메뉴 건너뛰기




Volumn 17, Issue 5, 2013, Pages 809-817

Ion mobility-mass spectrometry of intact protein-ligand complexes for pharmaceutical drug discovery and development

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; LIGAND; MOLECULAR SCAFFOLD; MONOCYTE CHEMOTACTIC PROTEIN 1; PROTEIN;

EID: 84887151962     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2013.06.019     Document Type: Review
Times cited : (71)

References (93)
  • 1
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: methods and applications
    • Kitchen D.B., Decornez H., Furr J.R., Bajorath J. Docking and scoring in virtual screening for drug discovery: methods and applications. Nat Rev Drug Discov 2004, 3:935-949.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Furr, J.R.3    Bajorath, J.4
  • 2
    • 4644335402 scopus 로고    scopus 로고
    • Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine
    • Weston A.D., Hood L. Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine. J Proteome Res 2004, 3:179-196.
    • (2004) J Proteome Res , vol.3 , pp. 179-196
    • Weston, A.D.1    Hood, L.2
  • 3
    • 18344396306 scopus 로고    scopus 로고
    • Biochemical applications of mass spectrometry in pharmaceutical drug discovery
    • Geoghegan K.F., Kelly M.A. Biochemical applications of mass spectrometry in pharmaceutical drug discovery. Mass Spectrom Rev 2005, 24:347-366.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 347-366
    • Geoghegan, K.F.1    Kelly, M.A.2
  • 5
    • 9644302954 scopus 로고    scopus 로고
    • A general technique to rank protein-ligand binding affinities and determine allosteric versus direct binding site competition in compound mixtures
    • Annis D.A., Nazef N., Chuang C.-C., Scott M.P., Nash H.M. A general technique to rank protein-ligand binding affinities and determine allosteric versus direct binding site competition in compound mixtures. J Am Chem Soc 2004, 126:15495-15503.
    • (2004) J Am Chem Soc , vol.126 , pp. 15495-15503
    • Annis, D.A.1    Nazef, N.2    Chuang, C.-C.3    Scott, M.P.4    Nash, H.M.5
  • 6
    • 0041317054 scopus 로고    scopus 로고
    • Electrospray wings for molecular elephants (Nobel lecture)
    • Fenn J.B. Electrospray wings for molecular elephants (Nobel lecture). Angew Chem Int Ed 2003, 42:3871-3894.
    • (2003) Angew Chem Int Ed , vol.42 , pp. 3871-3894
    • Fenn, J.B.1
  • 7
    • 47249124173 scopus 로고    scopus 로고
    • A multi-angular mass spectrometric view at cyclic nucleotide dependent protein kinases: in vivo characterization and structure/function relationships
    • Scholten A., Aye T.T., Heck A.J. A multi-angular mass spectrometric view at cyclic nucleotide dependent protein kinases: in vivo characterization and structure/function relationships. Mass Spectrom Rev 2008, 27:331-353.
    • (2008) Mass Spectrom Rev , vol.27 , pp. 331-353
    • Scholten, A.1    Aye, T.T.2    Heck, A.J.3
  • 9
    • 2542530042 scopus 로고    scopus 로고
    • The PDBbind database: collection of binding affinities for protein-ligand complexes with known three-dimensional structures
    • Wang R., Fang X., Lu Y., Wang S. The PDBbind database: collection of binding affinities for protein-ligand complexes with known three-dimensional structures. J Med Chem 2004, 47:2977-2980.
    • (2004) J Med Chem , vol.47 , pp. 2977-2980
    • Wang, R.1    Fang, X.2    Lu, Y.3    Wang, S.4
  • 10
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: the long and uncertain path to clinical utility
    • Rifai N., Gillette M.A., Carr S.A. Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat Biotechnol 2006, 24:971-983.
    • (2006) Nat Biotechnol , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 11
    • 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., Robinson C.V. Protein complexes in the gas phase: technology for structural genomics and proteomics. Chem Rev 2007, 107:3544-3567.
    • (2007) Chem Rev , vol.107 , pp. 3544-3567
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 12
    • 0001413545 scopus 로고
    • Detection of noncovalent receptor ligand complexes by mass spectrometry
    • Ganem B., Li Y.T., Henion J.D. Detection of noncovalent receptor ligand complexes by mass spectrometry. J Am Chem Soc 1991, 113:6294-6296.
    • (1991) J Am Chem Soc , vol.113 , pp. 6294-6296
    • Ganem, B.1    Li, Y.T.2    Henion, J.D.3
  • 13
    • 0001401150 scopus 로고
    • Observation of the heme globin complex in native myoglobin by electrospray-ionization mass spectrometry
    • Katta V., Chait B.T. Observation of the heme globin complex in native myoglobin by electrospray-ionization mass spectrometry. J Am Chem Soc 1991, 113:8534-8535.
    • (1991) J Am Chem Soc , vol.113 , pp. 8534-8535
    • Katta, V.1    Chait, B.T.2
  • 14
    • 0036312378 scopus 로고    scopus 로고
    • Qualitative characterization of biomolecular zinc complexes by collisionally induced dissociation
    • Afonso C., Hathout Y., Fenselau C. Qualitative characterization of biomolecular zinc complexes by collisionally induced dissociation. J Mass Spectrom 2002, 37:755-759.
    • (2002) J Mass Spectrom , vol.37 , pp. 755-759
    • Afonso, C.1    Hathout, Y.2    Fenselau, C.3
  • 16
    • 35348832312 scopus 로고    scopus 로고
    • Affinity selection-mass spectrometry screening techniques for small molecule drug discovery
    • Annis D.A., Nickbarg E., Yang X., Ziebell M.R., Whitehurst C.E. Affinity selection-mass spectrometry screening techniques for small molecule drug discovery. Curr Opin Chem Biol 2007, 11:518-526.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 518-526
    • Annis, D.A.1    Nickbarg, E.2    Yang, X.3    Ziebell, M.R.4    Whitehurst, C.E.5
  • 17
    • 33745652264 scopus 로고    scopus 로고
    • Applications of ESI-MS in drug discovery: interrogation of noncovalent complexes
    • Hofstadler S.A., Sannes-Lowery K.A. Applications of ESI-MS in drug discovery: interrogation of noncovalent complexes. Nat Rev Drug Discov 2006, 5:585-595.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 585-595
    • Hofstadler, S.A.1    Sannes-Lowery, K.A.2
  • 18
    • 0141958921 scopus 로고    scopus 로고
    • Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry
    • Wang W., Kitova E.N., Klassen J.S. Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 2003, 75:4945-4955.
    • (2003) Anal Chem , vol.75 , pp. 4945-4955
    • Wang, W.1    Kitova, E.N.2    Klassen, J.S.3
  • 19
    • 77958179943 scopus 로고    scopus 로고
    • Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
    • El-Hawiet A., Kitova E.N., Liu L., Klassen J.S. Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 2010, 21:1893-1899.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1893-1899
    • El-Hawiet, A.1    Kitova, E.N.2    Liu, L.3    Klassen, J.S.4
  • 20
    • 80655131110 scopus 로고    scopus 로고
    • Thermodynamic analysis of protein-ligand interactions in complex biological mixtures using a shotgun proteomics approach
    • DeArmond P.D., Xu Y., Strickland E.C., Daniels K.G., Fitzgerald M.C. Thermodynamic analysis of protein-ligand interactions in complex biological mixtures using a shotgun proteomics approach. J Proteome Res 2011, 10:4948-4958.
    • (2011) J Proteome Res , vol.10 , pp. 4948-4958
    • DeArmond, P.D.1    Xu, Y.2    Strickland, E.C.3    Daniels, K.G.4    Fitzgerald, M.C.5
  • 21
    • 77954653768 scopus 로고    scopus 로고
    • Combinatorial electrostatic collision-induced dissociative chemical cross-linking reagents for probing protein surface topology
    • Liu F., Goshe M.B. Combinatorial electrostatic collision-induced dissociative chemical cross-linking reagents for probing protein surface topology. Anal Chem 2010, 82:6215-6223.
    • (2010) Anal Chem , vol.82 , pp. 6215-6223
    • Liu, F.1    Goshe, M.B.2
  • 22
    • 0037076525 scopus 로고    scopus 로고
    • Probing the topology of the glycine receptor by chemical modification coupled to mass spectrometry
    • Leite J.F., Cascio M. Probing the topology of the glycine receptor by chemical modification coupled to mass spectrometry. Biochemistry 2002, 41:6140-6148.
    • (2002) Biochemistry , vol.41 , pp. 6140-6148
    • Leite, J.F.1    Cascio, M.2
  • 23
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions
    • Sinz A. Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions. Mass Spectrom Rev 2006, 25:663-682.
    • (2006) Mass Spectrom Rev , vol.25 , pp. 663-682
    • Sinz, A.1
  • 24
    • 0031082985 scopus 로고    scopus 로고
    • Ion-molecule reactions as probes of gas-phase structures of peptides and proteins
    • Green M.K., Lebrilla C.B. Ion-molecule reactions as probes of gas-phase structures of peptides and proteins. Mass Spectrom Rev 1997, 16:53-71.
    • (1997) Mass Spectrom Rev , vol.16 , pp. 53-71
    • Green, M.K.1    Lebrilla, C.B.2
  • 25
    • 1442333529 scopus 로고    scopus 로고
    • Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants
    • Zhu M.M., Rempel D.L., Gross M.L. Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants. J Am Soc Mass Spectrom 2004, 15:388-397.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 388-397
    • Zhu, M.M.1    Rempel, D.L.2    Gross, M.L.3
  • 26
    • 11844258744 scopus 로고    scopus 로고
    • PLIMSTEX: a novel mass spectrometric method for the quantification of protein-ligand interactions in solution
    • Zhu M.M., Chitta R., Gross M.L. PLIMSTEX: a novel mass spectrometric method for the quantification of protein-ligand interactions in solution. Int J Mass spectrom 2005, 240:213-220.
    • (2005) Int J Mass spectrom , vol.240 , pp. 213-220
    • Zhu, M.M.1    Chitta, R.2    Gross, M.L.3
  • 31
    • 34547881888 scopus 로고    scopus 로고
    • Profiling and imaging of tissues by imaging ion mobility-mass spectrometry
    • McLean J.A., Ridenour W.B., Caprioli R.M. Profiling and imaging of tissues by imaging ion mobility-mass spectrometry. J Mass Spectrom 2007, 42:1099-1105.
    • (2007) J Mass Spectrom , vol.42 , pp. 1099-1105
    • McLean, J.A.1    Ridenour, W.B.2    Caprioli, R.M.3
  • 32
    • 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 2008, 5:927-933.
    • (2008) Nat Methods , vol.5 , pp. 927-933
    • Heck, A.J.1
  • 33
    • 84861145145 scopus 로고    scopus 로고
    • Mass spectrometry based tools to investigate protein-ligand interactions for drug discovery
    • Pacholarz K.J., Garlish R.A., Taylor R.J., Barran P.E. Mass spectrometry based tools to investigate protein-ligand interactions for drug discovery. Chem Soc Rev 2012, 41:4335-4355.
    • (2012) Chem Soc Rev , vol.41 , pp. 4335-4355
    • Pacholarz, K.J.1    Garlish, R.A.2    Taylor, R.J.3    Barran, P.E.4
  • 36
    • 84873865528 scopus 로고    scopus 로고
    • Protein structure in the gas phase: the influence of side-chain microsolvation
    • Warnke S., von Helden G., Pagel K. Protein structure in the gas phase: the influence of side-chain microsolvation. J Am Chem Soc 2013, 135:1177-1180.
    • (2013) J Am Chem Soc , vol.135 , pp. 1177-1180
    • Warnke, S.1    von Helden, G.2    Pagel, K.3
  • 40
    • 34249947523 scopus 로고    scopus 로고
    • Intermolecular interactions in biomolecular systems examined by mass spectrometry
    • Wyttenbach T., Bowers M.T. Intermolecular interactions in biomolecular systems examined by mass spectrometry. Annu Rev Phys Chem 2007, 58:511-533.
    • (2007) Annu Rev Phys Chem , vol.58 , pp. 511-533
    • Wyttenbach, T.1    Bowers, M.T.2
  • 42
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon M., Robinson C.V. The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu Rev Biochem 2007, 76:167-193.
    • (2007) Annu Rev Biochem , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 43
    • 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
    • Felitsyn N., Kitova E.N., Klassen J.S. Thermal decomposition of a gaseous multiprotein complex studied by blackbody infrared radiative dissociation, investigating the origin of the asymmetric dissociation behavior. Anal Chem 2001, 73:4647-4661.
    • (2001) Anal Chem , vol.73 , pp. 4647-4661
    • Felitsyn, N.1    Kitova, E.N.2    Klassen, J.S.3
  • 44
    • 4744373182 scopus 로고    scopus 로고
    • Further studies on the origins of asymmetric charge partitioning in protein homodimers
    • Jurchen J.C., Garcia D.E., Williams E.R. Further studies on the origins of asymmetric charge partitioning in protein homodimers. J Am Soc Mass Spectrom 2004, 15:1408-1415.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 1408-1415
    • Jurchen, J.C.1    Garcia, D.E.2    Williams, E.R.3
  • 45
    • 0037420384 scopus 로고    scopus 로고
    • Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers
    • Jurchen J.C., Williams E.R. Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers. J Am Chem Soc 2003, 125:2817-2826.
    • (2003) J Am Chem Soc , vol.125 , pp. 2817-2826
    • Jurchen, J.C.1    Williams, E.R.2
  • 46
    • 0030913630 scopus 로고    scopus 로고
    • Conformations, unfolding, and refolding of apomyoglobin in vacuum: an activation barrier for gas-phase protein folding
    • Shelimov K.B., Jarrold M.F. Conformations, unfolding, and refolding of apomyoglobin in vacuum: an activation barrier for gas-phase protein folding. J Am Chem Soc 1997, 119:2987-2994.
    • (1997) J Am Chem Soc , vol.119 , pp. 2987-2994
    • Shelimov, K.B.1    Jarrold, M.F.2
  • 47
    • 60649094510 scopus 로고    scopus 로고
    • Collisional activation of protein complexes: picking up the pieces
    • Benesch J.L. Collisional activation of protein complexes: picking up the pieces. J Am Soc Mass Spectrom 2009, 20:341-348.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 341-348
    • Benesch, J.L.1
  • 48
    • 0033620367 scopus 로고    scopus 로고
    • Thermal unfolding of unsolvated cytochrome c: experiment and molecular dynamics simulations
    • Mao Y., Woenckhaus J., Kolafa J., Ratner M.A., Jarrold M.F. Thermal unfolding of unsolvated cytochrome c: experiment and molecular dynamics simulations. J Am Chem Soc 1999, 121:2712-2721.
    • (1999) J Am Chem Soc , vol.121 , pp. 2712-2721
    • Mao, Y.1    Woenckhaus, J.2    Kolafa, J.3    Ratner, M.A.4    Jarrold, M.F.5
  • 52
    • 84878105806 scopus 로고    scopus 로고
    • Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly
    • Woods L., Radford S., Ashcroft A. Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly. Biochim Biophys Acta (BBA)-Prot Proteom 2012, 1834:1257-1268.
    • (2012) Biochim Biophys Acta (BBA)-Prot Proteom , vol.1834 , pp. 1257-1268
    • Woods, L.1    Radford, S.2    Ashcroft, A.3
  • 55
    • 77957784477 scopus 로고    scopus 로고
    • Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes
    • Politis A., Park A.Y., Hyung S.-J., Barsky D., Ruotolo B.T., Robinson C.V. Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. PLoS ONE 2010, 5:e12080.
    • (2010) PLoS ONE , vol.5
    • Politis, A.1    Park, A.Y.2    Hyung, S.-J.3    Barsky, D.4    Ruotolo, B.T.5    Robinson, C.V.6
  • 57
    • 0030939178 scopus 로고    scopus 로고
    • Protein structure in vacuo: gas-phase conformations of BPTI and cytochrome c
    • Shelimov K.B., Clemmer D.E., Hudgins R.R., Jarrold M.F. Protein structure in vacuo: gas-phase conformations of BPTI and cytochrome c. J Am Chem Soc 1997, 119:2240-2248.
    • (1997) J Am Chem Soc , vol.119 , pp. 2240-2248
    • Shelimov, K.B.1    Clemmer, D.E.2    Hudgins, R.R.3    Jarrold, M.F.4
  • 58
    • 35648957210 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes
    • Ruotolo B.T., Hyung S.J., Robinson P.M., Giles K., Bateman R.H., Robinson C.V. Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes. Angew Chem Int Ed 2007, 46:8001-8004.
    • (2007) Angew Chem Int Ed , vol.46 , pp. 8001-8004
    • Ruotolo, B.T.1    Hyung, S.J.2    Robinson, P.M.3    Giles, K.4    Bateman, R.H.5    Robinson, C.V.6
  • 59
    • 64749105610 scopus 로고    scopus 로고
    • Gas-phase unfolding and disassembly reveals stability differences in ligand-bound multiprotein complexes
    • Hyung S.-J., Robinson C.V., Ruotolo B.T. Gas-phase unfolding and disassembly reveals stability differences in ligand-bound multiprotein complexes. Chem Biol 2009, 16:382-390.
    • (2009) Chem Biol , vol.16 , pp. 382-390
    • Hyung, S.-J.1    Robinson, C.V.2    Ruotolo, B.T.3
  • 60
    • 70349108740 scopus 로고    scopus 로고
    • Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: the effect of ligand binding on conformational stability
    • Hopper J.T., Oldham N.J. Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: the effect of ligand binding on conformational stability. J Am Soc Mass Spectrom 2009, 20:1851-1858.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 1851-1858
    • Hopper, J.T.1    Oldham, N.J.2
  • 61
    • 84882242085 scopus 로고    scopus 로고
    • Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase
    • Han L., Hyung S.J., Ruotolo B.T. Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase. Angew Chem Int Ed 2012, 124:5790-5793.
    • (2012) Angew Chem Int Ed , vol.124 , pp. 5790-5793
    • Han, L.1    Hyung, S.J.2    Ruotolo, B.T.3
  • 62
    • 79960579141 scopus 로고    scopus 로고
    • Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent
    • Han L., Hyung S.-J., Mayers J.J., Ruotolo B.T. Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent. J Am Chem Soc 2011, 133:11358-11367.
    • (2011) J Am Chem Soc , vol.133 , pp. 11358-11367
    • Han, L.1    Hyung, S.-J.2    Mayers, J.J.3    Ruotolo, B.T.4
  • 63
    • 84874521109 scopus 로고    scopus 로고
    • Traveling-wave ion mobility-mass spectrometry reveals additional mechanistic details in the stabilization of protein complex ions through tuned salt additives
    • Han L., Ruotolo B.T. Traveling-wave ion mobility-mass spectrometry reveals additional mechanistic details in the stabilization of protein complex ions through tuned salt additives. Int J Ion Mobil Spectrom 2013, 1-10.
    • (2013) Int J Ion Mobil Spectrom , pp. 1-10
    • Han, L.1    Ruotolo, B.T.2
  • 64
    • 0030810477 scopus 로고    scopus 로고
    • Collision-induced dissociation threshold energies of protonated glycine, glycinamide, and some related small peptides and peptide amino amides
    • Klassen J.S., Kebarle P. Collision-induced dissociation threshold energies of protonated glycine, glycinamide, and some related small peptides and peptide amino amides. J Am Chem Soc 1997, 119:6552-6563.
    • (1997) J Am Chem Soc , vol.119 , pp. 6552-6563
    • Klassen, J.S.1    Kebarle, P.2
  • 65
    • 0035894045 scopus 로고    scopus 로고
    • Monitoring structural changes of proteins in an ion trap over ~10-200ms: unfolding transitions in cytochrome c ions
    • Badman E.R., Hoaglund-Hyzer C.S., Clemmer D.E. Monitoring structural changes of proteins in an ion trap over ~10-200ms: unfolding transitions in cytochrome c ions. Anal Chem 2001, 73:6000-6007.
    • (2001) Anal Chem , vol.73 , pp. 6000-6007
    • Badman, E.R.1    Hoaglund-Hyzer, C.S.2    Clemmer, D.E.3
  • 66
    • 84860170318 scopus 로고    scopus 로고
    • Protein subunits released by surface collisions of noncovalent complexes: nativelike compact structures revealed by ion mobility mass spectrometry
    • Zhou M., Dagan S., Wysocki V.H. Protein subunits released by surface collisions of noncovalent complexes: nativelike compact structures revealed by ion mobility mass spectrometry. Angew Chem Int Ed 2012, 51:4336-4339.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 4336-4339
    • Zhou, M.1    Dagan, S.2    Wysocki, V.H.3
  • 67
    • 84873664528 scopus 로고    scopus 로고
    • Impact of charge state on gas-phase behaviors of noncovalent protein complexes in collision induced dissociation and surface induced dissociation
    • Zhou M., Dagan S., Wysocki V.H. Impact of charge state on gas-phase behaviors of noncovalent protein complexes in collision induced dissociation and surface induced dissociation. Analyst 2013, 138:1353-1362.
    • (2013) Analyst , vol.138 , pp. 1353-1362
    • Zhou, M.1    Dagan, S.2    Wysocki, V.H.3
  • 68
    • 33748572634 scopus 로고    scopus 로고
    • Aspects of native proteins are retained in vacuum
    • Ruotolo B.T., Robinson C.V. Aspects of native proteins are retained in vacuum. Curr Opin Chem Biol 2006, 10:402-408.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 402-408
    • Ruotolo, B.T.1    Robinson, C.V.2
  • 69
    • 79251613176 scopus 로고    scopus 로고
    • Interrogating viral capsid assembly with ion mobility-mass spectrometry
    • Uetrecht C., Barbu I.M., Shoemaker G.K., van Duijn E., Heck A.J. Interrogating viral capsid assembly with ion mobility-mass spectrometry. Nat Chem 2010, 3:126-132.
    • (2010) Nat Chem , vol.3 , pp. 126-132
    • Uetrecht, C.1    Barbu, I.M.2    Shoemaker, G.K.3    van Duijn, E.4    Heck, A.J.5
  • 70
  • 71
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo J.A. Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom Rev 1997, 16:1-23.
    • (1997) Mass Spectrom Rev , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 72
    • 80053577815 scopus 로고    scopus 로고
    • Mass spectrometry: come of age for structural and dynamical biology
    • Benesch J.L., Ruotolo B.T. Mass spectrometry: come of age for structural and dynamical biology. Curr Opin Struct Biol 2011, 21:641-649.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 641-649
    • Benesch, J.L.1    Ruotolo, B.T.2
  • 73
    • 1442324456 scopus 로고    scopus 로고
    • Influence of basic residue content on fragment ion peak intensities in low-energy collision-induced dissociation spectra of peptides
    • Tabb D.L., Huang Y., Wysocki V.H., Yates J.R. Influence of basic residue content on fragment ion peak intensities in low-energy collision-induced dissociation spectra of peptides. Anal Chem 2004, 76:1243-1248.
    • (2004) Anal Chem , vol.76 , pp. 1243-1248
    • Tabb, D.L.1    Huang, Y.2    Wysocki, V.H.3    Yates, J.R.4
  • 74
    • 70349741035 scopus 로고    scopus 로고
    • An ion mobility-mass spectrometry investigation of monocyte chemoattractant protein-1
    • Schenauer M.R., Leary J.A. An ion mobility-mass spectrometry investigation of monocyte chemoattractant protein-1. Int J Mass Spectrom 2009, 287:70-76.
    • (2009) Int J Mass Spectrom , vol.287 , pp. 70-76
    • Schenauer, M.R.1    Leary, J.A.2
  • 76
    • 0001697163 scopus 로고
    • Protein-carbohydrate interaction: 2. Inhibiton studies on interaction of concanavalin A with polysaccharides
    • Goldstei I.j., Hollerma C.e., Smith E.E. Protein-carbohydrate interaction: 2. Inhibiton studies on interaction of concanavalin A with polysaccharides. Biochemistry 1965, 4:876-882.
    • (1965) Biochemistry , vol.4 , pp. 876-882
    • Goldstei, I.1    Hollerma, C.2    Smith, E.E.3
  • 77
    • 75649146242 scopus 로고    scopus 로고
    • The effect of calcium ions and peptide ligands on the relative stabilities of the calmodulin dumbbell and compact structures
    • Wyttenbach T., Grabenauer M., Thalassinos K., Scrivens J.H., Bowers M.T. The effect of calcium ions and peptide ligands on the relative stabilities of the calmodulin dumbbell and compact structures. J Phys Chem B 2009, 114:437-447.
    • (2009) J Phys Chem B , vol.114 , pp. 437-447
    • Wyttenbach, T.1    Grabenauer, M.2    Thalassinos, K.3    Scrivens, J.H.4    Bowers, M.T.5
  • 78
    • 0029160568 scopus 로고
    • Calcium-induced conformational transioin revealed by the structure of apo calmodulin
    • Zhang M., Tanaka T., Ikura M. Calcium-induced conformational transioin revealed by the structure of apo calmodulin. Nat Struct Biol 1995, 2:758-767.
    • (1995) Nat Struct Biol , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 79
    • 77951829683 scopus 로고    scopus 로고
    • Combination of noncovalent mass spectrometry and traveling wave ion mobility spectrometry reveals sugar-induced conformational changes of central glycolytic genes repressor/DNA complex
    • Atmanene C.d., Chaix D., Bessin Y., Declerck N., Van Dorsselaer A., Sanglier-Cianferani S. Combination of noncovalent mass spectrometry and traveling wave ion mobility spectrometry reveals sugar-induced conformational changes of central glycolytic genes repressor/DNA complex. Anal Chem 2010, 82:3597-3605.
    • (2010) Anal Chem , vol.82 , pp. 3597-3605
    • Atmanene, C.1    Chaix, D.2    Bessin, Y.3    Declerck, N.4    Van Dorsselaer, A.5    Sanglier-Cianferani, S.6
  • 80
    • 47749151093 scopus 로고    scopus 로고
    • Crystal structures of the effector-binding domain of repressor central glycolytic gene regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates
    • Rezacova P., Kozisek M., Moy S.F., Sieglova I., Joachimiak A., Machlus M., Otwinowski Z. Crystal structures of the effector-binding domain of repressor central glycolytic gene regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates. Mol Microbiol 2008, 69:895-910.
    • (2008) Mol Microbiol , vol.69 , pp. 895-910
    • Rezacova, P.1    Kozisek, M.2    Moy, S.F.3    Sieglova, I.4    Joachimiak, A.5    Machlus, M.6    Otwinowski, Z.7
  • 83
    • 84870336361 scopus 로고    scopus 로고
    • Small-Molecule Inhibition of c-MYC: MAX leucine zipper formation is revealed by ion mobility mass spectrometry
    • Harvey S.R., Porrini M., Stachl C., MacMillan D., Zinzalla G., Barran P.E. Small-Molecule Inhibition of c-MYC: MAX leucine zipper formation is revealed by ion mobility mass spectrometry. J Am Chem Soc 2012, 134:19384-19392.
    • (2012) J Am Chem Soc , vol.134 , pp. 19384-19392
    • Harvey, S.R.1    Porrini, M.2    Stachl, C.3    MacMillan, D.4    Zinzalla, G.5    Barran, P.E.6
  • 85
    • 79251631002 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
    • Bleiholder C., Dupuis N.F., Wyttenbach T., Bowers M.T. Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation. Nat Chem 2010, 3:172-177.
    • (2010) Nat Chem , vol.3 , pp. 172-177
    • Bleiholder, C.1    Dupuis, N.F.2    Wyttenbach, T.3    Bowers, M.T.4
  • 86
    • 84863011516 scopus 로고    scopus 로고
    • A beta(39-42) modulates A beta oligomerization but not fibril formation
    • Gessel M.M., Wu C., Li H.Y., Bitan G., Shea J.E., Bowers M.T. A beta(39-42) modulates A beta oligomerization but not fibril formation. Biochemistry 2012, 51:108-117.
    • (2012) Biochemistry , vol.51 , pp. 108-117
    • Gessel, M.M.1    Wu, C.2    Li, H.Y.3    Bitan, G.4    Shea, J.E.5    Bowers, M.T.6
  • 87
    • 61649098771 scopus 로고    scopus 로고
    • The structure of Aβ42 C-terminal fragments probed by a combined experimental and theoretical study
    • Wu C., Murray M.M., Bernstein S.L., Condron M.M., Bitan G., Shea J.-E., Bowers M.T. The structure of Aβ42 C-terminal fragments probed by a combined experimental and theoretical study. J Mol Biol 2009, 387:492-501.
    • (2009) J Mol Biol , vol.387 , pp. 492-501
    • Wu, C.1    Murray, M.M.2    Bernstein, S.L.3    Condron, M.M.4    Bitan, G.5    Shea, J.-E.6    Bowers, M.T.7
  • 89
    • 37549040575 scopus 로고    scopus 로고
    • The challenge of drugging undruggable targets in cancer: Lessons learned from targeting BCL-2 family members
    • Verdine G.L., Walensky L.D. The challenge of drugging undruggable targets in cancer: Lessons learned from targeting BCL-2 family members. Clin Cancer Res 2007, 13:7264-7270.
    • (2007) Clin Cancer Res , vol.13 , pp. 7264-7270
    • Verdine, G.L.1    Walensky, L.D.2
  • 90
    • 78649254350 scopus 로고    scopus 로고
    • Accessing new chemical space for 'undruggable' targets
    • Dandapani S., Marcaurelle L.A. Accessing new chemical space for 'undruggable' targets. Nat Chem Biol 2010, 6:861-863.
    • (2010) Nat Chem Biol , vol.6 , pp. 861-863
    • Dandapani, S.1    Marcaurelle, L.A.2
  • 91
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu Y., Gray N.S. Rational design of inhibitors that bind to inactive kinase conformations. Nat Chem Biol 2006, 2:358-364.
    • (2006) Nat Chem Biol , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 92
    • 49649108911 scopus 로고    scopus 로고
    • Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib
    • Vajpai N., Strauss A., Fendrich G., Cowan-Jacob S.W., Manley P.W., Grzesiek S., Jahnke W. Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. J Biol Chem 2008, 283:18292-18302.
    • (2008) J Biol Chem , vol.283 , pp. 18292-18302
    • Vajpai, N.1    Strauss, A.2    Fendrich, G.3    Cowan-Jacob, S.W.4    Manley, P.W.5    Grzesiek, S.6    Jahnke, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.