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Volumn 15, Issue 10, 2016, Pages 679-698

Biophysics in drug discovery: Impact, challenges and opportunities

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; DRUG;

EID: 84981532009     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd.2016.123     Document Type: Review
Times cited : (286)

References (158)
  • 1
    • 84909587217 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing toward the reality
    • Arkin, M. R., Tang, Y. & Wells, J. A. Small-molecule inhibitors of protein-protein interactions: progressing toward the reality. Chem. Biol. 21, 1102-1114 (2014).
    • (2014) Chem. Biol , vol.21 , pp. 1102-1114
    • Arkin, M.R.1    Tang, Y.2    Wells, J.A.3
  • 2
    • 84893018543 scopus 로고    scopus 로고
    • Protein-protein interactions as druggable targets: Recent technological advances
    • Higueruelo, A. P., Jubb, H. & Blundell, T. L. Protein-protein interactions as druggable targets: recent technological advances. Curr. Opin. Pharmacol. 13, 791-796 (2013).
    • (2013) Curr. Opin. Pharmacol , vol.13 , pp. 791-796
    • Higueruelo, A.P.1    Jubb, H.2    Blundell, T.L.3
  • 3
    • 80255131239 scopus 로고    scopus 로고
    • Kinetic efficiency: The missing metric for enhancing compound quality?
    • Holdgate, G. A. & Gill, A. L. Kinetic efficiency: the missing metric for enhancing compound quality? Drug Discov. Today 16, 910-913 (2011).
    • (2011) Drug Discov Today , vol.16 , pp. 910-913
    • Holdgate, G.A.1    Gill, A.L.2
  • 4
    • 84957845231 scopus 로고    scopus 로고
    • The drug-Target residence time model: A 10 year retrospective
    • Copeland, R. A. The drug-Target residence time model: a 10 year retrospective. Nat. Rev. Drug Discov. 15, 87-95 (2016).
    • (2016) Nat. Rev. Drug Discov , vol.15 , pp. 87-95
    • Copeland, R.A.1
  • 5
    • 33748325882 scopus 로고    scopus 로고
    • Drug-Target residence time, and its implications for lead optimization
    • Copeland, R. A., Pompliano, D. L. & Meek, T. D. Drug-Target residence time, and its implications for lead optimization. Nat. Rev. Drug Discov. 5, 730-739 (2006).
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 6
    • 84881315859 scopus 로고    scopus 로고
    • The 'rule of three' for fragment-based drug discovery: Where are we now?
    • Jhoti, H., Williams, G., Rees, D. C. & Murray, C. W. The 'rule of three' for fragment-based drug discovery: where are we now? Nat. Rev. Drug Discov. 12, 644-645 (2013).
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 644-645
    • Jhoti, H.1    Williams, G.2    Rees, D.C.3    Murray, C.W.4
  • 7
    • 84881423067 scopus 로고    scopus 로고
    • Integrated biophysical approach to fragment screening, and validation for fragment-based lead discovery
    • Silvestre, H. L., Blundell, T. L., Abell, C. & Ciulli, A. Integrated biophysical approach to fragment screening, and validation for fragment-based lead discovery. Proc. Natl Acad. Sci. USA 110, 12984-12989 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 12984-12989
    • Silvestre, H.L.1    Blundell, T.L.2    Abell, C.3    Ciulli, A.4
  • 8
    • 84989257519 scopus 로고    scopus 로고
    • Fragments in the clinic: 2015 edition
    • Erlanson, D. A. & Zartler, E. Fragments in the clinic: 2015 edition. Practical Fragments, http://practicalfragments.blogspot.fr/2015/01/fragments-in-clinic-2015-edition.html (2015).
    • (2015) Practical Fragments
    • Erlanson, D.A.1    Zartler, E.2
  • 9
    • 84926158682 scopus 로고    scopus 로고
    • Applying thermodynamic profiling in lead finding, and optimization
    • Klebe, G. Applying thermodynamic profiling in lead finding, and optimization. Nat. Rev. Drug Discov. 14, 95-110 (2015
    • (2015) Nat. Rev. Drug Discov , vol.14 , pp. 95-110
    • Klebe, G.1
  • 10
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • Leeson, P. D. & Springthorpe, B. The influence of drug-like concepts on decision-making in medicinal chemistry. Nat. Rev. Drug Discov. 6, 881-890 (2007).
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 11
    • 15944394229 scopus 로고    scopus 로고
    • High-Throughput X ray crystallography for drug discovery
    • Blundell, T. L. & Patel, S. High-Throughput X ray crystallography for drug discovery. Curr. Opin. Pharmacol. 4, 490-496 (2004).
    • (2004) Curr. Opin. Pharmacol , vol.4 , pp. 490-496
    • Blundell, T.L.1    Patel, S.2
  • 12
    • 84894899532 scopus 로고    scopus 로고
    • NMR-based analysis of protein-ligand interactions
    • Cala, O., Guilliere, F. & Krimm, I. NMR-based analysis of protein-ligand interactions. Anal. Bioanal. Chem. 406, 943-956 (2014).
    • (2014) Anal. Bioanal. Chem , vol.406 , pp. 943-956
    • Cala, O.1    Guilliere, F.2    Krimm, I.3
  • 13
    • 51249121331 scopus 로고    scopus 로고
    • Perspectives on NMR in drug discovery: A technique comes of age
    • Pellecchia, M., et al. Perspectives on NMR in drug discovery: a technique comes of age. Nat. Rev. Drug Discov. 7, 738-745 (2008).
    • (2008) Nat. Rev. Drug Discov , vol.7 , pp. 738-745
    • Pellecchia, M.1
  • 15
    • 0036633640 scopus 로고    scopus 로고
    • Optical biosensors in drug discovery
    • Cooper, M. A. Optical biosensors in drug discovery. Nat. Rev. Drug Discov. 1, 515-528 (2002).
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 515-528
    • Cooper, M.A.1
  • 16
    • 84860124363 scopus 로고    scopus 로고
    • Application of optical biosensors in small-molecule screening activities
    • Geschwindner, S., Carlsson, J. F. & Knecht, W. Application of optical biosensors in small-molecule screening activities. Sensors (Basel) 12, 4311-4323 (2012).
    • (2012) Sensors (Basel) , vol.12 , pp. 4311-4323
    • Geschwindner, S.1    Carlsson, J.F.2    Knecht, W.3
  • 17
    • 33750565735 scopus 로고    scopus 로고
    • Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology
    • Huber, W. & Mueller, F. Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology. Curr. Pharm. Des. 12, 3999-4021 (2006).
    • (2006) Curr. Pharm. des , vol.12 , pp. 3999-4021
    • Huber, W.1    Mueller, F.2
  • 18
    • 36249028775 scopus 로고    scopus 로고
    • SPR-based fragment screening: Advantages, and applications
    • Neumann, T., Junker, H. D., Schmidt, K. & Sekul, R. SPR-based fragment screening: advantages, and applications. Curr. Top. Med. Chem. 7, 1630-1642 (2007).
    • (2007) Curr. Top. Med. Chem , vol.7 , pp. 1630-1642
    • Neumann, T.1    Junker, H.D.2    Schmidt, K.3    Sekul, R.4
  • 20
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo, M. C., et al. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 332, 153-159 (2004).
    • (2004) Anal. Biochem , vol.332 , pp. 153-159
    • Lo, M.C.1
  • 21
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F. H., Berglund, H. & Vedadi, M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2, 2212-2221 (2007).
    • (2007) Nat. Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 22
    • 74149083849 scopus 로고    scopus 로고
    • Adding calorimetric data to decision making in lead discovery: A hot tip
    • Ladbury, J. E., Klebe, G. & Freire, E. Adding calorimetric data to decision making in lead discovery: a hot tip. Nat. Rev. Drug Discov. 9, 23-27 (2010).
    • (2010) Nat. Rev. Drug Discov , vol.9 , pp. 23-27
    • Ladbury, J.E.1    Klebe, G.2    Freire, E.3
  • 23
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • Chaires, J. B. Calorimetry, and thermodynamics in drug design. Annu. Rev. Biophys. 37, 135-151 (2008).
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 135-151
    • Chaires, J.B.1
  • 24
    • 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. 5, 585-595 (2006).
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 585-595
    • Hofstadler, S.A.1    Sannes-Lowery, K.A.2
  • 26
    • 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. 11, 518-526 (2007).
    • (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
  • 27
    • 79951907062 scopus 로고    scopus 로고
    • Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions
    • Chalmers, M. J., Busby, S. A., Pascal, B. D., West, G. M. & Griffin, P. R. Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions. Expert Rev. Proteom. 8, 43-59 (2011).
    • (2011) Expert Rev. Proteom , vol.8 , pp. 43-59
    • Chalmers, M.J.1    Busby, S.A.2    Pascal, B.D.3    West, G.M.4    Griffin, P.R.5
  • 28
    • 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. 40, 1224-1234 (2011).
    • (2011) Chem. Soc. Rev , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 29
    • 84884497350 scopus 로고    scopus 로고
    • Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions
    • Seidel, S. A., et al. Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions. Methods 59, 301-315 (2013).
    • (2013) Methods , vol.59 , pp. 301-315
    • Seidel, S.A.1
  • 30
    • 84867498176 scopus 로고    scopus 로고
    • Label-free microscale thermophoresis discriminates sites, and affinity of protein-ligand binding
    • Seidel, S. A., et al. Label-free microscale thermophoresis discriminates sites, and affinity of protein-ligand binding. Angew. Chem. Int. 51, 10656-10659 (2012).
    • (2012) Angew. Chem. Int , vol.51 , pp. 10656-10659
    • Seidel, S.A.1
  • 31
    • 84899417553 scopus 로고    scopus 로고
    • Weak protein-ligand interactions studied by small-Angle X ray scattering
    • Tuukkanen, A. T. & Svergun, D. I. Weak protein-ligand interactions studied by small-Angle X ray scattering. FEBS J. 281, 1974-1987 (2014).
    • (2014) FEBS J. , Issue.281 , pp. 1974-1987
    • Tuukkanen, A.T.1    Svergun, D.I.2
  • 32
    • 84941358320 scopus 로고    scopus 로고
    • Investigating increasingly complex macromolecular systems with small-Angle X ray scattering
    • Vestergaard, B. & Sayers, Z. Investigating increasingly complex macromolecular systems with small-Angle X ray scattering. IUCrJ 1, 523-529 (2014).
    • (2014) IUCrJ , vol.1 , pp. 523-529
    • Vestergaard, B.1    Sayers, Z.2
  • 34
    • 34447498398 scopus 로고    scopus 로고
    • A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: Applications of acoustic physics to the analysis of biomolecular interactions
    • Cooper, M. A. & Singleton, V. T. A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: applications of acoustic physics to the analysis of biomolecular interactions. J. Mol. Recognit 20, 154-184 (2007).
    • (2007) J. Mol Recognit , vol.20 , pp. 154-184
    • Cooper, M.A.1    Singleton, V.T.2
  • 35
    • 27644582140 scopus 로고    scopus 로고
    • Measuring the affinity of a radioligand with its receptor using a rotating cell dish with in situ reference area
    • Björke, H. & Andersson, K. Measuring the affinity of a radioligand with its receptor using a rotating cell dish with in situ reference area. Appl. Radiat. Isot. 64, 32-37 (2006).
    • (2006) Appl. Radiat. Isot , vol.64 , pp. 32-37
    • Björke, H.1    Andersson, K.2
  • 36
    • 74249116139 scopus 로고    scopus 로고
    • Fragment library screening, and lead characterization using SPR biosensors
    • Danielson, U. H. Fragment library screening, and lead characterization using SPR biosensors. Curr. Top. Med. Chem. 9, 1725-1735 (2009).
    • (2009) Curr. Top. Med. Chem , vol.9 , pp. 1725-1735
    • Danielson, U.H.1
  • 37
    • 79952383501 scopus 로고    scopus 로고
    • From experimental design to validated hits a comprehensive walk-Through of fragment lead identification using surface plasmon resonance
    • Giannetti, A. M. From experimental design to validated hits a comprehensive walk-Through of fragment lead identification using surface plasmon resonance. Methods Enzymol. 493, 169-218 (2011).
    • (2011) Methods Enzymol , vol.493 , pp. 169-218
    • Giannetti, A.M.1
  • 38
    • 84929533115 scopus 로고    scopus 로고
    • Learning from our mistakes: The 'unknown knowns' in fragment screening
    • Davis, B. J. & Erlanson, D. A. Learning from our mistakes: the 'unknown knowns' in fragment screening. Bioorg. Med. Chem. Lett. 23, 2844-2852 (2013).
    • (2013) Bioorg. Med. Chem. Lett , vol.23 , pp. 2844-2852
    • Davis, B.J.1    Erlanson, D.A.2
  • 39
    • 84860557228 scopus 로고    scopus 로고
    • Reliable determinations of protein-ligand interactions by direct ESI MS measurements Are we there yet? J
    • 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. 23, 431-441 (2012).
    • (2012) 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
  • 40
    • 79952429629 scopus 로고    scopus 로고
    • Experiences in fragment-based lead discovery
    • Hubbard, R. E. & Murray, J. B. Experiences in fragment-based lead discovery. Methods Enzymol. 493, 509-531 (2011).
    • (2011) Methods Enzymol , vol.493 , pp. 509-531
    • Hubbard, R.E.1    Murray, J.B.2
  • 41
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-Affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P. & Fesik, S. W. Discovering high-Affinity ligands for proteins: SAR by NMR. Science 274, 1531-1534 (1996).
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 42
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances, and lessons learned
    • Hajduk, P. J. & Greer, J. A decade of fragment-based drug design: strategic advances, and lessons learned. Nat. Rev. Drug Discov. 6, 211-219 (2007).
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 43
    • 0033773899 scopus 로고    scopus 로고
    • Discovering novel ligands for macromolecules using X ray crystallographic screening
    • Nienaber, V. L., et al. Discovering novel ligands for macromolecules using X ray crystallographic screening. Nat. Biotechnol. 18, 1105-1108 (2000).
    • (2000) Nat. Biotechnol , vol.18 , pp. 1105-1108
    • Nienaber, V.L.1
  • 44
    • 0038198865 scopus 로고    scopus 로고
    • High-Throughput crystallography to enhance drug discovery
    • Sharff, A. & Jhoti, H. High-Throughput crystallography to enhance drug discovery. Curr. Opin. Chem. Biol. 7, 340-345 (2003).
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 340-345
    • Sharff, A.1    Jhoti, H.2
  • 46
    • 36248956723 scopus 로고    scopus 로고
    • The SeeDs approach: Integrating fragments into drug discovery
    • Hubbard, R. E., Davis, B., Chen, I. & Drysdale, M. J. The SeeDs approach: integrating fragments into drug discovery. Curr. Top. Med. Chem. 7, 1568-1581 (2007).
    • (2007) Curr. Top. Med. Chem , vol.7 , pp. 1568-1581
    • Hubbard, R.E.1    Davis, B.2    Chen, I.3    Drysdale, M.J.4
  • 47
    • 45749114201 scopus 로고    scopus 로고
    • Identification of MMP 12 inhibitors by using biosensor-based screening of a fragment library
    • Nordström, H., et al. Identification of MMP 12 inhibitors by using biosensor-based screening of a fragment library. J. Med. Chem. 51, 3449-3459 (2008).
    • (2008) J. Med. Chem , vol.51 , pp. 3449-3459
    • Nordström, H.1
  • 48
    • 79958779889 scopus 로고    scopus 로고
    • Fragment-based drug design - Tools, practical approaches, and examples
    • Kuo, L. C. Fragment-based drug design - tools, practical approaches, and examples. Preface. Methods Enzymol. 493, xxi-xxii (2011).
    • (2011) Preface. Methods Enzymol , vol.493 , pp. xxi-xxii
    • Kuo, L.C.1
  • 49
    • 84940460179 scopus 로고    scopus 로고
    • One question, multiple answers: Biochemical, and biophysical screening methods retrieve deviating fragment hit lists
    • Schiebel, J., et al. One question, multiple answers: biochemical, and biophysical screening methods retrieve deviating fragment hit lists. ChemMedChem. 10, 1511-1521 (2015).
    • (2015) ChemMedChem , vol.10 , pp. 1511-1521
    • Schiebel, J.1
  • 50
    • 84858141881 scopus 로고    scopus 로고
    • Combining biophysical screening, and X ray crystallography for fragment-based drug discovery
    • Hennig, M., Ruf, A. & Huber, W. Combining biophysical screening, and X ray crystallography for fragment-based drug discovery. Top. Curr. Chem. 317, 115-143 (2012).
    • (2012) Top. Curr. Chem , vol.317 , pp. 115-143
    • Hennig, M.1    Ruf, A.2    Huber, W.3
  • 51
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • Zhang, J., et al. Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature 463, 501-506 (2010).
    • (2010) Nature , vol.463 , pp. 501-506
    • Zhang, J.1
  • 52
    • 77955927300 scopus 로고    scopus 로고
    • Allosteric non-bisphosphonate FPPS inhibitors identified by fragment-based discovery
    • Jahnke, W., et al. Allosteric non-bisphosphonate FPPS inhibitors identified by fragment-based discovery. Nat. Chem. Biol. 6, 660-666 (2010).
    • (2010) Nat. Chem. Biol , vol.6 , pp. 660-666
    • Jahnke, W.1
  • 53
    • 84915820942 scopus 로고    scopus 로고
    • Discovery of selective small-molecule activators of a bacterial glycoside hydrolase
    • Darby, J. F., et al. Discovery of selective small-molecule activators of a bacterial glycoside hydrolase. Angew. Chem. Int. 53, 13419-13423 (2014).
    • (2014) Angew. Chem. Int , vol.53 , pp. 13419-13423
    • Darby, J.F.1
  • 54
    • 84870810902 scopus 로고    scopus 로고
    • Biophysical, and computational fragment-based approaches to targeting protein-protein interactions: Applications in structure-guided drug discovery
    • Winter, A., et al. Biophysical, and computational fragment-based approaches to targeting protein-protein interactions: applications in structure-guided drug discovery. Q. Rev. Biophys. 45, 383-426 (2012).
    • (2012) Q. Rev. Biophys , vol.45 , pp. 383-426
    • Winter, A.1
  • 55
    • 84989273888 scopus 로고    scopus 로고
    • eds Sittampalam G. S. et al. Bethesda (MD
    • Iversen, P. W., et al. in Assay Guidance Manual (eds Sittampalam, G. S. et al.) (Bethesda (MD), 2004).
    • (2004) Assay Guidance Manual
    • Iversen, P.W.1
  • 56
    • 84961918312 scopus 로고    scopus 로고
    • Integrating biophysics with HTS-driven drug discovery projects
    • Folmer, R. H. Integrating biophysics with HTS-driven drug discovery projects. Drug Discov. Today 21, 491-498 (2016).
    • (2016) Drug Discov. Today , vol.21 , pp. 491-498
    • Folmer, R.H.1
  • 57
    • 84902125945 scopus 로고    scopus 로고
    • Applications of biophysics in high-Throughput screening hit validation
    • Genick, C. C., et al. Applications of biophysics in high-Throughput screening hit validation. J. Biomol. Screen 19, 707-714 (2014).
    • (2014) J. Biomol. Screen , vol.19 , pp. 707-714
    • Genick, C.C.1
  • 58
    • 18244380348 scopus 로고    scopus 로고
    • High-density miniaturized thermal shift assays as a general strategy for drug discovery
    • Pantoliano, M. W., et al. High-density miniaturized thermal shift assays as a general strategy for drug discovery. J. Biomol. Screen 6, 429-440 (2001).
    • (2001) J. Biomol. Screen , vol.6 , pp. 429-440
    • Pantoliano, M.W.1
  • 59
    • 35848962300 scopus 로고    scopus 로고
    • Mass spectrometric techniques for label-free high-Throughput screening in drug discovery
    • Roddy, T. P., et al. Mass spectrometric techniques for label-free high-Throughput screening in drug discovery. Anal. Chem. 79, 8207-8213 (2007).
    • (2007) Anal. Chem , vol.79 , pp. 8207-8213
    • Roddy, T.P.1
  • 60
    • 84908530414 scopus 로고    scopus 로고
    • Chemistry: Chemical con artists foil drug discovery
    • Baell, J. & Walters, M. A. Chemistry: chemical con artists foil drug discovery. Nature 513, 481-483 (2014).
    • (2014) Nature , vol.513 , pp. 481-483
    • Baell, J.1    Walters, M.A.2
  • 61
    • 0141923641 scopus 로고    scopus 로고
    • Identification, and prediction of promiscuous aggregating inhibitors among known drugs
    • Seidler, J., McGovern, S. L., Doman, T. N. & Shoichet, B. K. Identification, and prediction of promiscuous aggregating inhibitors among known drugs. J. Med. Chem. 46, 4477-4486 (2003).
    • (2003) J. Med. Chem , vol.46 , pp. 4477-4486
    • Seidler, J.1    McGovern, S.L.2    Doman, T.N.3    Shoichet, B.K.4
  • 62
    • 77956185674 scopus 로고    scopus 로고
    • Affinity-based, biophysical methods to detect, and analyze ligand binding to recombinant proteins: Matching high information content with high throughput
    • Holdgate, G. A., Anderson, M., Edfeldt, F. & Geschwindner, S. Affinity-based, biophysical methods to detect, and analyze ligand binding to recombinant proteins: matching high information content with high throughput. J. Struct. Biol. 172, 142-157 (2010).
    • (2010) J. Struct. Biol , vol.172 , pp. 142-157
    • Holdgate, G.A.1    Anderson, M.2    Edfeldt, F.3    Geschwindner, S.4
  • 63
    • 77956225829 scopus 로고    scopus 로고
    • Inhibition of HIV 1 by non-nucleoside reverse transcriptase inhibitors via an induced fit mechanism-Importance of slow dissociation, and relaxation rates for antiviral efficacy
    • Elinder, M., et al. Inhibition of HIV 1 by non-nucleoside reverse transcriptase inhibitors via an induced fit mechanism-Importance of slow dissociation, and relaxation rates for antiviral efficacy. Biochem. Pharmacol. 80, 1133-1140 (2010).
    • (2010) Biochem. Pharmacol , vol.80 , pp. 1133-1140
    • Elinder, M.1
  • 64
    • 77956592818 scopus 로고    scopus 로고
    • Interaction kinetic, and structural dynamic analysis of ligand binding to acetylcholine-binding protein
    • Geitmann, M., et al. Interaction kinetic, and structural dynamic analysis of ligand binding to acetylcholine-binding protein. Biochemistry 49, 8143-8154 (2010).
    • (2010) Biochemistry , vol.49 , pp. 8143-8154
    • Geitmann, M.1
  • 65
    • 84866426155 scopus 로고    scopus 로고
    • Kinetic, and mechanistic differences in the interactions between caldendrin, and calmodulin with AKAP79 suggest different roles in synaptic function
    • Seeger, C., Gorny, X., Reddy, P. P., Seidenbecher, C. & Danielson, U. H. Kinetic, and mechanistic differences in the interactions between caldendrin, and calmodulin with AKAP79 suggest different roles in synaptic function. J. Mol. Recognit 25, 495-503 (2012).
    • (2012) J. Mol. Recognit , vol.25 , pp. 495-503
    • Seeger, C.1    Gorny, X.2    Reddy, P.P.3    Seidenbecher, C.4    Danielson, U.H.5
  • 66
    • 84873540049 scopus 로고    scopus 로고
    • ABT 199, a potent, and selective BCL 2 inhibitor, achieves antitumor activity while sparing platelets
    • Souers, A. J., et al. ABT 199, a potent, and selective BCL 2 inhibitor, achieves antitumor activity while sparing platelets. Nat. Med. 19, 202-208 (2013).
    • (2013) Nat. Med , vol.19 , pp. 202-208
    • Souers, A.J.1
  • 67
    • 84867683811 scopus 로고    scopus 로고
    • Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function
    • Saalau-Bethell, S. M., et al. Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function. Nat. Chem. Biol. 8, 920-925 (2012).
    • (2012) Nat. Chem. Biol , vol.8 , pp. 920-925
    • Saalau-Bethell, S.M.1
  • 68
    • 84872301920 scopus 로고    scopus 로고
    • Discovery of potent myeloid cell leukemia 1 (Mcl 1) inhibitors using fragment-based methods, and structure-based design
    • Friberg, A., et al. Discovery of potent myeloid cell leukemia 1 (Mcl 1) inhibitors using fragment-based methods, and structure-based design. J. Med. Chem. 56, 15-30 (2013).
    • (2013) J. Med. Chem , vol.56 , pp. 15-30
    • Friberg, A.1
  • 69
    • 84859463451 scopus 로고    scopus 로고
    • Small-molecule ligands bind to a distinct pocket in Ras, and inhibit SOS-mediated nucleotide exchange activity
    • Maurer, T., et al. Small-molecule ligands bind to a distinct pocket in Ras, and inhibit SOS-mediated nucleotide exchange activity. Proc. Natl Acad. Sci. USA 109, 5299-5304 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 5299-5304
    • Maurer, T.1
  • 70
    • 84862649997 scopus 로고    scopus 로고
    • Discovery of small molecules that bind to K Ras, and inhibit Sos-mediated activation
    • Sun, Q., et al. Discovery of small molecules that bind to K Ras, and inhibit Sos-mediated activation. Angew. Chem. Int. 51, 6140-6143 (2012).
    • (2012) Angew. Chem. Int , vol.51 , pp. 6140-6143
    • Sun, Q.1
  • 71
    • 84888639050 scopus 로고    scopus 로고
    • K Ras(G12C) inhibitors allosterically control GTP affinity, and effector interactions
    • Ostrem, J M., Peters, U., Sos, M. L., Wells, J. A. & Shokat, K. M. K Ras(G12C) inhibitors allosterically control GTP affinity, and effector interactions. Nature 503, 548-551 (2013).
    • (2013) Nature , vol.503 , pp. 548-551
    • Ostrem, J.M.1    Peters, U.2    Sos, M.L.3    Wells, J.A.4    Shokat, K.M.5
  • 72
    • 84946742931 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors of tau aggregation by targeting monomeric tau as a potential therapeutic approach for tauopathies
    • Pickhardt, M., et al. Identification of small molecule inhibitors of tau aggregation by targeting monomeric tau as a potential therapeutic approach for tauopathies. Curr. Alzheimer Res. 12, 814-828 (2015).
    • (2015) Curr. Alzheimer Res , vol.12 , pp. 814-828
    • Pickhardt, M.1
  • 73
    • 79956140184 scopus 로고    scopus 로고
    • Getting pharmaceutical R&D back on target
    • Bunnage, M. E. Getting pharmaceutical R&D back on target. Nat. Chem. Biol. 7, 335-339 (2011).
    • (2011) Nat. Chem. Biol , vol.7 , pp. 335-339
    • Bunnage, M.E.1
  • 74
    • 84879748358 scopus 로고    scopus 로고
    • Monitoring drug target engagement in cells, and tissues using the cellular thermal shift assay
    • Martinez Molina, D., et al. Monitoring drug target engagement in cells, and tissues using the cellular thermal shift assay. Science 341, 84-87 (2013).
    • (2013) Science , vol.341 , pp. 84-87
    • Martinez Molina, D.1
  • 75
    • 84948953323 scopus 로고    scopus 로고
    • Thermal proteome profiling monitors ligand interactions with cellular membrane proteins
    • Reinhard, F. B., et al. Thermal proteome profiling monitors ligand interactions with cellular membrane proteins. Nat. Methods 12, 1129-1131 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 1129-1131
    • Reinhard, F.B.1
  • 76
    • 84907485591 scopus 로고    scopus 로고
    • Tracking cancer drugs in living cells by thermal profiling of the proteome
    • Savitski, M. M., et al. Tracking cancer drugs in living cells by thermal profiling of the proteome. Science 346, 1255784 (2014).
    • (2014) Science , vol.346 , pp. 1255784
    • Savitski, M.M.1
  • 77
    • 84954095264 scopus 로고    scopus 로고
    • The cellular thermal shift assay: A novel biophysical assay for in situ drug target engagement, and mechanistic biomarker studies
    • Martinez Molina, D. & Nordlund, P. The cellular thermal shift assay: a novel biophysical assay for in situ drug target engagement, and mechanistic biomarker studies. Annu. Rev. Pharmacol. Toxicol. 56, 141-161 (2016).
    • (2016) Annu. Rev. Pharmacol. Toxicol , vol.56 , pp. 141-161
    • Martinez Molina, D.1    Nordlund, P.2
  • 78
    • 33745902222 scopus 로고    scopus 로고
    • Analyzing ligand, and small molecule binding activity of solubilized GPCRs using biosensor technology
    • Navratilova, I., Dioszegi, M. & Myszka, D. G. Analyzing ligand, and small molecule binding activity of solubilized GPCRs using biosensor technology. Anal. Biochem. 355, 132-139 (2006).
    • (2006) Anal. Biochem , vol.355 , pp. 132-139
    • Navratilova, I.1    Dioszegi, M.2    Myszka, D.G.3
  • 79
    • 15444376596 scopus 로고    scopus 로고
    • Solubilization, stabilization, and purification of chemokine receptors using biosensor technology
    • Navratilova, I., Sodroski, J. & Myszka, D. G. Solubilization, stabilization, and purification of chemokine receptors using biosensor technology. Anal. Biochem. 339, 271-281 (2005
    • (2005) Anal. Biochem , vol.339 , pp. 271-281
    • Navratilova, I.1    Sodroski, J.2    Myszka, D.G.3
  • 80
    • 84885440727 scopus 로고    scopus 로고
    • Discovery of β2 adrenergic receptor ligands using biosensor fragment screening of tagged wild-Type receptor
    • Aristotelous, T., et al. Discovery of β2 adrenergic receptor ligands using biosensor fragment screening of tagged wild-Type receptor. ACS Med. Chem. Lett. 4, 1005-1010 (2013).
    • (2013) ACS Med. Chem. Lett , vol.4 , pp. 1005-1010
    • Aristotelous, T.1
  • 81
    • 84923298549 scopus 로고    scopus 로고
    • Capture-stabilize approach for membrane protein SPR assays
    • Chu, R., Reczek, D. & Brondyk, W. Capture-stabilize approach for membrane protein SPR assays. Sci. Rep. 4, 7360 (2014).
    • (2014) Sci. Rep , vol.4 , pp. 7360
    • Chu, R.1    Reczek, D.2    Brondyk, W.3
  • 82
    • 84877716938 scopus 로고    scopus 로고
    • Biophysical fragment screening of the β1 adrenergic receptor: Identification of high affinity arylpiperazine leads using structure-based drug design
    • Christopher, J. A., et al. Biophysical fragment screening of the β1 adrenergic receptor: identification of high affinity arylpiperazine leads using structure-based drug design. J. Med. Chem. 56, 3446-3455 (2013).
    • (2013) J. Med. Chem , vol.56 , pp. 3446-3455
    • Christopher, J.A.1
  • 83
    • 84938866055 scopus 로고    scopus 로고
    • Purification of stabilized GPCRs for structural, and biophysical analyses
    • Errey, J. C., Dore, A. S., Zhukov, A., Marshall, F. H. & Cooke, R. M. Purification of stabilized GPCRs for structural, and biophysical analyses. Methods Mol. Biol. 1335, 1-15 (2015).
    • (2015) Methods Mol. Biol , vol.1335 , pp. 1-15
    • Errey, J.C.1    Dore, A.S.2    Zhukov, A.3    Marshall, F.H.4    Cooke, R.M.5
  • 84
    • 79952382815 scopus 로고    scopus 로고
    • Fragment screening of stabilized G protein-coupled receptors using biophysical methods
    • Congreve, M., et al. Fragment screening of stabilized G protein-coupled receptors using biophysical methods. Methods Enzymol. 493, 115-136 (2011).
    • (2011) Methods Enzymol , vol.493 , pp. 115-136
    • Congreve, M.1
  • 85
    • 84929312161 scopus 로고    scopus 로고
    • Discovery of HTL6641, a dual orexin receptor antagonist with differentiated pharmacodynamic properties
    • Christopher, J. A., et al. Discovery of HTL6641, a dual orexin receptor antagonist with differentiated pharmacodynamic properties. MedChemComm 6, 947-955 (2015).
    • (2015) MedChemComm , vol.6 , pp. 947-955
    • Christopher, J.A.1
  • 86
    • 84893854581 scopus 로고    scopus 로고
    • Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli
    • Egloff, P., et al. Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli. Proc. Natl Acad. Sci. USA 111, E655-E662 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E655-E662
    • Egloff, P.1
  • 87
    • 84871572340 scopus 로고    scopus 로고
    • Fragment screening of GPCRs using biophysical methods: Identification of ligands of the adenosine A2A receptor with novel biological activity
    • Chen, D., et al. Fragment screening of GPCRs using biophysical methods: identification of ligands of the adenosine A2A receptor with novel biological activity. ACS Chem. Biol. 7, 2064-2073 (2012).
    • (2012) ACS Chem. Biol , vol.7 , pp. 2064-2073
    • Chen, D.1
  • 88
    • 77956015631 scopus 로고    scopus 로고
    • Application of fragment-based drug discovery to membrane proteins: Identification of ligands of the integral membrane enzyme DsbB
    • Fruh, V., et al. Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB. Chem. Biol. 17, 881-891 (2010).
    • (2010) Chem. Biol , vol.17 , pp. 881-891
    • Fruh, V.1
  • 89
    • 84924047517 scopus 로고    scopus 로고
    • Real-Time monitoring of binding events on a thermostabilized human A2A receptor embedded in a lipid bilayer by surface plasmon resonance
    • Bocquet, N., et al. Real-Time monitoring of binding events on a thermostabilized human A2A receptor embedded in a lipid bilayer by surface plasmon resonance. Biochim. Biophys. Acta 1848, 1224-1233 (2015).
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 1224-1233
    • Bocquet, N.1
  • 90
    • 84864861302 scopus 로고    scopus 로고
    • Structure of the acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1
    • Dawson, R. J., et al. Structure of the acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1. Nat. Commun. 3, 936 (2012).
    • (2012) Nat. Commun , vol.3 , pp. 936
    • Dawson, R.J.1
  • 91
    • 84861974582 scopus 로고    scopus 로고
    • Histaminergic pharmacology of homo-oligomeric β3 ?-Aminobutyric acid type A receptors characterized by surface plasmon resonance biosensor technology
    • Seeger, C., et al. Histaminergic pharmacology of homo-oligomeric β3 ?-Aminobutyric acid type A receptors characterized by surface plasmon resonance biosensor technology. Biochem. Pharmacol. 84, 341-351 (2012).
    • (2012) Biochem. Pharmacol , vol.84 , pp. 341-351
    • Seeger, C.1
  • 92
    • 84871927415 scopus 로고    scopus 로고
    • Structural basis of ligand recognition in 5 HT3 receptors
    • Kesters, D., et al. Structural basis of ligand recognition in 5 HT3 receptors. EMBO Rep. 14, 49-56 (2013).
    • (2013) EMBO Rep , vol.14 , pp. 49-56
    • Kesters, D.1
  • 93
    • 84929179462 scopus 로고    scopus 로고
    • Molecular blueprint of allosteric binding sites in a homologue of the agonist-binding domain of the alpha7 nicotinic acetylcholine receptor
    • Spurny, R., et al. Molecular blueprint of allosteric binding sites in a homologue of the agonist-binding domain of the alpha7 nicotinic acetylcholine receptor. Proc. Natl Acad. Sci. USA 112, E2543-2552 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E2543-E2552
    • Spurny, R.1
  • 94
    • 84877121934 scopus 로고    scopus 로고
    • Isothermal titration calorimetry with micelles: Thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein
    • Perspicace, S., et al. Isothermal titration calorimetry with micelles: thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein. FEBS Open Bio. 3, 204-211 (2013).
    • (2013) FEBS Open Bio , vol.3 , pp. 204-211
    • Perspicace, S.1
  • 95
    • 79951896735 scopus 로고    scopus 로고
    • Electrons, photons, and force: Quantitative single-molecule measurements from physics to biology
    • Claridge, S. A., Schwartz, J. J. & Weiss, P. S. Electrons, photons, and force: quantitative single-molecule measurements from physics to biology. ACS Nano. 5, 693-729 (2011).
    • (2011) ACS Nano , vol.5 , pp. 693-729
    • Claridge, S.A.1    Schwartz, J.J.2    Weiss, P.S.3
  • 96
  • 97
    • 44449097780 scopus 로고    scopus 로고
    • Do it yourself guide: How to use the modern single-molecule toolkit
    • Walter, N. G., Huang, C. Y., Manzo, A. J. & Sobhy, M. A. Do it yourself guide: how to use the modern single-molecule toolkit. Nat. Methods 5, 475-489 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 475-489
    • Walter, N.G.1    Huang, C.Y.2    Manzo, A.J.3    Sobhy, M.A.4
  • 98
    • 84881230259 scopus 로고    scopus 로고
    • Making connections - Strategies for single molecule fluorescence biophysics
    • Grohmann, D., Werner, F. & Tinnefeld, P. Making connections - strategies for single molecule fluorescence biophysics. Curr. Opin. Chem. Biol. 17, 691-698 (2013).
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 691-698
    • Grohmann, D.1    Werner, F.2    Tinnefeld, P.3
  • 99
    • 33748614065 scopus 로고    scopus 로고
    • Single molecule studies of enzyme mechanisms
    • Smiley, R. D. & Hammes, G. G. Single molecule studies of enzyme mechanisms. Chem. Rev. 106, 3080-3094 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 3080-3094
    • Smiley, R.D.1    Hammes, G.G.2
  • 100
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • Roy, R., Hohng, S. & Ha, T. A practical guide to single-molecule FRET. Nat. Methods 5, 507-516 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 101
    • 84928309434 scopus 로고    scopus 로고
    • Drug discovery at the single molecule level: Inhibition-in solution assay of membrane-reconstituted beta-secretase using single-molecule imaging
    • Gunnarsson, A., et al. Drug discovery at the single molecule level: inhibition-in solution assay of membrane-reconstituted beta-secretase using single-molecule imaging. Anal. Chem. 87, 4100-4103 (2015).
    • (2015) Anal. Chem , vol.87 , pp. 4100-4103
    • Gunnarsson, A.1
  • 102
    • 84878077090 scopus 로고    scopus 로고
    • Lab on a chip technologies for single-molecule studies
    • Zhao, Y., et al. Lab on a chip technologies for single-molecule studies. Lab. Chip 13, 2183-2198 (2013).
    • (2013) Lab. Chip , vol.13 , pp. 2183-2198
    • Zhao, Y.1
  • 103
    • 84907022539 scopus 로고    scopus 로고
    • Structural biology: 'seeing' crystals the XFEL way
    • Marx, V. Structural biology: 'seeing' crystals the XFEL way. Nat. Methods 11, 903-908 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 903-908
    • Marx, V.1
  • 104
    • 84924278628 scopus 로고    scopus 로고
    • Serial femtosecond crystallography: The first five years
    • Schlichting, I. Serial femtosecond crystallography: the first five years. IUCrJ 2, 246-255 (2015).
    • (2015) IUCrJ , vol.2 , pp. 246-255
    • Schlichting, I.1
  • 105
    • 84923368907 scopus 로고    scopus 로고
    • How cryo em is revolutionizing structural biology
    • Bai, X. C., McMullan, G. & Scheres, S. H. How cryo EM is revolutionizing structural biology. Trends Biochem. Sci. 40, 49-57 (2015).
    • (2015) Trends Biochem. Sci , vol.40 , pp. 49-57
    • Bai, X.C.1    McMullan, G.2    Scheres, S.H.3
  • 106
    • 84928379119 scopus 로고    scopus 로고
    • A primer to single-particle cryo-electron microscopy
    • Cheng, Y., Grigorieff, N., Penczek, P. A. & Walz, T. A primer to single-particle cryo-electron microscopy. Cell 161, 438-449 (2015).
    • (2015) Cell , vol.161 , pp. 438-449
    • Cheng, Y.1    Grigorieff, N.2    Penczek, P.A.3    Walz, T.4
  • 107
    • 84940835264 scopus 로고    scopus 로고
    • Metalloprotein structures at ambient conditions, and in real-Time: Biological crystallography, and spectroscopy using X ray free electron lasers
    • Kern, J., Yachandra, V. K. & Yano, J. Metalloprotein structures at ambient conditions, and in real-Time: biological crystallography, and spectroscopy using X ray free electron lasers. Curr. Opin. Struct. Biol. 34, 87-98 (2015).
    • (2015) Curr. Opin. Struct. Biol , vol.34 , pp. 87-98
    • Kern, J.1    Yachandra, V.K.2    Yano, J.3
  • 108
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 109
    • 84941254172 scopus 로고    scopus 로고
    • An atomic structure of human gamma-secretase
    • Bai, X. C., et al. An atomic structure of human gamma-secretase. Nature 525, 212-217 (2015).
    • (2015) Nature , vol.525 , pp. 212-217
    • Bai, X.C.1
  • 110
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 resolution cryo em structure of beta-galactosidase in complex with a cell-permeant inhibitor
    • Bartesaghi, A., et al. 2.2 ? resolution cryo EM structure of beta-galactosidase in complex with a cell-permeant inhibitor. Science 348, 1147-1151 (2015).
    • (2015) Science , vol.348 , pp. 1147-1151
    • Bartesaghi, A.1
  • 111
    • 0029003107 scopus 로고
    • The potential, and limitations of neutrons, electrons, and X rays for atomic resolution microscopy of unstained biological molecules
    • Henderson, R. The potential, and limitations of neutrons, electrons, and X rays for atomic resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 28, 171-193 (1995).
    • (1995) Q. Rev. Biophys , vol.28 , pp. 171-193
    • Henderson, R.1
  • 112
    • 0343484958 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction between HIV 1 protease, and inhibitors using optical biosensor technology
    • Markgren, P. O., Hdmdldinen, M. & Danielson, U. H. Kinetic analysis of the interaction between HIV 1 protease, and inhibitors using optical biosensor technology. Anal. Biochem. 279, 71-78 (2000).
    • (2000) Anal. Biochem. , vol.279 , pp. 71-78
    • Markgren, P.O.1    Hdmdldinen, M.2    Danielson, U.H.3
  • 113
    • 84876724694 scopus 로고    scopus 로고
    • The advantage of biosensor analysis over enzyme inhibition studies for slow dissociating inhibitors - Characterization of hydroxamate-based matrix metalloproteinase 12 inhibitors
    • Gossas, T., et al. The advantage of biosensor analysis over enzyme inhibition studies for slow dissociating inhibitors - characterization of hydroxamate-based matrix metalloproteinase 12 inhibitors. MedChemComm 4, 432-442 (2013).
    • (2013) MedChemComm , vol.4 , pp. 432-442
    • Gossas, T.1
  • 114
    • 84960881030 scopus 로고    scopus 로고
    • Kinetically selective inhibitors of human carbonic anhydrase isoenzymes I, II, VII, IX, XII, and XIII
    • Talibov, V. O., Linkiviene, V., Matulis, D. & Danielson, U. H. Kinetically selective inhibitors of human carbonic anhydrase isoenzymes I, II, VII, IX, XII, and XIII. J. Med. Chem. 59, 2083-2093 (2016).
    • (2016) J. Med. Chem , vol.59 , pp. 2083-2093
    • Talibov, V.O.1    Linkiviene, V.2    Matulis, D.3    Danielson, U.H.4
  • 115
    • 79955694305 scopus 로고    scopus 로고
    • A surface plasmon resonance-based biosensor with full-length BACE1 in a reconstituted membrane
    • Christopeit, T., et al. A surface plasmon resonance-based biosensor with full-length BACE1 in a reconstituted membrane. Anal. Biochem. 414, 14-22 (2011).
    • (2011) Anal. Biochem , vol.414 , pp. 14-22
    • Christopeit, T.1
  • 116
    • 77956013896 scopus 로고    scopus 로고
    • Effect of the protonation state of the titratable residues on the inhibitor affinity to BACE 1
    • Dominguez, J. L., et al. Effect of the protonation state of the titratable residues on the inhibitor affinity to BACE 1. Biochemistry 49, 7255-7263 (2010).
    • (2010) Biochemistry , vol.49 , pp. 7255-7263
    • Dominguez, J.L.1
  • 117
    • 84878626336 scopus 로고    scopus 로고
    • On the active site protonation state in aspartic proteases: Implications for drug design
    • Sussman, F., Villaverde, M. C., Dominguez, J. L. & Danielson, U. H. On the active site protonation state in aspartic proteases: implications for drug design. Curr. Pharm. Des. 19, 4257-4275 (2013).
    • (2013) Curr. Pharm. des , vol.19 , pp. 4257-4275
    • Sussman, F.1    Villaverde, M.C.2    Dominguez, J.L.3    Danielson, U.H.4
  • 118
    • 84949324412 scopus 로고    scopus 로고
    • Design strategies to address kinetics of drug binding, and residence time
    • Cusack, K. P., et al. Design strategies to address kinetics of drug binding, and residence time. Bioorg. Med. Chem. Lett. 25, 2019-2027 (2015).
    • (2015) Bioorg. Med. Chem. Lett , vol.25 , pp. 2019-2027
    • Cusack, K.P.1
  • 119
    • 58449131873 scopus 로고    scopus 로고
    • The role of binding kinetics in therapeutically useful drug action
    • Swinney, D. C. The role of binding kinetics in therapeutically useful drug action. Curr. Opin. Drug Discov. Devel 12, 31-39 (2009).
    • (2009) Curr. Opin. Drug Discov. Devel , vol.12 , pp. 31-39
    • Swinney, D.C.1
  • 120
    • 84881171375 scopus 로고    scopus 로고
    • Pharmacokinetics, and the drug-Target residence time concept
    • Dahl, G. & ?kerud, T. Pharmacokinetics, and the drug-Target residence time concept. Drug Discov. Today 18, 697-707 (2013).
    • (2013) Drug Discov. Today , vol.18 , pp. 697-707
    • Dahl, G.1    Kerud, T.2
  • 121
    • 84879925936 scopus 로고    scopus 로고
    • Molecular determinants of drug-receptor binding kinetics
    • Pan, A. C., Borhani, D. W., Dror, R. O. & Shaw, D. E. Molecular determinants of drug-receptor binding kinetics. Drug Discov. Today 18, 667-673 (2013).
    • (2013) Drug Discov. Today , vol.18 , pp. 667-673
    • Pan, A.C.1    Borhani, D.W.2    Dror, R.O.3    Shaw, D.E.4
  • 122
    • 84931572829 scopus 로고    scopus 로고
    • Prolonged, and tunable residence time using reversible covalent kinase inhibitors
    • Bradshaw, J. M., et al. Prolonged, and tunable residence time using reversible covalent kinase inhibitors. Nat. Chem. Biol. 11, 525-531 (2015).
    • (2015) Nat. Chem. Biol , vol.11 , pp. 525-531
    • Bradshaw, J.M.1
  • 123
    • 77957229353 scopus 로고    scopus 로고
    • Thermodynamics guided lead discovery, and optimization
    • Ferenczy, G. G. & Keseru, G. M. Thermodynamics guided lead discovery, and optimization. Drug Discov. Today 15, 919-932 (2010).
    • (2010) Drug Discov. Today , vol.15 , pp. 919-932
    • Ferenczy, G.G.1    Keseru, G.M.2
  • 124
    • 34548421643 scopus 로고    scopus 로고
    • Thermodynamics of binding interactions in the rational drug design process
    • Holdgate, G. A. Thermodynamics of binding interactions in the rational drug design process. Expert Opin. Drug Discov. 2, 1103-1114 (2007).
    • (2007) Expert Opin. Drug Discov , vol.2 , pp. 1103-1114
    • Holdgate, G.A.1
  • 125
    • 84877768087 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Role, and ramifications in biomolecular ligand recognition, and design
    • Chodera, J. D. & Mobley, D. L. Entropy-enthalpy compensation: role, and ramifications in biomolecular ligand recognition, and design. Annu. Rev. Biophys. 42, 121-142 (2013).
    • (2013) Annu. Rev. Biophys , vol.42 , pp. 121-142
    • Chodera, J.D.1    Mobley, D.L.2
  • 126
    • 84921777888 scopus 로고    scopus 로고
    • The use of thermodynamic, and kinetic data in drug discovery: Decisive insight or increasing the puzzlement?
    • Klebe, G. The use of thermodynamic, and kinetic data in drug discovery: decisive insight or increasing the puzzlement? ChemMedChem. 10, 229-231 (2015).
    • (2015) Chem. Med. Chem. , vol.10 , pp. 229-231
    • Klebe, G.1
  • 127
    • 84940501243 scopus 로고    scopus 로고
    • Ligand binding thermodynamics in drug discovery: Still a hot tip?
    • Geschwindner, S., Ulander, J. & Johansson, P. Ligand binding thermodynamics in drug discovery: still a hot tip? J. Med. Chem. 58, 6321-6335 (2015).
    • (2015) J. Med. Chem , vol.58 , pp. 6321-6335
    • Geschwindner, S.1    Ulander, J.2    Johansson, P.3
  • 128
    • 84910003834 scopus 로고    scopus 로고
    • A universal homogeneous assay for high-Throughput determination of binding kinetics
    • Schiele, F., Ayaz, P. & Fernandez-Montalvan, A. A universal homogeneous assay for high-Throughput determination of binding kinetics. Anal. Biochem. 468, 42-49 (2014).
    • (2014) Anal. Biochem , vol.468 , pp. 42-49
    • Schiele, F.1    Ayaz, P.2    Fernandez-Montalvan, A.3
  • 129
    • 0021336303 scopus 로고
    • The kinetics of competitive radioligand binding predicted by the law of mass action
    • Motulsky, H. J. & Mahan, L. C. The kinetics of competitive radioligand binding predicted by the law of mass action. Mol. Pharmacol. 25, 1-9 (1984).
    • (1984) Mol. Pharmacol , vol.25 , pp. 1-9
    • Motulsky, H.J.1    Mahan, L.C.2
  • 130
    • 84924606514 scopus 로고    scopus 로고
    • Isothermal microcalorimetry accurately detects bacteria, tumorous microtissues, and parasitic worms in a label-free well-plate assay
    • Braissant, O., et al. Isothermal microcalorimetry accurately detects bacteria, tumorous microtissues, and parasitic worms in a label-free well-plate assay. Biotechnol. J. 10, 460-468 (2015).
    • (2015) Biotechnol. J. , vol.10 , pp. 460-468
    • Braissant, O.1
  • 131
    • 84964595271 scopus 로고    scopus 로고
    • Unique tool for cellular structural biology: In cell NMR
    • Luchinat, E. & Banci, L. A. Unique tool for cellular structural biology: in cell NMR. J. Biol. Chem. 291, 3776-3784 (2016).
    • (2016) J. Biol. Chem , vol.291 , pp. 3776-3784
    • Luchinat, E.1    Banci, L.A.2
  • 132
    • 84871694264 scopus 로고    scopus 로고
    • The physics of life: One molecule at a time
    • Leake, M. C. The physics of life: one molecule at a time. Phil. Trans. R. Soc. B 368, 20120248 (2013).
    • (2013) Phil. Trans. R. Soc B , vol.368 , pp. 20120248
    • Leake, M.C.1
  • 133
    • 84939950570 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of seven-Transmembrane receptors
    • Aristotelous, T., Hopkins, A. L. & Navratilova, I. Surface plasmon resonance analysis of seven-Transmembrane receptors. Methods Enzymol. 556, 499-525 (2015).
    • (2015) Methods Enzymol , vol.556 , pp. 499-525
    • Aristotelous, T.1    Hopkins, A.L.2    Navratilova, I.3
  • 135
    • 84888364004 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy for characterisation of membrane protein-ligand interactions, and its potential for drug discovery
    • Patching, S. G. Surface plasmon resonance spectroscopy for characterisation of membrane protein-ligand interactions, and its potential for drug discovery. Biochim. Biophys. Acta 1838, 43-55 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 43-55
    • Patching, S.G.1
  • 136
    • 84896752267 scopus 로고    scopus 로고
    • Identification, and optimization of PDE10A inhibitors using fragment-based screening by nanocalorimetry, and X ray crystallography
    • Recht, M. I., et al. Identification, and optimization of PDE10A inhibitors using fragment-based screening by nanocalorimetry, and X ray crystallography. J. Biomol. Screen 19, 497-507 (2014).
    • (2014) J. Biomol. Screen , vol.19 , pp. 497-507
    • Recht, M.I.1
  • 137
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl 2 family proteins induces regression of solid tumours
    • Oltersdorf, T., et al. An inhibitor of Bcl 2 family proteins induces regression of solid tumours. Nature 435, 677-681 (2005).
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1
  • 138
    • 38349157746 scopus 로고    scopus 로고
    • 4, 5 diarylisoxazole Hsp90 chaperone inhibitors: Potential therapeutic agents for the treatment of cancer
    • Brough, P. A., et al. 4, 5 diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer. J. Med. Chem. 51, 196-218 (2008).
    • (2008) J. Med. Chem , vol.51 , pp. 196-218
    • Brough, P.A.1
  • 139
    • 84898474395 scopus 로고    scopus 로고
    • Off-rate screening (ORS) by surface plasmon resonance An efficient method to kinetically sample hit to lead chemical space from unpurified reaction products
    • Murray, J. B., Roughley, S. D., Matassova, N. & Brough, P. A. Off-rate screening (ORS) by surface plasmon resonance. An efficient method to kinetically sample hit to lead chemical space from unpurified reaction products. J. Med. Chem. 57, 2845-2850 (2014).
    • (2014) J. Med. Chem , vol.57 , pp. 2845-2850
    • Murray, J.B.1    Roughley, S.D.2    Matassova, N.3    Brough, P.A.4
  • 140
    • 68549115383 scopus 로고    scopus 로고
    • Combining hit identification strategies: Fragment-based, and in silico approaches to orally active 2 aminothieno[2, 3 d]pyrimidine inhibitors of the Hsp90 molecular chaperone
    • Brough, P. A., et al. Combining hit identification strategies: fragment-based, and in silico approaches to orally active 2 aminothieno[2, 3 d]pyrimidine inhibitors of the Hsp90 molecular chaperone. J. Med. Chem. 52, 4794-4809 (2009).
    • (2009) J. Med. Chem , vol.52 , pp. 4794-4809
    • Brough, P.A.1
  • 141
    • 84946494366 scopus 로고    scopus 로고
    • Discovery of novel allosteric non-bisphosphonate inhibitors of farnesyl pyrophosphate synthase by integrated lead finding
    • Marzinzik, A. L., et al. Discovery of novel allosteric non-bisphosphonate inhibitors of farnesyl pyrophosphate synthase by integrated lead finding. ChemMedChem. 10, 1884-1891 (2015).
    • (2015) ChemMedChem , vol.10 , pp. 1884-1891
    • Marzinzik, A.L.1
  • 142
    • 84879844246 scopus 로고    scopus 로고
    • Fragment-based drug discovery using NMR spectroscopy
    • Harner, M. J., Frank, A. O. & Fesik, S. W. Fragment-based drug discovery using NMR spectroscopy. J. Biomol. NMR 56, 65-75 (2013).
    • (2013) J. Biomol. NMR , vol.56 , pp. 65-75
    • Harner, M.J.1    Frank, A.O.2    Fesik, S.W.3
  • 143
    • 84872928524 scopus 로고    scopus 로고
    • HTS by NMR of combinatorial libraries: A fragment-based approach to ligand discovery
    • Wu, B., et al. HTS by NMR of combinatorial libraries: a fragment-based approach to ligand discovery. Chem. Biol. 20, 19-33 (2013).
    • (2013) Chem. Biol , vol.20 , pp. 19-33
    • Wu, B.1
  • 144
    • 84937115962 scopus 로고    scopus 로고
    • High-Throughput screening by nuclear magnetic resonance (HTS by NMR) for the identification of PPIs antagonists
    • Wu, B., et al. High-Throughput screening by nuclear magnetic resonance (HTS by NMR) for the identification of PPIs antagonists. Curr. Top. Med. Chem. 15, 2032-2042 (2015
    • (2015) Curr. Top. Med. Chem , vol.15 , pp. 2032-2042
    • Wu, B.1
  • 145
    • 22544442178 scopus 로고    scopus 로고
    • Differential scanning calorimetry in life science: Thermodynamics, stability, molecular recognition, and application in drug design
    • Bruylants, G., Wouters, J. & Michaux, C. Differential scanning calorimetry in life science: thermodynamics, stability, molecular recognition, and application in drug design. Curr. Med. Chem. 12, 2011-2020 (2005).
    • (2005) Curr. Med. Chem , vol.12 , pp. 2011-2020
    • Bruylants, G.1    Wouters, J.2    Michaux, C.3
  • 146
    • 69749094463 scopus 로고    scopus 로고
    • Label-free detection of biomolecular interactions using BioLayer interferometry for kinetic characterization
    • Concepcion, J., et al. Label-free detection of biomolecular interactions using BioLayer interferometry for kinetic characterization. Comb. Chem. High Throughput Screen. 12, 791-800 (2009).
    • (2009) Comb. Chem. High Throughput Screen , vol.12 , pp. 791-800
    • Concepcion, J.1
  • 147
    • 84904558949 scopus 로고    scopus 로고
    • Bio-layer interferometry for measuring kinetics of protein-protein interactions, and allosteric ligand effects
    • Shah, N. B. & Duncan, T. M. Bio-layer interferometry for measuring kinetics of protein-protein interactions, and allosteric ligand effects. J. Vis. Exp. 18, e51383 (2014).
    • (2014) J. Vis. Exp , vol.18 , pp. e51383
    • Shah, N.B.1    Duncan, T.M.2
  • 148
    • 80051787791 scopus 로고    scopus 로고
    • Biosensor-based small molecule fragment screening with biolayer interferometry
    • Wartchow, C. A., et al. Biosensor-based small molecule fragment screening with biolayer interferometry. J. Comput. Aided Mol. Des. 25, 669-676 (2011).
    • (2011) J. Comput. Aided Mol. des , vol.25 , pp. 669-676
    • Wartchow, C.A.1
  • 149
    • 79953839803 scopus 로고    scopus 로고
    • Label-free quantification of membrane-ligand interactions using backscattering interferometry
    • Baksh, M. M., Kussrow, A. K., Mileni, M., Finn, M. G. & Bornhop, D. J. Label-free quantification of membrane-ligand interactions using backscattering interferometry. Nat. Biotechnol. 29, 357-360 (2011).
    • (2011) Nat. Biotechnol , vol.29 , pp. 357-360
    • Baksh, M.M.1    Kussrow, A.K.2    Mileni, M.3    Finn, M.G.4    Bornhop, D.J.5
  • 150
    • 34648815160 scopus 로고    scopus 로고
    • Free-solution, label-free molecular interactions studied by back-scattering interferometry
    • Bornhop, D. J., et al. Free-solution, label-free molecular interactions studied by back-scattering interferometry. Science 317, 1732-1736 (2007).
    • (2007) Science , vol.317 , pp. 1732-1736
    • Bornhop, D.J.1
  • 151
    • 84928905645 scopus 로고    scopus 로고
    • Label-free detection of small-molecule binding to a GPCR in the membrane environment
    • Heym, R. G., Hornberger, W. B., Lakics, V. & Terstappen, G. C. Label-free detection of small-molecule binding to a GPCR in the membrane environment. Biochim. Biophys. Acta 1854, 979-986 (2015).
    • (2015) Biochim. Biophys. Acta , vol.1854 , pp. 979-986
    • Heym, R.G.1    Hornberger, W.B.2    Lakics, V.3    Terstappen, G.C.4
  • 152
    • 33745098276 scopus 로고    scopus 로고
    • SAW sensor system for marker-free molecular interaction analysis
    • Perpeet, M., et al. SAW sensor system for marker-free molecular interaction analysis. Anal. Lett. 39, 1747-1757 (2006).
    • (2006) Anal. Lett , vol.39 , pp. 1747-1757
    • Perpeet, M.1
  • 153
    • 84941085413 scopus 로고    scopus 로고
    • Protein conformational changes are detected, and resolved site specifically by second-harmonic generation
    • Moree, B., et al. Protein conformational changes are detected, and resolved site specifically by second-harmonic generation. Biophys. J. 109, 806-815 (2015).
    • (2015) Biophys. J. , vol.109 , pp. 806-815
    • Moree, B.1
  • 154
    • 84946949732 scopus 로고    scopus 로고
    • Small molecules detected by second-harmonic generation modulate the conformation of monomeric α-synuclein, and reduce its aggregation in cells
    • Moree, B., et al. Small molecules detected by second-harmonic generation modulate the conformation of monomeric α-synuclein, and reduce its aggregation in cells. J. Biol. Chem. 290, 27582-27593 (2015).
    • (2015) J. Biol. Chem , vol.290 , pp. 27582-27593
    • Moree, B.1
  • 155
    • 33747597796 scopus 로고    scopus 로고
    • Detection of protein conformational change by optical second-harmonic generation
    • Salafsky, J. S. Detection of protein conformational change by optical second-harmonic generation. J. Chem. Phys. 125, 074701 (2006).
    • (2006) J. Chem. Phys , vol.125 , pp. 074701
    • Salafsky, J.S.1
  • 156
    • 79955638458 scopus 로고    scopus 로고
    • Grating coupled optical waveguide interferometer for label-free biosensing
    • Kozma, P., Hamori, A., Kurunczi, S., Cottier, K. & Horvath, R. Grating coupled optical waveguide interferometer for label-free biosensing. Sens. Actuators B: Chem. 155, 446-450 (2011).
    • (2011) Sens. Actuators B: Chem , vol.155 , pp. 446-450
    • Kozma, P.1    Hamori, A.2    Kurunczi, S.3    Cottier, K.4    Horvath, R.5
  • 157
    • 84896539896 scopus 로고    scopus 로고
    • Integrated planar optical waveguide interferometer biosensors: A comparative review
    • Kozma, P., Kehl, F., Ehrentreich-Forster, E., Stamm, C. & Bier, F. F. Integrated planar optical waveguide interferometer biosensors: a comparative review. Biosens. Bioelectron. 58, 287-307 (2014).
    • (2014) Biosens. Bioelectron , vol.58 , pp. 287-307
    • Kozma, P.1    Kehl, F.2    Ehrentreich-Forster, E.3    Stamm, C.4    Bier, F.F.5
  • 158
    • 84880313703 scopus 로고    scopus 로고
    • Protein analysis by time-resolved measurements with an electro-switchable DNA chip
    • Langer, A., et al. Protein analysis by time-resolved measurements with an electro-switchable DNA chip. Nat. Commun. 4, 2099 (2013
    • (2013) Nat. Commun , vol.4 , pp. 2099
    • Langer, A.1


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