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Volumn , Issue 40, 2010, Pages

Analyzing large protein complexes by structural mass spectrometry

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EID: 80355140625     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/1954     Document Type: Article
Times cited : (49)

References (28)
  • 1
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts, B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92 (3), 291-294 (1998).
    • (1998) Cell , vol.92 , Issue.3 , pp. 291-294
    • Alberts, B.1
  • 2
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: Technology for structural genomics and proteomics
    • Benesch, J. L., Ruotolo, B. T., Simmons, D. A., and Robinson, C. V. Protein complexes in the gas phase: technology for structural genomics and proteomics. Chem Rev 107 (8), 3544-3567 (2007).
    • (2007) Chem Rev , vol.107 , Issue.8 , pp. 3544-3567
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 3
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • Heck, A. J. Native mass spectrometry: a bridge between interactomics and structural biology. Nat Methods 5 (11), 927-933 (2008).
    • (2008) Nat Methods , vol.5 , Issue.11 , pp. 927-933
    • Heck, A.J.1
  • 4
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon, M., and Robinson, C. V. The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu Rev Biochem 76, 167-193 (2007).
    • (2007) Annu Rev Biochem , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 5
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • Hernandez, H., and Robinson, C. V. Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat Protoc 2 (3), 715-726 (2007).
    • (2007) Nat Protoc , vol.2 , Issue.3 , pp. 715-726
    • Hernandez, H.1    Robinson, C.V.2
  • 6
    • 0029685702 scopus 로고    scopus 로고
    • Analytical properties of the nanoelectrospray ion source
    • Wilm, M., and Mann, M. Analytical properties of the nanoelectrospray ion source. Analytical Chemistry 68 (1), 1-8 (1996).
    • (1996) Analytical Chemistry , vol.68 , Issue.1 , pp. 1-8
    • Wilm, M.1    Mann, M.2
  • 7
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott, F. et al. A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal Chem 74 (6), 1402-1407 (2002).
    • (2002) Anal Chem , vol.74 , Issue.6 , pp. 1402-1407
    • Sobott, F.1
  • 8
    • 33750696329 scopus 로고    scopus 로고
    • Improving the performance of a quadrupole time-of-flight instrument for macromolecular mass spectrometry
    • van den Heuvel, R. H. et al. Improving the performance of a quadrupole time-of-flight instrument for macromolecular mass spectrometry. Anal Chem 78 (21), 7473-7483 (2006).
    • (2006) Anal Chem , vol.78 , Issue.21 , pp. 7473-7483
    • van den Heuvel, R.H.1
  • 9
    • 1542723081 scopus 로고    scopus 로고
    • Collisional cooling of large ions in electrospray mass spectrometry
    • Chernushevich, I. V., and Thomson, B. A. Collisional cooling of large ions in electrospray mass spectrometry. Anal Chem 76 (6), 1754-1760 (2004).
    • (2004) Anal Chem , vol.76 , Issue.6 , pp. 1754-1760
    • Chernushevich, I.V.1    Thomson, B.A.2
  • 10
    • 0002124332 scopus 로고    scopus 로고
    • Electrospray ionization of large multiply charged species proceeds via Dole s charged residue model
    • de la Mora, J. Electrospray ionization of large multiply charged species proceeds via Dole s charged residue model. Anal Chim Acta 406, 93-104 (2000).
    • (2000) Anal Chim Acta , vol.406 , pp. 93-104
    • de la Mora, J.1
  • 11
    • 35148867690 scopus 로고    scopus 로고
    • Optimizing macromolecular tandem mass spectrometry of large non-covalent complexes using heavy collision gases
    • Lorenzen, K. et al. Optimizing macromolecular tandem mass spectrometry of large non-covalent complexes using heavy collision gases. Int J Mass Spectrom 268, 198-206 (2007).
    • (2007) Int J Mass Spectrom , vol.268 , pp. 198-206
    • Lorenzen, K.1
  • 12
    • 61449115835 scopus 로고    scopus 로고
    • Quadrupole-time-of-flight mass spectrometer modified for higher-energy dissociation reduces protein assemblies to peptide fragments
    • Benesch, J. L. et al. Quadrupole-time-of-flight mass spectrometer modified for higher-energy dissociation reduces protein assemblies to peptide fragments. Anal Chem 81 (3), 1270-1274 (2009).
    • (2009) Anal Chem , vol.81 , Issue.3 , pp. 1270-1274
    • Benesch, J.L.1
  • 13
    • 44649150563 scopus 로고    scopus 로고
    • Subunit architecture of intact protein complexes from mass spectrometry and homology modeling
    • Taverner, T. et al. Subunit architecture of intact protein complexes from mass spectrometry and homology modeling. Acc Chem Res 41 (5), 617-627 (2008).
    • (2008) Acc Chem Res , vol.41 , Issue.5 , pp. 617-627
    • Taverner, T.1
  • 14
    • 84990671434 scopus 로고
    • The application of MaxEnt to high resolution mass spectrometry
    • Ferrige, A. G., Seddon, M. J., Skilling, J., and Ordsmith, N. The application of MaxEnt to high resolution mass spectrometry. Mass Spectrom 6, 765-770 (1992).
    • (1992) Mass Spectrom , vol.6 , pp. 765-770
    • Ferrige, A.G.1    Seddon, M.J.2    Skilling, J.3    Ordsmith, N.4
  • 15
    • 33747475197 scopus 로고    scopus 로고
    • Resolving stoichiometries and oligomeric states of glutamate synthase protein complexes with curve fitting and simulation of electrospray mass spectra
    • van Breukelen, B., Barendregt, A., Heck, A. J., and van den Heuvel, R. H. Resolving stoichiometries and oligomeric states of glutamate synthase protein complexes with curve fitting and simulation of electrospray mass spectra. Rapid Commun Mass Spectrom 20 (16), 2490-2496 (2006).
    • (2006) Rapid Commun Mass Spectrom , vol.20 , Issue.16 , pp. 2490-2496
    • van Breukelen, B.1    Barendregt, A.2    Heck, A.J.3    van den Heuvel, R.H.4
  • 16
    • 58149191374 scopus 로고    scopus 로고
    • Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality
    • Sharon, M. et al. Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality. Structure 17 (1), 31-40 (2009).
    • (2009) Structure , vol.17 , Issue.1 , pp. 31-40
    • Sharon, M.1
  • 17
    • 33744816815 scopus 로고    scopus 로고
    • Subunit architecture of multimeric complexes isolated directly from cells
    • Hernandez, H. et al. Subunit architecture of multimeric complexes isolated directly from cells. EMBO Rep 7 (6), 605-610 (2006).
    • (2006) EMBO Rep , vol.7 , Issue.6 , pp. 605-610
    • Hernandez, H.1
  • 18
    • 33751415081 scopus 로고    scopus 로고
    • Reconstruction of functional beta-propeller lectins via homo-oligomeric assembly of shorter fragments
    • Yadid, I. and Tawfik, D. S. Reconstruction of functional beta-propeller lectins via homo-oligomeric assembly of shorter fragments. J Mol Biol 365 (1), 10-17 (2007).
    • (2007) J Mol Biol , vol.365 , Issue.1 , pp. 10-17
    • Yadid, I.1    Tawfik, D.S.2
  • 19
    • 14544299737 scopus 로고    scopus 로고
    • Mass spectrometry of intact ribosomes
    • Videler, H. et al. Mass spectrometry of intact ribosomes. FEBS Lett 579 (4), 943-947 (2005).
    • (2005) FEBS Lett , vol.579 , Issue.4 , pp. 943-947
    • Videler, H.1
  • 20
    • 48249109172 scopus 로고    scopus 로고
    • High-resolution mass spectrometry of viral assemblies: Molecular composition and stability of dimorphic hepatitis B virus capsids
    • Uetrecht, C. et al. 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 (27), 9216-9220 (2008).
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.27 , pp. 9216-9220
    • Uetrecht, C.1
  • 21
    • 51649114059 scopus 로고    scopus 로고
    • Stability and shape of hepatitis B virus capsids in vacuo
    • Uetrecht, C. et al. Stability and shape of hepatitis B virus capsids in vacuo. Angew Chem Int Ed Engl 47 (33), 6247-6251 (2008).
    • (2008) Angew Chem Int Ed Engl , vol.47 , Issue.33 , pp. 6247-6251
    • Uetrecht, C.1
  • 22
    • 57249114953 scopus 로고    scopus 로고
    • Insights into virus capsid assembly from non-covalent mass spectrometry
    • Morton, V. L., Stockley, P. G., Stonehouse, N. J., and Ashcroft, A. E. Insights into virus capsid assembly from non-covalent mass spectrometry. Mass Spectrom Rev 27 (6), 575-595 (2008).
    • (2008) Mass Spectrom Rev , vol.27 , Issue.6 , pp. 575-595
    • Morton, V.L.1    Stockley, P.G.2    Stonehouse, N.J.3    Ashcroft, A.E.4
  • 23
    • 33646910002 scopus 로고    scopus 로고
    • 20S proteasomes have the potential to keep substrates in store for continual degradation
    • Sharon, M. et al. 20S proteasomes have the potential to keep substrates in store for continual degradation. J Biol Chem 281 (14), 9569-9575 (2006).
    • (2006) J Biol Chem , vol.281 , Issue.14 , pp. 9569-9575
    • Sharon, M.1
  • 24
    • 34247616673 scopus 로고    scopus 로고
    • Inter-ring communication allows the GroEL chaperonin complex to distinguish between different substrates
    • van Duijn, E., Heck, A. J., and van der Vies, S. M. Inter-ring communication allows the GroEL chaperonin complex to distinguish between different substrates. Protein Sci 16 (5), 956-965 (2007).
    • (2007) Protein Sci , vol.16 , Issue.5 , pp. 956-965
    • van Duijn, E.1    Heck, A.J.2    van der Vies, S.M.3
  • 25
    • 33646045893 scopus 로고    scopus 로고
    • Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring
    • van Duijn, E. et al. Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring. J Am Chem Soc 128 (14), 4694-4702 (2006).
    • (2006) J Am Chem Soc , vol.128 , Issue.14 , pp. 4694-4702
    • van Duijn, E.1
  • 26
    • 58149344947 scopus 로고    scopus 로고
    • Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes
    • Synowsky, S. A., van Wijk, M., Raijmakers, R., and Heck, A. J. Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes. J Mol Biol 385 (4), 1300-1313 (2009).
    • (2009) J Mol Biol , vol.385 , Issue.4 , pp. 1300-1313
    • Synowsky, S.A.1    van Wijk, M.2    Raijmakers, R.3    Heck, A.J.4
  • 27
    • 33747347236 scopus 로고    scopus 로고
    • Structural organization of the 19S proteasome lid: Insights from MS of intact complexes
    • Sharon, M. et al. Structural organization of the 19S proteasome lid: insights from MS of intact complexes. PLoS Biol 4 (8), e267 (2006).
    • (2006) PLoS Biol , vol.4 , Issue.8
    • Sharon, M.1
  • 28
    • 57449083256 scopus 로고    scopus 로고
    • Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3
    • Zhou, M. et al. Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3. Proc Natl Acad Sci U S A 105 (47), 18139-18144 (2008).
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.47 , pp. 18139-18144
    • Zhou, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.