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Volumn 11, Issue 8, 2016, Pages 1414-1427

Protein-observed 19F-NMR for fragment screening, affinity quantification and druggability assessment

Author keywords

[No Author keywords available]

Indexed keywords

BRD4 PROTEIN; BRDT PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; KIX PROTEIN; PEPTIDES AND PROTEINS; UNCLASSIFIED DRUG; DRUG; LIGAND; PROTEIN;

EID: 84979955137     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2016.079     Document Type: Article
Times cited : (75)

References (60)
  • 1
    • 79952428086 scopus 로고    scopus 로고
    • Practical aspects of NMR-based fragment screening
    • Lepre, C.A. Practical aspects of NMR-based fragment screening. Methods Enzymol. 493, 219-239 (2011
    • (2011) Methods Enzymol , vol.493 , pp. 219-239
    • Lepre, C.A.1
  • 2
    • 0344012137 scopus 로고    scopus 로고
    • Apintu General NMR method for rapid efficient, and reliable biochemical screening
    • Dalvit, C., et al. Apintu General NMR method for rapid, efficient, and reliable biochemical screening. J. Am. Chem. Soc. 125, 14620-14625 (2003
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 14620-14625
    • Dalvit, C.1
  • 3
    • 0037256228 scopus 로고    scopus 로고
    • NMR methods for the determination of protein-ligand dissociation constants
    • Fielding, L. NMR methods for the determination of protein-ligand dissociation constants. Curr. Top. Med. Chem. 3, 39-53 (2003
    • (2003) Curr. Top. Med. Chem , vol.3 , pp. 39-53
    • Fielding, L.1
  • 4
    • 84880167453 scopus 로고    scopus 로고
    • Using chemical shift perturbation to characterise ligand binding
    • Williamson, M.P. Using chemical shift perturbation to characterise ligand binding. Prog. Nucl. Magn. Reson. Spectrosc. 73, 1-16 (2013
    • (2013) Prog. Nucl. Magn. Reson. Spectrosc , vol.73 , pp. 1-16
    • Williamson, M.P.1
  • 5
    • 79851483555 scopus 로고    scopus 로고
    • Apintu Practical use of ligand efficiency indices out of the fragment-based approach: Ligand efficiency-guided lead identification of soluble epoxide hydrolase inhibitors
    • Tanaka D., et al. Apintu Practical use of ligand efficiency indices out of the fragment-based approach: ligand efficiency-guided lead identification of soluble epoxide hydrolase inhibitors. J. Med. Chem. 54, 851-857 (2010
    • (2010) J. Med. Chem , vol.54 , pp. 851-857
    • Tanaka, D.1
  • 7
    • 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
  • 9
    • 84868481873 scopus 로고    scopus 로고
    • Vemurafenib: The first drug approved for BRAF-mutant cancer
    • Bollag G., et al. Vemurafenib: the first drug approved for BRAF-mutant cancer. Nat. Rev. Drug Discov. 11, 873-886 (2012
    • (2012) Nat. Rev. Drug Discov , vol.11 , pp. 873-886
    • Bollag, G.1
  • 10
    • 33847381100 scopus 로고    scopus 로고
    • Apintu decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk, P.J., & Greer, J. Apintu 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
  • 11
    • 84974626866 scopus 로고    scopus 로고
    • Protein-observed fluorine NMR: A bioorthogonal approach for small molecule discovery
    • Arntson, K.E., & Pomerantz, W.C.K. Protein-observed fluorine NMR: a bioorthogonal approach for small molecule discovery. J. Med. Chem. 59, 5158-5171 (2016
    • (2016) J. Med. Chem , vol.59 , pp. 5158-5171
    • Arntson, K.E.1    Pomerantz, W.C.K.2
  • 12
    • 84857625337 scopus 로고    scopus 로고
    • Current applications of 19F NMR to studies of protein structure and dynamics
    • Kitevski-LeBlanc, J.L., & Prosser, R.S. Current applications of 19F NMR to studies of protein structure and dynamics. Prog. Nucl. Magn. Reson. Spectrosc. 62, 1-33 (2012
    • (2012) Prog. Nucl. Magn. Reson. Spectrosc , vol.62 , pp. 1-33
    • Kitevski-LeBlanc, J.L.1    Prosser, R.S.2
  • 13
    • 84947487324 scopus 로고    scopus 로고
    • 19)F-Modified proteins and (19)F-containing ligands as tools in solution NMR studies of protein interactions
    • Sharaf N.G., & Gronenborn, A.M. (19)F-Modified proteins and (19)F-containing ligands as tools in solution NMR studies of protein interactions. Methods Enzymol. 565, 67-95 2015
    • (2015) Methods Enzymol , vol.565 , pp. 67-95
    • Sharaf, N.G.1    Gronenborn, A.M.2
  • 15
    • 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
  • 16
    • 84891897444 scopus 로고    scopus 로고
    • Design and evaluation of the performance of an NMR screening fragment library
    • Doak, B.C., Morton, C.J., Simpson, J.S., & Scanlon, M.J. Design and evaluation of the performance of an NMR screening fragment library. Aust. J. Chem. 66, 1465-1472 (2013
    • (2013) Aust. J. Chem , vol.66 , pp. 1465-1472
    • Doak, B.C.1    Morton, C.J.2    Simpson, J.S.3    Scanlon, M.J.4
  • 17
    • 36549033318 scopus 로고    scopus 로고
    • Integration of fragment screening and library design
    • Siegal, G., Ab, E., & Schultz, J. Integration of fragment screening and library design. Drug Discov. Today 12, 1032-1039 (2007
    • (2007) Drug Discov. Today , vol.12 , pp. 1032-1039
    • Siegal, G.1    Ab, E.2    Schultz, J.3
  • 18
    • 84891896449 scopus 로고    scopus 로고
    • Development of inhibitors of Plasmodium falciparum apical membrane antigen 1 based on fragment screening
    • Lim S.S., et al. Development of inhibitors of Plasmodium falciparum apical membrane antigen 1 based on fragment screening. Aust. J. Chem. 66, 1530 (2013
    • (2013) Aust. J. Chem , vol.66 , pp. 1530
    • Lim, S.S.1
  • 19
    • 84891893976 scopus 로고    scopus 로고
    • Detection and prevention of aggregation-based false positives in STD-NMR-based fragment screening
    • Vom A., et al. Detection and prevention of aggregation-based false positives in STD-NMR-based fragment screening. Aust. J. Chem. 66, 1518 (2013
    • (2013) Aust. J. Chem , vol.66 , pp. 1518
    • Vom, A.1
  • 20
    • 0038207989 scopus 로고    scopus 로고
    • Fluorine-NMR experiments for high-Throughput screening: Theoretical aspects, practical considerations, and range of applicability
    • Dalvit, C., Fagerness, P.E., Hadden, D.T., Sarver, R.W., & Stockman, B.J. Fluorine-NMR experiments for high-Throughput screening: theoretical aspects, practical considerations, and range of applicability. J. Am. Chem. Soc. 125, 7696-7703 (2003
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 7696-7703
    • Dalvit, C.1    Fagerness, P.E.2    Hadden, D.T.3    Sarver, R.W.4    Stockman, B.J.5
  • 21
    • 84892581838 scopus 로고    scopus 로고
    • Is NMR fragment screening fine-Tuned to assess druggability of protein-protein interactions?
    • Dias D.M., et al. Is NMR fragment screening fine-Tuned to assess druggability of protein-protein interactions? ACS Med. Chem. Lett. 5, 23-28 (2013
    • (2013) ACS Med. Chem. Lett , vol.5 , pp. 23-28
    • Dias, D.M.1
  • 22
    • 84865263199 scopus 로고    scopus 로고
    • Profiling the dynamic interfaces of fluorinated transcription complexes for ligand discovery and characterization
    • Pomerantz W.C., et al. Profiling the dynamic interfaces of fluorinated transcription complexes for ligand discovery and characterization. ACS Chem. Biol. 7, 1345-1350 (2012
    • (2012) ACS Chem. Biol , vol.7 , pp. 1345-1350
    • Pomerantz, W.C.1
  • 23
    • 84924373564 scopus 로고    scopus 로고
    • Fragment screening and druggability assessment for the CBP/p300 KIX domain through protein-observed 19F NMR spectroscopy
    • Gee, C.T., Koleski, E.J., & Pomerantz, W.C. Fragment screening and druggability assessment for the CBP/p300 KIX domain through protein-observed 19F NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 54, 3735-3739 (2015
    • (2015) Angew. Chem. Int. Ed. Engl , vol.54 , pp. 3735-3739
    • Gee, C.T.1    Koleski, E.J.2    Pomerantz, W.C.3
  • 24
    • 84908073324 scopus 로고    scopus 로고
    • 19F NMR as a probe of ligand interactions with the iNOS binding site of SPRY domain-containing SOCS box protein 2
    • Leung E.W., et al. 19F NMR as a probe of ligand interactions with the iNOS binding site of SPRY domain-containing SOCS box protein 2. Chem. Biol. Drug Des. 84, 616-625 (2014
    • (2014) Chem Biol. Drug des , vol.84 , pp. 616-625
    • Leung, E.W.1
  • 25
    • 84906076014 scopus 로고    scopus 로고
    • Ligand-induced conformational change of Plasmodium falciparum AMA1 detected using 19F NMR
    • Ge X., et al. Ligand-induced conformational change of Plasmodium falciparum AMA1 detected using 19F NMR. J. Med. Chem. 57, 6419-6427 (2014
    • (2014) J. Med. Chem , vol.57 , pp. 6419-6427
    • Ge, X.1
  • 26
    • 84901271098 scopus 로고    scopus 로고
    • 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b?x from human protein disulphide isomerase (hPDI
    • Curtis-Marof R., et al. 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b?x from human protein disulphide isomerase (hPDI). Org. Biomol. Chem. 12, 3808-3812 (2014
    • (2014) Org Biomol. Chem , vol.12 , pp. 3808-3812
    • Curtis-Marof, R.1
  • 27
    • 84919675043 scopus 로고    scopus 로고
    • Fluorinated aromatic amino acids are sensitive 19F NMR probes for bromodomain-ligand interactions
    • Mishra, N.K., Urick, A.K., Ember, S.W., Schonbrunn, E., & Pomerantz, W.C. Fluorinated aromatic amino acids are sensitive 19F NMR probes for bromodomain-ligand interactions. ACS Chem. Biol. 9, 2755-2760 (2014
    • (2014) ACS Chem. Biol , vol.9 , pp. 2755-2760
    • Mishra, N.K.1    Urick, A.K.2    Ember, S.W.3    Schonbrunn, E.4    Pomerantz, W.C.5
  • 28
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in beta(2)-Adrenergic receptor characterized by F-19-NMR
    • Liu, J.J., Horst, R., Katritch, V., Stevens, R.C., & Wuthrich, K. Biased signaling pathways in beta(2)-Adrenergic receptor characterized by F-19-NMR. Science 335, 1106-1110 (2012
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wuthrich, K.5
  • 29
    • 33646160625 scopus 로고    scopus 로고
    • Structural studies of Bcl-xL/ligand complexes using 19F NMR
    • Yu, L., Hajduk, P.J., Mack, J., & Olejniczak, E.T. Structural studies of Bcl-xL/ligand complexes using 19F NMR. J. Biomol. NMR 34, 221-227 (2006
    • (2006) J. Biomol. NMR , vol.34 , pp. 221-227
    • Yu, L.1    Hajduk, P.J.2    Mack, J.3    Olejniczak, E.T.4
  • 30
    • 84944769253 scopus 로고    scopus 로고
    • Dual screening of BPTF and Brd4 using protein-observed fluorine NMR Uncovers new bromodomain probe molecules
    • Urick A.K. et al. Dual screening of BPTF and Brd4 using protein-observed fluorine NMR Uncovers new bromodomain probe molecules. ACS Chem. Biol. 10 2246-2256 2015
    • (2015) ACS Chem. Biol , vol.10 , pp. 2246-2256
    • Urick, A.K.1
  • 31
    • 10744222300 scopus 로고    scopus 로고
    • RAMPED-UP NMR: Multiplexed NMR-based screening for drug discovery
    • Zartler E.R., et al. RAMPED-UP NMR: multiplexed NMR-based screening for drug discovery. J. Am. Chem. Soc. 125, 10941-10946 (2003
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 10941-10946
    • Zartler, E.R.1
  • 32
    • 0013283113 scopus 로고
    • Fluorotyrosine alkaline phosphatase from Escherichia coli: Preparation, properties, and fluorine-19 nuclear magnetic resonance spectrum
    • Sykes, B.D., Weingarten, H.I., & Schlesinger, M.J. Fluorotyrosine alkaline phosphatase from Escherichia coli: preparation, properties, and fluorine-19 nuclear magnetic resonance spectrum. Proc. Natl. Acad. Sci. USA 71, 469-473 (1974
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 469-473
    • Sykes, B.D.1    Weingarten, H.I.2    Schlesinger, M.J.3
  • 33
    • 1542379799 scopus 로고    scopus 로고
    • The preparation of 19F-labeled proteins for NMR studies
    • eds. Michael L., Johnson Jo M. Holt & K. Ackers Gary) (Academic Press, 2004
    • Frieden, C., Hoeltzli, S.D., & Bann, J.G. The preparation of 19F-labeled proteins for NMR studies. in Methods Enzymol. Vol. 380 (eds. Michael, L., Johnson Jo M. Holt & K. Ackers Gary) 400-415 (Academic Press, 2004
    • Methods Enzymol , vol.380 , pp. 400-415
    • Frieden, C.1    Hoeltzli, S.D.2    Bann, J.G.3
  • 34
    • 84867301057 scopus 로고    scopus 로고
    • Simple and inexpensive incorporation of 19F-Tryptophan for protein NMR spectroscopy
    • Crowley, P.B., Kyne, C., & Monteith, W.B. Simple and inexpensive incorporation of 19F-Tryptophan for protein NMR spectroscopy. Chem. Commun. 48, 10681-10683 (2012
    • (2012) Chem. Commun , vol.48 , pp. 10681-10683
    • Crowley, P.B.1    Kyne, C.2    Monteith, W.B.3
  • 35
    • 84887940786 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitor dinaciclib interacts with the acetyl-lysine recognition site of bromodomains
    • Martin, M.P., Olesen, S.H., Georg, G.I., & Schönbrunn, E. Cyclin-dependent kinase inhibitor dinaciclib interacts with the acetyl-lysine recognition site of bromodomains. ACS Chem. Biol. 8, 2360-2365 (2013
    • (2013) ACS Chem. Biol , vol.8 , pp. 2360-2365
    • Martin, M.P.1    Olesen, S.H.2    Georg, G.I.3    Schönbrunn, E.4
  • 36
    • 0010478921 scopus 로고
    • The NMR time scale
    • Bryant, R.G. The NMR time scale. J. Chem. Educ. 60, 933 (1983
    • (1983) J. Chem. Educ , vol.60 , pp. 933
    • Bryant, R.G.1
  • 37
    • 33947475965 scopus 로고
    • Apintu proton magnetic resonance study of hindered internal rotation in some substituted N, N-dimethylamides
    • Rogers, M.T., & Woodbrey, J.C. Apintu proton magnetic resonance study of hindered internal rotation in some substituted N, N-dimethylamides. J. Phys. Chem. 66, 540-546 (1962
    • (1962) J. Phys. Chem , vol.66 , pp. 540-546
    • Rogers, M.T.1    Woodbrey, J.C.2
  • 38
    • 0016697706 scopus 로고
    • Fluorotyrosine alkaline phosphatase: Internal mobility of individual tyrosines and the role of chemical shift anisotropy as a 19F nuclear spin relaxation mechanism in proteins
    • Hull, W.E., & Sykes, B.D. Fluorotyrosine alkaline phosphatase: internal mobility of individual tyrosines and the role of chemical shift anisotropy as a 19F nuclear spin relaxation mechanism in proteins. J. Mol. Biol. 98, 121-153 (1975
    • (1975) J. Mol. Biol , vol.98 , pp. 121-153
    • Hull, W.E.1    Sykes, B.D.2
  • 39
    • 0024539619 scopus 로고
    • Membrane-bound D-lactate dehydrogenase of Escherichia coli: A model for protein interactions in membranes
    • Ho, C., Pratt, E.A., & Rule, G.S. Membrane-bound D-lactate dehydrogenase of Escherichia coli: a model for protein interactions in membranes. Biochim. Biophys. Acta 988, 173-184 (1989
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 173-184
    • Ho, C.1    Pratt, E.A.2    Rule, G.S.3
  • 40
    • 0033598692 scopus 로고    scopus 로고
    • NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: Applicability of solution 19F NMR
    • Klein-Seetharaman, J., Getmanova, E.V., Loewen, M.C., Reeves, P.J., & Khorana, H.G. NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: applicability of solution 19F NMR. Proc. Natl. Acad. Sci. USA 96, 13744-13749 (1999
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13744-13749
    • Klein-Seetharaman, J.1    Getmanova, E.V.2    Loewen, M.C.3    Reeves, P.J.4    Khorana, H.G.5
  • 41
    • 84867793026 scopus 로고    scopus 로고
    • Role of detergents in conformational exchange of a G protein-coupled receptor
    • Chung K.Y., et al. Role of detergents in conformational exchange of a G protein-coupled receptor. J. Biol. Chem. 287, 36305-36311 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 36305-36311
    • Chung, K.Y.1
  • 42
    • 84875459494 scopus 로고    scopus 로고
    • Resolution of oligomeric species during the aggregation of Abeta1-40 using (19)F NMR
    • Suzuki Y., et al. Resolution of oligomeric species during the aggregation of Abeta1-40 using (19)F NMR. Biochemistry 52, 1903-1912 (2013
    • (2013) Biochemistry , vol.52 , pp. 1903-1912
    • Suzuki, Y.1
  • 43
    • 74849140345 scopus 로고    scopus 로고
    • Protein (19)F NMR in Escherichia coli
    • Li C., et al. Protein (19)F NMR in Escherichia coli. J. Am. Chem. Soc. 132, 321 (2010
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 321
    • Li, C.1
  • 44
    • 38449084295 scopus 로고    scopus 로고
    • Preparation of site-specifically labeled fluorinated proteins for 19F-NMR structural characterization
    • Hammill, J.T., Miyake-Stoner, S., Hazen, J.L., Jackson, J.C., & Mehl, R.A. Preparation of site-specifically labeled fluorinated proteins for 19F-NMR structural characterization. Nat. Protoc. 2, 2601-2607 (2007
    • (2007) Nat. Protoc , vol.2 , pp. 2601-2607
    • Hammill, J.T.1    Miyake-Stoner, S.2    Hazen, J.L.3    Jackson, J.C.4    Mehl, R.A.5
  • 45
    • 0141454913 scopus 로고    scopus 로고
    • 19)F NMR studies of the leucine-isoleucine-valine binding protein: Evidence that a closed conformation exists in solution
    • Salopek-Sondi, B., Vaughan, M.D., Skeels, M.C., Honek, J.F., & Luck, L.A. (19)F NMR studies of the leucine-isoleucine-valine binding protein: evidence that a closed conformation exists in solution. J. Biomol. Struct. Dyn. 21, 235-246 (2003
    • (2003) J. Biomol Struct. Dyn , vol.21 , pp. 235-246
    • Salopek-Sondi, B.1    Vaughan, M.D.2    Skeels, M.C.3    Honek, J.F.4    Luck, L.A.5
  • 46
    • 0030939030 scopus 로고    scopus 로고
    • Incorporation of trifluoromethionine into a phage lysozyme: Implications and a new marker for use in protein 19F NMR
    • Duewel, H., Daub, E., Robinson, V., & Honek, J.F. Incorporation of trifluoromethionine into a phage lysozyme: implications and a new marker for use in protein 19F NMR. Biochemistry 36, 3404-3416 (1997
    • (1997) Biochemistry , vol.36 , pp. 3404-3416
    • Duewel, H.1    Daub, E.2    Robinson, V.3    Honek, J.F.4
  • 47
    • 0035823858 scopus 로고    scopus 로고
    • Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host
    • Tang, Y., & Tirrell, D.A. Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host. J. Am. Chem. Soc. 123, 11089-11090 (2001
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 11089-11090
    • Tang, Y.1    Tirrell, D.A.2
  • 48
    • 0035814931 scopus 로고    scopus 로고
    • Stabilization of coiled-coil peptide domains by introduction of trifluoroleucine
    • Tang Y., et al. Stabilization of coiled-coil peptide domains by introduction of trifluoroleucine. Biochemistry 40, 2790-2796 (2001
    • (2001) Biochemistry , vol.40 , pp. 2790-2796
    • Tang, Y.1
  • 49
    • 30744471668 scopus 로고    scopus 로고
    • Modulating protein structure with fluorous amino acids: Increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine
    • Lee, H.Y., Lee, K.H., Al-Hashimi, H.M., & Marsh, E.N. Modulating protein structure with fluorous amino acids: increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine. J. Am. Chem. Soc. 128, 337-343 (2006
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 337-343
    • Lee, H.Y.1    Lee, K.H.2    Al-Hashimi, H.M.3    Marsh, E.N.4
  • 50
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A.A., & Thorn, K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9 (1998
    • (1998) J. Mol. Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 51
    • 17144373303 scopus 로고    scopus 로고
    • Druggability indices for protein targets derived from NMR-based screening data
    • Hajduk, P.J., Huth, J.R., & Fesik, S.W. Druggability indices for protein targets derived from NMR-based screening data. J. Med. Chem. 48, 2518-2525 (2005
    • (2005) J. Med. Chem , vol.48 , pp. 2518-2525
    • Hajduk, P.J.1    Huth, J.R.2    Fesik, S.W.3
  • 52
    • 84895094959 scopus 로고    scopus 로고
    • FP tethering: A screening technique to rapidly identify compounds that disrupt protein-protein interactions
    • Lodge, J.M., Justin Rettenmaier, T., Wells, J.A., Pomerantz, W.C., & Mapp, A.K. FP tethering: a screening technique to rapidly identify compounds that disrupt protein-protein interactions. Medchemcomm. 5, 370-375 (2014
    • (2014) Medchemcomm , vol.5 , pp. 370-375
    • Lodge, J.M.1    Justin Rettenmaier, T.2    Wells, J.A.3    Pomerantz, W.C.4    Mapp, A.K.5
  • 53
    • 0025093242 scopus 로고
    • The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate Application to fluorotryptophan labelling to the H(+)-ATPase of Escherichia coli and NMR studies
    • Kim, H.W., Perez, J.A., Ferguson, S.J., & Campbell, I.D. The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate. Application to fluorotryptophan labelling to the H(+)-ATPase of Escherichia coli and NMR studies. FEBS Lett. 272, 34-36 (1990
    • (1990) FEBS Lett , vol.272 , pp. 34-36
    • Kim, H.W.1    Perez, J.A.2    Ferguson, S.J.3    Campbell, I.D.4
  • 54
    • 0034681157 scopus 로고    scopus 로고
    • Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: A (19)F-NMR study
    • Bai, P., Luo, L., & Peng, Z. Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study. Biochemistry 39, 372-380 (2000
    • (2000) Biochemistry , vol.39 , pp. 372-380
    • Bai, P.1    Luo, L.2    Peng, Z.3
  • 55
    • 20444397413 scopus 로고    scopus 로고
    • Quantitation of protein expression in a cell-free system: Efficient detection of yields and 19F NMR to identify folded protein
    • Neerathilingam, M., Greene, L.H., Colebrooke, S.A., Campbell, I.D., & Staunton, D. Quantitation of protein expression in a cell-free system: efficient detection of yields and 19F NMR to identify folded protein. J. Biomol. NMR 31, 11-19 (2005
    • (2005) J. Biomol. NMR , vol.31 , pp. 11-19
    • Neerathilingam, M.1    Greene, L.H.2    Colebrooke, S.A.3    Campbell, I.D.4    Staunton, D.5
  • 56
    • 0033169005 scopus 로고    scopus 로고
    • Concentration measurement by proton NMR using the ERETIC method
    • Akoka, S., Barantin, L., & Trierweiler, M. Concentration measurement by proton NMR using the ERETIC method. Anal. Chem. 71, 2554-2557 (1999
    • (1999) Anal. Chem , vol.71 , pp. 2554-2557
    • Akoka, S.1    Barantin, L.2    Trierweiler, M.3
  • 57
    • 25444475544 scopus 로고    scopus 로고
    • Sensitivity improvement in 19F NMR-based screening experiments: Theoretical considerations and experimental applications
    • Dalvit C., et al. Sensitivity improvement in 19F NMR-based screening experiments: theoretical considerations and experimental applications. J. Am. Chem. Soc. 127, 13380-13385 (2005
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 13380-13385
    • Dalvit, C.1
  • 58
    • 32244442013 scopus 로고    scopus 로고
    • Mono-, di-, tri-, and tetra-substituted fluorotyrosines: New probes for enzymes that use tyrosyl radicals in catalysis
    • Seyedsayamdost, M.R., Reece, S.Y., Nocera, D.G., & Stubbe, J. Mono-, di-, tri-, and tetra-substituted fluorotyrosines: new probes for enzymes that use tyrosyl radicals in catalysis. J. Am. Chem. Soc. 128, 1569-1579 (2006
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 1569-1579
    • Seyedsayamdost, M.R.1    Reece, S.Y.2    Nocera, D.G.3    Stubbe, J.4
  • 59
    • 0031937870 scopus 로고    scopus 로고
    • Expansion of the genetic code: Site-directed p-fluoro-phenylalanine incorporation in Escherichia coli
    • Furter, R. Expansion of the genetic code: site-directed p-fluoro-phenylalanine incorporation in Escherichia coli. Prot. Sci. 7, 419-426 (1998
    • (1998) Prot. Sci , vol.7 , pp. 419-426
    • Furter, R.1
  • 60
    • 67849121879 scopus 로고    scopus 로고
    • Apintu mutagenesis-free approach to assignment of 19F NMR resonances in biosynthetically labeled proteins
    • Kitevski-LeBlanc, J.L., Al-Abdul-Wahid, M.S., & Prosser, R.S. Apintu mutagenesis-free approach to assignment of 19F NMR resonances in biosynthetically labeled proteins. J. Am. Chem. Soc. 131, 2054-2055 (2009
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 2054-2055
    • Kitevski-LeBlanc, J.L.1    Al-Abdul-Wahid, M.S.2    Prosser, R.S.3


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