis reveals novel molecules involved in insulin signaling pathway
    • Wang Y, Li R, Du D, Zhang C, Yuan H, Zeng R, Chen Z (2006) Proteomic analysis reveals novel molecules involved in insulin signaling pathway. J Proteome Res 5:846-855
    • (2006) J Proteome Res , vol.5 , pp. 846-855
    • Wang, Y.1    Li, R.2    Du, D.3    Zhang, C.4    Yuan, H.5    Zeng, R.6    Chen, Z.7
  • 43
    • 0032948126 scopus 로고    scopus 로고
    • 2D protein electrophoresis: Can it be perfected?
    • Celis JE, Gromov P (1999) 2D protein electrophoresis: can it be perfected? Curr Opin Biotechnol 10:16-21
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 16-21
    • Celis, J.E.1    Gromov, P.2
  • 50
    • 77950974821 scopus 로고    scopus 로고
    • Determination of elemental compositions by gas chromatography/time-of-flight mass spectrometry using chemical and electron ionization
    • Abate S, Ahn YG, Kind T, Cataldi TR, Fiehn O (2010) Determination of elemental compositions by gas chromatography/time-of-flight mass spectrometry using chemical and electron ionization. Rapid Commun Mass Spectrom 24:1172-1180
    • (2010) Rapid Commun Mass Spectrom , vol.24 , pp. 1172-1180
    • Abate, S.1    Ahn, Y.G.2    Kind, T.3    Cataldi, T.R.4    Fiehn, O.5
  • 53
    • 0019453020 scopus 로고
    • Negative chemical ionization mass spectrometry: Applications in environmental analytical chemistry
    • Dougherty RC (1981) Negative chemical ionization mass spectrometry: applications in environmental analytical chemistry. Biomed Mass Spectrom 8:283-292
    • (1981) Biomed Mass Spectrom , vol.8 , pp. 283-292
    • Dougherty, R.C.1
  • 54
    • 33745592760 scopus 로고    scopus 로고
    • Derivatization in mass spectrometry-8. Soft ionization mass spectrometry of small molecules
    • Zaikin VG, Halket JM (2006) Derivatization in mass spectrometry-8. Soft ionization mass spectrometry of small molecules. Eur J Mass Spectrom (Chichester, Eng) 12:79-115
    • (2006) Eur J Mass Spectrom (Chichester, Eng) , vol.12 , pp. 79-115
    • Zaikin, V.G.1    Halket, J.M.2
  • 55
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: A primer
    • Marshall AG, Hendrickson CL, Jackson GS (1998) Fourier transform ion cyclotron resonance mass spectrometry: a primer. Mass Spectrom Rev 17:1-35
    • (1998) Mass Spectrom Rev , vol.17 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 56
    • 0034665968 scopus 로고    scopus 로고
    • Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI fourier transform ion cyclotron resonance mass spectrometry
    • Martin SE, Shabanowitz J, Hunt DF, Marto JA (2000) Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 72:4266-4274
    • (2000) Anal Chem , vol.72 , pp. 4266-4274
    • Martin, S.E.1    Shabanowitz, J.2    Hunt, D.F.3    Marto, J.A.4
  • 58
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates JR, Ruse CI, Nakorchevsky A (2009) Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 11:49-79
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 59
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R (2006) Mass spectrometry and protein analysis. Science 312: 212-217
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 60
    • 34248180415 scopus 로고    scopus 로고
    • Two-dimensional difference gel electrophoresis
    • Viswanathan S, Unlu M, Minden JS (2006) Two-dimensional difference gel electrophoresis. Nat Protoc 1:1351-1358
    • (2006) Nat Protoc , vol.1 , pp. 1351-1358
    • Viswanathan, S.1    Unlu, M.2    Minden, J.S.3
  • 61
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1:376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 62
    • 0035861914 scopus 로고    scopus 로고
    • Dual inhibition of sister chromatid separation at metaphase
    • Stemmann O, Zou H, Gerber SA, Gygi SP, Kirschner MW (2001) Dual inhibition of sister chromatid separation at metaphase. Cell 107:715-726
    • (2001) Cell , vol.107 , pp. 715-726
    • Stemmann, O.1    Zou, H.2    Gerber, S.A.3    Gygi, S.P.4    Kirschner, M.W.5
  • 63
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson L, Hunter CL (2006) Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol Cell Proteomics 5:573-588
    • (2006) Mol Cell Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 64
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H, Sadygov RG, Yates JR III (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76:4193-4201
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 66
    • 0141502007 scopus 로고    scopus 로고
    • Shotgun proteomics: Integrating technologies to answer biological questions
    • McDonald WH, Yates JR III (2003) Shotgun proteomics: integrating technologies to answer biological questions. Curr Opin Mol Ther 5:302-309
    • (2003) Curr Opin Mol Ther , vol.5 , pp. 302-309
    • McDonald, W.H.1    Yates, J.R.2
  • 69
    • 79952108572 scopus 로고    scopus 로고
    • Unbiased detection of posttranslational modifications using mass spectrometry
    • Savitski MF, Savitski MM (2010) Unbiased detection of posttranslational modifications using mass spectrometry. Methods Mol Biol 673:203-210
    • (2010) Methods Mol Biol , vol.673 , pp. 203-210
    • Savitski, M.F.1    Savitski, M.M.2
  • 70
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro RG (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12:43R-56R
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 71
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • Marino K, Bones J, Kattla JJ, Rudd PM (2010) A systematic approach to protein glycosylation analysis: a path through the maze. Nat Chem Biol 6:713-723
    • (2010) Nat Chem Biol , vol.6 , pp. 713-723
    • Marino, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4
  • 72
    • 80051711268 scopus 로고    scopus 로고
    • Industry and regulatory experience of the glycosylation of monoclonal antibodies
    • Read EK, Park JT, Brorson KA (2011) Industry and regulatory experience of the glycosylation of monoclonal antibodies. Biotechnol Appl Biochem 58:213-219
    • (2011) Biotechnol Appl Biochem , vol.58 , pp. 213-219
    • Read, E.K.1    Park, J.T.2    Brorson, K.A.3
  • 73
    • 53149151450 scopus 로고    scopus 로고
    • Evaluation of glycosylation for quality assurance of antibody pharmaceuticals by capillary electrophoresis
    • Kamoda S, Kakehi K (2008) Evaluation of glycosylation for quality assurance of antibody pharmaceuticals by capillary electrophoresis. Electrophoresis 29:3595-3604
    • (2008) Electrophoresis , vol.29 , pp. 3595-3604
    • Kamoda, S.1    Kakehi, K.2
  • 74
    • 84859396316 scopus 로고    scopus 로고
    • Effective use of mass spectrometry for glycan and glycopeptide structural analysis
    • Leymarie N, Zaia J (2012) Effective use of mass spectrometry for glycan and glycopeptide structural analysis. Anal Chem 84:3040-3048
    • (2012) Anal Chem , vol.84 , pp. 3040-3048
    • Leymarie, N.1    Zaia, J.2
  • 75
    • 78651105000 scopus 로고    scopus 로고
    • Mass spectrometry based glycoproteomics- from a proteomics perspective
    • Pan S, Chen R, Aebersold R, Brentnall TA (2011) Mass spectrometry based glycoproteomics- from a proteomics perspective. Mol Cell Proteomics 10(R110):003251
    • (2011) Mol Cell Proteomics , vol.10 , pp. 003251
    • Pan, S.1    Chen, R.2    Aebersold, R.3    Brentnall, T.A.4
  • 76
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • Morelle W, Michalski JC (2007) Analysis of protein glycosylation by mass spectrometry. Nat Protoc 2:1585-1602
    • (2007) Nat Protoc , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.C.2
  • 78
    • 44049093407 scopus 로고    scopus 로고
    • Glycoprotein enrichment through lectin affinity techniques
    • Mechref Y, Madera M, Novotny MV (2008) Glycoprotein enrichment through lectin affinity techniques. Methods Mol Biol 424:373-396
    • (2008) Methods Mol Biol , vol.424 , pp. 373-396
    • Mechref, Y.1    Madera, M.2    Novotny, M.V.3
  • 79
    • 33846818820 scopus 로고    scopus 로고
    • Chemical methods for glycoprotein discovery
    • Bond MR, Kohler JJ (2007) Chemical methods for glycoprotein discovery. Curr Opin Chem Biol 11:52-58
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 52-58
    • Bond, M.R.1    Kohler, J.J.2
  • 80
    • 67650713930 scopus 로고    scopus 로고
    • The chemical biology of protein phosphorylation
    • Tarrant MK, Cole PA (2009) The chemical biology of protein phosphorylation. Annu Rev Biochem 78:797-825
    • (2009) Annu Rev Biochem , vol.78 , pp. 797-825
    • Tarrant, M.K.1    Cole, P.A.2
  • 81
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T (2001) Oncogenic kinase signalling. Nature 411:355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 82
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture
    • Cohen P (2001) The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture. Eur J Biochem 268:5001-5010
    • (2001) Eur J Biochem , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 83
    • 78649251547 scopus 로고    scopus 로고
    • Tau phosphorylation and aggregation as a therapeutic target in tauopathies
    • Badiola N, Suarez-Calvet M, Lleo A (2010) Tau phosphorylation and aggregation as a therapeutic target in tauopathies. CNS Neurol Disord Drug Targets 9:727-740
    • (2010) CNS Neurol Disord Drug Targets , vol.9 , pp. 727-740
    • Badiola, N.1    Suarez-Calvet, M.2    Lleo, A.3
  • 84
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twenty-first century?
    • Cohen P (2002) Protein kinases-the major drug targets of the twenty-first century? Nat Rev Drug Discov 1:309-315
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 309-315
    • Cohen, P.1
  • 85
    • 77955167321 scopus 로고    scopus 로고
    • Multifaceted polo-like kinases: Drug targets and antitargets for cancer therapy
    • Strebhardt K (2010) Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy. Nat Rev Drug Discov 9:643-660
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 643-660
    • Strebhardt, K.1
  • 86
    • 0037709383 scopus 로고    scopus 로고
    • Unique scanning capabilities of a new hybrid linear ion trap mass spectrometer (Q TRAP) used for high sensitivity proteomics applications
    • Le Blanc JC, Hager JW, Ilisiu AM, Hunter C, Zhong F, Chu I (2003) Unique scanning capabilities of a new hybrid linear ion trap mass spectrometer (Q TRAP) used for high sensitivity proteomics applications. Proteomics 3:859-869
    • (2003) Proteomics , vol.3 , pp. 859-869
    • Le Blanc, J.C.1    Hager, J.W.2    Ilisiu, A.M.3    Hunter, C.4    Zhong, F.5    Chu, I.6
  • 88
    • 21044458153 scopus 로고    scopus 로고
    • Identification of phosphopeptides by MALDI Q-TOF MS in positive and negative ion modes after methyl esterification
    • Xu CF, Lu Y, Ma J, Mohammadi M, Neubert TA (2005) Identification of phosphopeptides by MALDI Q-TOF MS in positive and negative ion modes after methyl esterification. Mol Cell Proteomics 4:809-818
    • (2005) Mol Cell Proteomics , vol.4 , pp. 809-818
    • Xu, C.F.1    Lu, Y.2    Ma, J.3    Mohammadi, M.4    Neubert, T.A.5
  • 89
    • 84867041794 scopus 로고    scopus 로고
    • Advances in phosphopeptide enrichment techniques for phosphoproteomics
    • Beltran L, Cutillas PR (2012) Advances in phosphopeptide enrichment techniques for phosphoproteomics. Amino Acids 43:1009-1024
    • (2012) Amino Acids , vol.43 , pp. 1009-1024
    • Beltran, L.1    Cutillas, P.R.2
  • 90
    • 30544443201 scopus 로고    scopus 로고
    • Identification of phosphorylation sites using microimmobilized metal affinity chromatography
    • Corthals GL, Aebersold R, Goodlett DR (2005) Identification of phosphorylation sites using microimmobilized metal affinity chromatography. Methods Enzymol 405:66-81
    • (2005) Methods Enzymol , vol.405 , pp. 66-81
    • Corthals, G.L.1    Aebersold, R.2    Goodlett, D.R.3
  • 92
    • 0036882287 scopus 로고    scopus 로고
    • Protein disulfide bond determination by mass spectrometry
    • Gorman JJ, Wallis TP, Pitt JJ (2002) Protein disulfide bond determination by mass spectrometry. Mass Spectrom Rev 21:183-216
    • (2002) Mass Spectrom Rev , vol.21 , pp. 183-216
    • Gorman, J.J.1    Wallis, T.P.2    Pitt, J.J.3
  • 96
    • 44049105535 scopus 로고    scopus 로고
    • Experimental and computational approaches to quantitative proteomics: Status quo and outlook
    • Panchaud A, Affolter M, Moreillon P, Kussmann M (2008) Experimental and computational approaches to quantitative proteomics: status quo and outlook. J Proteomics 71:19-33
    • (2008) J Proteomics , vol.71 , pp. 19-33
    • Panchaud, A.1    Affolter, M.2    Moreillon, P.3    Kussmann, M.4
  • 97
    • 44049093545 scopus 로고    scopus 로고
    • Quantitation of protein in samples prepared for 2-D electrophoresis
    • Berkelman T (2008) Quantitation of protein in samples prepared for 2-D electrophoresis. Methods Mol Biol 424:43-49
    • (2008) Methods Mol Biol , vol.424 , pp. 43-49
    • Berkelman, T.1
  • 99
    • 79960396255 scopus 로고    scopus 로고
    • Liquid chromatography-mass spectrometry- based quantitative proteomics
    • Xie F, Liu T, Qian WJ, Petyuk VA, Smith RD (2011) Liquid chromatography-mass spectrometry- based quantitative proteomics. J Biol Chem 286:25443-25449
    • (2011) J Biol Chem , vol.286 , pp. 25443-25449
    • Xie, F.1    Liu, T.2    Qian, W.J.3    Petyuk, V.A.4    Smith, R.D.5
  • 102
    • 33746285299 scopus 로고    scopus 로고
    • Label-free quantitative proteomics using large peptide data sets generated by nanoflow liquid chromatography and mass spectrometry
    • Ono M, Shitashige M, Honda K, Isobe T, Kuwabara H, Matsuzuki H, Hirohashi S, Yamada T (2006) Label-free quantitative proteomics using large peptide data sets generated by nanoflow liquid chromatography and mass spectrometry. Mol Cell Proteomics 5:1338-1347
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1338-1347
    • Ono, M.1    Shitashige, M.2    Honda, K.3    Isobe, T.4    Kuwabara, H.5    Matsuzuki, H.6    Hirohashi, S.7    Yamada, T.8
  • 105
    • 0042887140 scopus 로고    scopus 로고
    • Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry
    • Strittmatter EF, Ferguson PL, Tang K, Smith RD (2003) Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry. J Am Soc Mass Spectrom 14:980-991
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 980-991
    • Strittmatter, E.F.1    Ferguson, P.L.2    Tang, K.3    Smith, R.D.4
  • 106
    • 0036523809 scopus 로고    scopus 로고
    • Minimizing resolution of isotopically coded peptides in comparative proteomics
    • Zhang R, Regnier FE (2002) Minimizing resolution of isotopically coded peptides in comparative proteomics. J Proteome Res 1:139-147
    • (2002) J Proteome Res , vol.1 , pp. 139-147
    • Zhang, R.1    Regnier, F.E.2
  • 107
    • 3543121341 scopus 로고    scopus 로고
    • Quantification in proteomics through stable isotope coding: A review
    • Julka S, Regnier F (2004) Quantification in proteomics through stable isotope coding: a review. J Proteome Res 3:350-363
    • (2004) J Proteome Res , vol.3 , pp. 350-363
    • Julka, S.1    Regnier, F.2
  • 108
    • 20544459800 scopus 로고    scopus 로고
    • Absolute quantification strategies in proteomics based on mass spectrometry
    • Bronstrup M (2004) Absolute quantification strategies in proteomics based on mass spectrometry. Expert Rev Proteomics 1:503-512
    • (2004) Expert Rev Proteomics , vol.1 , pp. 503-512
    • Bronstrup, M.1
  • 109
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, Kirschner MW, Gygi SP (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci U S A 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
  • 110
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick DS, Gerber SA, Gygi SP (2005) The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 35:265-273
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 111
    • 82755163975 scopus 로고    scopus 로고
    • Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling
    • Zhang G, Neubert TA (2011) Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling. J Proteome Res 10:5454-5462
    • (2011) J Proteome Res , vol.10 , pp. 5454-5462
    • Zhang, G.1    Neubert, T.A.2
  • 112
    • 79955791663 scopus 로고    scopus 로고
    • Study of neurotrophin-3 signaling in primary cultured neurons using multiplex stable isotope labeling with amino acids in cell culture
    • Zhang G, Deinhardt K, Chao MV, Neubert TA (2011) Study of neurotrophin-3 signaling in primary cultured neurons using multiplex stable isotope labeling with amino acids in cell culture. J Proteome Res 10:2546-2554
    • (2011) J Proteome Res , vol.10 , pp. 2546-2554
    • Zhang, G.1    Deinhardt, K.2    Chao, M.V.3    Neubert, T.A.4
  • 115
    • 77952145032 scopus 로고    scopus 로고
    • Super-SILAC for tumors and tissues
    • Neubert TA, Tempst P (2010) Super-SILAC for tumors and tissues. Nat Methods 7:361-362
    • (2010) Nat Methods , vol.7 , pp. 361-362
    • Neubert, T.A.1    Tempst, P.2
  • 116
    • 65349131823 scopus 로고    scopus 로고
    • Use of stable isotope labeling by amino acids in cell culture (SILAC) for phosphotyrosine protein identification and quantitation
    • Zhang G, Neubert TA (2009) Use of stable isotope labeling by amino acids in cell culture (SILAC) for phosphotyrosine protein identification and quantitation. Methods Mol Biol 527:79-92
    • (2009) Methods Mol Biol , vol.527 , pp. 79-92
    • Zhang, G.1    Neubert, T.A.2
  • 117
    • 65249144498 scopus 로고    scopus 로고
    • Evaluation of the variation in sample preparation for comparative proteomics using stable isotope labeling by amino acids in cell culture
    • Zhang G, Fenyo D, Neubert TA (2009) Evaluation of the variation in sample preparation for comparative proteomics using stable isotope labeling by amino acids in cell culture. J Proteome Res 8:1285-1292
    • (2009) J Proteome Res , vol.8 , pp. 1285-1292
    • Zhang, G.1    Fenyo, D.2    Neubert, T.A.3
  • 118
    • 58149382072 scopus 로고    scopus 로고
    • Screening for EphB signaling effectors using SILAC with a linear ion trap-orbitrap mass spectrometer
    • Zhang G, Fenyo D, Neubert TA (2008) Screening for EphB signaling effectors using SILAC with a linear ion trap-orbitrap mass spectrometer. J Proteome Res 7:4715-4726
    • (2008) J Proteome Res , vol.7 , pp. 4715-4726
    • Zhang, G.1    Fenyo, D.2    Neubert, T.A.3
  • 119
    • 33644669753 scopus 로고    scopus 로고
    • Automated comparative proteomics based on multiplex tandem mass spectrometry and stable isotope labeling
    • Zhang G, Neubert TA (2006) Automated comparative proteomics based on multiplex tandem mass spectrometry and stable isotope labeling. Mol Cell Proteomics 5:401-411
    • (2006) Mol Cell Proteomics , vol.5 , pp. 401-411
    • Zhang, G.1    Neubert, T.A.2
  • 122
    • 80054723147 scopus 로고    scopus 로고
    • In vivo quantitative proteomics: The SILAC mouse
    • Zanivan S, Krueger M, Mann M (2012) In vivo quantitative proteomics: the SILAC mouse. Methods Mol Biol 757:435-450
    • (2012) Methods Mol Biol , vol.757 , pp. 435-450
    • Zanivan, S.1    Krueger, M.2    Mann, M.3
  • 123
    • 77949733292 scopus 로고    scopus 로고
    • jTraqX: A free, platform independent tool for isobaric tag quantitation at the protein level
    • Muth T, Keller D, Puetz SM, Martens L, Sickmann A, Boehm AM (2010) jTraqX: a free, platform independent tool for isobaric tag quantitation at the protein level. Proteomics 10:1223-1225
    • (2010) Proteomics , vol.10 , pp. 1223-1225
    • Muth, T.1    Keller, D.2    Puetz, S.M.3    Martens, L.4    Sickmann, A.5    Boehm, A.M.6
  • 126
    • 84864987862 scopus 로고    scopus 로고
    • The use of selected reaction monitoring in quantitative proteomics
    • Holman SW, Sims PF, Eyers CE (2012) The use of selected reaction monitoring in quantitative proteomics. Bioanalysis 4:1763-1786
    • (2012) Bioanalysis , vol.4 , pp. 1763-1786
    • Holman, S.W.1    Sims, P.F.2    Eyers, C.E.3
  • 127
    • 34250722602 scopus 로고    scopus 로고
    • Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks
    • Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM (2007) Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A 104:5860-5865
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5860-5865
    • Wolf-Yadlin, A.1    Hautaniemi, S.2    Lauffenburger, D.A.3    White, F.M.4
  • 131
    • 77955505357 scopus 로고    scopus 로고
    • Protein-protein interactions essentials: Key concepts to building and analyzing interactome networks
    • De Las Rivas J, Fontanillo C (2010) Protein-protein interactions essentials: key concepts to building and analyzing interactome networks. PLoS Comput Biol 6:e1000807
    • (2010) PLoS Comput Biol , vol.6
    • De Las Rivas, J.1    Fontanillo, C.2
  • 132
    • 0037172803 scopus 로고    scopus 로고
    • Stoichiometries of proteinprotein/ DNA binding and conformational changes for the transition-state regulator AbrB measured by pseudo cell-size exclusion chromatography-mass spectrometry
    • Cavanagh J, Thompson R, Bobay B, Benson LM, Naylor S (2002) Stoichiometries of proteinprotein/ DNA binding and conformational changes for the transition-state regulator AbrB measured by pseudo cell-size exclusion chromatography-mass spectrometry. Biochemistry 41:7859-7865
    • (2002) Biochemistry , vol.41 , pp. 7859-7865
    • Cavanagh, J.1    Thompson, R.2    Bobay, B.3    Benson, L.M.4    Naylor, S.5
  • 133
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line lightscattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen J, Arakawa T, Philo JS (1996) Size-exclusion chromatography with on-line lightscattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal Biochem 240:155-166
    • (1996) Anal Biochem , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 135
    • 33749372201 scopus 로고    scopus 로고
    • Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals
    • Berkowitz SA (2006) Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals. AAPS J 8:E590-E605
    • (2006) AAPS J , vol.8 , pp. E590-E605
    • Berkowitz, S.A.1
  • 136
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky EM, Fields S (1995) Protein-protein interactions: methods for detection and analysis. Microbiol Rev 59:94-123
    • (1995) Microbiol Rev , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 137
    • 84855854555 scopus 로고    scopus 로고
    • Identification of potential tumor differentiation factor (TDF) receptor from steroid-responsive and steroid-resistant breast cancer cells
    • Sokolowska I, Woods AG, Gawinowicz MA, Roy U, Darie CC (2012) Identification of potential tumor differentiation factor (TDF) receptor from steroid-responsive and steroid-resistant breast cancer cells. J Biol Chem 287:1719-1733
    • (2012) J Biol Chem , vol.287 , pp. 1719-1733
    • Sokolowska, I.1    Woods, A.G.2    Gawinowicz, M.A.3    Roy, U.4    Darie, C.C.5
  • 138
    • 84873991171 scopus 로고    scopus 로고
    • Investigation of stable and transient protein-protein interactions: Past, present, and future
    • Ngounou Wetie AG, Sokolowska I, Woods AG, Roy U, Loo JA, Darie CC (2013) Investigation of stable and transient protein-protein interactions: past, present, and future. Proteomics 13(3-4):538-557
    • (2013) Proteomics , vol.13 , Issue.3 , pp. 538-557
    • Ngounou Wetie, A.G.1    Sokolowska, I.2    Woods, A.G.3    Roy, U.4    Loo, J.A.5    Darie, C.C.6
  • 139
    • 84863447582 scopus 로고    scopus 로고
    • Identification of a potential tumor differentiation factor receptor candidate in prostate cancer cells
    • Sokolowska I, Woods AG, Gawinowicz MA, Roy U, Darie CC (2012) Identification of a potential tumor differentiation factor receptor candidate in prostate cancer cells. FEBS J 279:2579-2594
    • (2012) FEBS J , vol.279 , pp. 2579-2594
    • Sokolowska, I.1    Woods, A.G.2    Gawinowicz, M.A.3    Roy, U.4    Darie, C.C.5
  • 143
  • 144
    • 33745943572 scopus 로고    scopus 로고
    • Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes
    • Krause F (2006) Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes. Electrophoresis 27:2759-2781
    • (2006) Electrophoresis , vol.27 , pp. 2759-2781
    • Krause, F.1
  • 145
    • 77950685492 scopus 로고    scopus 로고
    • Laser-induced liquid bead ion desorption-MS of protein complexes from blue-native gels, a sensitive topdown proteomic approach
    • Sokolova L, Wittig I, Barth HD, Schagger H, Brutschy B, Brandt U (2010) Laser-induced liquid bead ion desorption-MS of protein complexes from blue-native gels, a sensitive topdown proteomic approach. Proteomics 10:1401-1407
    • (2010) Proteomics , vol.10 , pp. 1401-1407
    • Sokolova, L.1    Wittig, I.2    Barth, H.D.3    Schagger, H.4    Brutschy, B.5    Brandt, U.6
  • 146
    • 81855192712 scopus 로고    scopus 로고
    • Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry
    • Darie CC, Deinhardt K, Zhang G, Cardasis HS, Chao MV, Neubert TA (2011) Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry. Proteomics 11:4514-4528
    • (2011) Proteomics , vol.11 , pp. 4514-4528
    • Darie, C.C.1    Deinhardt, K.2    Zhang, G.3    Cardasis, H.S.4    Chao, M.V.5    Neubert, T.A.6
  • 147
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck AJ, Van Den Heuvel RH (2004) Investigation of intact protein complexes by mass spectrometry. Mass Spectrom Rev 23:368-389
    • (2004) Mass Spectrom Rev , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 151
    • 84856614421 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry for structural proteomics
    • Zhong Y, Hyung SJ, Ruotolo BT (2012) Ion mobility-mass spectrometry for structural proteomics. Expert Rev Proteomics 9:47-58
    • (2012) Expert Rev Proteomics , vol.9 , pp. 47-58
    • Zhong, Y.1    Hyung, S.J.2    Ruotolo, B.T.3
  • 152
    • 0037435031 scopus 로고    scopus 로고
    • From words to literature in structural proteomics
    • Sali A, Glaeser R, Earnest T, Baumeister W (2003) From words to literature in structural proteomics. Nature 422:216-225
    • (2003) Nature , vol.422 , pp. 216-225
    • Sali, A.1    Glaeser, R.2    Earnest, T.3    Baumeister, W.4
  • 153
    • 78649877318 scopus 로고    scopus 로고
    • How useful is ion mobility mass spectrometry for structural biology? The relationship between protein crystal structures and their collision cross sections in the gas phase
    • Jurneczko E, Barran PE (2011) How useful is ion mobility mass spectrometry for structural biology? The relationship between protein crystal structures and their collision cross sections in the gas phase. Analyst 136:20-28
    • (2011) Analyst , vol.136 , pp. 20-28
    • Jurneczko, E.1    Barran, P.E.2
  • 154
    • 58149182318 scopus 로고    scopus 로고
    • Travelling wave ion mobility mass spectrometry studies of protein structure: Biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements
    • Scarff CA, Thalassinos K, Hilton GR, Scrivens JH (2008) Travelling wave ion mobility mass spectrometry studies of protein structure: biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements. Rapid Commun Mass Spectrom 22:3297-3304
    • (2008) Rapid Commun Mass Spectrom , vol.22 , pp. 3297-3304
    • Scarff, C.A.1    Thalassinos, K.2    Hilton, G.R.3    Scrivens, J.H.4
  • 155
    • 0036603768 scopus 로고    scopus 로고
    • Alternative splicing: Combinatorial output from the genome
    • Roberts GC, Smith CW (2002) Alternative splicing: combinatorial output from the genome. Curr Opin Chem Biol 6:375-383
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 375-383
    • Roberts, G.C.1    Smith, C.W.2
  • 156
    • 84859301166 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics for translational research: A technical overview
    • Paulo JA, Kadiyala V, Banks PA, Steen H, Conwell DL (2012) Mass spectrometry-based proteomics for translational research: a technical overview. Yale J Biol Med 85:59-73
    • (2012) Yale J Biol Med , vol.85 , pp. 59-73
    • Paulo, J.A.1    Kadiyala, V.2    Banks, P.A.3    Steen, H.4    Conwell, D.L.5
  • 159
    • 84934437180 scopus 로고    scopus 로고
    • Membrane-bound complement regulatory proteins as biomarkers and potential therapeutic targets for SLE
    • Das N, Biswas B, Khera R (2013) Membrane-bound complement regulatory proteins as biomarkers and potential therapeutic targets for SLE. Adv Exp Med Biol 734:55-81
    • (2013) Adv Exp Med Biol , vol.734 , pp. 55-81
    • Das, N.1    Biswas, B.2    Khera, R.3
  • 160
    • 0034000699 scopus 로고    scopus 로고
    • VEGF receptor signaling in tumor angiogenesis
    • McMahon G (2000) VEGF receptor signaling in tumor angiogenesis. Oncologist 5(Suppl 1): 3-10
    • (2000) Oncologist , vol.5 , pp. 3-10
    • McMahon, G.1
  • 161
    • 0034789517 scopus 로고    scopus 로고
    • Receptor tyrosine kinase signalling as a target for cancer intervention strategies
    • Zwick E, Bange J, Ullrich A (2001) Receptor tyrosine kinase signalling as a target for cancer intervention strategies. Endocr Relat Cancer 8:161-173
    • (2001) Endocr Relat Cancer , vol.8 , pp. 161-173
    • Zwick, E.1    Bange, J.2    Ullrich, A.3
  • 163
    • 84856005633 scopus 로고    scopus 로고
    • Profiling of integral membrane proteins and their post translational modifications using high-resolution mass spectrometry
    • Souda P, Ryan CM, Cramer WA, Whitelegge J (2011) Profiling of integral membrane proteins and their post translational modifications using high-resolution mass spectrometry. Methods 55:330-336
    • (2011) Methods , vol.55 , pp. 330-336
    • Souda, P.1    Ryan, C.M.2    Cramer, W.A.3    Whitelegge, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.