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Volumn 13, Issue 3-4, 2013, Pages 438-456

Chemical cross-linkers for protein structure studies by mass spectrometry

Author keywords

Cross link; MS; Protein; Structure; Technology

Indexed keywords

AMINE; ARGININE; ASPARTIC ACID; CARBOXYLIC ACID; GLUTAMIC ACID; GLYCOPROTEIN; GUANIDINE; ION; ISOTOPE; LYSINE; PEPTIDE; SUGAR;

EID: 84873988417     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201200305     Document Type: Review
Times cited : (61)

References (112)
  • 2
    • 10644254712 scopus 로고    scopus 로고
    • Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry
    • Vasilescu, J., Guo, X., Kast, J., Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry. Proteomics 2004, 4, 3845-3854.
    • (2004) Proteomics , vol.4 , pp. 3845-3854
    • Vasilescu, J.1    Guo, X.2    Kast, J.3
  • 3
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: a primer
    • Marshall, A. G., Hendrickson, C. L., Jackson, G. S., Fourier transform ion cyclotron resonance mass spectrometry: a primer. Mass Spectrom. Rev. 1998, 17, 1-35.
    • (1998) Mass Spectrom. Rev. , vol.17 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 4
    • 18344364097 scopus 로고    scopus 로고
    • The Orbitrap: a new mass spectrometer
    • Hu, Q., Noll, R. J., Li, H., Makarov, A. et al., The Orbitrap: a new mass spectrometer. J. Mass Spectrom. 2005, 40, 430-443.
    • (2005) J. Mass Spectrom. , vol.40 , pp. 430-443
    • Hu, Q.1    Noll, R.J.2    Li, H.3    Makarov, A.4
  • 5
    • 77955381399 scopus 로고    scopus 로고
    • Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics
    • Leitner, A., Walzthoeni, T., Kahraman, A., Herzog, F. et al., Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics. Mol. Cell Proteomics 2010, 9, 1634-1649.
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 1634-1649
    • Leitner, A.1    Walzthoeni, T.2    Kahraman, A.3    Herzog, F.4
  • 6
    • 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. 2010, 29, 862-876.
    • (2010) Mass Spectrom Rev. , vol.29 , pp. 862-876
    • Petrotchenko, E.V.1    Borchers, C.H.2
  • 7
    • 47549096059 scopus 로고    scopus 로고
    • Mass spectrometric analysis of cross-linking sites for the structure of proteins and protein complexes
    • Jin Lee, Y., Mass spectrometric analysis of cross-linking sites for the structure of proteins and protein complexes. Mol. Biosyst. 2008, 4, 816-823.
    • (2008) Mol. Biosyst. , vol.4 , pp. 816-823
    • Jin Lee, Y.1
  • 8
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions
    • Sinz, A., Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions. Mass Spectrom. Rev. 2006, 25, 663-682.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 663-682
    • Sinz, A.1
  • 9
    • 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. 2003, 331, 303-313.
    • (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
  • 10
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz, A., Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Spectrom. 2003, 38, 1225-1237.
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 12
    • 34447538183 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry as structure determination tools
    • Novak, P., Giannakopulos, A. E., Chemical cross-linking and mass spectrometry as structure determination tools. Eur. J. Mass Spectrom. 2007, 13, 105-113.
    • (2007) Eur. J. Mass Spectrom. , vol.13 , pp. 105-113
    • Novak, P.1    Giannakopulos, A.E.2
  • 13
    • 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. 2010, 82, 2636-2642.
    • (2010) Anal. Chem. , vol.82 , pp. 2636-2642
    • Singh, P.1    Panchaud, A.2    Goodlett, D.R.3
  • 14
    • 22644437896 scopus 로고    scopus 로고
    • Identification and mapping of protein-protein interactions by a combination of cross-linking, cleavage, and proteomics
    • Trakselis, M. A., Alley, S. C., Ishmael, F. T., Identification and mapping of protein-protein interactions by a combination of cross-linking, cleavage, and proteomics. Bioconjug. Chem. 2005, 16, 741-750.
    • (2005) Bioconjug. Chem. , vol.16 , pp. 741-750
    • Trakselis, M.A.1    Alley, S.C.2    Ishmael, F.T.3
  • 16
    • 82555186441 scopus 로고    scopus 로고
    • Bioinformatics tools for the structural elucidation of multi-subunit protein complexes by mass spectrometric analysis of protein-protein cross-links
    • Mayne, S. L. N., Patterton, H.-G., Bioinformatics tools for the structural elucidation of multi-subunit protein complexes by mass spectrometric analysis of protein-protein cross-links. Brief Bioinform. 2011, 12, 660-671.
    • (2011) Brief Bioinform. , vol.12 , pp. 660-671
    • Mayne, S.L.N.1    Patterton, H.-G.2
  • 17
    • 0033518556 scopus 로고    scopus 로고
    • Top down versus bottom up protein characterization by tandem high-resolution mass spectrometry
    • Kelleher, N. L., Lin, H. Y., Valaskovic, G. A., Aaserud, D. J. et al., Top down versus bottom up protein characterization by tandem high-resolution mass spectrometry. J. Am. Chem. Soc. 1999, 121, 806-812.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 806-812
    • Kelleher, N.L.1    Lin, H.Y.2    Valaskovic, G.A.3    Aaserud, D.J.4
  • 18
    • 0033591076 scopus 로고    scopus 로고
    • Biochemistry: biomolecule mass spectrometry
    • McLafferty, F. W., Biochemistry: biomolecule mass spectrometry. Science 1999, 284, 1289-1290.
    • (1999) Science , vol.284 , pp. 1289-1290
    • McLafferty, F.W.1
  • 19
    • 0037236038 scopus 로고    scopus 로고
    • A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry
    • Kruppa, G. H., Schoeniger, J., Young, M. M., A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry. Rapid Commun. Mass Spectrom. 2003, 17, 155-162.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 155-162
    • Kruppa, G.H.1    Schoeniger, J.2    Young, M.M.3
  • 20
    • 23844481127 scopus 로고    scopus 로고
    • Unambiguous assignment of intramolecular chemical cross-links in modified mammalian membrane proteins by Fourier transform-tandem mass spectrometry
    • Novak, P., Haskins, W. E., Ayson, M. J., Jacobsen, R. B. et al., Unambiguous assignment of intramolecular chemical cross-links in modified mammalian membrane proteins by Fourier transform-tandem mass spectrometry. Anal. Chem. 2005, 77, 5101-5106.
    • (2005) Anal. Chem. , vol.77 , pp. 5101-5106
    • Novak, P.1    Haskins, W.E.2    Ayson, M.J.3    Jacobsen, R.B.4
  • 21
    • 70350625165 scopus 로고    scopus 로고
    • Top-down protein fragmentation by infrared multiphoton dissociation in a dual pressure linear ion trap
    • Madsen, J. A., Gardner, M. W., Smith, S. I., Ledvina, A. R. et al., Top-down protein fragmentation by infrared multiphoton dissociation in a dual pressure linear ion trap. Anal. Chem. 2009, 81, 8677-8686.
    • (2009) Anal. Chem. , vol.81 , pp. 8677-8686
    • Madsen, J.A.1    Gardner, M.W.2    Smith, S.I.3    Ledvina, A.R.4
  • 22
    • 33750971747 scopus 로고    scopus 로고
    • Top-down ESI-ECD-FT-ICR mass spectrometry localizes noncovalent protein-ligand binding sites
    • Xie, Y., Zhang, J., Yin, S., Loo, J. A., Top-down ESI-ECD-FT-ICR mass spectrometry localizes noncovalent protein-ligand binding sites. J. Am. Chem. Soc. 2006, 128, 14432-14433.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14432-14433
    • Xie, Y.1    Zhang, J.2    Yin, S.3    Loo, J.A.4
  • 23
    • 23944500826 scopus 로고    scopus 로고
    • Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)
    • Wu, S.-L., Kim, J., Hancock, W. S., Karger, B., Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR). J. Proteome Res. 2005, 4, 1155-1170.
    • (2005) J. Proteome Res. , vol.4 , pp. 1155-1170
    • Wu, S.-L.1    Kim, J.2    Hancock, W.S.3    Karger, B.4
  • 24
    • 42949113985 scopus 로고    scopus 로고
    • Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase
    • Taouatas, N., Drugan, M. M., Heck, A. J. R., Mohammed, S., Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. Nat. Methods 2008, 5, 405-407.
    • (2008) Nat. Methods , vol.5 , pp. 405-407
    • Taouatas, N.1    Drugan, M.M.2    Heck, A.J.R.3    Mohammed, S.4
  • 25
    • 84863807078 scopus 로고    scopus 로고
    • Use of proteinase K non-specific digestion for selective and comprehensive identification of interpeptide crosslinks: application to prion proteins
    • Petrotchenko, E. V., Serpa, J. J., Hardie, D. B., Berjanskii, M. et al., Use of proteinase K non-specific digestion for selective and comprehensive identification of interpeptide crosslinks: application to prion proteins. Mol. Cell Proteomics 2012, 11, M111.01352.
    • (2012) Mol. Cell Proteomics , vol.11
    • Petrotchenko, E.V.1    Serpa, J.J.2    Hardie, D.B.3    Berjanskii, M.4
  • 26
    • 0842286010 scopus 로고    scopus 로고
    • A top-down approach to protein structure studies using chemical cross-linking and Fourier transform mass spectrometry
    • Novak, P., Young, M. M., Schoeniger, J. S., Kruppa, G. H., A top-down approach to protein structure studies using chemical cross-linking and Fourier transform mass spectrometry. Eur. J. Mass Spectrom. 2003, 9, 623-631.
    • (2003) Eur. J. Mass Spectrom. , vol.9 , pp. 623-631
    • Novak, P.1    Young, M.M.2    Schoeniger, J.S.3    Kruppa, G.H.4
  • 27
    • 84864455743 scopus 로고    scopus 로고
    • A protease for "middle-down" proteomics
    • Wu, C., Tran, J. C., Zamdborg, L., Durbin, K. R. et al., A protease for "middle-down" proteomics. Nat. Methods 2012, 9, 822-824.
    • (2012) Nat. Methods , vol.9 , pp. 822-824
    • Wu, C.1    Tran, J.C.2    Zamdborg, L.3    Durbin, K.R.4
  • 28
    • 62449282062 scopus 로고    scopus 로고
    • Total chemical synthesis of proteins
    • Kent, S. B. H., Total chemical synthesis of proteins. Chem. Soc. Rev. 2009, 38, 338-3351.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 338-3351
    • Kent, S.B.H.1
  • 29
    • 58149476769 scopus 로고    scopus 로고
    • A summary of the measured pK values of the ionizable groups in folded proteins
    • Grimsley, G. R., Scholtz, J. M., Pace, C. N., A summary of the measured pK values of the ionizable groups in folded proteins. Protein Science 2009, 18, 247-251.
    • (2009) Protein Science , vol.18 , pp. 247-251
    • Grimsley, G.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 30
    • 33947488929 scopus 로고
    • The use of esters of N-hydroxysuccinimide in peptide synthesis
    • Anderson, G. W. G., Zimmerman, J. J. E., Callahan, F. M., The use of esters of N-hydroxysuccinimide in peptide synthesis. J. Am. Chem. Soc. 1964, 86, 1839-1842.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 1839-1842
    • Anderson, G.W.G.1    Zimmerman, J.J.E.2    Callahan, F.M.3
  • 33
    • 33845894960 scopus 로고    scopus 로고
    • Convenient synthesis of α-amino acid-derived cyclic amides for use as building blocks for protease inhibitors
    • Sergeev, M. E., Voyushina, T. L., Convenient synthesis of α-amino acid-derived cyclic amides for use as building blocks for protease inhibitors. Lett. Org. Chem. 2006, 3, 857-860.
    • (2006) Lett. Org. Chem. , vol.3 , pp. 857-860
    • Sergeev, M.E.1    Voyushina, T.L.2
  • 34
    • 0001224198 scopus 로고
    • A new diazoacylating reagent: preparation, structure, and use of succinimidyl diazoacetate
    • Ouihia, A., Rene, L., Guilhem, J., Pascard, C., Badet, B., A new diazoacylating reagent: preparation, structure, and use of succinimidyl diazoacetate. J. Org. Chem. 1993, 58, 1641-1642.
    • (1993) J. Org. Chem. , vol.58 , pp. 1641-1642
    • Ouihia, A.1    Rene, L.2    Guilhem, J.3    Pascard, C.4    Badet, B.5
  • 35
    • 64349120214 scopus 로고    scopus 로고
    • Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues
    • Guo, Z.-F., Sun, Y., Zheng, S., Guo, Z., Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues. Biochemistry 2009, 48, 1712-1722.
    • (2009) Biochemistry , vol.48 , pp. 1712-1722
    • Guo, Z.-F.1    Sun, Y.2    Zheng, S.3    Guo, Z.4
  • 36
    • 77249172705 scopus 로고    scopus 로고
    • Chemical delivery system of metaiodobenzylguanidine (MIBG) to the central nervous system
    • Gourand, F., Mercey, G., Ibazizène, M., Tirel, O. et al., Chemical delivery system of metaiodobenzylguanidine (MIBG) to the central nervous system. J. Med. Chem. 2010, 53, 1281-1287.
    • (2010) J. Med. Chem. , vol.53 , pp. 1281-1287
    • Gourand, F.1    Mercey, G.2    Ibazizène, M.3    Tirel, O.4
  • 37
    • 0000288638 scopus 로고
    • The reaction of imidoesters with proteins and related small molecules
    • Hunter, M. J. M., Ludwig, M. L., The reaction of imidoesters with proteins and related small molecules. J. Am. Chem. Soc. 1962, 84, 3491-3504.
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 3491-3504
    • Hunter, M.J.M.1    Ludwig, M.L.2
  • 38
    • 0008285074 scopus 로고
    • Effects of the amidination reaction on antibody activity and on the physical properties of some proteins
    • Wofsy, L., Singer, S. J., Effects of the amidination reaction on antibody activity and on the physical properties of some proteins. Biochemistry 1963, 2, 104-116.
    • (1963) Biochemistry , vol.2 , pp. 104-116
    • Wofsy, L.1    Singer, S.J.2
  • 39
    • 0021378320 scopus 로고
    • The preparation of fully N-epsilon-acetimidylated cytochrome c
    • Wallace, C. J., Harris, D. E., The preparation of fully N-epsilon-acetimidylated cytochrome c. J. Biol. Chem. 1984, 217, 589-594.
    • (1984) J. Biol. Chem. , vol.217 , pp. 589-594
    • Wallace, C.J.1    Harris, D.E.2
  • 40
    • 0001292486 scopus 로고
    • Mechanism of the reaction of imido esters with amines
    • Hand, E. S., Jencks, W. P., Mechanism of the reaction of imido esters with amines. J. Am. Chem. Soc. 1962, 84, 3505-3514.
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 3505-3514
    • Hand, E.S.1    Jencks, W.P.2
  • 41
    • 77956575647 scopus 로고    scopus 로고
    • Novel amidinating cross-linker for facilitating analyses of protein structures and interactions
    • Lauber, M. A., Reilly, J. P., Novel amidinating cross-linker for facilitating analyses of protein structures and interactions. Anal. Chem. 2010, 82, 7736-7743.
    • (2010) Anal. Chem. , vol.82 , pp. 7736-7743
    • Lauber, M.A.1    Reilly, J.P.2
  • 42
    • 77955394572 scopus 로고    scopus 로고
    • Optimization of formaldehyde cross-linking for protein interaction analysis of non-tagged integrin beta1
    • Klockenbusch, C., Kast, J., Optimization of formaldehyde cross-linking for protein interaction analysis of non-tagged integrin beta1. J. Biomed. Biotechnol. 2010, 2010, 927585.
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 927585
    • Klockenbusch, C.1    Kast, J.2
  • 43
    • 36749037222 scopus 로고    scopus 로고
    • A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9
    • Kovalenko, O. V., Yang, X. H., Hemler, M. E., A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9. Mol. Cell Proteomics 2007, 6, 1855-1867.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 1855-1867
    • Kovalenko, O.V.1    Yang, X.H.2    Hemler, M.E.3
  • 44
    • 0017112799 scopus 로고
    • N-(1-pyrene)maleimide: a fluorescent crosslinking reagent
    • Wu, C.-W., Yarbrough, L. R., Wu, F. Y. H., N-(1-pyrene)maleimide: a fluorescent crosslinking reagent. Biochemistry 1976, 15, 2863-2868.
    • (1976) Biochemistry , vol.15 , pp. 2863-2868
    • Wu, C.-W.1    Yarbrough, L.R.2    Wu, F.Y.H.3
  • 45
    • 41149141793 scopus 로고    scopus 로고
    • Efficient site-specific labeling of proteins via cysteines
    • Kim, Y., Ho, S. O., Gassman, N. R., Korlann, Y. et al., Efficient site-specific labeling of proteins via cysteines. Bioconjug. Chem. 2008, 19, 786-791.
    • (2008) Bioconjug. Chem. , vol.19 , pp. 786-791
    • Kim, Y.1    Ho, S.O.2    Gassman, N.R.3    Korlann, Y.4
  • 46
    • 0033979830 scopus 로고    scopus 로고
    • Differential reactivity of maleimide and bromoacetyl functions with thiols: application to the preparation of liposomal diepitope constructs
    • Schelté, P., Boeckler, C., Frisch, B., Schuber, F., Differential reactivity of maleimide and bromoacetyl functions with thiols: application to the preparation of liposomal diepitope constructs. Bioconjug. Chem. 2000, 11, 118-123.
    • (2000) Bioconjug. Chem. , vol.11 , pp. 118-123
    • Schelté, P.1    Boeckler, C.2    Frisch, B.3    Schuber, F.4
  • 47
    • 0025904668 scopus 로고
    • A carbohydrate-directed heterobifunctional cross-linking reagent for the synthesis of immunoconjugates
    • Zara, J. J., Wood, R. D., Boon, P., Kim, C.-H. et al., A carbohydrate-directed heterobifunctional cross-linking reagent for the synthesis of immunoconjugates. Anal. Biochem. 1991, 194, 156-162.
    • (1991) Anal. Biochem. , vol.194 , pp. 156-162
    • Zara, J.J.1    Wood, R.D.2    Boon, P.3    Kim, C.-H.4
  • 48
    • 0028360823 scopus 로고
    • A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odorless reducing agent more stable and effective than dithiothreitol
    • Han, J. C. C., Han, G. Y. Y., A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odorless reducing agent more stable and effective than dithiothreitol. Anal. Biochm. 1994, 220, 5-10.
    • (1994) Anal. Biochm. , vol.220 , pp. 5-10
    • Han, J.C.C.1    Han, G.Y.Y.2
  • 49
    • 0347134635 scopus 로고    scopus 로고
    • Thiol-reactive dyes for fluorescence labeling of proteomic samples
    • Tyagarajan, K., Pretzer, E., Wiktorowicz, J. E., Thiol-reactive dyes for fluorescence labeling of proteomic samples. Electrophoresis 2003, 24, 2348-2358.
    • (2003) Electrophoresis , vol.24 , pp. 2348-2358
    • Tyagarajan, K.1    Pretzer, E.2    Wiktorowicz, J.E.3
  • 50
    • 0037333877 scopus 로고    scopus 로고
    • The role of dicarbonyl compounds in non-enzymatic crosslinking: a structure-activity study
    • Meade, S. J., Miller, A. G., Gerrard, J. A., The role of dicarbonyl compounds in non-enzymatic crosslinking: a structure-activity study. Bioorg. Med. Chem. 2003, 11, 853-862.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 853-862
    • Meade, S.J.1    Miller, A.G.2    Gerrard, J.A.3
  • 51
    • 0033492137 scopus 로고    scopus 로고
    • Cross-linking of proteins by Maillard processes: characterization and detection of lysine-arginine cross-links derived from glyoxal and methylglyoxal
    • Lederer, M. O., Klaiber, R. G., Cross-linking of proteins by Maillard processes: characterization and detection of lysine-arginine cross-links derived from glyoxal and methylglyoxal. Bioorg. Med. Chem. 1999, 7, 2499-2507.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 2499-2507
    • Lederer, M.O.1    Klaiber, R.G.2
  • 52
    • 34250753915 scopus 로고    scopus 로고
    • Functional investigations of retroviral proteinribonucleic acid complexes by nanospray Fourier transform ion cyclotron resonance mass spectrometry
    • Fabris, D., Chaudhari, P., Hagan, N., Turner, K., Functional investigations of retroviral proteinribonucleic acid complexes by nanospray Fourier transform ion cyclotron resonance mass spectrometry. Eur. J. Mass Spectrom. 2007, 13, 29- 33.
    • (2007) Eur. J. Mass Spectrom. , vol.13 , pp. 29-33
    • Fabris, D.1    Chaudhari, P.2    Hagan, N.3    Turner, K.4
  • 53
    • 51249122849 scopus 로고    scopus 로고
    • Nested Arg-specific bifunctional crosslinkers for MS-based structural analysis of proteins and protein assemblies
    • Zhang, Q., Crosland, E., Fabris, D., Nested Arg-specific bifunctional crosslinkers for MS-based structural analysis of proteins and protein assemblies. Anal. Chim. Acta. 2008, 627, 117-128.
    • (2008) Anal. Chim. Acta. , vol.627 , pp. 117-128
    • Zhang, Q.1    Crosland, E.2    Fabris, D.3
  • 54
    • 60049084141 scopus 로고    scopus 로고
    • Intra-molecular cross-linking of acidic residues for protein structure studies
    • Novak, P., Kruppa, G. H., Intra-molecular cross-linking of acidic residues for protein structure studies. Eur. J. Mass Spectrom. 2008, 14, 355-365.
    • (2008) Eur. J. Mass Spectrom. , vol.14 , pp. 355-365
    • Novak, P.1    Kruppa, G.H.2
  • 55
    • 0035937542 scopus 로고    scopus 로고
    • Glycoprotein structure determination by mass spectrometry
    • Dell, A., Glycoprotein structure determination by mass spectrometry. Science 2001, 291, 2351-2356.
    • (2001) Science , vol.291 , pp. 2351-2356
    • Dell, A.1
  • 56
    • 0025185802 scopus 로고
    • Evaluation in vitro of adriamycin immunoconjugates synthesized using an acid-sensitive hydrazone linker
    • Greenfield, R. S., Kaneko, T., Daues, A., Edson, M. A. et al., Evaluation in vitro of adriamycin immunoconjugates synthesized using an acid-sensitive hydrazone linker. Cancer Res. 1990, 50, 6600-6607.
    • (1990) Cancer Res. , vol.50 , pp. 6600-6607
    • Greenfield, R.S.1    Kaneko, T.2    Daues, A.3    Edson, M.A.4
  • 57
    • 0024007567 scopus 로고
    • Biocytin hydrazide-a selective label for sialic acids, galactose, and other sugars in glycoconjugates using avidin-biotin technology
    • Bayer, E. A., Ben-Hur, H., Wilchek, M., Biocytin hydrazide-a selective label for sialic acids, galactose, and other sugars in glycoconjugates using avidin-biotin technology. Anal. Biochem. 1988, 170, 271-281.
    • (1988) Anal. Biochem. , vol.170 , pp. 271-281
    • Bayer, E.A.1    Ben-Hur, H.2    Wilchek, M.3
  • 58
    • 34547502435 scopus 로고    scopus 로고
    • Genetically encoding unnatural amino acids for cellular and neuronal studies
    • Wang, W., Takimoto, J. K., Louie, G. V., Baiga, T. J. et al., Genetically encoding unnatural amino acids for cellular and neuronal studies. Nat. Neurosci. 2007, 10, 1063-1072.
    • (2007) Nat. Neurosci. , vol.10 , pp. 1063-1072
    • Wang, W.1    Takimoto, J.K.2    Louie, G.V.3    Baiga, T.J.4
  • 59
    • 0038661197 scopus 로고    scopus 로고
    • A new strategy for the site-specific modification of proteins in vivo
    • Zhang, Z., Smith, B. A. C., Wang, L., Brock, A. et al., A new strategy for the site-specific modification of proteins in vivo. Biochemistry 2003, 42, 6735-6746.
    • (2003) Biochemistry , vol.42 , pp. 6735-6746
    • Zhang, Z.1    Smith, B.A.C.2    Wang, L.3    Brock, A.4
  • 60
    • 0037021352 scopus 로고    scopus 로고
    • In vivo photocrosslinking with unnatural amino acid mutagenesis
    • Chin, J. W., Schultz, P. G., In vivo photocrosslinking with unnatural amino acid mutagenesis. Chembiochem 2002, 3, 1135-1137.
    • (2002) Chembiochem , vol.3 , pp. 1135-1137
    • Chin, J.W.1    Schultz, P.G.2
  • 61
    • 0029787761 scopus 로고    scopus 로고
    • Site-specific protein modification using a ketone handle
    • Cornish, V. W., Hahn, K. M., Schultz, P. G., Site-specific protein modification using a ketone handle. J. Am. Chem. Soc. 1996, 118, 8150-8151.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8150-8151
    • Cornish, V.W.1    Hahn, K.M.2    Schultz, P.G.3
  • 62
    • 18744396951 scopus 로고    scopus 로고
    • Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid
    • Hino, N., Okazaki, Y., Kobayashi, T., Hayashi, A. et al., Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid. Nat. Methods 2005, 2, 201-206.
    • (2005) Nat. Methods , vol.2 , pp. 201-206
    • Hino, N.1    Okazaki, Y.2    Kobayashi, T.3    Hayashi, A.4
  • 63
    • 38849085321 scopus 로고    scopus 로고
    • A genetically encoded diazirine photocrosslinker in Escherichia coli
    • Tippmann, E. M., Liu, W., Summerer, D., Mack, A. V., Schultz, P. G., A genetically encoded diazirine photocrosslinker in Escherichia coli. Chembiochem 2007, 8, 2210-2214.
    • (2007) Chembiochem , vol.8 , pp. 2210-2214
    • Tippmann, E.M.1    Liu, W.2    Summerer, D.3    Mack, A.V.4    Schultz, P.G.5
  • 64
    • 0141732270 scopus 로고    scopus 로고
    • Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae
    • Deiters, A., Cropp, T. A., Mukherji, M., Chin, J. W. et al., Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae. J. Am. Chem. Soc. 2003, 125, 11782-11783.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11782-11783
    • Deiters, A.1    Cropp, T.A.2    Mukherji, M.3    Chin, J.W.4
  • 65
    • 0037036727 scopus 로고    scopus 로고
    • Addition of p-Azido-l-phenylalanine to the genetic code of Escherichia coli
    • Chin, J. W., Santoro, S. W., Martin, A. B., King, D. S. et al., Addition of p-Azido-l-phenylalanine to the genetic code of Escherichia coli. J. Am. Chem. Soc. 2002, 124, 9026-9027.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9026-9027
    • Chin, J.W.1    Santoro, S.W.2    Martin, A.B.3    King, D.S.4
  • 66
    • 0037422608 scopus 로고    scopus 로고
    • Addition of the keto functional group to the genetic code of Escherichia coli
    • Wang, L., Zhang, Z., Brock, A., Schultz, P. G., Addition of the keto functional group to the genetic code of Escherichia coli. Proc. Natl. Acad. Sci. USA 2003, 100, 56-61.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 56-61
    • Wang, L.1    Zhang, Z.2    Brock, A.3    Schultz, P.G.4
  • 67
    • 0034823319 scopus 로고    scopus 로고
    • Chemoselective approaches to glycoprotein assembly
    • Hang, H. C., Bertozzi, C. R., Chemoselective approaches to glycoprotein assembly. Acc. Chem. Res. 2001, 34, 727-736.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 727-736
    • Hang, H.C.1    Bertozzi, C.R.2
  • 69
    • 68349146256 scopus 로고    scopus 로고
    • Protein-DNA photo-crosslinking with a genetically encoded benzophenone-containing amino acid
    • Lee, H. S., Dimla, R. D., Schultz, P. G., Protein-DNA photo-crosslinking with a genetically encoded benzophenone-containing amino acid. Bioorg. Med. Chem. Lett. 2009, 19, 5222-5224.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5222-5224
    • Lee, H.S.1    Dimla, R.D.2    Schultz, P.G.3
  • 70
    • 84859874809 scopus 로고    scopus 로고
    • Probing the conformation of the ISWI ATPase domain with genetically encoded photoreactive crosslinkers and mass spectrometry
    • Forné, I., Ludwigsen, J., Imhof, A., Becker, P. B., Mueller-Planitz, F., Probing the conformation of the ISWI ATPase domain with genetically encoded photoreactive crosslinkers and mass spectrometry. Mol. Cell Proteomics 2012, 11, M111.012088.
    • (2012) Mol. Cell Proteomics , vol.11
    • Forné, I.1    Ludwigsen, J.2    Imhof, A.3    Becker, P.B.4    Mueller-Planitz, F.5
  • 72
    • 26244461164 scopus 로고    scopus 로고
    • Development and application of diazirines in biological and synthetic macromolecular systems
    • Blencowe, A., Hayes, W., Development and application of diazirines in biological and synthetic macromolecular systems. Soft Matter 2005, 1, 178-205.
    • (2005) Soft Matter , vol.1 , pp. 178-205
    • Blencowe, A.1    Hayes, W.2
  • 74
    • 0034309923 scopus 로고    scopus 로고
    • Photoactivatable reagents based on aryl(trifluoromethyl)diazirines: synthesis and application for studying nucleic acid-protein interactions
    • Korshunova, G. A., Sumbatyan, N. V., Topin, A. N., Mtchedlidze, M. T., Photoactivatable reagents based on aryl(trifluoromethyl)diazirines: synthesis and application for studying nucleic acid-protein interactions. Mol. Biol. 2000, 34, 823-839.
    • (2000) Mol. Biol. , vol.34 , pp. 823-839
    • Korshunova, G.A.1    Sumbatyan, N.V.2    Topin, A.N.3    Mtchedlidze, M.T.4
  • 75
    • 0035326345 scopus 로고    scopus 로고
    • Isotope-tagged cross-linking reagents. A new tool in mass spectrometric protein interaction analysis
    • Müller, D. R., Schindler, P., Towbin, H., Wirth, U. et al., Isotope-tagged cross-linking reagents. A new tool in mass spectrometric protein interaction analysis. Anal. Chem. 2001, 73, 1927-1934.
    • (2001) Anal. Chem. , vol.73 , pp. 1927-1934
    • Müller, D.R.1    Schindler, P.2    Towbin, H.3    Wirth, U.4
  • 76
    • 0036714166 scopus 로고    scopus 로고
    • Identification of cross-linked peptides for protein interaction studies using mass spectrometry and 18O labeling
    • Back, J. W., Notenboom, V., de Koning, L. J., Muijsers, A. O. et al., Identification of cross-linked peptides for protein interaction studies using mass spectrometry and 18O labeling. Anal. Chem. 2002, 74, 4417-4422.
    • (2002) Anal. Chem. , vol.74 , pp. 4417-4422
    • Back, J.W.1    Notenboom, V.2    de Koning, L.J.3    Muijsers, A.O.4
  • 77
    • 3242772209 scopus 로고    scopus 로고
    • Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
    • Huang, B. X., Kim, H.-Y., Dass, C., Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. J. Am. Soc. Mass Spectrom. 2004, 15, 1237-1247.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1237-1247
    • Huang, B.X.1    Kim, H.-Y.2    Dass, C.3
  • 78
    • 77954370396 scopus 로고    scopus 로고
    • Isotope signatures allow identification of chemically cross-linked peptides by mass spectrometry: a novel method to determine inter-residue distances in protein structures through cross-linking
    • Zelter, A., Hoopmann, M. R., Vernon, R., Baker, D. et al., Isotope signatures allow identification of chemically cross-linked peptides by mass spectrometry: a novel method to determine inter-residue distances in protein structures through cross-linking. J. Proteome Res. 2010, 9, 3583-3589.
    • (2010) J. Proteome Res. , vol.9 , pp. 3583-3589
    • Zelter, A.1    Hoopmann, M.R.2    Vernon, R.3    Baker, D.4
  • 79
    • 0033543508 scopus 로고    scopus 로고
    • Protein cross-links: universal isolation and characterization by isotopic derivatization and electrospray ionization mass spectrometry
    • Chen, X., Chen, Y. H., Anderson, V. E., Protein cross-links: universal isolation and characterization by isotopic derivatization and electrospray ionization mass spectrometry. Anal. Biochem. 1999, 273, 192-203.
    • (1999) Anal. Biochem. , vol.273 , pp. 192-203
    • Chen, X.1    Chen, Y.H.2    Anderson, V.E.3
  • 80
    • 76149136920 scopus 로고    scopus 로고
    • Use of a combination of isotopically coded cross-linkers and isotopically coded N-terminal modification reagents for selective identification of inter-peptide crosslinks
    • Petrotchenko, E. V., Serpa, J. J., Borchers, C. H., Use of a combination of isotopically coded cross-linkers and isotopically coded N-terminal modification reagents for selective identification of inter-peptide crosslinks. Anal. Chem. 2010, 82, 817-823.
    • (2010) Anal. Chem. , vol.82 , pp. 817-823
    • Petrotchenko, E.V.1    Serpa, J.J.2    Borchers, C.H.3
  • 81
    • 77249179311 scopus 로고    scopus 로고
    • ICC-CLASS: isotopically-coded cleavable crosslinking analysis software suite
    • Petrotchenko, E. V., Borchers, C. H., ICC-CLASS: isotopically-coded cleavable crosslinking analysis software suite. BMC Bioinformatics 2010, 11, 64.
    • (2010) BMC Bioinformatics , vol.11 , pp. 64
    • Petrotchenko, E.V.1    Borchers, C.H.2
  • 82
    • 0035564728 scopus 로고    scopus 로고
    • A new crosslinker for mass spectrometric analysis of the quaternary structure of protein complexes
    • Back, J. W., Hartog, A. F., Dekker, H. L., Muijsers, A. O. et al., A new crosslinker for mass spectrometric analysis of the quaternary structure of protein complexes. J. Am. Soc. Mass Spectrom. 2001, 12, 222-227.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 222-227
    • Back, J.W.1    Hartog, A.F.2    Dekker, H.L.3    Muijsers, A.O.4
  • 83
    • 33845310551 scopus 로고    scopus 로고
    • Collision-induced dissociative chemical cross-linking reagents and methodology: applications to protein structural characterization using tandem mass spectrometry analysis
    • Soderblom, E. J., Goshe, M. B., Collision-induced dissociative chemical cross-linking reagents and methodology: applications to protein structural characterization using tandem mass spectrometry analysis. Anal. Chem. 2006, 78, 8059-8068.
    • (2006) Anal. Chem. , vol.78 , pp. 8059-8068
    • Soderblom, E.J.1    Goshe, M.B.2
  • 84
    • 35649027426 scopus 로고    scopus 로고
    • Tandem mass spectrometry acquisition approaches to enhance identification of protein-protein interactions using low-energy collision-induced dissociative chemical crosslinking reagents
    • Soderblom, E. J., Bobay, B. G., Cavanagh, J., Goshe, M. B., Tandem mass spectrometry acquisition approaches to enhance identification of protein-protein interactions using low-energy collision-induced dissociative chemical crosslinking reagents. Rapid Commun. Mass Spectrom. 2007, 21, 3395-3408.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3395-3408
    • Soderblom, E.J.1    Bobay, B.G.2    Cavanagh, J.3    Goshe, M.B.4
  • 85
    • 77954653768 scopus 로고    scopus 로고
    • Combinatorial electrostatic collision-induced dissociative chemical cross-linking reagents for probing protein surface topology
    • Liu, F., Goshe, M. B., Combinatorial electrostatic collision-induced dissociative chemical cross-linking reagents for probing protein surface topology. Anal. Chem. 2010, 82, 6215-6223.
    • (2010) Anal. Chem. , vol.82 , pp. 6215-6223
    • Liu, F.1    Goshe, M.B.2
  • 86
    • 77957975473 scopus 로고    scopus 로고
    • Topographic studies of the GroEL-GroES chaperonin complex by chemical cross-linking using diformyl ethynylbenzene: the power of high resolution electron transfer dissociation for determination of both peptide sequences and their attachment sites
    • Trnka, M. J., Burlingame, A. L., Topographic studies of the GroEL-GroES chaperonin complex by chemical cross-linking using diformyl ethynylbenzene: the power of high resolution electron transfer dissociation for determination of both peptide sequences and their attachment sites. Mol. Cell Proteomics 2010, 9, 2306-2317.
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 2306-2317
    • Trnka, M.J.1    Burlingame, A.L.2
  • 87
    • 78651092959 scopus 로고    scopus 로고
    • Development of a novel cross-linking strategy for fast and accurate identification of cross-linked peptides of protein complexes
    • Kao, A., Chiu, C.-Li, Vellucci, D., Yang, Y. et al., Development of a novel cross-linking strategy for fast and accurate identification of cross-linked peptides of protein complexes. Mol. Cell Proteomics 2011, 10, M110.002212.
    • (2011) Mol. Cell Proteomics , vol.10
    • Kao, A.1    Chiu, C.-L.2    Vellucci, D.3    Yang, Y.4
  • 88
    • 77955856359 scopus 로고    scopus 로고
    • Chemical cross-linking with a diazirine photoactivatable cross-linker investigated by MALDI- and ESI-MS/MS
    • Gomes, A. F., Gozzo, F. C., Chemical cross-linking with a diazirine photoactivatable cross-linker investigated by MALDI- and ESI-MS/MS. J. Mass Spectrom. 2010, 45, 892-899.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 892-899
    • Gomes, A.F.1    Gozzo, F.C.2
  • 89
    • 77952536672 scopus 로고    scopus 로고
    • A new cross-linking strategy: protein interaction reporter (PIR) technology for protein-protein interaction studies
    • Tang, X., Bruce, J. E., A new cross-linking strategy: protein interaction reporter (PIR) technology for protein-protein interaction studies. Mol. Biosyst. 2010, 6, 939-947.
    • (2010) Mol. Biosyst. , vol.6 , pp. 939-947
    • Tang, X.1    Bruce, J.E.2
  • 90
    • 11844289583 scopus 로고    scopus 로고
    • Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions
    • Tang, X., Munske, G. R., Siems, W. F., Bruce, J. E., Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Anal. Chem. 2005, 77, 311-318.
    • (2005) Anal. Chem. , vol.77 , pp. 311-318
    • Tang, X.1    Munske, G.R.2    Siems, W.F.3    Bruce, J.E.4
  • 91
    • 77951870471 scopus 로고    scopus 로고
    • A photocleavable and mass spectrometry identifiable cross-linker for protein interaction studies
    • Yang, L., Tang, X., Weisbrod, C. R., Munske, G. R. et al., A photocleavable and mass spectrometry identifiable cross-linker for protein interaction studies. Anal. Chem. 2010, 82, 3556-3566.
    • (2010) Anal. Chem. , vol.82 , pp. 3556-3566
    • Yang, L.1    Tang, X.2    Weisbrod, C.R.3    Munske, G.R.4
  • 92
    • 76249127683 scopus 로고    scopus 로고
    • Collision-induced dissociative chemical cross-linking reagent for protein structure characterization: applied Edman chemistry in the gas phase
    • Dreiocker, F., Mueller, M. Q., Sinz, A., Schaefer, M. et al., Collision-induced dissociative chemical cross-linking reagent for protein structure characterization: applied Edman chemistry in the gas phase. J. Mass Spectrom. 2010, 45, 178-189.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 178-189
    • Dreiocker, F.1    Mueller, M.Q.2    Sinz, A.3    Schaefer, M.4
  • 93
    • 77955857315 scopus 로고    scopus 로고
    • Fragmentation behavior of a thiourea-based reagent for protein structure analysis by collision-induced dissociative chemical cross-linking
    • Müller, M. Q., Dreiocker, F., Ihling, C. H., Schäfer, M. et al., Fragmentation behavior of a thiourea-based reagent for protein structure analysis by collision-induced dissociative chemical cross-linking. J. Mass Spectrom. 2010, 45, 880-891.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 880-891
    • Müller, M.Q.1    Dreiocker, F.2    Ihling, C.H.3    Schäfer, M.4
  • 94
    • 77955636430 scopus 로고    scopus 로고
    • Cleavable cross-linker for protein structure analysis: reliable identification of cross-linking products by tandem MS
    • Müller, M. Q., Dreiocker, F., Ihling, C. H., Schäfer, M. et al., Cleavable cross-linker for protein structure analysis: reliable identification of cross-linking products by tandem MS. Anal. Chem. 2010, 82, 6958-6968.
    • (2010) Anal. Chem. , vol.82 , pp. 6958-6968
    • Müller, M.Q.1    Dreiocker, F.2    Ihling, C.H.3    Schäfer, M.4
  • 95
    • 78650112481 scopus 로고    scopus 로고
    • A universal matrix-assisted laser desorption/ionization cleavable cross-linker for protein structure analysis
    • Müller, M. Q., Zeiser, J. J., Dreiocker, F., Pich, A. et al., A universal matrix-assisted laser desorption/ionization cleavable cross-linker for protein structure analysis. Rapid Commun. Mass Spectrom. 2011, 25, 155-161.
    • (2011) Rapid Commun. Mass Spectrom. , vol.25 , pp. 155-161
    • Müller, M.Q.1    Zeiser, J.J.2    Dreiocker, F.3    Pich, A.4
  • 96
    • 84856283123 scopus 로고    scopus 로고
    • Quaternary diamines as mass spectrometry cleavable crosslinkers for protein interactions
    • Clifford-Nunn, B., Showalter, H. D. H., Andrews, P. C., Quaternary diamines as mass spectrometry cleavable crosslinkers for protein interactions. J. Am. Soc. Mass Spectrom. 2012, 23, 201-212.
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 201-212
    • Clifford-Nunn, B.1    Showalter, H.D.H.2    Andrews, P.C.3
  • 97
    • 46849122861 scopus 로고    scopus 로고
    • Chromogenic cross-linker for the characterization of protein structure by infrared multiphoton dissociation mass spectrometry
    • Gardner, M. W., Vasicek, L. A., Shabbir, S., Anslyn, E. V. et al., Chromogenic cross-linker for the characterization of protein structure by infrared multiphoton dissociation mass spectrometry. Anal. Chem. 2008, 80, 4807-4819.
    • (2008) Anal. Chem. , vol.80 , pp. 4807-4819
    • Gardner, M.W.1    Vasicek, L.A.2    Shabbir, S.3    Anslyn, E.V.4
  • 98
    • 24044520965 scopus 로고    scopus 로고
    • Isotopically coded cleavable cross-linker for studying protein-protein interaction and protein complexes
    • Petrotchenko, E. V., Olkhovik, V. K., Borchers, C. H., Isotopically coded cleavable cross-linker for studying protein-protein interaction and protein complexes. Mol. Cell Proteomics 2005, 4, 1167-1179.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1167-1179
    • Petrotchenko, E.V.1    Olkhovik, V.K.2    Borchers, C.H.3
  • 99
    • 61649117943 scopus 로고    scopus 로고
    • BiPS, a photocleavable, isotopically coded, fluorescent cross-linker for structural proteomics
    • Petrotchenko, E. V., Xiao, K., Cable, J., Chen, Y. et al., BiPS, a photocleavable, isotopically coded, fluorescent cross-linker for structural proteomics. Mol. Cell Proteomics 2009, 8, 273-286.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 273-286
    • Petrotchenko, E.V.1    Xiao, K.2    Cable, J.3    Chen, Y.4
  • 100
    • 77958022947 scopus 로고    scopus 로고
    • An isotopically coded CID-cleavable biotinylated cross-linker for structural proteomics
    • Petrotchenko, E. V., Serpa, J. J., Borchers, C. H., An isotopically coded CID-cleavable biotinylated cross-linker for structural proteomics. Mol. Cell Proteomics 2011, 10, M110.001420.
    • (2011) Mol. Cell Proteomics , vol.10
    • Petrotchenko, E.V.1    Serpa, J.J.2    Borchers, C.H.3
  • 101
    • 84863388262 scopus 로고    scopus 로고
    • Designer reagents for mass spectrometry-based proteomics: clickable cross-linkers for elucidation of protein structures and interactions
    • Sohn, C. H., Agnew, H. D., Lee, J. E., Sweredoski, M. J. et al., Designer reagents for mass spectrometry-based proteomics: clickable cross-linkers for elucidation of protein structures and interactions. Anal. Chem. 2012, 84, 2662-2669.
    • (2012) Anal. Chem. , vol.84 , pp. 2662-2669
    • Sohn, C.H.1    Agnew, H.D.2    Lee, J.E.3    Sweredoski, M.J.4
  • 102
    • 34547192061 scopus 로고    scopus 로고
    • Discrimination and selective enhancement of signals in the MALDI mass spectrum of a protein by combining a matrix-based label for lysine residues with a neutral matrix
    • Lascoux, D., Paramelle, D., Subra, G., Heymann, M. et al., Discrimination and selective enhancement of signals in the MALDI mass spectrum of a protein by combining a matrix-based label for lysine residues with a neutral matrix. Angew. Chem. Int. Ed. Engl. 2007, 46, 5594-5597.
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 5594-5597
    • Lascoux, D.1    Paramelle, D.2    Subra, G.3    Heymann, M.4
  • 103
  • 104
    • 73249135169 scopus 로고    scopus 로고
    • A new generation of cross-linkers for selective detection by MALDI MS
    • Paramelle, D., Cantel, S., Enjalbal, C., Amblard, M. et al., A new generation of cross-linkers for selective detection by MALDI MS. Proteomics 2009, 9, 5384-5388.
    • (2009) Proteomics , vol.9 , pp. 5384-5388
    • Paramelle, D.1    Cantel, S.2    Enjalbal, C.3    Amblard, M.4
  • 105
    • 56649088350 scopus 로고    scopus 로고
    • MSX-3D: a tool to validate 3D protein models using mass spectrometry
    • Heymann, M., Paramelle, D., Subra, G., Forest, E. et al., MSX-3D: a tool to validate 3D protein models using mass spectrometry. Bioinformatics 2008, 24, 2782-2783.
    • (2008) Bioinformatics , vol.24 , pp. 2782-2783
    • Heymann, M.1    Paramelle, D.2    Subra, G.3    Forest, E.4
  • 106
    • 66149192287 scopus 로고    scopus 로고
    • Synthesis of biotin-tagged chemical cross-linkers and their applications for mass spectrometry
    • Kang, S., Mou, L., Lanman, J., Velu, S. et al., Synthesis of biotin-tagged chemical cross-linkers and their applications for mass spectrometry. Rapid Commun. Mass Spectrom. 2009, 23, 1719-1726.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 1719-1726
    • Kang, S.1    Mou, L.2    Lanman, J.3    Velu, S.4
  • 107
    • 2442604553 scopus 로고    scopus 로고
    • Mass spectrometric detection of affinity purified crosslinked peptides
    • Hurst, G. B., Lankford, T. K., Kennel, S. J., Mass spectrometric detection of affinity purified crosslinked peptides. J. Am. Soc. Mass Spectrom. 2004, 15, 832-839.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 832-839
    • Hurst, G.B.1    Lankford, T.K.2    Kennel, S.J.3
  • 108
    • 84856708858 scopus 로고    scopus 로고
    • An integrated chemical cross-linking and mass spectrometry approach to study protein complex architecture and function
    • Luo, J., Fishburn, J., Hahn, S., Ranish, J., An integrated chemical cross-linking and mass spectrometry approach to study protein complex architecture and function. Mol. Cell Proteomics 2012, 11, M111.008318.
    • (2012) Mol. Cell Proteomics , vol.11
    • Luo, J.1    Fishburn, J.2    Hahn, S.3    Ranish, J.4
  • 109
    • 69749093506 scopus 로고    scopus 로고
    • Nonprotein based enrichment method to analyze peptide cross-linking in protein complexes
    • Yan, F., Che, F.-Y., Rykunov, D., Nieves, E. et al., Nonprotein based enrichment method to analyze peptide cross-linking in protein complexes. Anal. Chem. 2009, 81, 7149-7159.
    • (2009) Anal. Chem. , vol.81 , pp. 7149-7159
    • Yan, F.1    Che, F.-Y.2    Rykunov, D.3    Nieves, E.4
  • 110
    • 79953049446 scopus 로고    scopus 로고
    • Solid-phase cross-linking (SPCL): a new tool for protein structure studies
    • Paramelle, D., Enjalbal, C., Amblard, M., Forest, E. et al., Solid-phase cross-linking (SPCL): a new tool for protein structure studies. Proteomics 2011, 11, 1277-1286.
    • (2011) Proteomics , vol.11 , pp. 1277-1286
    • Paramelle, D.1    Enjalbal, C.2    Amblard, M.3    Forest, E.4
  • 111
    • 1542349027 scopus 로고    scopus 로고
    • Nonswelling macroporous synbeads for improved efficiency of solid-phase biotransformations
    • Basso, A., Braiuca, P., De Martin, L., Ebert, C. et al., Nonswelling macroporous synbeads for improved efficiency of solid-phase biotransformations. Chemistry 2004, 10, 1007-1013.
    • (2004) Chemistry , vol.10 , pp. 1007-1013
    • Basso, A.1    Braiuca, P.2    De Martin, L.3    Ebert, C.4
  • 112
    • 84862782006 scopus 로고    scopus 로고
    • Selective enrichment and identification of cross-linked peptides to study 3-D structures of protein complexes by mass spectrometry
    • Buncherd, H., Nessen, M. A., Nouse, N., Stelder, S. K. et al., Selective enrichment and identification of cross-linked peptides to study 3-D structures of protein complexes by mass spectrometry. J. Proteomics 2012, 75, 2205-2215.
    • (2012) J. Proteomics , vol.75 , pp. 2205-2215
    • Buncherd, H.1    Nessen, M.A.2    Nouse, N.3    Stelder, S.K.4


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