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Volumn 19, Issue 5, 2012, Pages 599-607

Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 18.1; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

EID: 84861637257     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.04.007     Document Type: Article
Times cited : (63)

References (69)
  • 1
    • 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.P. 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
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.P.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 4
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • W.E. Balch, R.I. Morimoto, A. Dillin, and J.W. Kelly Adapting proteostasis for disease intervention Science 319 2008 916 919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 5
  • 6
    • 80054746164 scopus 로고    scopus 로고
    • αb-crystallin polydispersity is a consequence of unbiased quaternary dynamics
    • A.J. Baldwin, H. Lioe, C.V. Robinson, L.E. Kay, and J.L.P. Benesch αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics J. Mol. Biol. 413 2011 297 309
    • (2011) J. Mol. Biol. , vol.413 , pp. 297-309
    • Baldwin, A.J.1    Lioe, H.2    Robinson, C.V.3    Kay, L.E.4    Benesch, J.L.P.5
  • 7
    • 1542320089 scopus 로고    scopus 로고
    • The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions
    • E. Basha, G.J. Lee, L.A. Breci, A.C. Hausrath, N.R. Buan, K.C. Giese, and E. Vierling The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions J. Biol. Chem. 279 2004 7566 7575
    • (2004) J. Biol. Chem. , vol.279 , pp. 7566-7575
    • Basha, E.1    Lee, G.J.2    Breci, L.A.3    Hausrath, A.C.4    Buan, N.R.5    Giese, K.C.6    Vierling, E.7
  • 8
    • 84858003372 scopus 로고    scopus 로고
    • Small heat shock proteins and α-crystallins: Dynamic proteins with flexible functions
    • E. Basha, H.O. O'Neill, and E. Vierling Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions Trends Biochem. Sci. 37 2012 106 117
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 106-117
    • Basha, E.1    O'Neill, H.O.2    Vierling, E.3
  • 10
    • 60649094510 scopus 로고    scopus 로고
    • Collisional activation of protein complexes: Picking up the pieces
    • J.L.P. Benesch Collisional activation of protein complexes: picking up the pieces J. Am. Soc. Mass Spectrom. 20 2009 341 348
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 341-348
    • Benesch, J.L.P.1
  • 11
    • 80053577815 scopus 로고    scopus 로고
    • Mass spectrometry: Come of age for structural and dynamical biology
    • J.L.P. Benesch, and B.T. Ruotolo Mass spectrometry: come of age for structural and dynamical biology Curr. Opin. Struct. Biol. 21 2011 641 649
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 641-649
    • Benesch, J.L.P.1    Ruotolo, B.T.2
  • 12
    • 33745192792 scopus 로고    scopus 로고
    • Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
    • J.L.P. Benesch, J.A. Aquilina, B.T. Ruotolo, F. Sobott, and C.V. Robinson Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies Chem. Biol. 13 2006 597 605
    • (2006) Chem. Biol. , vol.13 , pp. 597-605
    • Benesch, J.L.P.1    Aquilina, J.A.2    Ruotolo, B.T.3    Sobott, F.4    Robinson, C.V.5
  • 13
    • 61449115835 scopus 로고    scopus 로고
    • Quadrupole-time-of-flight mass spectrometer modified for higher-energy dissociation reduces protein assemblies to peptide fragments
    • J.L.P. Benesch, B.T. Ruotolo, F. Sobott, J. Wildgoose, A. Gilbert, R. Bateman, and C.V. Robinson Quadrupole-time-of-flight mass spectrometer modified for higher-energy dissociation reduces protein assemblies to peptide fragments Anal. Chem. 81 2009 1270 1274
    • (2009) Anal. Chem. , vol.81 , pp. 1270-1274
    • Benesch, J.L.P.1    Ruotolo, B.T.2    Sobott, F.3    Wildgoose, J.4    Gilbert, A.5    Bateman, R.6    Robinson, C.V.7
  • 16
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • B. Bukau, J. Weissman, and A. Horwich Molecular chaperones and protein quality control Cell 125 2006 443 451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 17
    • 84861588583 scopus 로고    scopus 로고
    • Alteration of protein folding and degradation in motor neuron diseases: Implications and protective functions of small heat shock proteins
    • 10.1016/j.bbr.2011.1003.1031
    • S. Carra, V. Crippa, P. Rusmini, A. Boncoraglio, M. Minoia, E. Giorgetti, H.H. Kampinga, and A. Poletti Alteration of protein folding and degradation in motor neuron diseases: Implications and protective functions of small heat shock proteins Prog. Neurobiol. 2011 10.1016/j.bbr.2011.1003.1031
    • (2011) Prog. Neurobiol.
    • Carra, S.1    Crippa, V.2    Rusmini, P.3    Boncoraglio, A.4    Minoia, M.5    Giorgetti, E.6    Kampinga, H.H.7    Poletti, A.8
  • 18
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin: A structural and kinetic spectroscopic study
    • J.A. Carver, R.A. Lindner, C. Lyon, D. Canet, H. Hernandez, C.M. Dobson, and C. Redfield The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin: a structural and kinetic spectroscopic study J. Mol. Biol. 318 2002 815 827
    • (2002) J. Mol. Biol. , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 19
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    • A.G. Cashikar, M. Duennwald, and S.L. Lindquist A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104 J. Biol. Chem. 280 2005 23869 23875
    • (2005) J. Biol. Chem. , vol.280 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 20
    • 0242291110 scopus 로고    scopus 로고
    • Mass spectrometric analysis of DNA mixtures: Instrumental effects responsible for decreased sensitivity with increasing mass
    • X. Chen, M.S. Westphall, and L.M. Smith Mass spectrometric analysis of DNA mixtures: instrumental effects responsible for decreased sensitivity with increasing mass Anal. Chem. 75 2003 5944 5952
    • (2003) Anal. Chem. , vol.75 , pp. 5944-5952
    • Chen, X.1    Westphall, M.S.2    Smith, L.M.3
  • 21
    • 55549133282 scopus 로고    scopus 로고
    • Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry
    • G. Cheng, E. Basha, V.H. Wysocki, and E. Vierling Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry J. Biol. Chem. 283 2008 26634 26642
    • (2008) J. Biol. Chem. , vol.283 , pp. 26634-26642
    • Cheng, G.1    Basha, E.2    Wysocki, V.H.3    Vierling, E.4
  • 22
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • J.I. Clark, and P.J. Muchowski Small heat-shock proteins and their potential role in human disease Curr. Opin. Struct. Biol. 10 2000 52 59
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 52-59
    • Clark, J.I.1    Muchowski, P.J.2
  • 23
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • E. Conti, N.P. Franks, and P. Brick Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes Structure 4 1996 287 298
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 24
    • 26944453184 scopus 로고    scopus 로고
    • Small heat shock proteins in inherited peripheral neuropathies
    • I. Dierick, J. Irobi, P. De Jonghe, and V. Timmerman Small heat shock proteins in inherited peripheral neuropathies Ann. Med. 37 2005 413 422
    • (2005) Ann. Med. , vol.37 , pp. 413-422
    • Dierick, I.1    Irobi, J.2    De Jonghe, P.3    Timmerman, V.4
  • 26
    • 38649115030 scopus 로고    scopus 로고
    • Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain
    • T.M. Franzmann, P. Menhorn, S. Walter, and J. Buchner Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain Mol. Cell 29 2008 207 216
    • (2008) Mol. Cell , vol.29 , pp. 207-216
    • Franzmann, T.M.1    Menhorn, P.2    Walter, S.3    Buchner, J.4
  • 27
    • 0036534727 scopus 로고    scopus 로고
    • The ion detection efficiency of microchannel plates (MCPs)
    • G.W. Fraser The ion detection efficiency of microchannel plates (MCPs) Int. J. Mass Spectrom. 215 2002 13 30
    • (2002) Int. J. Mass Spectrom. , vol.215 , pp. 13-30
    • Fraser, G.W.1
  • 28
    • 0346463052 scopus 로고    scopus 로고
    • Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes
    • K.L. Friedrich, K.C. Giese, N.R. Buan, and E. Vierling Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes J. Biol. Chem. 279 2004 1080 1089
    • (2004) J. Biol. Chem. , vol.279 , pp. 1080-1089
    • Friedrich, K.L.1    Giese, K.C.2    Buan, N.R.3    Vierling, E.4
  • 29
    • 0028331873 scopus 로고
    • Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases
    • W.B. Gleason, Z. Fu, J. Birktoft, and L. Banaszak Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases Biochemistry 33 1994 2078 2088
    • (1994) Biochemistry , vol.33 , pp. 2078-2088
    • Gleason, W.B.1    Fu, Z.2    Birktoft, J.3    Banaszak, L.4
  • 30
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: Implications to protein folding pathways in the cell
    • Y. Gong, Y. Kakihara, N. Krogan, J. Greenblatt, A. Emili, Z. Zhang, and W.A. Houry An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell Mol. Syst. Biol. 5 2009 275
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5    Zhang, Z.6    Houry, W.A.7
  • 31
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • D.A. Haley, M.P. Bova, Q.L. Huang, H.S. Mchaourab, and P.L. Stewart Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies J. Mol. Biol. 298 2000 261 272
    • (2000) J. Mol. Biol. , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    McHaourab, H.S.4    Stewart, P.L.5
  • 32
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • F.U. Hartl, A. Bracher, and M. Hayer-Hartl Molecular chaperones in protein folding and proteostasis Nature 475 2011 324 332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 35
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • A.J. Heck Native mass spectrometry: a bridge between interactomics and structural biology Nat. Methods 5 2008 927 933
    • (2008) Nat. Methods , vol.5 , pp. 927-933
    • Heck, A.J.1
  • 36
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • H. Hernández, and C.V. Robinson Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry Nat. Protoc. 2 2007 715 726
    • (2007) Nat. Protoc. , vol.2 , pp. 715-726
    • Hernández, H.1    Robinson, C.V.2
  • 37
    • 84860772345 scopus 로고    scopus 로고
    • Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry
    • G.R. Hilton, and J.L.P. Benesch Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry J. R. Soc. Interface 9 2012 801 816
    • (2012) J. R. Soc. Interface , vol.9 , pp. 801-816
    • Hilton, G.R.1    Benesch, J.L.P.2
  • 39
    • 70349470609 scopus 로고    scopus 로고
    • Substrate binding site flexibility of the small heat shock protein molecular chaperones
    • N. Jaya, V. Garcia, and E. Vierling Substrate binding site flexibility of the small heat shock protein molecular chaperones Proc. Natl. Acad. Sci. USA 106 2009 15604 15609
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15604-15609
    • Jaya, N.1    Garcia, V.2    Vierling, E.3
  • 40
  • 41
    • 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. Hernánndez, 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    Hernánndez, H.2    Sterling, A.3    Baumert, M.4    Allen, M.H.5    Robinson, C.V.6
  • 42
    • 77957841871 scopus 로고    scopus 로고
    • Independent evolution of the core domain and its flanking sequences in small heat shock proteins
    • T. Kriehuber, T. Rattei, T. Weinmaier, A. Bepperling, M. Haslbeck, and J. Buchner Independent evolution of the core domain and its flanking sequences in small heat shock proteins FASEB J. 24 2010 3633 3642
    • (2010) FASEB J. , vol.24 , pp. 3633-3642
    • Kriehuber, T.1    Rattei, T.2    Weinmaier, T.3    Bepperling, A.4    Haslbeck, M.5    Buchner, J.6
  • 43
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 45
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • G.J. Lee, N. Pokala, and E. Vierling Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea J. Biol. Chem. 270 1995 10432 10438
    • (1995) J. Biol. Chem. , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 46
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • G.J. Lee, A.M. Roseman, H.R. Saibil, and E. Vierling A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state EMBO J. 16 1997 659 671
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 47
    • 0242354113 scopus 로고    scopus 로고
    • Shifts in peptide and protein charge state distributions with varying spray tip orifice diameter in nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry
    • Y. Li, and R.B. Cole Shifts in peptide and protein charge state distributions with varying spray tip orifice diameter in nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry Anal. Chem. 75 2003 5739 5746
    • (2003) Anal. Chem. , vol.75 , pp. 5739-5746
    • Li, Y.1    Cole, R.B.2
  • 48
    • 0035865589 scopus 로고    scopus 로고
    • The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin
    • R.A. Lindner, T.M. Treweek, and J.A. Carver The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin Biochem. J. 354 2001 79 87
    • (2001) Biochem. J. , vol.354 , pp. 79-87
    • Lindner, R.A.1    Treweek, T.M.2    Carver, J.A.3
  • 49
    • 68449102172 scopus 로고    scopus 로고
    • Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
    • J. Malmström, M. Beck, A. Schmidt, V. Lange, E.W. Deutsch, and R. Aebersold Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans Nature 460 2009 762 765
    • (2009) Nature , vol.460 , pp. 762-765
    • Malmström, J.1    Beck, M.2    Schmidt, A.3    Lange, V.4    Deutsch, E.W.5    Aebersold, R.6
  • 50
    • 66149117827 scopus 로고    scopus 로고
    • Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins
    • H.S. McHaourab, J.A. Godar, and P.L. Stewart Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins Biochemistry 48 2009 3828 3837
    • (2009) Biochemistry , vol.48 , pp. 3828-3837
    • McHaourab, H.S.1    Godar, J.A.2    Stewart, P.L.3
  • 51
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • A.R. McKay, B.T. Ruotolo, L.L. Ilag, and C.V. Robinson Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes J. Am. Chem. Soc. 128 2006 11433 11442
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11433-11442
    • McKay, A.R.1    Ruotolo, B.T.2    Ilag, L.L.3    Robinson, C.V.4
  • 52
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • A. Mogk, C. Schlieker, K.L. Friedrich, H.J. Schönfeld, E. Vierling, and B. Bukau Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK J. Biol. Chem. 278 2003 31033 31042
    • (2003) J. Biol. Chem. , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schönfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 53
    • 84857034481 scopus 로고    scopus 로고
    • Linking structural change with functional regulation-insights from mass spectrometry
    • N. Morgner, and C.V. Robinson Linking structural change with functional regulation-insights from mass spectrometry Curr. Opin. Struct. Biol. 22 2012 44 51
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 44-51
    • Morgner, N.1    Robinson, C.V.2
  • 54
    • 84858721879 scopus 로고    scopus 로고
    • Massign: An assignment strategy for maximizing information from the mass spectra of heterogeneous protein assemblies
    • N. Morgner, and C.V. Robinson Massign: an assignment strategy for maximizing information from the mass spectra of heterogeneous protein assemblies Anal. Chem. 84 2012 2939 2948
    • (2012) Anal. Chem. , vol.84 , pp. 2939-2948
    • Morgner, N.1    Robinson, C.V.2
  • 55
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 56
    • 69849105732 scopus 로고    scopus 로고
    • Subunit architecture of multiprotein assemblies determined using restraints from gas-phase measurements
    • T.L. Pukala, B.T. Ruotolo, M. Zhou, A. Politis, R. Stefanescu, J.A. Leary, and C.V. Robinson Subunit architecture of multiprotein assemblies determined using restraints from gas-phase measurements Structure 17 2009 1235 1243
    • (2009) Structure , vol.17 , pp. 1235-1243
    • Pukala, T.L.1    Ruotolo, B.T.2    Zhou, M.3    Politis, A.4    Stefanescu, R.5    Leary, J.A.6    Robinson, C.V.7
  • 57
    • 0033016166 scopus 로고    scopus 로고
    • Fatal attraction: When chaperone turns harlot
    • R. Quinlan, and P. Van Den Ijssel Fatal attraction: when chaperone turns harlot Nat. Med. 5 1999 25 26
    • (1999) Nat. Med. , vol.5 , pp. 25-26
    • Quinlan, R.1    Van Den Ijssel, P.2
  • 58
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • C.V. Robinson, A. Sali, and W. Baumeister The molecular sociology of the cell Nature 450 2007 973 982
    • (2007) Nature , vol.450 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 59
  • 60
    • 33750294048 scopus 로고    scopus 로고
    • Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry
    • A.M. Smith, T.R. Jahn, A.E. Ashcroft, and S.E. Radford Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry J. Mol. Biol. 364 2006 9 19
    • (2006) J. Mol. Biol. , vol.364 , pp. 9-19
    • Smith, A.M.1    Jahn, T.R.2    Ashcroft, A.E.3    Radford, S.E.4
  • 61
    • 77951081386 scopus 로고    scopus 로고
    • Elongated oligomers in β2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
    • D.P. Smith, S.E. Radford, and A.E. Ashcroft Elongated oligomers in β2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry Proc. Natl. Acad. Sci. USA 107 2010 6794 6798
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6794-6798
    • Smith, D.P.1    Radford, S.E.2    Ashcroft, A.E.3
  • 62
    • 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.P. 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.P.2    Vierling, E.3    Robinson, C.V.4
  • 63
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • F. Sobott, H. Hernández, 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
    • (2002) Anal. Chem. , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernández, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 65
    • 0038043235 scopus 로고    scopus 로고
    • Analysis of the interaction of small heat shock proteins with unfolding proteins
    • T. Stromer, M. Ehrnsperger, M. Gaestel, and J. Buchner Analysis of the interaction of small heat shock proteins with unfolding proteins J. Biol. Chem. 278 2003 18015 18021
    • (2003) J. Biol. Chem. , vol.278 , pp. 18015-18021
    • Stromer, T.1    Ehrnsperger, M.2    Gaestel, M.3    Buchner, J.4
  • 66
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Y. Sun, and T.H. MacRae The small heat shock proteins and their role in human disease FEBS J. 272 2005 2613 2627
    • (2005) FEBS J. , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 67
    • 33747475197 scopus 로고    scopus 로고
    • Resolving stoichiometries and oligomeric states of glutamate synthase protein complexes with curve fitting and simulation of electrospray mass spectra
    • B. van Breukelen, A. Barendregt, A.J. Heck, and R.H. van den Heuvel Resolving stoichiometries and oligomeric states of glutamate synthase protein complexes with curve fitting and simulation of electrospray mass spectra Rapid Commun. Mass Spectrom. 20 2006 2490 2496
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 2490-2496
    • Van Breukelen, B.1    Barendregt, A.2    Heck, A.J.3    Van Den Heuvel, R.H.4
  • 68
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • E.R. Waters, G.J. Lee, and E. Vierling Evolution, structure and function of the small heat shock proteins in plants J. Exp. Bot. 47 1996 325 338
    • (1996) J. Exp. Bot. , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 69
    • 34249947523 scopus 로고    scopus 로고
    • Intermolecular interactions in biomolecular systems examined by mass spectrometry
    • T. Wyttenbach, and M.T. Bowers Intermolecular interactions in biomolecular systems examined by mass spectrometry Annu. Rev. Phys. Chem. 58 2007 511 533
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 511-533
    • Wyttenbach, T.1    Bowers, M.T.2


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