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Volumn 26, Issue 6, 2012, Pages 653-658

Optimizing the enrichment of cross-linked products for mass spectrometric protein analysis

Author keywords

[No Author keywords available]

Indexed keywords

BODY FLUIDS; CHROMATOGRAPHY; CROSSLINKING; MASS SPECTROMETERS; MASS SPECTROMETRY; STRUCTURAL ANALYSIS;

EID: 84857097692     PISSN: 09514198     EISSN: 10970231     Source Type: Journal    
DOI: 10.1002/rcm.6150     Document Type: Article
Times cited : (82)

References (20)
  • 1
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • B. W. Gibson, M. M. Young, N. Tang, J. C. Hempel, C. M. Oshiro, E. W. Taylor, I. D. Kuntz, G. Dollinger,. High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc. Natl. Acad. Sci. USA 2000, 97, 5802.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5802
    • Gibson, B.W.1    Young, M.M.2    Tang, N.3    Hempel, J.C.4    Oshiro, C.M.5    Taylor, E.W.6    Kuntz, I.D.7    Dollinger, G.8
  • 2
    • 0042349690 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for protein structural modeling
    • J. W. Back, L. de Jong, A. O. Muijsers, C. G. de Koster,. Chemical cross-linking and mass spectrometry for protein structural modeling. J. Mol. Biol. 2003, 331, 303.
    • (2003) J. Mol. Biol. , vol.331 , pp. 303
    • Back, J.W.1    De Jong, L.2    Muijsers, A.O.3    De Koster, C.G.4
  • 3
    • 77955865480 scopus 로고    scopus 로고
    • Elucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3D
    • D. Fabris, E. T. Yu,. Elucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3D. J. Mass Spectrom. 2010, 45, 841.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 841
    • Fabris, D.1    Yu, E.T.2
  • 4
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions
    • A. Sinz,. Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions. Mass Spectrom. Rev. 2006, 25, 663.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 663
    • Sinz, A.1
  • 5
    • 77956058146 scopus 로고    scopus 로고
    • Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry
    • A. Sinz,. Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry. Anal. Bioanal. Chem. 2010, 397, 3433.
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 3433
    • Sinz, A.1
  • 6
    • 47549096059 scopus 로고    scopus 로고
    • Mass spectrometric analysis of cross-linking sites for the structure of proteins and protein complexes
    • Y. J. Lee,. Mass spectrometric analysis of cross-linking sites for the structure of proteins and protein complexes. Mol. Biosyst. 2008, 4, 816.
    • (2008) Mol. Biosyst. , vol.4 , pp. 816
    • Lee, Y.J.1
  • 7
    • 63049119068 scopus 로고    scopus 로고
    • Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry
    • J. E. Bruce, H. Z. Zhang, X. T. Tang, G. R. Munske, N. Tolic, G. A. Anderson,. Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry. Mol. Cell. Proteomics 2009, 8, 409.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 409
    • Bruce, J.E.1    Zhang, H.Z.2    Tang, X.T.3    Munske, G.R.4    Tolic, N.5    Anderson, G.A.6
  • 8
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • J. Rappsilber,. The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes. J. Struct. Biol. 2011, 173, 530.
    • (2011) J. Struct. Biol. , vol.173 , pp. 530
    • Rappsilber, J.1
  • 9
    • 78149438179 scopus 로고    scopus 로고
    • Crosslinking combined with mass spectrometry for structural proteomics
    • C. H. Borchers, E. V. Petrotchenko,. Crosslinking combined with mass spectrometry for structural proteomics. Mass Spectrom. Rev. 2010, 29, 862.
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 862
    • Borchers, C.H.1    Petrotchenko, E.V.2
  • 10
    • 84857072011 scopus 로고    scopus 로고
    • Bioconjugate techniques - Hermanson, GT
    • A. N. Glazer,. Bioconjugate techniques-Hermanson, GT. Nature 1996, 381, 290.
    • (1996) Nature , vol.381 , pp. 290
    • Glazer, A.N.1
  • 11
    • 2342615612 scopus 로고    scopus 로고
    • Unexpected products from the reaction of the synthetic cross-linker 3,3'-dithiobis(sulfosuccinimidyl propionate), DTSSP with peptides
    • C. L. Swaim, D. L. Smith, J. B. Smith,. Unexpected products from the reaction of the synthetic cross-linker 3,3'-dithiobis(sulfosuccinimidyl propionate), DTSSP with peptides. J. Am. Soc. Mass Spectrom. 2004, 15, 736.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 736
    • Swaim, C.L.1    Smith, D.L.2    Smith, J.B.3
  • 15
    • 0041846956 scopus 로고    scopus 로고
    • MS2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides
    • B. Schilling, R. H. Row, B. W. Gibson, X. Guo, M. M. Young,. MS2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides. J. Am. Soc. Mass Spectrom. 2003, 14, 834.
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 834
    • Schilling, B.1    Row, R.H.2    Gibson, B.W.3    Guo, X.4    Young, M.M.5
  • 18
    • 79961213851 scopus 로고    scopus 로고
    • Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry
    • J. P. Reilly, M. A. Lauber,. Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry. J. Proteome Res. 2011, 10, 3604.
    • (2011) J. Proteome Res. , vol.10 , pp. 3604
    • Reilly, J.P.1    Lauber, M.A.2
  • 20
    • 10744230472 scopus 로고    scopus 로고
    • Reversible fast-dimerization of bovine serum albumin detected by fluorescence resonance energy transfer
    • V. Levi, F. L. Gonzalez Flecha,. Reversible fast-dimerization of bovine serum albumin detected by fluorescence resonance energy transfer. Biochim. Biophys. Acta 2002, 1599, 141.
    • (2002) Biochim. Biophys. Acta , vol.1599 , pp. 141
    • Levi, V.1    Gonzalez Flecha, F.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.