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Volumn 8, Issue 5, 2004, Pages 519-526

Native protein mass spectrometry: From intact oligomers to functional machineries

Author keywords

C reactive protein; CRP; electrospray ionziation; ESI; gas phase electrophoretic molecular analysis; GEMMA; GltS; glutamate synthase; Hc; hemocyanin; HPr kinase phosphatase; HPrK P; m z; mass spectrometry; MGST1; microsomal glutathione transferase 1; MS

Indexed keywords

NANOPARTICLE; PROTEIN;

EID: 4644327652     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2004.08.006     Document Type: Review
Times cited : (271)

References (46)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • R. Aebersold, and M. Mann Mass spectrometry-based proteomics Nature 422 2003 198 207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 4
    • 0037307837 scopus 로고    scopus 로고
    • Stable isotope-coded proteomic mass spectrometry
    • M.B. Goshe, and R.D. Smith Stable isotope-coded proteomic mass spectrometry Curr Opin Biotechnol 14 2003 101 109
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 101-109
    • Goshe, M.B.1    Smith, R.D.2
  • 5
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • M. Mann, and O.N. Jensen Proteomic analysis of post-translational modifications Nat Biotechnol 21 2003 255 261
    • (2003) Nat Biotechnol , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 6
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • B. Alberts The cell as a collection of protein machines: preparing the next generation of molecular biologists Cell 92 1998 291 294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 7
    • 0034716184 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: A technology for studying noncovalent macromolecular complexes
    • J.A. Loo Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes Int J Mass Spectrom 200 2000 175 186
    • (2000) Int J Mass Spectrom , vol.200 , pp. 175-186
    • Loo, J.A.1
  • 8
    • 0037090377 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry
    • J.M. Daniel, S.D. Friess, S. Rajagopalan, S. Wendt, and R. Zenobi Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry Int J Mass Spectrom 216 2002 1 27
    • (2002) Int J Mass Spectrom , vol.216 , pp. 1-27
    • Daniel, J.M.1    Friess, S.D.2    Rajagopalan, S.3    Wendt, S.4    Zenobi, R.5
  • 9
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • A.J.R. Heck, and R.H. van den Heuvel Investigation of intact protein complexes by mass spectrometry Mass Spectrom Rev 23 2004 368 389 The most recent in-depth review about biomolecular MS that focuses on the analysis of intact proteins and protein complexes under pseudo-physiological conditions with special attention to the biophysical backgrounds in this field of research.
    • (2004) Mass Spectrom Rev , vol.23 , pp. 368-389
    • Heck, A.J.R.1    Van Den Heuvel, R.H.2
  • 10
    • 0036296745 scopus 로고    scopus 로고
    • Protein complexes take flight
    • C.V. Robinson Protein complexes take flight Nat Struct Biol 9 2002 505 506
    • (2002) Nat Struct Biol , vol.9 , pp. 505-506
    • Robinson, C.V.1
  • 12
    • 0029717657 scopus 로고    scopus 로고
    • High sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer
    • H.R. Morris, T. Paxton, A. Dell, J. Langhorne, M. Berg, R.S. Bordoli, J. Hoyes, and R.H. Bateman High sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer Rapid Commun Mass Spectrom 10 1996 889 896
    • (1996) Rapid Commun Mass Spectrom , vol.10 , pp. 889-896
    • Morris, H.R.1    Paxton, T.2    Dell, A.3    Langhorne, J.4    Berg, M.5    Bordoli, R.S.6    Hoyes, J.7    Bateman, R.H.8
  • 13
    • 0034124238 scopus 로고    scopus 로고
    • A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: Design and performance
    • A.V. Loboda, A.N. Krutchinsky, M. Bromirski, W. Ens, and K.G. Standing A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: design and performance Rapid Commun Mass Spectrom 14 2000 1047 1057
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 1047-1057
    • Loboda, A.V.1    Krutchinsky, A.N.2    Bromirski, M.3    Ens, W.4    Standing, K.G.5
  • 14
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • F. Sobott, H. Hernandez, M.G. McCammon, M.A. Tito, and C.V. Robinson A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies Anal Chem 74 2002 1402 1407 This paper reports the design and the first applications of a tandem mass spectrometer optimized for the analysis of large macromolecular assemblies.
    • (2002) Anal Chem , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 15
    • 0036277955 scopus 로고    scopus 로고
    • Screening transthyretin amyloid fibril inhibitors. Characterization of novel multiprotein, multiligand complexes by mass spectrometry
    • M.G. McCammon, D.J. Scott, C.A. Keetch, L.H. Greene, H.E. Purkey, H.M. Petrassi, J.W. Kelly, and C.V. Robinson Screening transthyretin amyloid fibril inhibitors. Characterization of novel multiprotein, multiligand complexes by mass spectrometry Structure 10 2002 851 863 Analysis of the multi-component transthyretin complex bound to retinol-binding protein with the cofactors retinol and thyroxine by tandem MS.
    • (2002) Structure , vol.10 , pp. 851-863
    • McCammon, M.G.1    Scott, D.J.2    Keetch, C.A.3    Greene, L.H.4    Purkey, H.E.5    Petrassi, H.M.6    Kelly, J.W.7    Robinson, C.V.8
  • 16
    • 0037064096 scopus 로고    scopus 로고
    • Subunit exchange of multimeric protein complexes Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray-mass spectrometry
    • F. Sobott, J.L. Benesch, E. Vierling, and C.V. Robinson Subunit exchange of multimeric protein complexes Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray-mass spectrometry J Biol Chem 277 2002 38921 38929
    • (2002) J Biol Chem , vol.277 , pp. 38921-38929
    • Sobott, F.1    Benesch, J.L.2    Vierling, E.3    Robinson, C.V.4
  • 18
    • 0035029535 scopus 로고    scopus 로고
    • The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument
    • N. Tahallah, M. Pinkse, C.S. Maier, and A.J. Heck The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument Rapid Commun Mass Spectrom 15 2001 596 601
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 596-601
    • Tahallah, N.1    Pinkse, M.2    Maier, C.S.3    Heck, A.J.4
  • 19
    • 1542723081 scopus 로고    scopus 로고
    • Collisional cooling of large ions in electrospray mass spectrometry
    • I.V. Chernushevich, and B.A. Thomson Collisional cooling of large ions in electrospray mass spectrometry Anal Chem 76 2004 1754 1760 This paper shows that an increased pressure improves collisional cooling and focusing of large ions such as the 20S proteasome. In addition, several methods to improve collisional cooling are suggested and analyzed.
    • (2004) Anal Chem , vol.76 , pp. 1754-1760
    • Chernushevich, I.V.1    Thomson, B.A.2
  • 20
    • 0034784941 scopus 로고    scopus 로고
    • Charge-reduced nano electrospray ionization combined with differential mobility analysis of peptides, proteins, glycoproteins, noncovalent protein complexes and viruses
    • G. Bacher, W.W. Szymanski, S.L. Kaufman, P. Zollner, D. Blaas, and G. Allmaier Charge-reduced nano electrospray ionization combined with differential mobility analysis of peptides, proteins, glycoproteins, noncovalent protein complexes and viruses J Mass Spectrom 36 2001 1038 1052 Alternative approach to MS to analyze large assemblies generated by electrospray in which gas-phase electrophoretic mobility molecular analysis is used to determine the molecular sizes of proteins, protein complexes and viruses.
    • (2001) J Mass Spectrom , vol.36 , pp. 1038-1052
    • Bacher, G.1    Szymanski, W.W.2    Kaufman, S.L.3    Zollner, P.4    Blaas, D.5    Allmaier, G.6
  • 21
    • 4544232304 scopus 로고    scopus 로고
    • Electrospray ionization of a whole virus: Analyzing mass, structure, and viability
    • B. Bothner, and G. Siuzdak Electrospray ionization of a whole virus: analyzing mass, structure, and viability ChemBioChem 5 2004 258 260
    • (2004) ChemBioChem , vol.5 , pp. 258-260
    • Bothner, B.1    Siuzdak, G.2
  • 23
    • 0141482197 scopus 로고    scopus 로고
    • Use of a microchip device coupled with mass spectrometry for ligand screening of a multi-protein target
    • C.A. Keetch, H. Hernanndez, A. Sterling, M. Baumert, M.H. Allen, and C.V. Robinson Use of a microchip device coupled with mass spectrometry for ligand screening of a multi-protein target Anal Chem 75 2003 4937 4941
    • (2003) Anal Chem , vol.75 , pp. 4937-4941
    • Keetch, C.A.1    Hernanndez, H.2    Sterling, A.3    Baumert, M.4    Allen, M.H.5    Robinson, C.V.6
  • 24
    • 0034282498 scopus 로고    scopus 로고
    • A fully integrated monolithic microchip electrospray device for mass spectrometry
    • G.A. Schultz, T.N. Corso, S.J. Prosser, and S. Zhang A fully integrated monolithic microchip electrospray device for mass spectrometry Anal Chem 72 2000 4058 4063
    • (2000) Anal Chem , vol.72 , pp. 4058-4063
    • Schultz, G.A.1    Corso, T.N.2    Prosser, S.J.3    Zhang, S.4
  • 25
    • 0036207578 scopus 로고    scopus 로고
    • Quadrupole time-of-flight mass spectrometry of the native hemocyanin of the deep-sea crab Bythograea thermydron
    • F. Zal, F. Chausson, E. Leize, A. Van Dorsselaer, F.H. Lallier, and B.N. Green Quadrupole time-of-flight mass spectrometry of the native hemocyanin of the deep-sea crab Bythograea thermydron Biomacromolecules 3 2002 229 231
    • (2002) Biomacromolecules , vol.3 , pp. 229-231
    • Zal, F.1    Chausson, F.2    Leize, E.3    Van Dorsselaer, A.4    Lallier, F.H.5    Green, B.N.6
  • 26
    • 0038162432 scopus 로고    scopus 로고
    • Comparative ESI-MS study of approximately 2.2 MDa native hemocyanins from deep-sea and shore crabs: From protein oligomeric state to biotope
    • S. Sanglier, E. Leize, A. Van Dorsselaer, and F. Zal Comparative ESI-MS study of approximately 2.2 MDa native hemocyanins from deep-sea and shore crabs: from protein oligomeric state to biotope J Am Soc Mass Spectrom 14 2003 419 429
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 419-429
    • Sanglier, S.1    Leize, E.2    Van Dorsselaer, A.3    Zal, F.4
  • 27
    • 0036756804 scopus 로고    scopus 로고
    • Electrospary ionizatoion mass spectrometry analysis revealed a ∼310 kDa noncovalent hexamer of HPr kinase/phosphatase from Bacillus subtilis
    • S. Sanglier, H. Ramstrom, J. Haiech, E. Leize, and A. Van Dorsselaer Electrospary ionizatoion mass spectrometry analysis revealed a ∼310 kDa noncovalent hexamer of HPr kinase/phosphatase from Bacillus subtilis Int J Mass Spectrom 219 2002 681 696
    • (2002) Int J Mass Spectrom , vol.219 , pp. 681-696
    • Sanglier, S.1    Ramstrom, H.2    Haiech, J.3    Leize, E.4    Van Dorsselaer, A.5
  • 28
    • 0037428510 scopus 로고    scopus 로고
    • Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis
    • H. Ramstrom, S. Sanglier, E. Leize-Wagner, C. Philippe, A. Van Dorsselaer, and J. Haiech Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis J Biol Chem 278 2003 1174 1185 Contribution to investigate the link between protein oligomerization and enzyme function by native MS on the bifunctional enzyme HPr kinase/phosphatase.
    • (2003) J Biol Chem , vol.278 , pp. 1174-1185
    • Ramstrom, H.1    Sanglier, S.2    Leize-Wagner, E.3    Philippe, C.4    Van Dorsselaer, A.5    Haiech, J.6
  • 29
    • 0037351309 scopus 로고    scopus 로고
    • Macromolecular assembly of Helicobacter pylori urease investigated by mass spectrometry
    • M.W. Pinkse, C.S. Maier, J.I. Kim, B.H. Oh, and A.J. Heck Macromolecular assembly of Helicobacter pylori urease investigated by mass spectrometry J Mass Spectrom 38 2003 315 320
    • (2003) J Mass Spectrom , vol.38 , pp. 315-320
    • Pinkse, M.W.1    Maier, C.S.2    Kim, J.I.3    Oh, B.H.4    Heck, A.J.5
  • 30
    • 1842728364 scopus 로고    scopus 로고
    • Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathionetransferase-1 by electrospray mass spectrometry
    • J. Lengqvist, R. Svensson, E. Evergren, R. Morgenstern, and W.J. Griffiths Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathionetransferase-1 by electrospray mass spectrometry J Biol Chem 279 2004 13311 13316 First example of the analysis of a detergent-solubilized intact oligomeric membrane protein by native ESI-MS.
    • (2004) J Biol Chem , vol.279 , pp. 13311-13316
    • Lengqvist, J.1    Svensson, R.2    Evergren, E.3    Morgenstern, R.4    Griffiths, W.J.5
  • 32
    • 0141703310 scopus 로고    scopus 로고
    • Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in alphaB-crystallin
    • J.A. Aquilina, J.L. Benesch, O.A. Bateman, C. Slingsby, and C.V. Robinson Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin Proc Natl Acad Sci USA 100 2003 10611 10616 This paper highlights the enormous potential of MS/MS to define the range and relative populations of different oligomers that constitute polydisperse assemblies even when these assemblies are not fully resolved in the mass spectra.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 33
    • 0001051186 scopus 로고
    • Observation of noncovalent complexes to the avidin tetramer by electrospray ionization mass spectrometry
    • B.L. Schwartz, K.J. Light-Wahl, and R.D. Smith Observation of noncovalent complexes to the avidin tetramer by electrospray ionization mass spectrometry J Am Chem Soc 5 1994 201 204
    • (1994) J Am Chem Soc , vol.5 , pp. 201-204
    • Schwartz, B.L.1    Light-Wahl, K.J.2    Smith, R.D.3
  • 34
    • 0035564266 scopus 로고    scopus 로고
    • Metastable ion formation and disparate charge separation in the gas-phase dissection of protein assemblies studied by orthogonal time-of-flight mass spectrometry
    • C. Versluis, A. van der Staaij, E. Stokvis, A.J. Heck, and B. de Craene Metastable ion formation and disparate charge separation in the gas-phase dissection of protein assemblies studied by orthogonal time-of-flight mass spectrometry J Am Soc Mass Spectrom 12 2001 329 336
    • (2001) J Am Soc Mass Spectrom , vol.12 , pp. 329-336
    • Versluis, C.1    Van Der Staaij, A.2    Stokvis, E.3    Heck, A.J.4    De Craene, B.5
  • 35
    • 0035476451 scopus 로고    scopus 로고
    • Thermal decomposition of a gaseous multiprotein complex studied by blackbody infrared radiative dissociation. Investigating the origin of the asymmetric dissociation behavior
    • N. Felitsyn, E.N. Kitova, and J.S. Klassen Thermal decomposition of a gaseous multiprotein complex studied by blackbody infrared radiative dissociation. Investigating the origin of the asymmetric dissociation behavior Anal Chem 73 2001 4647 4661
    • (2001) Anal Chem , vol.73 , pp. 4647-4661
    • Felitsyn, N.1    Kitova, E.N.2    Klassen, J.S.3
  • 36
    • 0346220289 scopus 로고    scopus 로고
    • Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD
    • U. Kirchner, A.H. Westphal, R. Muller, and W.J. van Berkel Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD J Biol Chem 278 2003 47545 47553
    • (2003) J Biol Chem , vol.278 , pp. 47545-47553
    • Kirchner, U.1    Westphal, A.H.2    Muller, R.3    Van Berkel, W.J.4
  • 37
    • 1842424838 scopus 로고    scopus 로고
    • Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action
    • R.H. van den Heuvel, A.H. Westphal, A.J. Heck, M.A. Walsh, S. Rovida, W.J. van Berkel, and A. Mattevi Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action J Biol Chem 279 2004 12860 12867
    • (2004) J Biol Chem , vol.279 , pp. 12860-12867
    • Van Den Heuvel, R.H.1    Westphal, A.H.2    Heck, A.J.3    Walsh, M.A.4    Rovida, S.5    Van Berkel, W.J.6    Mattevi, A.7
  • 38
    • 0037183992 scopus 로고    scopus 로고
    • Cofactor-dependent assembly of the flavoenzyme vanillyl-alcohol oxidase
    • N. Tahallah, R.H. Van Den Heuvel, W.A. Van Den Berg, C.S. Maier, W.J. Van Berkel, and A.J. Heck Cofactor-dependent assembly of the flavoenzyme vanillyl-alcohol oxidase J Biol Chem 277 2002 36425 36432 This paper reports on the cooperativity of cofactor binding and oligomerization of the large octameric protein VAO by using wild-type enzyme and a point-mutated variant.
    • (2002) J Biol Chem , vol.277 , pp. 36425-36432
    • Tahallah, N.1    Van Den Heuvel, R.H.2    Van Den Berg, W.A.3    Maier, C.S.4    Van Berkel, W.J.5    Heck, A.J.6
  • 39
    • 0034103427 scopus 로고    scopus 로고
    • Detection of intact megaDalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry
    • W.J. van Berkel, R.H. van den Heuvel, C. Versluis, and A.J. Heck Detection of intact megaDalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry Protein Sci 9 2000 435 439
    • (2000) Protein Sci , vol.9 , pp. 435-439
    • Van Berkel, W.J.1    Van Den Heuvel, R.H.2    Versluis, C.3    Heck, A.J.4
  • 40
    • 0142200478 scopus 로고    scopus 로고
    • Investigating interactions of the pentraxins serum amyloid P component and C-reactive protein by mass spectrometry
    • J.A. Aquilina, and C.V. Robinson Investigating interactions of the pentraxins serum amyloid P component and C-reactive protein by mass spectrometry Biochem J 375 2003 323 328
    • (2003) Biochem J , vol.375 , pp. 323-328
    • Aquilina, J.A.1    Robinson, C.V.2
  • 41
    • 1242351231 scopus 로고    scopus 로고
    • Mass spectrometry of Escherichia coli RNA polymerase: Interactions of the core enzyme with sigma70 and Rsd protein
    • L.L. Ilag, L.F. Westblade, C. Deshayes, A. Kolb, S.J. Busby, and C.V. Robinson Mass spectrometry of Escherichia coli RNA polymerase: interactions of the core enzyme with sigma70 and Rsd protein Structure 12 2004 269 275 Application of native ESI-MS to study the heterogeneous assembly of RNA polymerase and the interactions of core-RNA polymerase with factor σ70 and its regulator Rsd.
    • (2004) Structure , vol.12 , pp. 269-275
    • Ilag, L.L.1    Westblade, L.F.2    Deshayes, C.3    Kolb, A.4    Busby, S.J.5    Robinson, C.V.6
  • 45
    • 0037428392 scopus 로고    scopus 로고
    • Dissociation of intact Escherichia coli ribosomes in a mass spectrometer. Evidence for conformational change in a ribosome elongation factor G complex
    • C.L. Hanson, P. Fucini, L.L. Ilag, K.H. Nierhaus, and C.V. Robinson Dissociation of intact Escherichia coli ribosomes in a mass spectrometer. Evidence for conformational change in a ribosome elongation factor G complex J Biol Chem 278 2003 1259 1267 Investigation of factors, such as pH of solution and the presence of cofactors, that govern dissociation of proteins from ribosomes in the mass spectrometer and application of these data to probe conformational changes in ribosome complexes.
    • (2003) J Biol Chem , vol.278 , pp. 1259-1267
    • Hanson, C.L.1    Fucini, P.2    Ilag, L.L.3    Nierhaus, K.H.4    Robinson, C.V.5
  • 46
    • 2442527851 scopus 로고    scopus 로고
    • Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP
    • M.G. McCammon, H. Hernandez, F. Sobott, and C.V. Robinson Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP J Am Chem Soc 126 2004 5950 5951
    • (2004) J Am Chem Soc , vol.126 , pp. 5950-5951
    • McCammon, M.G.1    Hernandez, H.2    Sobott, F.3    Robinson, C.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.