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Volumn 28, Issue 1, 2014, Pages 105-111

HDX-MS guided drug discovery: Small molecules and biopharmaceuticals

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCOSYLCERAMIDASE; BIOSIMILAR AGENT; CELL NUCLEUS RECEPTOR; G PROTEIN COUPLED RECEPTOR; GLITAZONE DERIVATIVE; GLUCOSYLCERAMIDASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ANTAGONIST; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; RECOMBINANT PROTEIN; SR 1664; UNCLASSIFIED DRUG; DEUTERIUM; DRUG; HYDROGEN;

EID: 84908667545     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.08.007     Document Type: Review
Times cited : (80)

References (84)
  • 1
    • 79955586601 scopus 로고    scopus 로고
    • DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex
    • Zhang J., et al. DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex. Nat Struct Mol Biol 2011, 18:556-563.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 556-563
    • Zhang, J.1
  • 2
    • 84887408835 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase revealed by hydrogen/deuterium exchange mass spectrometry
    • Landgraf R.R., et al. Activation of AMP-activated protein kinase revealed by hydrogen/deuterium exchange mass spectrometry. Structure 2013, 21:1942-1953.
    • (2013) Structure , vol.21 , pp. 1942-1953
    • Landgraf, R.R.1
  • 3
    • 84904087801 scopus 로고    scopus 로고
    • Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry
    • Goswami D., et al. Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry. Structure 2014, 22:961-973.
    • (2014) Structure , vol.22 , pp. 961-973
    • Goswami, D.1
  • 4
    • 84865763488 scopus 로고    scopus 로고
    • HDX workbench: software for the analysis of H/D exchange MS data
    • Pascal B.D., et al. HDX workbench: software for the analysis of H/D exchange MS data. J Am Soc Mass Spectrom 2012, 23:1512-1521.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 1512-1521
    • Pascal, B.D.1
  • 5
    • 84861894726 scopus 로고    scopus 로고
    • Improved protein hydrogen/deuterium exchange mass spectrometry platform with fully automated data processing
    • Zhang Z., Zhang A., Xiao G. Improved protein hydrogen/deuterium exchange mass spectrometry platform with fully automated data processing. Anal Chem 2012, 84:4942-4949.
    • (2012) Anal Chem , vol.84 , pp. 4942-4949
    • Zhang, Z.1    Zhang, A.2    Xiao, G.3
  • 6
    • 84879536137 scopus 로고    scopus 로고
    • Feature based retention time alignment for improved HDX MS analysis
    • Venable J.D., Scuba W., Brock A. Feature based retention time alignment for improved HDX MS analysis. J Am Soc Mass Spectrom 2013, 24:642-645.
    • (2013) J Am Soc Mass Spectrom , vol.24 , pp. 642-645
    • Venable, J.D.1    Scuba, W.2    Brock, A.3
  • 7
    • 79954631587 scopus 로고    scopus 로고
    • Methods for the analysis of high precision differential hydrogen deuterium exchange data
    • Chalmers M.J., et al. Methods for the analysis of high precision differential hydrogen deuterium exchange data. Int J Mass Spectrom 2011, 302:59-68.
    • (2011) Int J Mass Spectrom , vol.302 , pp. 59-68
    • Chalmers, M.J.1
  • 8
    • 33144462544 scopus 로고    scopus 로고
    • Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry
    • Chalmers M.J., et al. Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry. Anal Chem 2006, 78:1005-1014.
    • (2006) Anal Chem , vol.78 , pp. 1005-1014
    • Chalmers, M.J.1
  • 9
    • 84901036938 scopus 로고    scopus 로고
    • Hexicon 2: automated processing of hydrogen-deuterium exchange mass spectrometry data with improved deuteration distribution estimation
    • Lindner R., et al. Hexicon 2: automated processing of hydrogen-deuterium exchange mass spectrometry data with improved deuteration distribution estimation. J Am Soc Mass Spectrom 2014, 25:1018-1028.
    • (2014) J Am Soc Mass Spectrom , vol.25 , pp. 1018-1028
    • Lindner, R.1
  • 10
    • 35148887302 scopus 로고    scopus 로고
    • Partial agonists activate PPARgamma using a helix 12 independent mechanism
    • Bruning J.B., et al. Partial agonists activate PPARgamma using a helix 12 independent mechanism. Structure 2007, 15:1258-1271.
    • (2007) Structure , vol.15 , pp. 1258-1271
    • Bruning, J.B.1
  • 11
    • 84863257556 scopus 로고    scopus 로고
    • Hydrophobic interactions improve selectivity to ERalpha for ben-zothiophene SERMs
    • Chalmers M.J., et al. Hydrophobic interactions improve selectivity to ERalpha for ben-zothiophene SERMs. ACS Med Chem Lett 2012, 3:207-210.
    • (2012) ACS Med Chem Lett , vol.3 , pp. 207-210
    • Chalmers, M.J.1
  • 12
    • 70350050562 scopus 로고    scopus 로고
    • Unique ligand binding patterns between estrogen receptor alpha and beta revealed by hydrogen-deuterium exchange
    • Dai S.Y., et al. Unique ligand binding patterns between estrogen receptor alpha and beta revealed by hydrogen-deuterium exchange. Biochemistry 2009, 48:9668-9676.
    • (2009) Biochemistry , vol.48 , pp. 9668-9676
    • Dai, S.Y.1
  • 13
    • 44449102870 scopus 로고    scopus 로고
    • Prediction of the tissue-specificity of selective estrogen receptor modulators by using a single biochemical method
    • Dai S.Y., et al. Prediction of the tissue-specificity of selective estrogen receptor modulators by using a single biochemical method. Proc Natl Acad Sci U S A 2008, 105:7171-7176.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 7171-7176
    • Dai, S.Y.1
  • 14
    • 84896721731 scopus 로고    scopus 로고
    • Inhibiting AMPylation: a novel screen to identify the first small molecule inhibitors of protein AMPylation
    • Lewallen D.M., et al. Inhibiting AMPylation: a novel screen to identify the first small molecule inhibitors of protein AMPylation. ACS Chem Biol 2014, 9:433-442.
    • (2014) ACS Chem Biol , vol.9 , pp. 433-442
    • Lewallen, D.M.1
  • 15
    • 42649104801 scopus 로고    scopus 로고
    • A unique mode of microtubule stabilization induced by peloruside A
    • Huzil J.T., et al. A unique mode of microtubule stabilization induced by peloruside A. J Mol Biol 2008, 378:1016-1030.
    • (2008) J Mol Biol , vol.378 , pp. 1016-1030
    • Huzil, J.T.1
  • 16
    • 84891844896 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry for probing higher order structure of protein therapeutics: methodology and applications
    • Wei H., et al. Hydrogen/deuterium exchange mass spectrometry for probing higher order structure of protein therapeutics: methodology and applications. Drug Discov Today 2014, 19:95-102.
    • (2014) Drug Discov Today , vol.19 , pp. 95-102
    • Wei, H.1
  • 17
    • 84883879484 scopus 로고    scopus 로고
    • Physicochemical and functional comparability between the proposed biosimilar rituximab GP2013 and originator rituximab
    • Visser J., et al. Physicochemical and functional comparability between the proposed biosimilar rituximab GP2013 and originator rituximab. BioDrugs 2013, 27:495-507.
    • (2013) BioDrugs , vol.27 , pp. 495-507
    • Visser, J.1
  • 18
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: a historical perspective
    • Englander S.W. Hydrogen exchange and mass spectrometry: a historical perspective. J Am Soc Mass Spectrom 2006, 17:1481-1489.
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 19
    • 70349632883 scopus 로고    scopus 로고
    • H/D exchange and mass spectrometry in the studies of protein conformation and dynamics: is there a need for a top-down approach?
    • Kaltashov I.A., Bobst C.E., Abzalimov R.R. H/D exchange and mass spectrometry in the studies of protein conformation and dynamics: is there a need for a top-down approach?. Anal Chem 2009, 81:7892-7899.
    • (2009) Anal Chem , vol.81 , pp. 7892-7899
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3
  • 20
    • 0035753065 scopus 로고    scopus 로고
    • High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: utility in pharmaceutical design
    • Woods V.L., Hamuro Y. High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: utility in pharmaceutical design. J Cell Biochem Suppl 2001, Suppl 37:89-98.
    • (2001) J Cell Biochem Suppl , vol.Suppl 37 , pp. 89-98
    • Woods, V.L.1    Hamuro, Y.2
  • 21
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • Engen J.R. Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS. Anal Chem 2009, 81:7870-7875.
    • (2009) Anal Chem , vol.81 , pp. 7870-7875
    • Engen, J.R.1
  • 22
    • 79951907062 scopus 로고    scopus 로고
    • Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions
    • Chalmers M.J., et al. Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions. Expert Rev Proteomics 2011, 8:43-59.
    • (2011) Expert Rev Proteomics , vol.8 , pp. 43-59
    • Chalmers, M.J.1
  • 23
    • 84928376080 scopus 로고    scopus 로고
    • Higher order structure characterization of protein therapeutics by hydrogen/deuterium exchange mass spectrometry
    • [Epub ahead of publication]
    • Huang R.Y., Chen G. Higher order structure characterization of protein therapeutics by hydrogen/deuterium exchange mass spectrometry. Anal Bioanal Chem 2014, [Epub ahead of publication].
    • (2014) Anal Bioanal Chem
    • Huang, R.Y.1    Chen, G.2
  • 24
    • 84903712533 scopus 로고    scopus 로고
    • Effects of protein-ligand interactions on hydrogen/deuterium exchange kinetics: canonical and noncanonical scenarios
    • Sowole M.A., Konermann L. Effects of protein-ligand interactions on hydrogen/deuterium exchange kinetics: canonical and noncanonical scenarios. Anal Chem 2014, 86:6715-6722.
    • (2014) Anal Chem , vol.86 , pp. 6715-6722
    • Sowole, M.A.1    Konermann, L.2
  • 25
    • 84891751622 scopus 로고    scopus 로고
    • The druggable genome: evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication
    • Rask-Andersen M., Masuram S., Schioth H.B. The druggable genome: evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication. Annu Rev Pharmacol Toxicol 2014, 54:9-26.
    • (2014) Annu Rev Pharmacol Toxicol , vol.54 , pp. 9-26
    • Rask-Andersen, M.1    Masuram, S.2    Schioth, H.B.3
  • 26
    • 84893715966 scopus 로고    scopus 로고
    • The therapeutic potential of nuclear receptor modulators for treatment of metabolic disorders: PPARgamma, RORs, and Rev-erbs
    • Marciano D.P., et al. The therapeutic potential of nuclear receptor modulators for treatment of metabolic disorders: PPARgamma, RORs, and Rev-erbs. Cell Metab 2014, 19:193-208.
    • (2014) Cell Metab , vol.19 , pp. 193-208
    • Marciano, D.P.1
  • 27
    • 84908676652 scopus 로고    scopus 로고
    • Identification of a novel selective inverse agonist probe and analogs for the Retinoic acid receptor-related Orphan Receptor Gamma (RORgamma)
    • Kumar N., et al. Identification of a novel selective inverse agonist probe and analogs for the Retinoic acid receptor-related Orphan Receptor Gamma (RORgamma). Probe Reports from the NIH Molecular Libraries Program 2010.
    • (2010) Probe Reports from the NIH Molecular Libraries Program
    • Kumar, N.1
  • 28
    • 84904325017 scopus 로고    scopus 로고
    • Conformational dynamics of human FXR-LBD ligand interactions studied by hydrogen/deuterium exchange mass spectrometry: insights into the antagonism of the hypolipidemic agent Z-guggulsterone
    • Yang L., et al. Conformational dynamics of human FXR-LBD ligand interactions studied by hydrogen/deuterium exchange mass spectrometry: insights into the antagonism of the hypolipidemic agent Z-guggulsterone. Biochim Biophys Acta 2014, 1844:1684-1693.
    • (2014) Biochim Biophys Acta , vol.1844 , pp. 1684-1693
    • Yang, L.1
  • 29
    • 77957770064 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange reveals distinct agonist/partial agonist receptor dynamics within vitamin D receptor/retinoid X receptor heterodimer
    • Zhang J., et al. Hydrogen/deuterium exchange reveals distinct agonist/partial agonist receptor dynamics within vitamin D receptor/retinoid X receptor heterodimer. Structure 2010, 18:1332-1341.
    • (2010) Structure , vol.18 , pp. 1332-1341
    • Zhang, J.1
  • 30
    • 33746495527 scopus 로고    scopus 로고
    • Hydrogen/deuterium-exchange (H/D-Ex) of PPARgamma LBD in the presence of various modulators
    • Hamuro Y., et al. Hydrogen/deuterium-exchange (H/D-Ex) of PPARgamma LBD in the presence of various modulators. Protein Sci 2006, 15:1883-1892.
    • (2006) Protein Sci , vol.15 , pp. 1883-1892
    • Hamuro, Y.1
  • 31
    • 84855795379 scopus 로고    scopus 로고
    • Ligand and receptor dynamics contribute to the mechanism of graded PPARgamma agonism
    • Hughes T.S., et al. Ligand and receptor dynamics contribute to the mechanism of graded PPARgamma agonism. Structure 2012, 20:139-150.
    • (2012) Structure , vol.20 , pp. 139-150
    • Hughes, T.S.1
  • 32
    • 80053131732 scopus 로고    scopus 로고
    • Antidiabetic actions of a non-agonist PPARgamma ligand blocking Cdk5-mediated phosphorylation
    • Choi J.H., et al. Antidiabetic actions of a non-agonist PPARgamma ligand blocking Cdk5-mediated phosphorylation. Nature 2011, 477:477-481.
    • (2011) Nature , vol.477 , pp. 477-481
    • Choi, J.H.1
  • 33
    • 84904364314 scopus 로고    scopus 로고
    • An alternate binding site for PPARgamma ligands
    • Hughes T.S., et al. An alternate binding site for PPARgamma ligands. Nat Commun 2014, 5:p3571.
    • (2014) Nat Commun , vol.5
    • Hughes, T.S.1
  • 34
    • 84871918476 scopus 로고    scopus 로고
    • The GPCR Network: a large-scale collaboration to determine human GPCR structure and function
    • Stevens R.C., et al. The GPCR Network: a large-scale collaboration to determine human GPCR structure and function. Nat Rev Drug Discov 2013, 12:25-34.
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 25-34
    • Stevens, R.C.1
  • 35
    • 0037082324 scopus 로고    scopus 로고
    • Target validation of G-protein coupled receptors
    • Wise A., Gearing K., Rees S. Target validation of G-protein coupled receptors. Drug Discov Today 2002, 7:235-246.
    • (2002) Drug Discov Today , vol.7 , pp. 235-246
    • Wise, A.1    Gearing, K.2    Rees, S.3
  • 36
    • 84896703861 scopus 로고    scopus 로고
    • Minireview: more than just a hammer: ligand "bias" and pharmaceutical discovery
    • Luttrell L.M. Minireview: more than just a hammer: ligand "bias" and pharmaceutical discovery. Mol Endocrinol 2014, 28:281-294.
    • (2014) Mol Endocrinol , vol.28 , pp. 281-294
    • Luttrell, L.M.1
  • 37
    • 84875227396 scopus 로고    scopus 로고
    • Signalling bias in new drug discovery: detection, quantification and therapeutic impact
    • Kenakin T., Christopoulos A. Signalling bias in new drug discovery: detection, quantification and therapeutic impact. Nat Rev Drug Discov 2013, 12:205-216.
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 205-216
    • Kenakin, T.1    Christopoulos, A.2
  • 38
    • 84855879360 scopus 로고    scopus 로고
    • The best of both worlds? Bitopic orthosteric/allosteric ligands of g protein-coupled receptors
    • Valant C., et al. The best of both worlds? Bitopic orthosteric/allosteric ligands of g protein-coupled receptors. Annu Rev Pharmacol Toxicol 2012, 52:153-178.
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 153-178
    • Valant, C.1
  • 39
    • 84881334295 scopus 로고    scopus 로고
    • Novel insights into biased agonism at G protein-coupled receptors and their potential for drug design
    • Marti-Solano M., et al. Novel insights into biased agonism at G protein-coupled receptors and their potential for drug design. Curr Pharm Des 2013, 19:5156-5166.
    • (2013) Curr Pharm Des , vol.19 , pp. 5156-5166
    • Marti-Solano, M.1
  • 40
    • 76149083241 scopus 로고    scopus 로고
    • Dynamics of the beta2-adrenergic G-protein coupled receptor revealed by hydrogen-deuterium exchange
    • Zhang X., et al. Dynamics of the beta2-adrenergic G-protein coupled receptor revealed by hydrogen-deuterium exchange. Anal Chem 2010, 82:1100-1108.
    • (2010) Anal Chem , vol.82 , pp. 1100-1108
    • Zhang, X.1
  • 41
    • 80054081804 scopus 로고    scopus 로고
    • Ligand-dependent perturbation of the conformational ensemble for the GPCR beta2 adrenergic receptor revealed by HDX
    • West G.M., et al. Ligand-dependent perturbation of the conformational ensemble for the GPCR beta2 adrenergic receptor revealed by HDX. Structure 2011, 19:1424-1432.
    • (2011) Structure , vol.19 , pp. 1424-1432
    • West, G.M.1
  • 42
    • 80053357815 scopus 로고    scopus 로고
    • Conformational changes in the G protein Gs induced by the beta2 adrenergic receptor
    • Chung K.Y., et al. Conformational changes in the G protein Gs induced by the beta2 adrenergic receptor. Nature 2011, 477:611-615.
    • (2011) Nature , vol.477 , pp. 611-615
    • Chung, K.Y.1
  • 43
    • 84874047567 scopus 로고    scopus 로고
    • Nepenthesin from monkey cups for hydrogen/deuterium exchange mass spectrometry
    • Rey M., et al. Nepenthesin from monkey cups for hydrogen/deuterium exchange mass spectrometry. Mol Cell Proteomics 2013, 12:464-472.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 464-472
    • Rey, M.1
  • 44
    • 84899870470 scopus 로고    scopus 로고
    • Aspartic protease nepenthesin-1 as a tool for digestion in hydrogen/deuterium exchange mass spectrometry
    • Kadek A., et al. Aspartic protease nepenthesin-1 as a tool for digestion in hydrogen/deuterium exchange mass spectrometry. Anal Chem 2014, 86:4287-4294.
    • (2014) Anal Chem , vol.86 , pp. 4287-4294
    • Kadek, A.1
  • 45
    • 84881322607 scopus 로고    scopus 로고
    • Affinity capture of biotinylated proteins at acidic conditions to facilitate hydrogen/deuterium exchange mass spectrometry analysis of multimeric protein complexes
    • Jensen P.F., et al. Affinity capture of biotinylated proteins at acidic conditions to facilitate hydrogen/deuterium exchange mass spectrometry analysis of multimeric protein complexes. Anal Chem 2013, 85:7052-7059.
    • (2013) Anal Chem , vol.85 , pp. 7052-7059
    • Jensen, P.F.1
  • 46
    • 77954193701 scopus 로고    scopus 로고
    • Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry
    • Hebling C.M., et al. Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry. Anal Chem 2010, 82:5415-5419.
    • (2010) Anal Chem , vol.82 , pp. 5415-5419
    • Hebling, C.M.1
  • 47
    • 84872858296 scopus 로고    scopus 로고
    • Which are the antibodies to watch in 2013?
    • Reichert J.M. Which are the antibodies to watch in 2013?. MAbs 2013, 5:1-4.
    • (2013) MAbs , vol.5 , pp. 1-4
    • Reichert, J.M.1
  • 48
    • 84863218474 scopus 로고    scopus 로고
    • Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars
    • Berkowitz S.A., et al. Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars. Nat Rev Drug Discov 2012, 11:527-540.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 527-540
    • Berkowitz, S.A.1
  • 49
    • 84892367060 scopus 로고    scopus 로고
    • Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies
    • Zhang H., Cui W., Gross M.L. Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies. FEBS Lett 2014, 588:308-317.
    • (2014) FEBS Lett , vol.588 , pp. 308-317
    • Zhang, H.1    Cui, W.2    Gross, M.L.3
  • 50
    • 84904065760 scopus 로고    scopus 로고
    • Current approaches to fine mapping of antigen antibody interactions
    • Abbott W.M., Damschroder M.M., Lowe D.C. Current approaches to fine mapping of antigen antibody interactions. Immunology 2014, 142:526-535.
    • (2014) Immunology , vol.142 , pp. 526-535
    • Abbott, W.M.1    Damschroder, M.M.2    Lowe, D.C.3
  • 51
    • 80052819877 scopus 로고    scopus 로고
    • Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry
    • Zhang Q., et al. Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 2011, 83:7129-7136.
    • (2011) Anal Chem , vol.83 , pp. 7129-7136
    • Zhang, Q.1
  • 52
    • 84889646833 scopus 로고    scopus 로고
    • Epitope mapping of inhibitory antibodies targeting the C2 domain of coagulation factor VIII by hydrogen-deuterium exchange mass spectrometry
    • Sevy A.M., et al. Epitope mapping of inhibitory antibodies targeting the C2 domain of coagulation factor VIII by hydrogen-deuterium exchange mass spectrometry. J Thromb Haemost 2013, 11:2128-2136.
    • (2013) J Thromb Haemost , vol.11 , pp. 2128-2136
    • Sevy, A.M.1
  • 53
    • 84877023961 scopus 로고    scopus 로고
    • Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids
    • Bereszczak J.Z., et al. Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids. J Am Chem Soc 2013, 135:6504-6512.
    • (2013) J Am Chem Soc , vol.135 , pp. 6504-6512
    • Bereszczak, J.Z.1
  • 54
    • 84863240753 scopus 로고    scopus 로고
    • Mapping of discontinuous conformational epitopes by amide hydrogen/deuterium exchange mass spectrometry and computational docking
    • Pandit D., et al. Mapping of discontinuous conformational epitopes by amide hydrogen/deuterium exchange mass spectrometry and computational docking. J Mol Recognit 2012, 25:114-124.
    • (2012) J Mol Recognit , vol.25 , pp. 114-124
    • Pandit, D.1
  • 55
    • 84861133426 scopus 로고    scopus 로고
    • The new multicomponent vaccine against meningococcal serogroup B, 4CMenB: immunological, functional and structural characterization of the antigens
    • Serruto D., et al. The new multicomponent vaccine against meningococcal serogroup B, 4CMenB: immunological, functional and structural characterization of the antigens. Vaccine 2012, 30(Suppl 2):B87-B97.
    • (2012) Vaccine , vol.30 , Issue.SUPPL 2
    • Serruto, D.1
  • 56
    • 84877616906 scopus 로고    scopus 로고
    • Conformational epitope mapping of Pru du 6, a major allergen from almond nut
    • Willison L.N., et al. Conformational epitope mapping of Pru du 6, a major allergen from almond nut. Mol Immunol 2013, 55:253-263.
    • (2013) Mol Immunol , vol.55 , pp. 253-263
    • Willison, L.N.1
  • 57
    • 84897562208 scopus 로고    scopus 로고
    • Understanding the conformational impact of chemical modifications on monoclonal antibodies with diverse sequence variations using HDX-MS and structural modeling
    • Zhang A., et al. Understanding the conformational impact of chemical modifications on monoclonal antibodies with diverse sequence variations using HDX-MS and structural modeling. Anal Chem 2014, 86:3468-3475.
    • (2014) Anal Chem , vol.86 , pp. 3468-3475
    • Zhang, A.1
  • 58
    • 84890900475 scopus 로고    scopus 로고
    • An antibody with a variable-region coiled-coil "knob" domain
    • Zhang Y., et al. An antibody with a variable-region coiled-coil "knob" domain. Angew Chem Int Ed Engl 2014, 53:132-135.
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 132-135
    • Zhang, Y.1
  • 60
    • 84900577244 scopus 로고    scopus 로고
    • Conformation and dynamics of interchain cysteine-linked antibody-drug conjugates as revealed by hydrogen/deuterium exchange mass spectrometry
    • Pan L.Y., Salas-Solano O., Valliere-Douglass J.F. Conformation and dynamics of interchain cysteine-linked antibody-drug conjugates as revealed by hydrogen/deuterium exchange mass spectrometry. Anal Chem 2014, 86:2657-2664.
    • (2014) Anal Chem , vol.86 , pp. 2657-2664
    • Pan, L.Y.1    Salas-Solano, O.2    Valliere-Douglass, J.F.3
  • 61
    • 84897841275 scopus 로고    scopus 로고
    • Identification of a small molecular insulin receptor agonist with potent antidiabetes activity
    • Qiang G., et al. Identification of a small molecular insulin receptor agonist with potent antidiabetes activity. Diabetes 2014, 63:1394-1409.
    • (2014) Diabetes , vol.63 , pp. 1394-1409
    • Qiang, G.1
  • 62
    • 80054939273 scopus 로고    scopus 로고
    • Analysis of oligomeric stability of insulin analogs using hydrogen/deuterium exchange mass spectrometry
    • Nakazawa S., et al. Analysis of oligomeric stability of insulin analogs using hydrogen/deuterium exchange mass spectrometry. Anal Biochem 2012, 420:61-67.
    • (2012) Anal Biochem , vol.420 , pp. 61-67
    • Nakazawa, S.1
  • 63
    • 84878110309 scopus 로고    scopus 로고
    • Analysis of the local dynamics of human insulin and a rapid-acting insulin analog by hydrogen/deuterium exchange mass spectrometry
    • Nakazawa S., et al. Analysis of the local dynamics of human insulin and a rapid-acting insulin analog by hydrogen/deuterium exchange mass spectrometry. Biochim Biophys Acta 2013, 1834:1210-1214.
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1210-1214
    • Nakazawa, S.1
  • 64
    • 78649674865 scopus 로고    scopus 로고
    • Impact of oxidation on protein therapeutics: conformational dynamics of intact and oxidized acid-beta-glucocerebrosidase at near-physiological pH
    • Bobst C.E., et al. Impact of oxidation on protein therapeutics: conformational dynamics of intact and oxidized acid-beta-glucocerebrosidase at near-physiological pH. Protein Sci 2010, 19:2366-2378.
    • (2010) Protein Sci , vol.19 , pp. 2366-2378
    • Bobst, C.E.1
  • 65
    • 36448938198 scopus 로고    scopus 로고
    • Development of a peptide probe for the occurrence of hydrogen (1H/2H) scrambling upon gas-phase fragmentation
    • Rand K.D., Jorgensen T.J. Development of a peptide probe for the occurrence of hydrogen (1H/2H) scrambling upon gas-phase fragmentation. Anal Chem 2007, 79:8686-8693.
    • (2007) Anal Chem , vol.79 , pp. 8686-8693
    • Rand, K.D.1    Jorgensen, T.J.2
  • 66
    • 84884996292 scopus 로고    scopus 로고
    • A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation
    • Abzalimov R.R., Bobst C.E., Kaltashov I.A. A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation. Anal Chem 2013, 85:9173-9180.
    • (2013) Anal Chem , vol.85 , pp. 9173-9180
    • Abzalimov, R.R.1    Bobst, C.E.2    Kaltashov, I.A.3
  • 67
    • 84863346540 scopus 로고    scopus 로고
    • Site-specific analysis of gas-phase hydrogen/deuterium exchange of peptides and proteins by electron transfer dissociation
    • Rand K.D., et al. Site-specific analysis of gas-phase hydrogen/deuterium exchange of peptides and proteins by electron transfer dissociation. Anal Chem 2012, 84:1931-1940.
    • (2012) Anal Chem , vol.84 , pp. 1931-1940
    • Rand, K.D.1
  • 68
    • 84856276827 scopus 로고    scopus 로고
    • Automated hydrogen/deuterium exchange electron transfer dissociation high resolution mass spectrometry measured at single-amide resolution
    • Landgraf R.R., Chalmers M.J., Griffin P.R. Automated hydrogen/deuterium exchange electron transfer dissociation high resolution mass spectrometry measured at single-amide resolution. J Am Soc Mass Spectrom 2012, 23:301-309.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 301-309
    • Landgraf, R.R.1    Chalmers, M.J.2    Griffin, P.R.3
  • 69
    • 84855370142 scopus 로고    scopus 로고
    • Structural interrogation of electrosprayed peptide ions by gas-phase H/D exchange and electron capture dissociation mass spectrometry
    • Pan J., et al. Structural interrogation of electrosprayed peptide ions by gas-phase H/D exchange and electron capture dissociation mass spectrometry. Anal Chem 2012, 84:373-378.
    • (2012) Anal Chem , vol.84 , pp. 373-378
    • Pan, J.1
  • 70
    • 84878650605 scopus 로고    scopus 로고
    • An electrospray ms-coupled microfluidic device for sub-second hydrogen/deuterium exchange pulse-labelling reveals allosteric effects in enzyme inhibition
    • Rob T., et al. An electrospray ms-coupled microfluidic device for sub-second hydrogen/deuterium exchange pulse-labelling reveals allosteric effects in enzyme inhibition. Lab Chip 2013, 13:2528-2532.
    • (2013) Lab Chip , vol.13 , pp. 2528-2532
    • Rob, T.1
  • 71
    • 84859904015 scopus 로고    scopus 로고
    • Measuring dynamics in weakly structured regions of proteins using microfluidics-enabled subsecond H/D exchange mass spectrometry
    • Rob T., et al. Measuring dynamics in weakly structured regions of proteins using microfluidics-enabled subsecond H/D exchange mass spectrometry. Anal Chem 2012, 84:3771-3779.
    • (2012) Anal Chem , vol.84 , pp. 3771-3779
    • Rob, T.1
  • 72
    • 84879939419 scopus 로고    scopus 로고
    • Characterizing rapid, activity-linked conformational transitions in proteins via sub-second hydrogen deuterium exchange mass spectrometry
    • Resetca D., Wilson D.J. Characterizing rapid, activity-linked conformational transitions in proteins via sub-second hydrogen deuterium exchange mass spectrometry. FEBS J 2013, 280:5616-5625.
    • (2013) FEBS J , vol.280 , pp. 5616-5625
    • Resetca, D.1    Wilson, D.J.2
  • 73
    • 84884575467 scopus 로고    scopus 로고
    • Time window expansion for HDX analysis of an intrinsically disordered protein
    • Goswami D., et al. Time window expansion for HDX analysis of an intrinsically disordered protein. J Am Soc Mass Spectrom 2013, 24:1584-1592.
    • (2013) J Am Soc Mass Spectrom , vol.24 , pp. 1584-1592
    • Goswami, D.1
  • 74
    • 36049032359 scopus 로고    scopus 로고
    • A two-stage differential hydrogen deuterium exchange method for the rapid characterization of protein/ligand interactions
    • Chalmers M.J., et al. A two-stage differential hydrogen deuterium exchange method for the rapid characterization of protein/ligand interactions. J Biomol Tech 2007, 18:194-204.
    • (2007) J Biomol Tech , vol.18 , pp. 194-204
    • Chalmers, M.J.1
  • 75
    • 84904060056 scopus 로고    scopus 로고
    • HDX reveals unique fragment ligands for the vitamin D receptor
    • Carson M.W., et al. HDX reveals unique fragment ligands for the vitamin D receptor. Bioorg Med Chem Lett 2014, 24:3459-3463.
    • (2014) Bioorg Med Chem Lett , vol.24 , pp. 3459-3463
    • Carson, M.W.1
  • 76
    • 84857539181 scopus 로고    scopus 로고
    • Plasticity of CYP2B enzymes: structural and solution biophysical methods
    • Wilderman P.R., Halpert J.R. Plasticity of CYP2B enzymes: structural and solution biophysical methods. Curr Drug Metab 2012, 13:167-176.
    • (2012) Curr Drug Metab , vol.13 , pp. 167-176
    • Wilderman, P.R.1    Halpert, J.R.2
  • 77
    • 70349448687 scopus 로고    scopus 로고
    • The solution structure and dynamics of the DH-PH module of PDZRhoGEF in isolation and in complex with nucleotide-free RhoA
    • Cierpicki T., et al. The solution structure and dynamics of the DH-PH module of PDZRhoGEF in isolation and in complex with nucleotide-free RhoA. Protein Sci 2009, 18:2067-2079.
    • (2009) Protein Sci , vol.18 , pp. 2067-2079
    • Cierpicki, T.1
  • 78
    • 84886011849 scopus 로고    scopus 로고
    • Isolate-specific differences in the conformational dynamics and antigenicity of HIV-1 gp120
    • Davenport T.M., et al. Isolate-specific differences in the conformational dynamics and antigenicity of HIV-1 gp120. J Virol 2013, 87:10855-10873.
    • (2013) J Virol , vol.87 , pp. 10855-10873
    • Davenport, T.M.1
  • 79
    • 84888109377 scopus 로고    scopus 로고
    • Folding of a large protein at high structural resolution
    • Walters B.T., et al. Folding of a large protein at high structural resolution. Proc Natl Acad Sci U S A 2013, 110:18898-18903.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 18898-18903
    • Walters, B.T.1
  • 80
    • 84893650116 scopus 로고    scopus 로고
    • Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states
    • Winkler A., et al. Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states. J Mol Biol 2014, 426:853-868.
    • (2014) J Mol Biol , vol.426 , pp. 853-868
    • Winkler, A.1
  • 81
    • 84890885083 scopus 로고    scopus 로고
    • Differential accessibility of a rotavirus VP6 epitope in trimers comprising type I, II, or III channels as revealed by binding of a human rotavirus VP6-specific antibody
    • Aiyegbo M.S., et al. Differential accessibility of a rotavirus VP6 epitope in trimers comprising type I, II, or III channels as revealed by binding of a human rotavirus VP6-specific antibody. J Virol 2014, 88:469-476.
    • (2014) J Virol , vol.88 , pp. 469-476
    • Aiyegbo, M.S.1
  • 82
    • 84873549557 scopus 로고    scopus 로고
    • A pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry
    • Noble A.J., et al. A pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry. Nat Struct Mol Biol 2013, 20:167-173.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 167-173
    • Noble, A.J.1
  • 83
    • 84876411185 scopus 로고    scopus 로고
    • Virus assembly and maturation: auto-regulation through allosteric molecular switches
    • Domitrovic T., et al. Virus assembly and maturation: auto-regulation through allosteric molecular switches. J Mol Biol 2013, 425:1488-1496.
    • (2013) J Mol Biol , vol.425 , pp. 1488-1496
    • Domitrovic, T.1
  • 84
    • 84903149823 scopus 로고    scopus 로고
    • Glucocorticoid receptor function regulated by coordinated action of the hsp90 and hsp70 chaperone cycles
    • Kirschke E., et al. Glucocorticoid receptor function regulated by coordinated action of the hsp90 and hsp70 chaperone cycles. Cell 2014, 157:1685-1697.
    • (2014) Cell , vol.157 , pp. 1685-1697
    • Kirschke, E.1


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