메뉴 건너뛰기




Volumn 23, Issue 4, 2012, Pages 708-717

Increased protein structural resolution from diethylpyrocarbonate-based covalent labeling and mass spectrometric detection

Author keywords

3 Dimensional protein structure; Electron transfer dissociation; Protein surface mapping

Indexed keywords

3-DIMENSIONAL STRUCTURES; AVERAGE DISTANCE; COVALENT LABELING; CYTOCHROME C; DIETHYLPYROCARBONATE; ELECTRON TRANSFER DISSOCIATION; HYDROXYL RADICALS; LABELING REAGENT; MASS SPECTROMETRIC ANALYSIS; MASS SPECTROMETRIC DETECTION; PROTEIN COMPLEXES; PROTEIN DIGESTION; PROTEIN STRUCTURES; PROTEIN SURFACE; PROTEOLYTIC DIGESTION; STRUCTURAL INFORMATION; ULTRASONIC IRRADIATION;

EID: 84862557685     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-011-0332-4     Document Type: Article
Times cited : (38)

References (56)
  • 1
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales, T.E., Engen, J.R.: Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170 (2006)
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 2
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • Engen, J.R.: Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS. Anal. Chem. 81, 7870-7875 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 7870-7875
    • Engen, J.R.1
  • 4
    • 77953480345 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: What is it and what can it tell us?
    • Marcsisin, S.R., Engen, J.R.: Hydrogen exchange mass spectrometry: what is it and what can it tell us? Anal. Bioanal. Chem. 397, 967-972 (2010)
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 967-972
    • Marcsisin, S.R.1    Engen, J.R.2
  • 5
    • 35448956141 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange-mass spectrometry: A powerful tool for probing protein structure, dynamics and interactions
    • Tsutsui, Y., Wintrode, P.L.: Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions. Curr. Med. Chem. 14, 2344-2358 (2007)
    • (2007) Curr. Med. Chem. , vol.14 , pp. 2344-2358
    • Tsutsui, Y.1    Wintrode, P.L.2
  • 6
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • Englander, S.W.: Hydrogen exchange and mass spectrometry: a historical perspective. J. Am. Soc. Mass Spectrom. 17, 1481-1489 (2006)
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 7
    • 78149438179 scopus 로고    scopus 로고
    • Crosslinking combined with mass spectrometry for structural proteomics
    • Petrotchenko, E.V., Borchers, C.H.: Crosslinking combined with mass spectrometry for structural proteomics. Mass Spectrom. Rev. 29, 862-876 (2010)
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 862-876
    • Petrotchenko, E.V.1    Borchers, C.H.2
  • 8
    • 77956058146 scopus 로고    scopus 로고
    • Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry
    • Sinz, A.: Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry. Anal. Bioanal. Chem. 397, 3433-3440 (2010)
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 3433-3440
    • Sinz, A.1
  • 9
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map threedimensional protein structures and protein-protein interactions
    • Sinz, A.: Chemical cross-linking and mass spectrometry to map threedimensional protein structures and protein-protein interactions. Mass Spectrom. Rev. 25, 663-682 (2006)
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 663-682
    • Sinz, A.1
  • 10
    • 0036882288 scopus 로고    scopus 로고
    • Analysis of protein-nucleic acid interactions by photochemical cross-linking and mass spectrometry
    • Steen, H., Jensen, O.N.: Analysis of protein-nucleic acid interactions by photochemical cross-linking and mass spectrometry. Mass Spectrom. Rev. 21, 163-182 (2002)
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 163-182
    • Steen, H.1    Jensen, O.N.2
  • 11
    • 77950415030 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry as a low-resolution protein structure determination technique
    • Singh, P., Panchaud, A., Goodlett, D.R.: Chemical cross-linking and mass spectrometry as a low-resolution protein structure determination technique. Anal. Chem. 82, 2636-2642 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 2636-2642
    • Singh, P.1    Panchaud, A.2    Goodlett, D.R.3
  • 13
    • 33646809337 scopus 로고    scopus 로고
    • Three dimensional structures of proteins and protein complexes from chemical cross-linking and mass spectrometry: A biochemical and computational overview
    • Chakravarti, B., Lewis, S.J., Chakravarti, D.N., Raval, A.: Three dimensional structures of proteins and protein complexes from chemical cross-linking and mass spectrometry: a biochemical and computational overview. Curr. Proteomics 3, 1-21 (2006)
    • (2006) Curr. Proteomics , vol.3 , pp. 1-21
    • Chakravarti, B.1    Lewis, S.J.2    Chakravarti, D.N.3    Raval, A.4
  • 14
    • 0042349690 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for protein structural modeling
    • Back, J.W., De Jong, L., Muijsers, A.O., De Koster, C.G.: Chemical cross-linking and mass spectrometry for protein structural modeling. J. Mol. Biol. 331, 303-313 (2003)
    • (2003) J. Mol. Biol. , vol.331 , pp. 303-313
    • Back, J.W.1    De Jong, L.2    Muijsers, A.O.3    De Koster, C.G.4
  • 15
    • 69849100869 scopus 로고    scopus 로고
    • Probing protein structure by amino acidspecific covalent labeling and mass spectrometry
    • Mendoza, V.L., Vachet, R.W.: Probing protein structure by amino acidspecific covalent labeling and mass spectrometry. Mass Spectrom. Rev. 28, 785-815 (2009)
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 785-815
    • Mendoza, V.L.1    Vachet, R.W.2
  • 16
    • 77955671120 scopus 로고    scopus 로고
    • Mass spectrometry combined with oxidative labeling for exploring protein structure and folding
    • Konermann, L., Stocks, B.B., Pan, Y., Tong, X.: Mass spectrometry combined with oxidative labeling for exploring protein structure and folding. Mass Spectrom. Rev. 29, 651-667 (2010)
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 651-667
    • Konermann, L.1    Stocks, B.B.2    Pan, Y.3    Tong, X.4
  • 17
  • 18
    • 43949144960 scopus 로고    scopus 로고
    • Exploring the mechanism of selective noncovalent adduct protein probing mass spectrometry utilizing site-directed mutagenesis to examine ubiquitin
    • Liu, Z.J., Cheng, S.J., Gailie, D.R., Julian, R.R.: Exploring the mechanism of selective noncovalent adduct protein probing mass spectrometry utilizing site-directed mutagenesis to examine ubiquitin. Anal. Chem. 80, 3846-3852 (2008)
    • (2008) Anal. Chem. , vol.80 , pp. 3846-3852
    • Liu, Z.J.1    Cheng, S.J.2    Gailie, D.R.3    Julian, R.R.4
  • 19
    • 55149085458 scopus 로고    scopus 로고
    • Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry
    • Ly, T., Julian, R.R.: Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry. J. Am. Soc. Mass Spectrom. 19, 1663-1672 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1663-1672
    • Ly, T.1    Julian, R.R.2
  • 20
    • 33747882757 scopus 로고    scopus 로고
    • Using ESI-MS to probe protein structure by sitespecific noncovalent attachment of 18-crown-6
    • Ly, T., Julian, R.R.: Using ESI-MS to probe protein structure by sitespecific noncovalent attachment of 18-crown-6. J. Am. Soc. Mass Spectrom. 17, 1209-1215 (2006)
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1209-1215
    • Ly, T.1    Julian, R.R.2
  • 22
    • 35648957210 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes
    • Ruotolo, B.T., Hyung, S.-J., Robinson, P.M., Giles, K., Bateman, R.H., Robinson, C.V.: ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes. Angew. Chem. Int. Ed. 46, 8001-8004 (2007)
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 8001-8004
    • Ruotolo, B.T.1    Hyung, S.-J.2    Robinson, P.M.3    Giles, K.4    Bateman, R.H.5    Robinson, C.V.6
  • 24
    • 42349091083 scopus 로고    scopus 로고
    • Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection
    • Mendoza, V.L., Vachet, R.W.: Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection. Anal. Chem. 80, 2895-2904 (2008)
    • (2008) Anal. Chem. , vol.80 , pp. 2895-2904
    • Mendoza, V.L.1    Vachet, R.W.2
  • 25
    • 79961041262 scopus 로고    scopus 로고
    • Structural insights into the pre-amyloid tetramer of β-2- microglobulin from covalent labeling and mass spectrometry
    • Mendoza, V.L., Baron-Rodriguez, M.A., Blanco, C., Vachet, R.W.: Structural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometry. Biochemistry 50, 6711-6722 (2011)
    • (2011) Biochemistry , vol.50 , pp. 6711-6722
    • Mendoza, V.L.1    Baron-Rodriguez, M.A.2    Blanco, C.3    Vachet, R.W.4
  • 26
    • 77449095000 scopus 로고    scopus 로고
    • Structure of the preamyloid dimer of β-2-microglobulin from covalent labeling and mass spectrometry
    • Mendoza, V.L., Antwi, K., Baron-Rodriguez, M.A., Blanco, C., Vachet, R. W.: Structure of the preamyloid dimer of β-2-microglobulin from covalent labeling and mass spectrometry. Biochemistry 49, 1522-1532 (2010)
    • (2010) Biochemistry , vol.49 , pp. 1522-1532
    • Mendoza, V.L.1    Antwi, K.2    Baron-Rodriguez, M.A.3    Blanco, C.4    Vachet, R.W.5
  • 28
    • 50849129564 scopus 로고    scopus 로고
    • Identification of the copper(II) coordinating residues in the prion protein by metal-catalyzed oxidation mass spectrometry: Evidence for multiple isomers at low copper(II) Loadings
    • Srikanth, R., Wilson, J., Burns, C.S., Vachet, R.W.: Identification of the copper(II) coordinating residues in the prion protein by metal-catalyzed oxidation mass spectrometry: Evidence for Multiple Isomers at Low Copper(II) Loadings. Biochemistry 47, 9258-9268 (2008)
    • (2008) Biochemistry , vol.47 , pp. 9258-9268
    • Srikanth, R.1    Wilson, J.2    Burns, C.S.3    Vachet, R.W.4
  • 29
    • 0030458684 scopus 로고    scopus 로고
    • Selective biochemical modification of functional residues in recombinant human macrophage colony-stimulating factor β (rhM-CSF β): Identification by mass spectrometry
    • Glocker, M.O., Kalkum, M., Yamamoto, R., Schreurs, J.: Selective biochemical modification of functional residues in recombinant human macrophage colony-stimulating factor β (rhM-CSF β): identification by mass spectrometry. Biochemistry 35, 14625-14633 (1996)
    • (1996) Biochemistry , vol.35 , pp. 14625-14633
    • Glocker, M.O.1    Kalkum, M.2    Yamamoto, R.3    Schreurs, J.4
  • 30
    • 0032521065 scopus 로고    scopus 로고
    • Determination of diethylpyrocarbonate- modified amino acid residues in α1-acid glycoprotein by high performance liquid chromatography electrospray ionization-mass spectrometry and matrix-assisted laser desorption/ionization time-of-flightmass spectrometry
    • Dage, J.L., Sun, H., Halsall, H.B.: Determination of diethylpyrocarbonate- modified amino acid residues in α1-acid glycoprotein by high performance liquid chromatography electrospray ionization-mass spectrometry and matrix-assisted laser desorption/ionization time-of-flightmass spectrometry. Anal. Biochem. 257, 176-185 (1998)
    • (1998) Anal. Biochem. , vol.257 , pp. 176-185
    • Dage, J.L.1    Sun, H.2    Halsall, H.B.3
  • 31
    • 0032031804 scopus 로고    scopus 로고
    • Structure characterization of functional histidine residues and carbethoxylated derivatives in peptides and proteins by mass spectrometry
    • Kalkum, M., Przybylski, M., Glocker, M.O.: Structure characterization of functional histidine residues and carbethoxylated derivatives in peptides and proteins by mass spectrometry. Bioconj. Chem. 9, 226-235 (1998)
    • (1998) Bioconj. Chem. , vol.9 , pp. 226-235
    • Kalkum, M.1    Przybylski, M.2    Glocker, M.O.3
  • 32
    • 0034724254 scopus 로고    scopus 로고
    • Diethyl pyrocarbonate modification abolishes fast electron accepting ability of cytochrome b561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: Identification of the modification sites by mass spectrometric analysis
    • Tsubaki, M., Kobayashi, K., Ichise, T., Takeuchi, F., Tagawa, S.: Diethyl pyrocarbonate modification abolishes fast electron accepting ability of cytochrome b561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: identification of the modification sites by mass spectrometric analysis. Biochemistry 39, 3276-3284 (2000)
    • (2000) Biochemistry , vol.39 , pp. 3276-3284
    • Tsubaki, M.1    Kobayashi, K.2    Ichise, T.3    Takeuchi, F.4    Tagawa, S.5
  • 33
    • 0242507462 scopus 로고    scopus 로고
    • Histidine-834 of human erythrocyte band 3 has an essential role in the conformational changes that occur during the band 3-mediated anion exchange
    • Jin, X.R., Abe, Y., Li, C.Y., Hamasaki, N.: Histidine-834 of human erythrocyte band 3 has an essential role in the conformational changes that occur during the band 3-mediated anion exchange. Biochemistry 42, 12927-12932 (2003)
    • (2003) Biochemistry , vol.42 , pp. 12927-12932
    • Jin, X.R.1    Abe, Y.2    Li, C.Y.3    Hamasaki, N.4
  • 34
    • 0037127206 scopus 로고    scopus 로고
    • Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrixassisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting
    • Qin, K., Yang, Y.,Mastrangelo, P., Westaway, D.: Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrixassisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting. J. Biol. Chem. 277, 1981-1990 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 1981-1990
    • Qin, K.1    Yang, Y.2    Mastrangelo, P.3    Westaway, D.4
  • 35
    • 0014955636 scopus 로고
    • Ethoxyformylation of proteins. Reaction of ethoxyformic anhydride with α-chymotrypsin, pepsin, and pancreatic ribonuclease at pH 4
    • Melchior Jr., W.B., Fahrney, D.: Ethoxyformylation of proteins. Reaction of ethoxyformic anhydride with α-chymotrypsin, pepsin, and pancreatic ribonuclease at pH 4. Biochemistry 9, 251-8 (1970)
    • (1970) Biochemistry , vol.9 , pp. 251-258
    • Melchior Jr., W.B.1    Fahrney, D.2
  • 36
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethylpyrocarbonate. Method
    • Miles, E.W.: Modification of histidyl residues in proteins by diethylpyrocarbonate. Method. Enzymol. 47, 431-42 (1977)
    • (1977) Enzymol. , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 37
    • 0031894593 scopus 로고    scopus 로고
    • Which effective property of amino acids is best preserved by the genetic code?
    • Trinquier, G., Sanejouand, Y.-H.: Which effective property of amino acids is best preserved by the genetic code? Protein Eng. 11, 153-169 (1998)
    • (1998) Protein Eng. , vol.11 , pp. 153-169
    • Trinquier, G.1    Sanejouand, Y.-H.2
  • 40
    • 0036838857 scopus 로고    scopus 로고
    • Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: A new approach to protein digestion in minutes
    • Pramanik, B.N., Mirza, U.A., Ing, Y.H., Liu, Y.-H., Bartner, P.L., Weber, P.C., Bose, A.K.: Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: a new approach to protein digestion in minutes. Protein Sci. 11, 2676-2687 (2002)
    • (2002) Protein Sci. , vol.11 , pp. 2676-2687
    • Pramanik, B.N.1    Mirza, U.A.2    Ing, Y.H.3    Liu, Y.-H.4    Bartner, P.L.5    Weber, P.C.6    Bose, A.K.7
  • 41
    • 26844475051 scopus 로고    scopus 로고
    • Ultra fast trypsin digestion of proteins by high intensity focused ultrasound
    • Lopez-Ferrer, D., Capelo, J.L., Vazquez, J.: Ultra fast trypsin digestion of proteins by high intensity focused ultrasound. J. Proteome Res. 4, 1569-1574 (2005)
    • (2005) J. Proteome Res. , vol.4 , pp. 1569-1574
    • Lopez-Ferrer, D.1    Capelo, J.L.2    Vazquez, J.3
  • 42
    • 34248532649 scopus 로고    scopus 로고
    • New findings for in-gel digestion accelerated by high-intensity focused ultrasound for protein identification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • Carreira, R.J., Cordeiro, F.M., Moro, A.J., Rivas, M.G., Rial-Otero, R., Gaspar, E.M., Moura, I., Capelo, J.L.: New findings for in-gel digestion accelerated by high-intensity focused ultrasound for protein identification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. J. Chromatogr. A 1153, 291-299 (2007)
    • (2007) J. Chromatogr. A , vol.1153 , pp. 291-299
    • Carreira, R.J.1    Cordeiro, F.M.2    Moro, A.J.3    Rivas, M.G.4    Rial-Otero, R.5    Gaspar, E.M.6    Moura, I.7    Capelo, J.L.8
  • 44
    • 31344455021 scopus 로고    scopus 로고
    • Rapid protein digestion and identification using monolithic enzymatic microreactor coupled with nano-liquid chromatographyelectrospray ionization mass spectrometry
    • Duan, J., Sun, L., Liang, Z., Zhang, J., Wang, H., Zhang, L., Zhang, W., Zhang, Y.: Rapid protein digestion and identification using monolithic enzymatic microreactor coupled with nano-liquid chromatographyelectrospray ionization mass spectrometry. J. Chromatogr. A 1106, 165-174 (2006)
    • (2006) J. Chromatogr. A , vol.1106 , pp. 165-174
    • Duan, J.1    Sun, L.2    Liang, Z.3    Zhang, J.4    Wang, H.5    Zhang, L.6    Zhang, W.7    Zhang, Y.8
  • 45
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R., Braun, W.: Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19, 319-333 (1998)
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 46
    • 24344483855 scopus 로고    scopus 로고
    • Toward rapid "green", predictable microwave-assisted synthesis
    • Roberts, B.A., Strauss, C.R.: Toward rapid, "green", predictable microwave-assisted synthesis. Acc. Chem. Res. 38, 653-661 (2005)
    • (2005) Acc. Chem. Res. , vol.38 , pp. 653-661
    • Roberts, B.A.1    Strauss, C.R.2
  • 47
    • 0003155051 scopus 로고
    • The rapid synthesis of organic compounds in microwave ovens
    • Gedye, R.N., Smith, F.E., Westaway, K.C.: The rapid synthesis of organic compounds in microwave ovens. Can. J. Chem. 66, 17-26 (1988)
    • (1988) Can. J. Chem. , vol.66 , pp. 17-26
    • Gedye, R.N.1    Smith, F.E.2    Westaway, K.C.3
  • 49
    • 46149129741 scopus 로고
    • Determination of amino acids on Merrifield resin by microwave hydrolysis
    • Yu, H.M., Chen, S.T., Chiou, S.H., Wang, K.T.: Determination of amino acids on Merrifield resin by microwave hydrolysis. J. Chromatogr. 456, 357-62 (1988)
    • (1988) J. Chromatogr. , vol.456 , pp. 357-362
    • Yu, H.M.1    Chen, S.T.2    Chiou, S.H.3    Wang, K.T.4
  • 50
    • 34047260707 scopus 로고    scopus 로고
    • Ultrasound-assisted preparation of liquid samples
    • de Castro, L.: M. D., Priego-Capote, F.: Ultrasound-assisted preparation of liquid samples. Talanta 72, 321-334 (2007)
    • (2007) Talanta , vol.72 , pp. 321-334
    • De Castro, L.1    Priego-Capote, F.2
  • 51
    • 69149100342 scopus 로고    scopus 로고
    • Top-down highresolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state
    • S12658/1-S12658/12
    • Ge, Y., Rybakova, I. N., Xu, Q., Moss, R. L.: Top-down highresolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state. Proc. Natl. Acad. Sci. U.S.A. 106, 12658-12663, S12658/1-S12658/12 (2009)
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 12658-12663
    • Ge, Y.1    Rybakova, I.N.2    Xu, Q.3    Moss, R.L.4
  • 52
    • 13944257472 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry of model peptides reveals diagnostic fragment ions for protein ubiquitination
    • Warren, M.R.E., Parker, C.E., Mocanu, V., Klapper, D., Borchers, C. H.: Electrospray ionization tandem mass spectrometry of model peptides reveals diagnostic fragment ions for protein ubiquitination. Rapid Commun. Mass Spectrom. 19, 429-437 (2005)
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 429-437
    • Warren, M.R.E.1    Parker, C.E.2    Mocanu, V.3    Klapper, D.4    Borchers, C.H.5
  • 53
    • 33750610338 scopus 로고    scopus 로고
    • Characterization of neurohistone variants and post-translational modifications by electron capture dissociation mass spectrometry
    • Garcia, B.A., Siuti, N., Thomas, C.E., Mizzen, C.A., Kelleher, N.L.: Characterization of neurohistone variants and post-translational modifications by electron capture dissociation mass spectrometry. Int. J. Mass Spectrom. 259, 184-196 (2007)
    • (2007) Int. J. Mass Spectrom. , vol.259 , pp. 184-196
    • Garcia, B.A.1    Siuti, N.2    Thomas, C.E.3    Mizzen, C.A.4    Kelleher, N.L.5
  • 55
    • 55949087964 scopus 로고    scopus 로고
    • Tissuespecific expression and post-translational modification of histone H3 variants
    • Garcia, B.A., Thomas, C.E., Kelleher, N.L., Mizzen, C.A.: Tissuespecific expression and post-translational modification of histone H3 variants. J. Proteome Res. 7, 4225-4236 (2008)
    • (2008) J. Proteome Res. , vol.7 , pp. 4225-4236
    • Garcia, B.A.1    Thomas, C.E.2    Kelleher, N.L.3    Mizzen, C.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.