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Volumn 34, Issue , 2015, Pages 7-16

Probing allosteric mechanisms using native mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; LIGAND; PROTEIN; PROTEIN BINDING;

EID: 84929577538     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2015.05.002     Document Type: Review
Times cited : (33)

References (57)
  • 1
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., Changeux J.P. On the nature of allosteric transitions: a plausible model. J Mol Biol 1965, 12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 2
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D.E, Némethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 1966, 5:365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Némethy, G.2    Filmer, D.3
  • 3
    • 0000450916 scopus 로고
    • The oxygen equilibrium of hemoglobin and its structural interpretation
    • Pauling L. The oxygen equilibrium of hemoglobin and its structural interpretation. Proc Natl Acad Sci U S A 1935, 21:181-191.
    • (1935) Proc Natl Acad Sci U S A , vol.21 , pp. 181-191
    • Pauling, L.1
  • 4
    • 0000802595 scopus 로고
    • Heme proteins
    • Wyman J. Heme proteins. Adv Protein Chem 1948, 4:407-531.
    • (1948) Adv Protein Chem , vol.4 , pp. 407-531
    • Wyman, J.1
  • 6
    • 9944263528 scopus 로고    scopus 로고
    • Searching for new allosteric sites in enzymes
    • Hardy J.A., Wells J.A. Searching for new allosteric sites in enzymes. Curr Opin Struct Biol 2004, 14:706-715.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 706-715
    • Hardy, J.A.1    Wells, J.A.2
  • 7
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • Nussinov R., Tsai C.J. Allostery in disease and in drug discovery. Cell 2013, 153:293-305.
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.J.2
  • 9
    • 84864462749 scopus 로고    scopus 로고
    • Conformational selection or induced fit? A critical appraisal of the kinetic mechanism
    • Vogt A.D., Di Cera E. Conformational selection or induced fit? A critical appraisal of the kinetic mechanism. Biochemistry 2012, 51:5894-5902.
    • (2012) Biochemistry , vol.51 , pp. 5894-5902
    • Vogt, A.D.1    Di Cera, E.2
  • 10
    • 84917681871 scopus 로고    scopus 로고
    • Mass spectrometry quantifies protein interactions - from molecular chaperones to membrane porins
    • Hopper J.T., Robinson C.V. Mass spectrometry quantifies protein interactions - from molecular chaperones to membrane porins. Angew Chem Int Ed Engl 2014, 53:14002-14015.
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 14002-14015
    • Hopper, J.T.1    Robinson, C.V.2
  • 11
    • 84906761614 scopus 로고    scopus 로고
    • Determination of thermodynamic and kinetic properties of biomolecules by mass spectrometry
    • Gülbakan B., Barylyuk K., Zenobi R. Determination of thermodynamic and kinetic properties of biomolecules by mass spectrometry. Curr Opin Biotechnol 2015, 31:65-72.
    • (2015) Curr Opin Biotechnol , vol.31 , pp. 65-72
    • Gülbakan, B.1    Barylyuk, K.2    Zenobi, R.3
  • 12
    • 84904342151 scopus 로고    scopus 로고
    • Analytical approaches for size and mass analysis of large protein assemblies
    • Snijder J., Heck A.J. Analytical approaches for size and mass analysis of large protein assemblies. Annu Rev Anal Chem 2014, 7:43-64.
    • (2014) Annu Rev Anal Chem , vol.7 , pp. 43-64
    • Snijder, J.1    Heck, A.J.2
  • 13
    • 84896689230 scopus 로고    scopus 로고
    • Structural, evolutionary, and assembly principles of protein oligomerization
    • Levy E.D., Teichmann S.A. Structural, evolutionary, and assembly principles of protein oligomerization. Prog Mol Biol Transl Sci 2013, 117:25-51.
    • (2013) Prog Mol Biol Transl Sci , vol.117 , pp. 25-51
    • Levy, E.D.1    Teichmann, S.A.2
  • 15
    • 80054746164 scopus 로고    scopus 로고
    • αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics
    • Baldwin A.J., Lioe H., Robinson C.V., Kay L.E., Benesch J.L. αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics. J Mol Biol 2011, 413:297-309.
    • (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.5
  • 16
    • 0036277955 scopus 로고    scopus 로고
    • Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry
    • McCammon M.G., Scott D.J., Keetch C.A., Greene L.H., Purkey H.E., Petrassi H.M., Kelly J.W., Robinson C.V. Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry. Structure 2002, 10:851-863.
    • (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
  • 17
    • 84869033783 scopus 로고    scopus 로고
    • High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies
    • Rose R.J., Damoc E., Denisov E., Makarov A., Heck A.J. High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies. Nat Methods 2012, 9:1084-1086.
    • (2012) Nat Methods , vol.9 , pp. 1084-1086
    • Rose, R.J.1    Damoc, E.2    Denisov, E.3    Makarov, A.4    Heck, A.J.5
  • 19
    • 84860557228 scopus 로고    scopus 로고
    • Reliable determinations of protein-ligand interactions by direct ESI-MS measurements. Are we there yet?
    • Kitova E.N., El-Hawiet A., Schnier P.D., Klassen J.S. Reliable determinations of protein-ligand interactions by direct ESI-MS measurements. Are we there yet?. J Am Soc Mass Spectrom 2012, 23:431-441.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 431-441
    • Kitova, E.N.1    El-Hawiet, A.2    Schnier, P.D.3    Klassen, J.S.4
  • 20
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • McKay A.R., Ruotolo B.T., Ilag L.L., Robinson C.V. Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes. J Am Chem Soc 2006, 128:11433-11442.
    • (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
  • 21
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • Hernández H., Robinson C.V. Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat Protoc 2007, 2:715-726.
    • (2007) Nat Protoc , vol.2 , pp. 715-726
    • Hernández, H.1    Robinson, C.V.2
  • 22
    • 25144435539 scopus 로고    scopus 로고
    • Blackbody infrared radiative dissociation of nonspecific protein-carbohydrate complexes produced by nanoelectrospray ionization: the nature of the noncovalent interactions
    • Wang W., Kitova E.N., Sun J., Klassen J.S. Blackbody infrared radiative dissociation of nonspecific protein-carbohydrate complexes produced by nanoelectrospray ionization: the nature of the noncovalent interactions. J Am Soc Mass Spectrom 2005, 16:1583-1594.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 1583-1594
    • Wang, W.1    Kitova, E.N.2    Sun, J.3    Klassen, J.S.4
  • 23
    • 33846194221 scopus 로고    scopus 로고
    • Method for stabilizing protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • Sun J., Kitova E.N., Klassen J.S. Method for stabilizing protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal Chem 2007, 79:416-425.
    • (2007) Anal Chem , vol.79 , pp. 416-425
    • Sun, J.1    Kitova, E.N.2    Klassen, J.S.3
  • 24
    • 76749128036 scopus 로고    scopus 로고
    • Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry
    • Sun N., Soya N., Kitova E.N., Klassen J.S. Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 2010, 21:472-481.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 472-481
    • Sun, N.1    Soya, N.2    Kitova, E.N.3    Klassen, J.S.4
  • 25
    • 58249083162 scopus 로고    scopus 로고
    • How to deal with weak interactions in noncovalent complexes analyzed by electrospray mass spectrometry: cyclopeptidic inhibitors of the nuclear receptor coactivator 1-STAT6
    • Touboul D., Maillard L., Grasslin A., Moumne R., Seitz M., Robinson J., Zenobi R. How to deal with weak interactions in noncovalent complexes analyzed by electrospray mass spectrometry: cyclopeptidic inhibitors of the nuclear receptor coactivator 1-STAT6. J Am Soc Mass Spectrom 2009, 20:303-311.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 303-311
    • Touboul, D.1    Maillard, L.2    Grasslin, A.3    Moumne, R.4    Seitz, M.5    Robinson, J.6    Zenobi, R.7
  • 26
    • 33747889827 scopus 로고    scopus 로고
    • A deconvolution method for the separation of specific versus nonspecific interactions in noncovalent protein-ligand complexes analyzed by ESI-FT-ICR mass spectrometry
    • Daubenfeld T., Bouin A.P., van der Rest G. A deconvolution method for the separation of specific versus nonspecific interactions in noncovalent protein-ligand complexes analyzed by ESI-FT-ICR mass spectrometry. J Am Soc Mass Spectrom 2006, 17:1239-1248.
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 1239-1248
    • Daubenfeld, T.1    Bouin, A.P.2    van der Rest, G.3
  • 27
    • 77956604461 scopus 로고    scopus 로고
    • A method for removing effects of nonspecific binding on the distribution of binding stoichiometries: application to mass spectroscopy data
    • Shimon L., Sharon M., Horovitz A. A method for removing effects of nonspecific binding on the distribution of binding stoichiometries: application to mass spectroscopy data. Biophys J 2010, 99:1645-1649.
    • (2010) Biophys J , vol.99 , pp. 1645-1649
    • Shimon, L.1    Sharon, M.2    Horovitz, A.3
  • 28
    • 79952511159 scopus 로고    scopus 로고
    • Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
    • Liu L., Kitova E.N., Klassen J.S. Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 2011, 22:310-318.
    • (2011) J Am Soc Mass Spectrom , vol.22 , pp. 310-318
    • Liu, L.1    Kitova, E.N.2    Klassen, J.S.3
  • 30
    • 84863152207 scopus 로고    scopus 로고
    • Study on the noncovalent interactions of saikosaponins and cytochrome c by electrospray ionization mass spectrometry
    • Liu Y.Z., Su B., Wang X. Study on the noncovalent interactions of saikosaponins and cytochrome c by electrospray ionization mass spectrometry. Rapid Commun Mass Spectrom 2012, 26:719-727.
    • (2012) Rapid Commun Mass Spectrom , vol.26 , pp. 719-727
    • Liu, Y.Z.1    Su, B.2    Wang, X.3
  • 31
    • 84868260683 scopus 로고    scopus 로고
    • Quantifying protein-ligand binding constants using electrospray ionization mass spectrometry: a systematic binding affinity study of a series of hydrophobically modified trypsin inhibitors
    • Cubrilovic D., Biela A., Sielaff F., Steinmetzer T., Klebe G., Zenobi R. Quantifying protein-ligand binding constants using electrospray ionization mass spectrometry: a systematic binding affinity study of a series of hydrophobically modified trypsin inhibitors. J Am Soc Mass Spectrom 2012, 23:1768-1777.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 1768-1777
    • Cubrilovic, D.1    Biela, A.2    Sielaff, F.3    Steinmetzer, T.4    Klebe, G.5    Zenobi, R.6
  • 32
    • 84892629413 scopus 로고    scopus 로고
    • Measuring positive cooperativity using the direct ESI-MS assay. Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide
    • Lin H., Kitova E.N., Klassen J.S. Measuring positive cooperativity using the direct ESI-MS assay. Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide. J Am Soc Mass Spectrom 2014, 25:104-110.
    • (2014) J Am Soc Mass Spectrom , vol.25 , pp. 104-110
    • Lin, H.1    Kitova, E.N.2    Klassen, J.S.3
  • 33
  • 34
    • 84890859658 scopus 로고    scopus 로고
    • Subunit dynamics and nucleotide-dependent asymmetry of an AAA(+) transcription complex
    • Zhang N., Gordiyenko Y., Joly N., Lawton E., Robinson C.V., Buck M. Subunit dynamics and nucleotide-dependent asymmetry of an AAA(+) transcription complex. J Mol Biol 2014, 426:71-83.
    • (2014) J Mol Biol , vol.426 , pp. 71-83
    • Zhang, N.1    Gordiyenko, Y.2    Joly, N.3    Lawton, E.4    Robinson, C.V.5    Buck, M.6
  • 35
    • 17844378217 scopus 로고    scopus 로고
    • Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
    • Rivenzon-Segal D., Wolf S.G., Shimon L., Willison K.R., Horovitz A. Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat Struct Mol Biol 2005, 12:233-237.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 233-237
    • Rivenzon-Segal, D.1    Wolf, S.G.2    Shimon, L.3    Willison, K.R.4    Horovitz, A.5
  • 37
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
    • Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 1995, 34:5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 38
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: a second look
    • Wyman J. Linked functions and reciprocal effects in hemoglobin: a second look. Adv Protein Chem 1964, 19:223-286.
    • (1964) Adv Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1
  • 39
    • 84896933849 scopus 로고    scopus 로고
    • The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics
    • Lanucara F., Holman S.W., Gray C.J., Eyers C.E. The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics. Nat Chem 2014, 6:281-294.
    • (2014) Nat Chem , vol.6 , pp. 281-294
    • Lanucara, F.1    Holman, S.W.2    Gray, C.J.3    Eyers, C.E.4
  • 40
    • 84878106641 scopus 로고    scopus 로고
    • Native ion mobility-mass spectrometry and related methods in structural biology
    • Konijnenberg A., Butterer A., Sobott F. Native ion mobility-mass spectrometry and related methods in structural biology. Biochim Biophys Acta 2013, 1834:1239-1256.
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1239-1256
    • Konijnenberg, A.1    Butterer, A.2    Sobott, F.3
  • 41
    • 79953170596 scopus 로고    scopus 로고
    • Cyclic AMP analog blocks kinase activation by stabilizing inactive conformation: conformational selection highlights a new concept in allosteric inhibitor design
    • M110.004390
    • Badireddy S., Yunfeng G., Ritchie M., Akamine P., Wu J., Kim C.W., Taylor S.S., Qingsong L., Swaminathan K., Anand G.S. Cyclic AMP analog blocks kinase activation by stabilizing inactive conformation: conformational selection highlights a new concept in allosteric inhibitor design. Mol Cell Proteomics 2011, 10. M110.004390.
    • (2011) Mol Cell Proteomics , vol.10
    • Badireddy, S.1    Yunfeng, G.2    Ritchie, M.3    Akamine, P.4    Wu, J.5    Kim, C.W.6    Taylor, S.S.7    Qingsong, L.8    Swaminathan, K.9    Anand, G.S.10
  • 43
    • 0015514402 scopus 로고
    • Ligand-induced dimer-to-tetramer transformation in cytosine triphosphate synthetase
    • Levitzki A., Koshland D.E. Ligand-induced dimer-to-tetramer transformation in cytosine triphosphate synthetase. Biochemistry 1972, 11:247-253.
    • (1972) Biochemistry , vol.11 , pp. 247-253
    • Levitzki, A.1    Koshland, D.E.2
  • 44
    • 0031956947 scopus 로고    scopus 로고
    • Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization time-of-flight mass spectrometry
    • Ayed A., Krutchinsky A.N., Ens W., Standing K.G., Duckworth H.W. Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 1998, 12:339-344.
    • (1998) Rapid Commun Mass Spectrom , vol.12 , pp. 339-344
    • Ayed, A.1    Krutchinsky, A.N.2    Ens, W.3    Standing, K.G.4    Duckworth, H.W.5
  • 45
    • 84864395066 scopus 로고    scopus 로고
    • Mapping the road to recovery: the ClpB/Hsp104 molecular chaperone
    • Hodson S., Marshall J.J., Burston S.G. Mapping the road to recovery: the ClpB/Hsp104 molecular chaperone. J Struct Biol 2012, 179:161-171.
    • (2012) J Struct Biol , vol.179 , pp. 161-171
    • Hodson, S.1    Marshall, J.J.2    Burston, S.G.3
  • 46
    • 84876732401 scopus 로고    scopus 로고
    • Impact of quaternary structure dynamics on allosteric drug discovery
    • Jaffe E.K. Impact of quaternary structure dynamics on allosteric drug discovery. Curr Top Med Chem 2013, 13:55-63.
    • (2013) Curr Top Med Chem , vol.13 , pp. 55-63
    • Jaffe, E.K.1
  • 50
    • 84887433399 scopus 로고    scopus 로고
    • 2 complexes are the protein-folding functional form of the chaperonin nanomachine
    • 2 complexes are the protein-folding functional form of the chaperonin nanomachine. Proc Natl Acad Sci U S A 2013, 110:E4298-E4305.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E4298-E4305
    • Yang, D.1    Ye, X.2    Lorimer, G.H.3
  • 51
    • 84884560241 scopus 로고    scopus 로고
    • Dissociation of multisubunit protein-ligand complexes in the gas phase: evidence for ligand migration
    • Zhang Y., Deng L., Kitova E.N., Klassen J.S. Dissociation of multisubunit protein-ligand complexes in the gas phase: evidence for ligand migration. J Am Soc Mass Spectrom 2013, 24:1573-1583.
    • (2013) J Am Soc Mass Spectrom , vol.24 , pp. 1573-1583
    • Zhang, Y.1    Deng, L.2    Kitova, E.N.3    Klassen, J.S.4
  • 52
    • 84898915327 scopus 로고    scopus 로고
    • Surface induced dissociation: dissecting noncovalent protein complexes in the gas phase
    • Zhou M., Wysocki V.H. Surface induced dissociation: dissecting noncovalent protein complexes in the gas phase. Acc Chem Res 2014, 47:1010-1018.
    • (2014) Acc Chem Res , vol.47 , pp. 1010-1018
    • Zhou, M.1    Wysocki, V.H.2
  • 53
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui Q., Karplus M. Allostery and cooperativity revisited. Protein Sci 2008, 17:1295-1307.
    • (2008) Protein Sci , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 54
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann L., Pan J., Liu Y.H. Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem Soc Rev 2011, 40:1224-1234.
    • (2011) Chem Soc Rev , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 55
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • Takamoto K., Chance M.R. Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Annu Rev Biophys Biomol Struct 2006, 35:251-276.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 251-276
    • Takamoto, K.1    Chance, M.R.2
  • 56
    • 84907025333 scopus 로고    scopus 로고
    • A comparative cross-linking strategy to probe conformational changes in protein complexes
    • Schmidt C., Robinson C.V. A comparative cross-linking strategy to probe conformational changes in protein complexes. Nat Protoc 2014, 9:2224-2236.
    • (2014) Nat Protoc , vol.9 , pp. 2224-2236
    • Schmidt, C.1    Robinson, C.V.2


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