메뉴 건너뛰기




Volumn 24, Issue 6, 2013, Pages 835-845

Complementary MS methods assist conformational characterization of antibodies with altered S-S bonding networks

Author keywords

Antibody characterization; Antibody mutants; Fast photochemical oxidation of proteins (FPOP); IgG2; Ion mobility; Protein structure; Top down

Indexed keywords

IGG2; ION MOBILITY; PHOTOCHEMICAL OXIDATION; PROTEIN STRUCTURES; TOPDOWN;

EID: 84877741020     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-013-0582-4     Document Type: Article
Times cited : (54)

References (52)
  • 1
    • 84863218474 scopus 로고    scopus 로고
    • Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars
    • 10.1038/nrd3746 1:CAS:528:DC%2BC38XpsVSqt74%3D
    • Berkowitz, S.A.; Engen, J.R.; Mazzeo, J.R.; Jones, G.B.: Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars. Nat. Rev. Drug Discov 11, 527-540 (2012)
    • (2012) Nat. Rev. Drug Discov , vol.11 , pp. 527-540
    • Berkowitz, S.A.1    Engen, J.R.2    Mazzeo, J.R.3    Jones, G.B.4
  • 2
    • 54349091558 scopus 로고    scopus 로고
    • Safety-related regulatory actions for biologicals approved in the United States and the European Union
    • 10.1001/jama.300.16.1887 1:CAS:528:DC%2BD1cXht12iur%2FN
    • Giezen, T.J.; Mantel-Teeuwisse, A.K.; Straus, S.M.; Schellekens, H.; Leufkens, H.G.; Egberts, A.C.: Safety-related regulatory actions for biologicals approved in the United States and the European Union. JAMA 300, 1887-1896 (2008)
    • (2008) JAMA , vol.300 , pp. 1887-1896
    • Giezen, T.J.1    Mantel-Teeuwisse, A.K.2    Straus, S.M.3    Schellekens, H.4    Leufkens, H.G.5    Egberts, A.C.6
  • 3
    • 35148834701 scopus 로고    scopus 로고
    • What's fueling the biotech engine?
    • 10.1038/nbt1007-1097 1:CAS:528:DC%2BD2sXhtFagt7vK
    • Aggarwal, S.: What's fueling the biotech engine? Nat. Biotechnol. 25, 1097-1104 (2007)
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1097-1104
    • Aggarwal, S.1
  • 4
    • 60149105523 scopus 로고    scopus 로고
    • Jama study casts cloud over biologic safety
    • 10.1038/nbt0109-11 1:CAS:528:DC%2BD1MXis1Oqug%3D%3D
    • Kling, J.: Jama study casts cloud over biologic safety. Nat. Biotechnol. 27, 11-12 (2009)
    • (2009) Nat. Biotechnol. , vol.27 , pp. 11-12
    • Kling, J.1
  • 7
    • 84861842454 scopus 로고    scopus 로고
    • Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry
    • 10.1021/ac3002885 1:CAS:528:DC%2BC38Xls1yqtro%3D
    • Beck, A.; Sanglier, C.; Van, D.A.: Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry. Anal. Chem. 84, 4637-4646 (2012)
    • (2012) Anal. Chem. , vol.84 , pp. 4637-4646
    • Beck, A.1    Sanglier, C.2    Van, D.A.3
  • 8
    • 79961116944 scopus 로고    scopus 로고
    • Developing the nation's biosimilars program
    • 10.1056/NEJMp1107285 1:CAS:528:DC%2BC3MXpvFSitL8%3D
    • Kozlowski, S.; Woodcock, J.; Midthun, K.; Sherman, R.B.: Developing the nation's biosimilars program. N. Engl. J. Med. 365, 385-388 (2011)
    • (2011) N. Engl. J. Med. , vol.365 , pp. 385-388
    • Kozlowski, S.1    Woodcock, J.2    Midthun, K.3    Sherman, R.B.4
  • 9
    • 83255165688 scopus 로고    scopus 로고
    • What's fueling the biotech engine-2010 to 2011
    • 10.1038/nbt.2060 1:CAS:528:DC%2BC3MXhs12gsbzE
    • Aggarwal, S.: What's fueling the biotech engine-2010 to 2011. Nat. Biotechnol. 29, 1083-1089 (2011)
    • (2011) Nat. Biotechnol. , vol.29 , pp. 1083-1089
    • Aggarwal, S.1
  • 10
    • 67649851892 scopus 로고    scopus 로고
    • Mabs: A business perspective
    • 10.4161/mabs.1.2.7736
    • Scolnik, P.A.: Mabs: A business perspective. MAbs 1, 179-184 (2009)
    • (2009) MAbs , vol.1 , pp. 179-184
    • Scolnik, P.A.1
  • 11
    • 34247876138 scopus 로고    scopus 로고
    • Development trends for monoclonal antibody cancer therapeutics
    • 10.1038/nrd2241 1:CAS:528:DC%2BD2sXkslyiu7g%3D
    • Reichert, J.M.; Valge-Archer, V.E.: Development trends for monoclonal antibody cancer therapeutics. Nat. Rev. Drug Discov. 6, 349-356 (2007)
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 349-356
    • Reichert, J.M.1    Valge-Archer, V.E.2
  • 12
    • 34748865088 scopus 로고    scopus 로고
    • Antibody therapeutics: Isotype and glycoform selection
    • 10.1517/14712598.7.9.1401 1:CAS:528:DC%2BD2sXps1Wns7g%3D
    • Jefferis, R.: Antibody therapeutics: Isotype and glycoform selection. Expert Opin Biol Ther 7, 1401-1413 (2007)
    • (2007) Expert Opin Biol Ther , vol.7 , pp. 1401-1413
    • Jefferis, R.1
  • 13
    • 33847751162 scopus 로고    scopus 로고
    • Human immunoglobulin G2 (IgG2) and IgG4, but not IgG1 or IgG3, protect mice against cryptococcus neoformans infection
    • 10.1128/IAI.01161-06 1:CAS:528:DC%2BD2sXivV2htbw%3D
    • Beenhouwer, D.O.; Yoo, E.M.; Lai, C.W.; Rocha, M.A.; Morrison, S.L.: Human immunoglobulin G2 (IgG2) and IgG4, but not IgG1 or IgG3, protect mice against cryptococcus neoformans infection. Infect. Immun. 75, 1424-1435 (2007)
    • (2007) Infect. Immun. , vol.75 , pp. 1424-1435
    • Beenhouwer, D.O.1    Yoo, E.M.2    Lai, C.W.3    Rocha, M.A.4    Morrison, S.L.5
  • 16
    • 77950281386 scopus 로고    scopus 로고
    • Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect fc gamma receptor or c1q binding
    • 10.1002/pro.352 1:CAS:528:DC%2BC3cXktFyrtLc%3D
    • Lightle, S.; Aykent, S.; Lacher, N.; Mitaksov, V.; Wells, K.; Zobel, J.; Oliphant, T.: Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect fc gamma receptor or c1q binding. Protein Sci. 19, 753-762 (2010)
    • (2010) Protein Sci. , vol.19 , pp. 753-762
    • Lightle, S.1    Aykent, S.2    Lacher, N.3    Mitaksov, V.4    Wells, K.5    Zobel, J.6    Oliphant, T.7
  • 17
    • 28844474910 scopus 로고    scopus 로고
    • Evidence for macromolecular protein rings in the absence of bulk water
    • 10.1126/science.1120177 1:CAS:528:DC%2BD2MXhtlSntLfE
    • Ruotolo, B.T.; Giles, K.; Campuzano, I.; Sandercock, A.M.; Bateman, R.H.; Robinson, C.V.: Evidence for macromolecular protein rings in the absence of bulk water. Science 310, 1658-1661 (2005)
    • (2005) Science , vol.310 , pp. 1658-1661
    • Ruotolo, B.T.1    Giles, K.2    Campuzano, I.3    Sandercock, A.M.4    Bateman, R.H.5    Robinson, C.V.6
  • 18
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: Technology for structural genomics and proteomics
    • 10.1021/cr068289b 1:CAS:528:DC%2BD2sXotVKhu7Y%3D
    • Benesch, J.L.; Ruotolo, B.T.; Simmons, D.A.; Robinson, C.V.: Protein complexes in the gas phase: Technology for structural genomics and proteomics. Chem. Rev. 107, 3544-3567 (2007)
    • (2007) Chem. Rev. , vol.107 , pp. 3544-3567
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 19
    • 48249109172 scopus 로고    scopus 로고
    • High-resolution mass spectrometry of viral assemblies: Molecular composition and stability of dimorphic hepatitis b virus capsids
    • 10.1073/pnas.0800406105 1:CAS:528:DC%2BD1cXosFakt70%3D
    • Uetrecht, C.; Versluis, C.; Watts, N.R.; Roos, W.H.; Wuite, G.J.; Wingfield, P.T.; Steven, A.C.; Heck, A.J.: High-resolution mass spectrometry of viral assemblies: Molecular composition and stability of dimorphic hepatitis b virus capsids. Proc. Natl. Acad. Sci. U.S.A. 105, 9216-9220 (2008)
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9216-9220
    • Uetrecht, C.1    Versluis, C.2    Watts, N.R.3    Roos, W.H.4    Wuite, G.J.5    Wingfield, P.T.6    Steven, A.C.7    Heck, A.J.8
  • 20
    • 78649529358 scopus 로고    scopus 로고
    • Native electrospray and electron-capture dissociation in fticr mass spectrometry provide top-down sequencing of a protein component in an intact protein assembly
    • 10.1016/j.jasms.2010.08.006 1:CAS:528:DC%2BC3cXhsVGisb7E
    • Zhang, H.; Cui, W.; Wen, J.; Blankenship, R.E.; Gross, M.L.: Native electrospray and electron-capture dissociation in fticr mass spectrometry provide top-down sequencing of a protein component in an intact protein assembly. J. Am. Soc. Mass Spectrom. 21, 1966-1968 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1966-1968
    • Zhang, H.1    Cui, W.2    Wen, J.3    Blankenship, R.E.4    Gross, M.L.5
  • 21
    • 76749099328 scopus 로고    scopus 로고
    • Conformation and dynamics of biopharmaceuticals: Transition of mass spectrometry-based tools from academe to industry
    • 10.1016/j.jasms.2009.10.013 1:CAS:528:DC%2BC3cXitlSntbg%3D
    • Kaltashov, I.A.; Bobst, C.E.; Abzalimov, R.R.; Berkowitz, S.A.; Houde, D.: Conformation and dynamics of biopharmaceuticals: Transition of mass spectrometry-based tools from academe to industry. J. Am. Soc. Mass Spectrom. 21, 323-337 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 323-337
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3    Berkowitz, S.A.4    Houde, D.5
  • 23
    • 77955606264 scopus 로고    scopus 로고
    • Resolving disulfide structural isoforms of IgG2 monoclonal antibodies by ion mobility mass spectrometry
    • 10.1021/ac1013139 1:CAS:528:DC%2BC3cXptFyjtrY%3D
    • Bagal, D.; Valliere-Douglass, J.F.; Balland, A.; Schnier, P.D.: Resolving disulfide structural isoforms of IgG2 monoclonal antibodies by ion mobility mass spectrometry. Anal. Chem. 82, 6751-6755 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 6751-6755
    • Bagal, D.1    Valliere-Douglass, J.F.2    Balland, A.3    Schnier, P.D.4
  • 24
    • 67650754060 scopus 로고    scopus 로고
    • Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer
    • 10.1016/j.jasms.2009.03.020 1:CAS:528:DC%2BD1MXptV2msL8%3D
    • Bondarenko, P.V.; Second, T.P.; Zabrouskov, V.; Makarov, A.A.; Zhang, Z.: Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer. J. Am. Soc. Mass Spectrom. 20, 1415-1424 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1415-1424
    • Bondarenko, P.V.1    Second, T.P.2    Zabrouskov, V.3    Makarov, A.A.4    Zhang, Z.5
  • 25
    • 82555170557 scopus 로고    scopus 로고
    • Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry
    • 10.1021/ac201293m 1:CAS:528:DC%2BC3MXhtlGlsLvN
    • Tsybin, Y.O.; Fornelli, L.; Stoermer, C.; Luebeck, M.; Parra, J.; Nallet, S.; Wurm, F.M.; Hartmer, R.: Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry. Anal. Chem. 83, 8919-8927 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 8919-8927
    • Tsybin, Y.O.1    Fornelli, L.2    Stoermer, C.3    Luebeck, M.4    Parra, J.5    Nallet, S.6    Wurm, F.M.7    Hartmer, R.8
  • 26
    • 0036102156 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
    • 10.1110/ps.4670102 1:CAS:528:DC%2BD38XktFWhu7w%3D
    • Baerga-Ortiz, A.; Hughes, C.A.; Mandell, J.G.; Komives, E.A.: Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein. Protein Sci. 11, 1300-1308 (2002)
    • (2002) Protein Sci. , vol.11 , pp. 1300-1308
    • Baerga-Ortiz, A.1    Hughes, C.A.2    Mandell, J.G.3    Komives, E.A.4
  • 27
    • 64849114588 scopus 로고    scopus 로고
    • Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry
    • 10.1021/ac9009287 1:CAS:528:DC%2BD1MXlvVWmtrw%3D
    • Houde, D.; Arndt, J.; Domeier, W.; Berkowitz, S.; Engen, J.R.: Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry. Anal. Chem. 81, 5966 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 5966
    • Houde, D.1    Arndt, J.2    Domeier, W.3    Berkowitz, S.4    Engen, J.R.5
  • 28
    • 80054704826 scopus 로고    scopus 로고
    • Fast photochemical oxidation of proteins for epitope mapping
    • 10.1021/ac2007366 1:CAS:528:DC%2BC3MXht1SltLvL
    • Jones, L.M.; Sperry, J.B.; Carroll, J.A.; Gross, M.L.: Fast photochemical oxidation of proteins for epitope mapping. Anal. Chem. 83, 7657-7661 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 7657-7661
    • Jones, L.M.1    Sperry, J.B.2    Carroll, J.A.3    Gross, M.L.4
  • 29
    • 81255175613 scopus 로고    scopus 로고
    • Revealing a positive charge patch on a recombinant monoclonal antibody by chemical labeling and mass spectrometry
    • 10.1021/ac2016129 1:CAS:528:DC%2BC3MXhtlalu7rK
    • Zhang, L.; Lilyestrom, W.; Li, C.; Scherer, T.; van Reis, R.; Zhang, B.: Revealing a positive charge patch on a recombinant monoclonal antibody by chemical labeling and mass spectrometry. Anal. Chem. 83, 8501-8508 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 8501-8508
    • Zhang, L.1    Lilyestrom, W.2    Li, C.3    Scherer, T.4    Van Reis, R.5    Zhang, B.6
  • 30
    • 84860758736 scopus 로고    scopus 로고
    • Conformational analysis of therapeutic proteins by hydroxyl radical protein footprinting
    • 10.1208/s12248-012-9336-7 1:CAS:528:DC%2BC38Xlslansbs%3D
    • Watson, C.; Sharp, J.S.: Conformational analysis of therapeutic proteins by hydroxyl radical protein footprinting. AAPS J 14, 206-217 (2012)
    • (2012) AAPS J , vol.14 , pp. 206-217
    • Watson, C.1    Sharp, J.S.2
  • 31
    • 80054688998 scopus 로고    scopus 로고
    • Characterization of glycosylation sites for a recombinant IgG1 monoclonal antibody and a ctla4-ig fusion protein by liquid chromatography-mass spectrometry peptide mapping
    • 10.1016/j.chroma.2011.08.089 1:CAS:528:DC%2BC3MXhtlejtrbF
    • Bongers, J.; Devincentis, J.; Fu, J.; Huang, P.; Kirkley, D.H.; Leister, K.; Liu, P.; Ludwig, R.; Rumney, K.; Tao, L.; Wu, W.; Russell, R.J.: Characterization of glycosylation sites for a recombinant IgG1 monoclonal antibody and a ctla4-ig fusion protein by liquid chromatography-mass spectrometry peptide mapping. J. Chromatogr. A 1218, 8140-8149 (2011)
    • (2011) J. Chromatogr. A , vol.1218 , pp. 8140-8149
    • Bongers, J.1    Devincentis, J.2    Fu, J.3    Huang, P.4    Kirkley, D.H.5    Leister, K.6    Liu, P.7    Ludwig, R.8    Rumney, K.9    Tao, L.10    Wu, W.11    Russell, R.J.12
  • 32
    • 77957333488 scopus 로고    scopus 로고
    • Mass spectrometric analysis of intact human monoclonal antibody aggregates fractionated by size-exclusion chromatography
    • 10.1007/s11095-010-0224-5
    • Kukrer, B.; Filipe, V.; van Duijn, E.; Kasper, P.T.; Vreeken, R.J.; Heck, A.J.; Jiskoot, W.: Mass spectrometric analysis of intact human monoclonal antibody aggregates fractionated by size-exclusion chromatography. Pharm. Res. 27, 2197-2204 (2010)
    • (2010) Pharm. Res. , vol.27 , pp. 2197-2204
    • Kukrer, B.1    Filipe, V.2    Van Duijn, E.3    Kasper, P.T.4    Vreeken, R.J.5    Heck, A.J.6    Jiskoot, W.7
  • 33
    • 81255144037 scopus 로고    scopus 로고
    • Unit mass baseline resolution for an intact 148 kDa therapeutic monoclonal antibody by fourier transform ion cyclotron resonance mass spectrometry
    • 10.1021/ac202429c 1:CAS:528:DC%2BC3MXhtlCmurjN
    • Valeja, S.G.; Kaiser, N.K.; Xian, F.; Hendrickson, C.L.; Rouse, J.C.; Marshall, A.G.: Unit mass baseline resolution for an intact 148 kDa therapeutic monoclonal antibody by fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 83, 8391-8395 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 8391-8395
    • Valeja, S.G.1    Kaiser, N.K.2    Xian, F.3    Hendrickson, C.L.4    Rouse, J.C.5    Marshall, A.G.6
  • 34
    • 35648957210 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes
    • 10.1002/anie.200702161 1:CAS:528:DC%2BD2sXht1Kitb3O
    • 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. Engl. 46, 8001-8004 (2007)
    • (2007) Angew. Chem. Int. Ed. Engl. , 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
  • 36
    • 18744397503 scopus 로고    scopus 로고
    • Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy
    • 10.1073/pnas.212643599 1:CAS:528:DC%2BD38Xps1egtb0%3D
    • Oh, H.; Breuker, K.; Sze, S.K.; Ge, Y.; Carpenter, B.K.; McLafferty, F.W.: Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 99, 15863-15868 (2002)
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15863-15868
    • Oh, H.1    Breuker, K.2    Sze, S.K.3    Ge, Y.4    Carpenter, B.K.5    McLafferty, F.W.6
  • 37
    • 27844593258 scopus 로고    scopus 로고
    • Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale
    • 10.1016/j.jasms.2005.09.008 1:CAS:528:DC%2BD2MXht1CmsbrJ
    • Hambly, D.M.; Gross, M.L.: Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale. J. Am. Soc. Mass Spectrom. 16, 2057-2063 (2005)
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 2057-2063
    • Hambly, D.M.1    Gross, M.L.2
  • 38
    • 68849107091 scopus 로고    scopus 로고
    • Fast photochemical oxidation of protein footprints faster than protein unfolding
    • 10.1021/ac901054w 1:CAS:528:DC%2BD1MXovFWltr0%3D
    • Gau, B.C.; Sharp, J.S.; Rempel, D.L.; Gross, M.L.: Fast photochemical oxidation of protein footprints faster than protein unfolding. Anal. Chem. 81, 6563-6571 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 6563-6571
    • Gau, B.C.1    Sharp, J.S.2    Rempel, D.L.3    Gross, M.L.4
  • 39
    • 78650772189 scopus 로고    scopus 로고
    • Fast photochemical oxidation of proteins for comparing structures of protein-ligand complexes: The calmodulin-peptide model system
    • 10.1021/ac102426d
    • Zhang, H.; Gau, B.C.; Jones, L.M.; Vidavsky, I.; Gross, M.L.: Fast photochemical oxidation of proteins for comparing structures of protein-ligand complexes: the calmodulin-peptide model system. Anal. Chem. 83, 311-318 (2010)
    • (2010) Anal. Chem. , vol.83 , pp. 311-318
    • Zhang, H.1    Gau, B.C.2    Jones, L.M.3    Vidavsky, I.4    Gross, M.L.5
  • 40
    • 79955412076 scopus 로고    scopus 로고
    • Native electrospray mass spectrometry reveals the nature and stoichiometry of pigments in the fmo photosynthetic antenna protein
    • 10.1021/bi200239k 1:CAS:528:DC%2BC3MXksVKiu70%3D
    • Wen, J.; Zhang, H.; Gross, M.L.; Blankenship, R.E.: Native electrospray mass spectrometry reveals the nature and stoichiometry of pigments in the fmo photosynthetic antenna protein. Biochemistry 50, 3502-3511 (2011)
    • (2011) Biochemistry , vol.50 , pp. 3502-3511
    • Wen, J.1    Zhang, H.2    Gross, M.L.3    Blankenship, R.E.4
  • 41
    • 83555173535 scopus 로고    scopus 로고
    • Disulfide scrambling in IgG2 monoclonal antibodies: Insights from molecular dynamics simulations
    • 10.1007/s11095-011-0503-9 1:CAS:528:DC%2BC3MXnsVWrurs%3D
    • Wang, X.; Kumar, S.; Singh, S.K.: Disulfide scrambling in IgG2 monoclonal antibodies: Insights from molecular dynamics simulations. Pharm. Res. 28, 3128-3144 (2011)
    • (2011) Pharm. Res. , vol.28 , pp. 3128-3144
    • Wang, X.1    Kumar, S.2    Singh, S.K.3
  • 42
    • 79960370853 scopus 로고    scopus 로고
    • Native electrospray and electron-capture dissociation fticr mass spectrometry for top-down studies of protein assemblies
    • 10.1021/ac200695d 1:CAS:528:DC%2BC3MXnvVaktrw%3D
    • Zhang, H.; Cui, W.; Wen, J.; Blankenship, R.E.; Gross, M.L.: Native electrospray and electron-capture dissociation fticr mass spectrometry for top-down studies of protein assemblies. Anal. Chem. 83, 5598-5606 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 5598-5606
    • Zhang, H.1    Cui, W.2    Wen, J.3    Blankenship, R.E.4    Gross, M.L.5
  • 43
    • 1442299864 scopus 로고    scopus 로고
    • Radiolytic modification of acidic amino acid residues in peptides: Probes for examining protein-protein interactions
    • 10.1021/ac035422g 1:CAS:528:DC%2BD2cXovVegsg%3D%3D
    • Xu, G.; Chance, M.R.: Radiolytic modification of acidic amino acid residues in peptides: Probes for examining protein-protein interactions. Anal. Chem. 76, 1213-1221 (2004)
    • (2004) Anal. Chem. , vol.76 , pp. 1213-1221
    • Xu, G.1    Chance, M.R.2
  • 44
    • 34548337296 scopus 로고    scopus 로고
    • Hydroxyl radical-mediated modification of proteins as probes for structural proteomics
    • 10.1021/cr0682047 1:CAS:528:DC%2BD2sXos1egs7s%3D
    • Xu, G.; Chance, M.R.: Hydroxyl radical-mediated modification of proteins as probes for structural proteomics. Chem. Rev. 107, 3514-3543 (2007)
    • (2007) Chem. Rev. , vol.107 , pp. 3514-3543
    • Xu, G.1    Chance, M.R.2
  • 45
    • 77956566214 scopus 로고    scopus 로고
    • Sulfate radical anion as a new reagent for fast photochemical oxidation of proteins
    • 10.1021/ac101760y 1:CAS:528:DC%2BC3cXhtVKrs7rL
    • Gau, B.C.; Chen, H.; Zhang, Y.; Gross, M.L.: Sulfate radical anion as a new reagent for fast photochemical oxidation of proteins. Anal. Chem. 82, 7821-7827 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 7821-7827
    • Gau, B.C.1    Chen, H.2    Zhang, Y.3    Gross, M.L.4
  • 46
    • 77956943767 scopus 로고    scopus 로고
    • Rapid and refined separation of human IgG2 disulfide isomers using superficially porous particles
    • 10.1002/jssc.201000230 1:CAS:528:DC%2BC3cXht12it7bK
    • Wang, Q.; Lacher, N.A.; Muralidhara, B.K.; Schlittler, M.R.; Aykent, S.; Demarest, C.W.: Rapid and refined separation of human IgG2 disulfide isomers using superficially porous particles. J. Sep. Sci. 33, 2671-2680 (2010)
    • (2010) J. Sep. Sci. , vol.33 , pp. 2671-2680
    • Wang, Q.1    Lacher, N.A.2    Muralidhara, B.K.3    Schlittler, M.R.4    Aykent, S.5    Demarest, C.W.6
  • 47
    • 77955412238 scopus 로고    scopus 로고
    • Post-translational modifications differentially affect IgG1 conformation and receptor binding
    • 10.1074/mcp.M900540-MCP200 1:CAS:528:DC%2BC3cXhtlWgtbrM
    • Houde, D.; Peng, Y.; Berkowitz, S.A.; Engen, J.R.: Post-translational modifications differentially affect IgG1 conformation and receptor binding. Mol. Cell. Proteom. 9, 1716-1728 (2010)
    • (2010) Mol. Cell. Proteom. , vol.9 , pp. 1716-1728
    • Houde, D.1    Peng, Y.2    Berkowitz, S.A.3    Engen, J.R.4
  • 48
    • 0003653070 scopus 로고
    • 2nd revised ed.; Elsevier/North-Holland: Amsterdam; The Netherlands
    • Allen, G.: Sequencing of proteins and peptides, 2nd revised ed.; Elsevier/North-Holland: Amsterdam; The Netherlands (1981)
    • (1981) Sequencing of Proteins and Peptides
    • Allen, G.1
  • 49
    • 41549169241 scopus 로고    scopus 로고
    • Specificity of immobilized porcine pepsin in h/d exchange compatible conditions
    • 10.1002/rcm.3467 1:CAS:528:DC%2BD1cXksFWku7Y%3D
    • Hamuro, Y.; Coales, S.J.; Molnar, K.S.; Tuske, S.J.; Morrow, J.A.: Specificity of immobilized porcine pepsin in h/d exchange compatible conditions. Rapid Commun. Mass Spectrom. 22, 1041-1046 (2008)
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 1041-1046
    • Hamuro, Y.1    Coales, S.J.2    Molnar, K.S.3    Tuske, S.J.4    Morrow, J.A.5
  • 50
    • 68049143439 scopus 로고    scopus 로고
    • On the relation between residue flexibility and local solvent accessibility in proteins
    • 10.1002/prot.22375 1:CAS:528:DC%2BD1MXns1ert70%3D
    • Zhang, H.; Zhang, T.; Chen, K.; Shen, S.; Ruan, J.; Kurgan, L.: On the relation between residue flexibility and local solvent accessibility in proteins. Proteins 76, 617-636 (2009)
    • (2009) Proteins , vol.76 , pp. 617-636
    • Zhang, H.1    Zhang, T.2    Chen, K.3    Shen, S.4    Ruan, J.5    Kurgan, L.6
  • 51
    • 0028869485 scopus 로고
    • The structural requirements for complement activation by IgG: Does it hinge on the hinge?
    • 10.1016/0167-5699(95)80094-8 1:CAS:528:DyaK2MXjsFegsLY%3D
    • Brekke, O.H.; Michaelsen, T.E.; Sandlie, I.: The structural requirements for complement activation by IgG: Does it hinge on the hinge? Immunol. Today 16, 85-90 (1995)
    • (1995) Immunol. Today , vol.16 , pp. 85-90
    • Brekke, O.H.1    Michaelsen, T.E.2    Sandlie, I.3
  • 52
    • 57349097173 scopus 로고    scopus 로고
    • Structural classification of cdr-h3 revisited: A lesson in antibody modeling
    • 10.1002/prot.22087 1:CAS:528:DC%2BD1cXhtlCgsbrF
    • Kuroda, D.; Shirai, H.; Kobori, M.; Nakamura, H.: Structural classification of cdr-h3 revisited: a lesson in antibody modeling. Proteins 73, 608-620 (2008)
    • (2008) Proteins , vol.73 , pp. 608-620
    • Kuroda, D.1    Shirai, H.2    Kobori, M.3    Nakamura, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.