메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages 2309-2324

A three-stage biophysical screening cascade for fragment-based drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING AFFINITY; BIOPHYSICS; CHEMICAL ANALYSIS; CHEMICAL INTERACTION; CONTROLLED STUDY; DIFFERENTIAL SCANNING FLUORIMETRY; DRUG DEVELOPMENT; FLUOROMETRY; FRAGMENT BASED DRUG DISCOVERY; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; MACROMOLECULE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; SCREENING; VALIDATION PROCESS; X RAY CRYSTALLOGRAPHY;

EID: 84887001050     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2013.130     Document Type: Article
Times cited : (106)

References (62)
  • 1
    • 67849113794 scopus 로고    scopus 로고
    • The rise of fragment-based drug discovery
    • Murray, C.W. & Rees, D.C. The rise of fragment-based drug discovery. Nat. Chem. 1, 187-192 (2009).
    • (2009) Nat. Chem , vol.1 , pp. 187-192
    • Murray, C.W.1    Rees, D.C.2
  • 2
    • 37549048176 scopus 로고    scopus 로고
    • Fragment-based approaches to enzyme inhibition
    • Ciulli, A. & Abell, C. Fragment-based approaches to enzyme inhibition. Curr. Opin. Biotechnol. 18, 489-496 (2007).
    • (2007) Curr. Opin. Biotechnol , vol.18 , pp. 489-496
    • Ciulli, A.1    Abell, C.2
  • 3
    • 0141726877 scopus 로고    scopus 로고
    • A 'Rule of Three' for fragment-based lead discovery?
    • DOI 10.1016/S1359-6446(03)02831-9, PII S1359644603028319
    • Congreve, M., Carr, R., Murray, C. & Jhoti, H. A ?rule of three? for fragment-based lead discovery? Drug Discov. Today 8, 876-877 (2003). (Pubitemid 37194496)
    • (2003) Drug Discovery Today , vol.8 , Issue.19 , pp. 876-877
    • Congreve, M.1    Carr, R.2    Murray, C.3    Jhoti, H.4
  • 4
    • 70350346470 scopus 로고    scopus 로고
    • Application of fragment growing and fragment linking to the discovery of inhibitors of Mycobacterium tuberculosis pantothenate synthetase
    • Hung, A. et al. Application of fragment growing and fragment linking to the discovery of inhibitors of Mycobacterium tuberculosis pantothenate synthetase. Angew. Chem. Int. Ed. 48, 8452-8456 (2009).
    • (2009) Angew. Chem. Int. Ed , vol.48 , pp. 8452-8456
    • Hung, A.1
  • 5
    • 84865835782 scopus 로고    scopus 로고
    • Application of fragment screening and merging to the discovery of inhibitors of the Mycobacterium tuberculosis cytochrome P450 CYP121
    • Hudson, S.A. et al. Application of fragment screening and merging to the discovery of inhibitors of the Mycobacterium tuberculosis cytochrome P450 CYP121. Angew. Chem. Int. Ed. 51, 9311-9316 (2012).
    • (2012) Angew. Chem. Int. Ed , vol.51 , pp. 9311-9316
    • Hudson, S.A.1
  • 7
    • 20444451242 scopus 로고    scopus 로고
    • The discovery of novel protein kinase inhibitors by using fragment-based high-throughput X-ray crystallography
    • DOI 10.1002/cbic.200400188
    • Gill, A., Cleasby, A. & Jhoti, H. The discovery of novel protein kinase inhibitors by using fragment-based high-throughput X-ray crystallography. Chembiochem. 6, 506-512 (2005). (Pubitemid 40868138)
    • (2005) ChemBioChem , vol.6 , Issue.3 , pp. 506-512
    • Gill, A.1    Cleasby, A.2    Jhoti, H.3
  • 9
    • 77951137401 scopus 로고    scopus 로고
    • A fragment-based approach to identifying ligands for riboswitches
    • Chen, L., Cressina, E., Leeper, F.J., Smith, A.G. & Abell, C. A fragment-based approach to identifying ligands for riboswitches. ACS Chem. Biol. 5, 355-358 (2010).
    • (2010) ACS Chem. Biol , vol.5 , pp. 355-358
    • Chen, L.1    Cressina, E.2    Leeper, F.J.3    Smith, A.G.4    Abell, C.5
  • 11
    • 84873433440 scopus 로고    scopus 로고
    • Using a fragment-based approach to target protein-protein interactions
    • Scott, D.E. et al. Using a fragment-based approach to target protein-protein interactions. Chembiochem. 14, 332-342 (2013).
    • (2013) Chembiochem , vol.14 , pp. 332-342
    • Scott, D.E.1
  • 12
    • 80053901141 scopus 로고    scopus 로고
    • FDA approves vemurafenib for treatment of metastatic melanoma
    • FDA approves vemurafenib for treatment of metastatic melanoma. Oncology 25, 906 (2011).
    • (2011) Oncology , vol.25 , pp. 906
  • 13
    • 84874414338 scopus 로고    scopus 로고
    • Fragment-based lead discovery grows up
    • Baker, M. Fragment-based lead discovery grows up. Nat. Rev. Drug Discov. 12, 5-7 (2012).
    • (2012) Nat. Rev. Drug Discov , vol.12 , pp. 5-7
    • Baker, M.1
  • 15
    • 67649341990 scopus 로고    scopus 로고
    • From fragment to clinical candidate - A historical perspective
    • Chessari, G. & Woodhead, A.J. From fragment to clinical candidate-a historical perspective. Drug Discov. Today 14, 668-675 (2009).
    • (2009) Drug Discov. Today , vol.14 , pp. 668-675
    • Chessari, G.1    Woodhead, A.J.2
  • 16
    • 84862869077 scopus 로고    scopus 로고
    • Fragment-based approaches in drug discovery and chemical biology
    • Scott, D.E., Coyne, A.G., Hudson, S.A. & Abell, C. Fragment-based approaches in drug discovery and chemical biology. Biochemistry 51, 4990-5003 (2012).
    • (2012) Biochemistry , vol.51 , pp. 4990-5003
    • Scott, D.E.1    Coyne, A.G.2    Hudson, S.A.3    Abell, C.4
  • 17
    • 84885516643 scopus 로고    scopus 로고
    • Ligand-observed NMR in fragment-based approaches
    • 1st edn. eds. Bertini, I., McGreevy, K.S. & Parigi, G. Wiley-VCH
    • Śledź, P., Abell, C. & Ciulli, A. Ligand-observed NMR in fragment-based approaches. in NMR of Biomolecules: Towards Mechanistic Systems Biology 1st edn. (eds. Bertini, I., McGreevy, K.S. & Parigi, G.), 265-281 (Wiley-VCH, 2012).
    • (2012) NMR of Biomolecules: Towards Mechanistic Systems Biology , pp. 265-281
    • Śledź, P.1    Abell, C.2    Ciulli, A.3
  • 18
    • 79952428084 scopus 로고    scopus 로고
    • Protein thermal shifts to identify low molecular weight fragments
    • Kranz, J.K. & Schalk-Hihi, C. Protein thermal shifts to identify low molecular weight fragments. Methods Enzymol. 493, 277-298 (2011).
    • (2011) Methods Enzymol , vol.493 , pp. 277-298
    • Kranz, J.K.1    Schalk-Hihi, C.2
  • 20
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell, T.L., Jhoti, H. & Abell, C. High-throughput crystallography for lead discovery in drug design. Nat. Rev. Drug Discov. 1, 45-54 (2002). (Pubitemid 37361403)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 21
    • 77956622674 scopus 로고    scopus 로고
    • Fragment screening by surface plasmon resonance
    • Navratilova, I. & Hopkins, A.L. Fragment screening by surface plasmon resonance. ACS Med. Chem. Lett. 1, 44-48 (2010).
    • (2010) ACS Med. Chem. Lett , vol.1 , pp. 44-48
    • Navratilova, I.1    Hopkins, A.L.2
  • 22
    • 33745652264 scopus 로고    scopus 로고
    • Applications of ESI-MS in drug discovery: Interrogation of noncovalent complexes
    • DOI 10.1038/nrd2083, PII N2083
    • 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). (Pubitemid 43971193)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.7 , pp. 585-595
    • Hofstadler, S.A.1    Sannes-Lowery, K.A.2
  • 23
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin, M.R. & Wells, J.A. Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream. Nat. Rev. Drug Discov. 3, 301-317 (2004). (Pubitemid 38499758)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 24
    • 84864400782 scopus 로고    scopus 로고
    • High-throughput interrogation of ligand binding mode using a fluorescence-based assay
    • Śledź, P., Lang, S., Stubbs, C.J. & Abell, C. High-throughput interrogation of ligand binding mode using a fluorescence-based assay. Angew. Chem. Int. Ed. 51, 7680-7683 (2012).
    • (2012) Angew. Chem. Int. Ed , vol.51 , pp. 7680-7683
    • Śledź, P.1    Lang, S.2    Stubbs, C.J.3    Abell, C.4
  • 25
    • 79954578345 scopus 로고    scopus 로고
    • From crystal packing to molecular recognition: Prediction and discovery of a binding site on the surface of polo-like kinase
    • Śledź, P. et al. From crystal packing to molecular recognition: Prediction and discovery of a binding site on the surface of polo-like kinase. Angew. Chem. Int. Ed. 50, 4003-4006 (2011).
    • (2011) Angew. Chem. Int. Ed , vol.50 , pp. 4003-4006
    • Śledź, P.1
  • 26
    • 84867010936 scopus 로고    scopus 로고
    • Using ligand-mapping simulations to design a ligand selectively targeting a cryptic surface pocket of polo-like kinase
    • Tan, Y.S. et al. Using ligand-mapping simulations to design a ligand selectively targeting a cryptic surface pocket of polo-like kinase.Angew. Chem. Int. Ed. 51, 10078-10081 (2012).
    • (2012) Angew. Chem. Int. Ed , vol.51 , pp. 10078-10081
    • Tan, Y.S.1
  • 28
    • 36549033318 scopus 로고    scopus 로고
    • Integration of fragment screening and library design
    • DOI 10.1016/j.drudis.2007.08.005, PII S1359644607003108
    • Siegal, G., Ab, E. & Schultz, J. Integration of fragment screening and library design. Drug Discov. Today 12, 1032-1039 (2007). (Pubitemid 350180558)
    • (2007) Drug Discovery Today , vol.12 , Issue.23-24 , pp. 1032-1039
    • Siegal, G.1    Ab, E.2    Schultz, J.3
  • 29
    • 79955566051 scopus 로고    scopus 로고
    • Route to three-dimensional fragments using diversity-oriented synthesis
    • Hung, A.W. et al. Route to three-dimensional fragments using diversity-oriented synthesis. Proc. Natl. Acad. Sci. USA 108, 6799-6804 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 6799-6804
    • Hung, A.W.1
  • 30
    • 84871599677 scopus 로고    scopus 로고
    • Natural-product-derived fragments for fragment-based ligand discovery
    • Over, B. et al. Natural-product-derived fragments for fragment-based ligand discovery. Nat. Chem. 5, 21-28 (2013).
    • (2013) Nat. Chem , vol.5 , pp. 21-28
    • Over, B.1
  • 31
    • 79952430797 scopus 로고    scopus 로고
    • Designing a diverse high-quality library for crystallography-based FBDD screening
    • Tounge, B.A. & Parker, M.H. Designing a diverse high-quality library for crystallography-based FBDD screening. Methods Enzymol. 493, 3-20 (2011).
    • (2011) Methods Enzymol , vol.493 , pp. 3-20
    • Tounge, B.A.1    Parker, M.H.2
  • 32
    • 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. 2, 2844-2852 (2013).
    • (2013) Bioorg. Med. Chem. Lett , vol.2 , pp. 2844-2852
    • Davis, B.J.1    Erlanson, D.A.2
  • 33
    • 34548040152 scopus 로고    scopus 로고
    • High throughput solubility measurement in drug discovery and development
    • DOI 10.1016/j.addr.2007.05.007, PII S0169409X07000786
    • Alsenz, J. & Kansy, M. High throughput solubility measurement in drug discovery and development. Adv. Drug Delivery Rev. 59, 546-567 (2007). (Pubitemid 47285404)
    • (2007) Advanced Drug Delivery Reviews , vol.59 , Issue.7 , pp. 546-567
    • Alsenz, J.1    Kansy, M.2
  • 34
    • 0842295943 scopus 로고    scopus 로고
    • The effect of freeze/thaw cycles on the stability of compounds in DMSO
    • Kozikowski, B.A. et al. The effect of freeze/thaw cycles on the stability of compounds in DMSO. J. Biomol. Screen 8, 210-215 (2003).
    • (2003) J. Biomol. Screen , vol.8 , pp. 210-215
    • Kozikowski, B.A.1
  • 35
    • 0030726361 scopus 로고    scopus 로고
    • PH and temperature-induced molten globule-like denatured states of equinatoxin II: A study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence
    • DOI 10.1021/bi971719v
    • Poklar, N., Lah, J., Salobir, M., Macek, P. & Vesnaver, G. pH and temperature-induced molten globule-like denatured states of equinatoxin II: A study by UV-melting, DSC, far-and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry 36, 14345-14352 (1997). (Pubitemid 27509926)
    • (1997) Biochemistry , vol.36 , Issue.47 , pp. 14345-14352
    • Poklar, N.1    Lah, J.2    Salobir, M.3    Macek, P.4    Vesnaver, G.5
  • 37
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • DOI 10.1016/j.ab.2004.04.031, PII S0003269704003756
    • Lo, M.-C. et al. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 332, 153-159 (2004). (Pubitemid 39099482)
    • (2004) Analytical Biochemistry , vol.332 , Issue.1 , pp. 153-159
    • Lo, M.-C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 38
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • DOI 10.1038/nprot.2007.321, PII NPROT.2007.321
    • 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). (Pubitemid 351565860)
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 39
  • 40
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • DOI 10.1016/j.ab.2006.07.027, PII S0003269706005355
    • Ericsson, U.B., Hallberg, B.M., Detitta, G.T., Dekker, N. & Nordlund, P. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357, 289-298 (2006). (Pubitemid 44430091)
    • (2006) Analytical Biochemistry , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 42
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • DOI 10.1126/science.274.5292.1531
    • 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). (Pubitemid 26403929)
    • (1996) Science , vol.274 , Issue.5292 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 43
    • 4344711355 scopus 로고    scopus 로고
    • Theory and applications of NMR-based screening in pharmaceutical research
    • Lepre, C.A., Moore, J.M. & Peng, J.W. Theory and applications of NMR-based screening in pharmaceutical research. Chem. Rev. 104, 3641-3676 (2004).
    • (2004) Chem. Rev , vol.104 , pp. 3641-3676
    • Lepre, C.A.1    Moore, J.M.2    Peng, J.W.3
  • 44
    • 35348922285 scopus 로고    scopus 로고
    • Fragment-based screening using X-ray crystallography and NMR spectroscopy
    • DOI 10.1016/j.cbpa.2007.07.010, PII S1367593107001032
    • Jhoti, H., Cleasby, A., Verdonk, M. & Williams, G. Fragment-based screening using X-ray crystallography and NMR spectroscopy. Curr. Opin. Chem. Biol. 11, 485-493 (2007). (Pubitemid 47588996)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.5 , pp. 485-493
    • Jhoti, H.1    Cleasby, A.2    Verdonk, M.3    Williams, G.4
  • 45
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • DOI 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0. CO;2-Q
    • Mayer, M. & Meyer, B. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem. Int. Ed. 38, 1784-1788 (1999). (Pubitemid 29290947)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 46
    • 0035692794 scopus 로고    scopus 로고
    • WaterLOGSY as a method for primary NMR screening: Practical aspects and range of applicability
    • DOI 10.1023/A:1013302231549
    • Dalvit, C., Fogliatto, G., Stewart, A., Veronesi, M. & Stockman, B. WaterLOGSY as a method for primary NMR screening: Practical aspects and range of applicability. J. Biomol. NMR 21, 349-359 (2001). (Pubitemid 34071389)
    • (2001) Journal of Biomolecular NMR , vol.21 , Issue.4 , pp. 349-359
    • Dalvit, C.1    Fogliatto, G.2    Stewart, A.3    Veronesi, M.4    Stockman, B.5
  • 47
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr, Y.H. & Purcell, M.E. Effects of diffusion on free precession in nuclear magnetic resonance experiments. Phys. Rev. 94, 630-638 (1954).
    • (1954) Phys. Rev , vol.94 , pp. 630-638
    • Carr, Y.H.1    Purcell, M.E.2
  • 48
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear relaxation times
    • Meiboom, S. & Gill, D. Modified spin-echo method for measuring nuclear relaxation times. Rev. Sci. Instrum. 29, 688-691 (1958).
    • (1958) Rev. Sci. Instrum , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 49
    • 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
  • 50
    • 70350422335 scopus 로고    scopus 로고
    • NMR methods in fragment screening: Theory and a comparison with other biophysical techniques
    • Dalvit, C. NMR methods in fragment screening: Theory and a comparison with other biophysical techniques. Drug Discov. Today 14, 1051-1057 (2009).
    • (2009) Drug Discov. Today , vol.14 , pp. 1051-1057
    • Dalvit, C.1
  • 51
    • 82455212567 scopus 로고    scopus 로고
    • STD-NMR: Application to transient interactions between biomolecules - A quantitative approach
    • Angulo, J. & Nieto, P.M. STD-NMR: Application to transient interactions between biomolecules-a quantitative approach. Eur. Biophys. J. 40, 1357-1369 (2011).
    • (2011) Eur. Biophys. J , vol.40 , pp. 1357-1369
    • Angulo, J.1    Nieto, P.M.2
  • 52
    • 0033789206 scopus 로고    scopus 로고
    • Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water
    • Dalvit, C. et al. Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water. J. Biomol. NMR 18, 65-68 (2000).
    • (2000) J. Biomol. NMR , vol.18 , pp. 65-68
    • Dalvit, C.1
  • 53
    • 0031576702 scopus 로고    scopus 로고
    • One-dimensional relaxation- and diffusion-edited NMR methods for screening compounds that bind to macromolecules
    • DOI 10.1021/ja9715962
    • Hajduk, P.J., Olejniczak, E.T. & Fesik, S.W. One-dimensional relaxation-and diffusion-edited NMR methods for screening compounds that bind to macromolecules. J. Am. Chem. Soc. 119, 12257-12261 (1997). (Pubitemid 28078713)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.50 , pp. 12257-12261
    • Hajduk, P.J.1    Olejniczak, E.T.2    Fesik, S.W.3
  • 54
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • DOI 10.1016/S0959-440X(00)00248-7
    • Leavitt, S. & Freire, E. Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr. Opin. Struct. Biol. 11, 560-566 (2001). (Pubitemid 32972017)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.5 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 55
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • DOI 10.1021/ja036166s
    • Turnbull, W.B. & Daranas, A.H. On the value of c: Can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125, 14859-14866 (2003). (Pubitemid 37475576)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.48 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 56
    • 21344447247 scopus 로고    scopus 로고
    • Isothermal titration calorimetry
    • Lewis, E.A. & Murphy, K.P. Isothermal titration calorimetry. Methods Mol. Biol. 305, 1-16 (2005).
    • (2005) Methods Mol. Biol , vol.305 , pp. 1-16
    • Lewis, E.A.1    Murphy, K.P.2
  • 57
    • 77955971738 scopus 로고    scopus 로고
    • Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design
    • Ladbury, J.E. Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design. Biochem. Soc. Trans. 38, 888-893 (2010).
    • (2010) Biochem. Soc. Trans , vol.38 , pp. 888-893
    • Ladbury, J.E.1
  • 58
    • 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
  • 59
    • 77950816491 scopus 로고    scopus 로고
    • Optimization of the interligand Overhauser effect for fragment linking: Application to inhibitor discovery against Mycobacterium tuberculosis pantothenate synthetase
    • Śledź, P. et al. Optimization of the interligand Overhauser effect for fragment linking: Application to inhibitor discovery against Mycobacterium tuberculosis pantothenate synthetase. J. Am. Chem. Soc. 132, 4544-4545 (2012).
    • (2012) J. Am. Chem. Soc , vol.132 , pp. 4544-4545
    • Śledź, P.1
  • 60
    • 0013882603 scopus 로고
    • Hydrogen ion buffers for biological research
    • Good, N.E. et al. Hydrogen ion buffers for biological research. Biochemistry 5, 467-477 (1966).
    • (1966) Biochemistry , vol.5 , pp. 467-477
    • Good, N.E.1
  • 61
    • 79960698472 scopus 로고
    • Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients
    • Hwang, T.L. & Shaka, A.J. Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients. J. Magn. Reson. Ser. A 112, 275-279 (1995).
    • (1995) J Magn Reson Ser A , vol.112 , pp. 275-279
    • Hwang, T.L.1    Shaka, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.