메뉴 건너뛰기




Volumn 59, Issue 11, 2016, Pages 5158-5171

Protein-Observed Fluorine NMR: A Bioorthogonal Approach for Small Molecule Discovery

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; LIGAND; PROTEIN; FLUORINE; MOLECULAR LIBRARY;

EID: 84974626866     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.5b01447     Document Type: Review
Times cited : (141)

References (109)
  • 1
    • 4544278491 scopus 로고    scopus 로고
    • Organic fluorine: Odd man out
    • Dunitz, J. D. Organic fluorine: odd man out ChemBioChem 2004, 5, 614-621 10.1002/cbic.200300801
    • (2004) ChemBioChem , vol.5 , pp. 614-621
    • Dunitz, J.D.1
  • 2
    • 0346731129 scopus 로고    scopus 로고
    • Perspective on fluorocarbon chemistry
    • Lemal, D. M. Perspective on fluorocarbon chemistry J. Org. Chem. 2004, 69, 1-11 10.1021/jo0302556
    • (2004) J. Org. Chem. , vol.69 , pp. 1-11
    • Lemal, D.M.1
  • 6
    • 84879554594 scopus 로고    scopus 로고
    • In vivo MRI cell tracking using perfluorocarbon probes and fluorine-19 detection
    • Ahrens, E. T.; Zhong, J. In vivo MRI cell tracking using perfluorocarbon probes and fluorine-19 detection NMR Biomed. 2013, 26, 860-871 10.1002/nbm.2948
    • (2013) NMR Biomed. , vol.26 , pp. 860-871
    • Ahrens, E.T.1    Zhong, J.2
  • 8
    • 84872855487 scopus 로고    scopus 로고
    • Hexafluorobenzene in comparison with perfluoro-15-crown-5-ether for repeated monitoring of oxygenation using 19F MRI in a mouse model
    • Mignion, L.; Magat, J.; Schakman, O.; Marbaix, E.; Gallez, B.; Jordan, B. F. Hexafluorobenzene in comparison with perfluoro-15-crown-5-ether for repeated monitoring of oxygenation using 19F MRI in a mouse model Magn. Reson. Med. 2013, 69, 248-254 10.1002/mrm.24245
    • (2013) Magn. Reson. Med. , vol.69 , pp. 248-254
    • Mignion, L.1    Magat, J.2    Schakman, O.3    Marbaix, E.4    Gallez, B.5    Jordan, B.F.6
  • 9
    • 36049036606 scopus 로고    scopus 로고
    • Ligand- and substrate-based F-19 NMR screening: Principles and applications to drug discovery
    • Dalvit, C. Ligand- and substrate-based F-19 NMR screening: Principles and applications to drug discovery Prog. Nucl. Magn. Reson. Spectrosc. 2007, 51, 243-I 10.1016/j.pnmrs.2007.07.002
    • (2007) Prog. Nucl. Magn. Reson. Spectrosc. , vol.51 , pp. 243I
    • Dalvit, C.1
  • 10
    • 0014201796 scopus 로고
    • Enzyme - Substrate interaction by nuclear magnetic resonance
    • Spotswood, T.; Evans, J. M.; Richards, J. H. Enzyme - substrate interaction by nuclear magnetic resonance J. Am. Chem. Soc. 1967, 89, 5052-5054 10.1021/ja00995a047
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 5052-5054
    • Spotswood, T.1    Evans, J.M.2    Richards, J.H.3
  • 11
    • 0016148772 scopus 로고
    • Fluorotyrosine alkaline-phosphatase- F-19 nuclear magnetic resonance relaxation times and molecular motion of individual fluorotyrosines
    • Hull, W. E.; Sykes, B. D. Fluorotyrosine alkaline-phosphatase- F-19 nuclear magnetic resonance relaxation times and molecular motion of individual fluorotyrosines Biochemistry 1974, 13, 3431-3437 10.1021/bi00714a002
    • (1974) Biochemistry , vol.13 , pp. 3431-3437
    • Hull, W.E.1    Sykes, B.D.2
  • 13
    • 84908073324 scopus 로고    scopus 로고
    • F-19 NMR as a probe of ligand interactions with the iNOS binding site of SPRY domain-containing SOCS box protein 2
    • Leung, E. W. W.; Yagi, H.; Harjani, J. R.; Mulcair, M. D.; Scanlon, M. J.; Baell, J. B.; Norton, R. S. F-19 NMR as a probe of ligand interactions with the iNOS binding site of SPRY domain-containing SOCS box protein 2 Chem. Biol. Drug Des. 2014, 84, 616-625 10.1111/cbdd.12355
    • (2014) Chem. Biol. Drug Des. , vol.84 , pp. 616-625
    • Leung, E.W.W.1    Yagi, H.2    Harjani, J.R.3    Mulcair, M.D.4    Scanlon, M.J.5    Baell, J.B.6    Norton, R.S.7
  • 14
    • 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. K. Fragment screening and druggability assessment for the CBP/p300 KIX domain through protein-observed 19F NMR spectroscopy Angew. Chem., Int. Ed. 2015, 54, 3735-3739 10.1002/anie.201411658
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 3735-3739
    • Gee, C.T.1    Koleski, E.J.2    Pomerantz, W.C.K.3
  • 15
    • 84919675043 scopus 로고    scopus 로고
    • Fluorinated aromatic amino acids are sensitive F-19 NMR probes for bromodomain-ligand interactions
    • Mishra, N. K.; Urick, A. K.; Ember, S. W. J.; Schoenbrunn, E.; Pomerantz, W. C. Fluorinated aromatic amino acids are sensitive F-19 NMR probes for bromodomain-ligand interactions ACS Chem. Biol. 2014, 9, 2755-2760 10.1021/cb5007344
    • (2014) ACS Chem. Biol. , vol.9 , pp. 2755-2760
    • Mishra, N.K.1    Urick, A.K.2    Ember, S.W.J.3    Schoenbrunn, E.4    Pomerantz, W.C.5
  • 16
    • 84865263199 scopus 로고    scopus 로고
    • Profiling the dynamic interfaces of fluorinated transcription complexes for ligand discovery and characterization
    • Pomerantz, W. C.; Wang, N.; Lipinski, A. K.; Wang, R.; Cierpicki, T.; Mapp, A. K. Profiling the dynamic interfaces of fluorinated transcription complexes for ligand discovery and characterization ACS Chem. Biol. 2012, 7, 1345-1350 10.1021/cb3002733
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1345-1350
    • Pomerantz, W.C.1    Wang, N.2    Lipinski, A.K.3    Wang, R.4    Cierpicki, T.5    Mapp, A.K.6
  • 18
    • 25444475544 scopus 로고    scopus 로고
    • Sensitivity improvement in F-19 NMR-based screening experiments: Theoretical considerations and experimental applications
    • Dalvit, C.; Mongelli, N.; Papeo, G.; Giordano, P.; Veronesi, M.; Moskau, D.; Kummerle, R. Sensitivity improvement in F-19 NMR-based screening experiments: Theoretical considerations and experimental applications J. Am. Chem. Soc. 2005, 127, 13380-13385 10.1021/ja0542385
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13380-13385
    • Dalvit, C.1    Mongelli, N.2    Papeo, G.3    Giordano, P.4    Veronesi, M.5    Moskau, D.6    Kummerle, R.7
  • 19
    • 0037010533 scopus 로고    scopus 로고
    • NMR screening techniques in drug discovery and drug design
    • Stockman, B. J.; Dalvit, C. NMR screening techniques in drug discovery and drug design Prog. Nucl. Magn. Reson. Spectrosc. 2002, 41, 187-231 10.1016/S0079-6565(02)00049-3
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc. , vol.41 , pp. 187-231
    • Stockman, B.J.1    Dalvit, C.2
  • 20
    • 1842663065 scopus 로고    scopus 로고
    • Some influences of fluorine in bioorganic chemistry
    • O'Hagan, D.; Rzepa, H. S. Some influences of fluorine in bioorganic chemistry Chem. Commun. 1997, 645-652 10.1039/a604140j
    • (1997) Chem. Commun. , pp. 645-652
    • O'Hagan, D.1    Rzepa, H.S.2
  • 21
    • 34848848499 scopus 로고    scopus 로고
    • Fluorine in pharmaceuticals: Looking beyond intuition
    • Muller, K.; Faeh, C.; Diederich, F. Fluorine in pharmaceuticals: Looking beyond intuition Science 2007, 317, 1881-1886 10.1126/science.1131943
    • (2007) Science , vol.317 , pp. 1881-1886
    • Muller, K.1    Faeh, C.2    Diederich, F.3
  • 22
    • 84897584974 scopus 로고    scopus 로고
    • Fluorine in pharmaceutical industry: Fluorine-containing drugs introduced to the market in the last decade (2001-2011)
    • Wang, J.; Sanchez-Rosello, M.; Acena, J. L.; del Pozo, C.; Sorochinsky, A. E.; Fustero, S.; Soloshonok, V. A.; Liu, H. Fluorine in pharmaceutical industry: fluorine-containing drugs introduced to the market in the last decade (2001-2011) Chem. Rev. 2014, 114, 2432-2506 10.1021/cr4002879
    • (2014) Chem. Rev. , vol.114 , pp. 2432-2506
    • Wang, J.1    Sanchez-Rosello, M.2    Acena, J.L.3    Del Pozo, C.4    Sorochinsky, A.E.5    Fustero, S.6    Soloshonok, V.A.7    Liu, H.8
  • 23
  • 24
    • 0037663879 scopus 로고    scopus 로고
    • A fluorine scan of thrombin inhibitors to map the fluorophilicity/fluorophobicity of an enzyme active site: Evidence for C-F center dot center dot center dot C=O interactions
    • Olsen, J. A.; Banner, D. W.; Seiler, P.; Sander, U. O.; D'Arcy, A.; Stihle, M.; Muller, K.; Diederich, F. A fluorine scan of thrombin inhibitors to map the fluorophilicity/fluorophobicity of an enzyme active site: Evidence for C-F center dot center dot center dot C=O interactions Angew. Chem., Int. Ed. 2003, 42, 2507-2511 10.1002/anie.200351268
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 2507-2511
    • Olsen, J.A.1    Banner, D.W.2    Seiler, P.3    Sander, U.O.4    D'Arcy, A.5    Stihle, M.6    Muller, K.7    Diederich, F.8
  • 25
    • 4544240958 scopus 로고    scopus 로고
    • Halogenation of drugs enhances membrane binding and permeation
    • Gerebtzoff, G.; Li-Blatter, X.; Fischer, H.; Frentzel, A.; Seelig, A. Halogenation of drugs enhances membrane binding and permeation ChemBioChem 2004, 5, 676-684 10.1002/cbic.200400017
    • (2004) ChemBioChem , vol.5 , pp. 676-684
    • Gerebtzoff, G.1    Li-Blatter, X.2    Fischer, H.3    Frentzel, A.4    Seelig, A.5
  • 26
    • 84974603054 scopus 로고    scopus 로고
    • Fluorine NMR
    • Gerig, J. T. Fluorine NMR. http://www.biophysics.org/Portals/1/PDFs/Education/gerig.pdf.
    • Gerig, J.T.1
  • 27
    • 84885905320 scopus 로고    scopus 로고
    • Application of the rule of shielding in the design of novel fluorinated structural motifs and peptidomimetics
    • Dalvit, C.; Ko, S. Y.; Vulpetti, A. Application of the rule of shielding in the design of novel fluorinated structural motifs and peptidomimetics J. Fluorine Chem. 2013, 152, 129-135 10.1016/j.jfluchem.2013.01.017
    • (2013) J. Fluorine Chem. , vol.152 , pp. 129-135
    • Dalvit, C.1    Ko, S.Y.2    Vulpetti, A.3
  • 28
    • 84889880731 scopus 로고    scopus 로고
    • Design and generation of highly diverse fluorinated fragment libraries and their efficient screening with improved F-19 NMR methodology
    • Vulpetti, A.; Dalvit, C. Design and generation of highly diverse fluorinated fragment libraries and their efficient screening with improved F-19 NMR methodology ChemMedChem 2013, 8, 2057-2069 10.1002/cmdc.201300351
    • (2013) ChemMedChem , vol.8 , pp. 2057-2069
    • Vulpetti, A.1    Dalvit, C.2
  • 30
    • 0028216598 scopus 로고
    • F-19 nuclear magnetic resonance spectroscopic study of fluorophenylalanine-labeled and fluorotryptophan-labeled avian egg-white lysozymes
    • Lian, C. Y.; Le, H. B.; Montez, B.; Patterson, J.; Harrell, S.; Laws, D.; Matsumura, I.; Pearson, J.; Oldfield, E. F-19 nuclear magnetic resonance spectroscopic study of fluorophenylalanine-labeled and fluorotryptophan-labeled avian egg-white lysozymes Biochemistry 1994, 33, 5238-5245 10.1021/bi00183a029
    • (1994) Biochemistry , vol.33 , pp. 5238-5245
    • Lian, C.Y.1    Le, H.B.2    Montez, B.3    Patterson, J.4    Harrell, S.5    Laws, D.6    Matsumura, I.7    Pearson, J.8    Oldfield, E.9
  • 31
    • 0001465616 scopus 로고
    • Chemical shifts in proteins- A shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Eschericia coli galactose binding-protein using a multipole shielding polarizability local reaction field moelcular dyanmics approach
    • Pearson, J. G.; Oldfield, E.; Lee, F. S.; Warshel, A. Chemical shifts in proteins- A shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Eschericia coli galactose binding-protein using a multipole shielding polarizability local reaction field moelcular dyanmics approach J. Am. Chem. Soc. 1993, 115, 6851-6862 10.1021/ja00068a049
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6851-6862
    • Pearson, J.G.1    Oldfield, E.2    Lee, F.S.3    Warshel, A.4
  • 32
    • 0034630843 scopus 로고    scopus 로고
    • Origins of fluorine NMR chemical shifts in fluorine-containing proteins
    • Lau, E. Y.; Gerig, J. T. Origins of fluorine NMR chemical shifts in fluorine-containing proteins J. Am. Chem. Soc. 2000, 122, 4408-4417 10.1021/ja992107w
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4408-4417
    • Lau, E.Y.1    Gerig, J.T.2
  • 33
    • 78650552642 scopus 로고    scopus 로고
    • Fluorine-protein interactions and F-19 NMR isotropic chemical shifts: An empirical correlation with implications for drug design
    • Dalvit, C.; Vulpetti, A. Fluorine-protein interactions and F-19 NMR isotropic chemical shifts: An empirical correlation with implications for drug design ChemMedChem 2011, 6, 104-114 10.1002/cmdc.201000412
    • (2011) ChemMedChem , vol.6 , pp. 104-114
    • Dalvit, C.1    Vulpetti, A.2
  • 34
    • 84857625337 scopus 로고    scopus 로고
    • Current applications of F-19 NMR to studies of protein structure and dynamics
    • Kitevski-LeBlanc, J. L.; Prosser, R. S. Current applications of F-19 NMR to studies of protein structure and dynamics Prog. Nucl. Magn. Reson. Spectrosc. 2012, 62, 1-33 10.1016/j.pnmrs.2011.06.003
    • (2012) Prog. Nucl. Magn. Reson. Spectrosc. , vol.62 , pp. 1-33
    • Kitevski-LeBlanc, J.L.1    Prosser, R.S.2
  • 35
    • 0029665619 scopus 로고    scopus 로고
    • Use of F-19 NMR to probe protein structure and conformational changes
    • Danielson, M. A.; Falke, J. J. Use of F-19 NMR to probe protein structure and conformational changes Annu. Rev. Biophys. Biomol. Struct. 1996, 25, 163-195 10.1146/annurev.bb.25.060196.001115
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 163-195
    • Danielson, M.A.1    Falke, J.J.2
  • 36
    • 0022555889 scopus 로고
    • Observation of internal motility of proteins by nuclear magnetic resonance in solution
    • Wagner, G.; Wuthrich, K. Observation of internal motility of proteins by nuclear magnetic resonance in solution Methods Enzymol. 1986, 131, 307-326 10.1016/0076-6879(86)31047-4
    • (1986) Methods Enzymol. , vol.131 , pp. 307-326
    • Wagner, G.1    Wuthrich, K.2
  • 37
    • 0016697706 scopus 로고
    • Fluorotyrosine alkaline phosphatase internal mobility of individual tyrosines and role of chemical shift anisotropy as a F-19 nuclear spin relaxation mechanism in proteins
    • Hull, W. E.; Sykes, B. D. Fluorotyrosine alkaline phosphatase internal mobility of individual tyrosines and role of chemical shift anisotropy as a F-19 nuclear spin relaxation mechanism in proteins J. Mol. Biol. 1975, 98, 121-153 10.1016/S0022-2836(75)80105-7
    • (1975) J. Mol. Biol. , vol.98 , pp. 121-153
    • Hull, W.E.1    Sykes, B.D.2
  • 38
    • 0029079665 scopus 로고
    • Stopped-flow NMR spectroscopy-real time unfolding studies of 6-F-19-tryptophan-labeled Eschericia Coli dihydrofolate reductase
    • Hoeltzli, S. D.; Frieden, C. Stopped-flow NMR spectroscopy-real time unfolding studies of 6-F-19-tryptophan-labeled Eschericia Coli dihydrofolate reductase Proc. Natl. Acad. Sci. U. S. A. 1995, 92, 9318-9322 10.1073/pnas.92.20.9318
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9318-9322
    • Hoeltzli, S.D.1    Frieden, C.2
  • 39
    • 0024539619 scopus 로고
    • Membrance-bound D-lactate dehydrogenase of Eschericia coli. A model for protein interactions in membranes
    • Ho, C.; Pratt, E. A.; Rule, G. S. Membrance-bound D-lactate dehydrogenase of Eschericia coli. A model for protein interactions in membranes Biochim. Biophys. Acta, Rev. Biomembr. 1989, 988, 173-184 10.1016/0304-4157(89)90018-X
    • (1989) Biochim. Biophys. Acta, Rev. Biomembr. , vol.988 , pp. 173-184
    • Ho, C.1    Pratt, E.A.2    Rule, G.S.3
  • 42
    • 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 2012, 335, 1106-1110 10.1126/science.1215802
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wuthrich, K.5
  • 44
    • 0030939030 scopus 로고    scopus 로고
    • Incorporation of trifluoromethionine into a phage lysozyme: Implications and a new marker for use in protein F-19 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 F-19 NMR Biochemistry 1997, 36, 3404-3416 10.1021/bi9617973
    • (1997) Biochemistry , vol.36 , pp. 3404-3416
    • Duewel, H.1    Daub, E.2    Robinson, V.3    Honek, J.F.4
  • 46
    • 38449084295 scopus 로고    scopus 로고
    • Preparation of site-specifically labeled fluorinated proteins for F-19-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 F-19-NMR structural characterization Nat. Protoc. 2007, 2, 2601-2607 10.1038/nprot.2007.379
    • (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
  • 47
    • 84939985643 scopus 로고    scopus 로고
    • A comparison of chemical shift sensitivity of trifluoromethyl tags: Optimizing resolution in F-19 NMR studies of proteins
    • Ye, L. B.; Larda, S. T.; Li, Y. F.; Manglik, A.; Prosser, R. S. A comparison of chemical shift sensitivity of trifluoromethyl tags: optimizing resolution in F-19 NMR studies of proteins J. Biomol. NMR 2015, 62, 97-103 10.1007/s10858-015-9922-y
    • (2015) J. Biomol. NMR , vol.62 , pp. 97-103
    • Ye, L.B.1    Larda, S.T.2    Li, Y.F.3    Manglik, A.4    Prosser, R.S.5
  • 48
    • 1542379799 scopus 로고    scopus 로고
    • The preparation of F-19-labeled proteins for NMR studies
    • Frieden, C.; Hoeltzli, S. D.; Bann, J. G. The preparation of F-19-labeled proteins for NMR studies Methods Enzymol. 2004, 380, 400-415 10.1016/S0076-6879(04)80018-1
    • (2004) Methods Enzymol. , vol.380 , pp. 400-415
    • Frieden, C.1    Hoeltzli, S.D.2    Bann, J.G.3
  • 49
    • 84865263199 scopus 로고    scopus 로고
    • Profiling the dynamic interfaces of fluorinated transcriptional complexes for ligand discovery and characterization
    • Pomerantz, W. C.; Wang, N. K.; Lipinski, A. K.; Wang, E. W.; Cierpicki, T.; Mapp, A. K. Profiling the dynamic interfaces of fluorinated transcriptional complexes for ligand discovery and characterization ACS Chem. Biol. 2012, 7, 1345-1350 10.1021/cb3002733
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1345-1350
    • Pomerantz, W.C.1    Wang, N.K.2    Lipinski, A.K.3    Wang, E.W.4    Cierpicki, T.5    Mapp, A.K.6
  • 50
    • 1042288303 scopus 로고    scopus 로고
    • Urea-dependent unfolding of murine adenosine deaminase: Sequential destabilization as measured by F-19 NMR
    • Shu, Q.; Frieden, C. Urea-dependent unfolding of murine adenosine deaminase: Sequential destabilization as measured by F-19 NMR Biochemistry 2004, 43, 1432-1439 10.1021/bi035651x
    • (2004) Biochemistry , vol.43 , pp. 1432-1439
    • Shu, Q.1    Frieden, C.2
  • 51
    • 0034003659 scopus 로고    scopus 로고
    • Efficient incorporation of unsaturated methionine analogues into proteins in vivo
    • van Hest, J. C. M.; Kiick, K. L.; Tirrell, D. A. Efficient incorporation of unsaturated methionine analogues into proteins in vivo J. Am. Chem. Soc. 2000, 122, 1282-1288 10.1021/ja992749j
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1282-1288
    • Van Hest, J.C.M.1    Kiick, K.L.2    Tirrell, D.A.3
  • 52
    • 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. 2001, 123, 11089-11090 10.1021/ja016652k
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11089-11090
    • Tang, Y.1    Tirrell, D.A.2
  • 53
    • 0025093242 scopus 로고
    • The specific incorporation of labeled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate-application to fluorotryptophan labeling to the H+-ATPase of Eschericia coli and NMR studies
    • Kim, H. W.; Perez, J. A.; Ferguson, S. J.; Campbell, I. D. The specific incorporation of labeled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate-application to fluorotryptophan labeling to the H+-ATPase of Eschericia coli and NMR studies FEBS Lett. 1990, 272, 34-36 10.1016/0014-5793(90)80442-L
    • (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
    • 0018932939 scopus 로고
    • The herbicide glyphosate is a potent inhibitor of 5-enolpyruvyl shikimic acid 3-phopshate synthase
    • Steinrucken, H. C.; Amrhein, N. The herbicide glyphosate is a potent inhibitor of 5-enolpyruvyl shikimic acid 3-phopshate synthase Biochem. Biophys. Res. Commun. 1980, 94, 1207-1212 10.1016/0006-291X(80)90547-1
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 1207-1212
    • Steinrucken, H.C.1    Amrhein, N.2
  • 55
    • 0042307439 scopus 로고    scopus 로고
    • Selective incorporation of F-19-labeled Trp side chains for NMR-spectroscopy-based ligand-protein interaction studies
    • Leone, M.; Rodriguez-Mias, R. A.; Pellecchia, M. Selective incorporation of F-19-labeled Trp side chains for NMR-spectroscopy-based ligand-protein interaction studies ChemBioChem 2003, 4, 649-650 10.1002/cbic.200300597
    • (2003) ChemBioChem , vol.4 , pp. 649-650
    • Leone, M.1    Rodriguez-Mias, R.A.2    Pellecchia, M.3
  • 56
    • 84867301057 scopus 로고    scopus 로고
    • Simple and inexpensive incorporation of F-19-Tryptophan for protein NMR spectroscopy
    • Crowley, P. B.; Kyne, C.; Monteith, W. B. Simple and inexpensive incorporation of F-19-Tryptophan for protein NMR spectroscopy Chem. Commun. 2012, 48, 10681-10683 10.1039/c2cc35347d
    • (2012) Chem. Commun. , vol.48 , pp. 10681-10683
    • Crowley, P.B.1    Kyne, C.2    Monteith, W.B.3
  • 57
    • 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. 1998, 280, 1-9 10.1006/jmbi.1998.1843
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 58
    • 84906254338 scopus 로고    scopus 로고
    • Anatomy of beta-strands at protein-protein interfaces
    • Watkins, A. M.; Arora, P. S. Anatomy of beta-strands at protein-protein interfaces ACS Chem. Biol. 2014, 9, 1747-1754 10.1021/cb500241y
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1747-1754
    • Watkins, A.M.1    Arora, P.S.2
  • 59
    • 80052566586 scopus 로고    scopus 로고
    • Assessing helical protein interfaces for inhibitor design
    • Bullock, B. N.; Jochim, A. L.; Arora, P. S. Assessing helical protein interfaces for inhibitor design J. Am. Chem. Soc. 2011, 133, 14220-14223 10.1021/ja206074j
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 14220-14223
    • Bullock, B.N.1    Jochim, A.L.2    Arora, P.S.3
  • 60
    • 84906327241 scopus 로고    scopus 로고
    • Comprehensive analysis of loops at protein-protein interfaces for macrocycle design
    • Gavenonis, J.; Sheneman, B. A.; Siegert, T. R.; Eshelman, M. R.; Kritzer, J. A. Comprehensive analysis of loops at protein-protein interfaces for macrocycle design Nat. Chem. Biol. 2014, 10, 716-722 10.1038/nchembio.1580
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 716-722
    • Gavenonis, J.1    Sheneman, B.A.2    Siegert, T.R.3    Eshelman, M.R.4    Kritzer, J.A.5
  • 62
    • 84901271098 scopus 로고    scopus 로고
    • F-19 NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI)
    • Curtis-Marof, R.; Doko, D.; Rowe, M. L.; Richards, K. L.; Williamson, R. A.; Howard, M. J. F-19 NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI) Org. Biomol. Chem. 2014, 12, 3808-3812 10.1039/c4ob00699b
    • (2014) Org. Biomol. Chem. , vol.12 , pp. 3808-3812
    • Curtis-Marof, R.1    Doko, D.2    Rowe, M.L.3    Richards, K.L.4    Williamson, R.A.5    Howard, M.J.6
  • 63
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang, L.; Brock, A.; Herberich, B.; Schultz, P. G. Expanding the genetic code of Escherichia coli Science 2001, 292, 498-500 10.1126/science.1060077
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 65
    • 7244229512 scopus 로고    scopus 로고
    • Folding and domain-domain interactions of the chaperone PapD measured by F-19 NMR
    • Bann, J. G.; Frieden, C. Folding and domain-domain interactions of the chaperone PapD measured by F-19 NMR Biochemistry 2004, 43, 13775-13786 10.1021/bi048614u
    • (2004) Biochemistry , vol.43 , pp. 13775-13786
    • Bann, J.G.1    Frieden, C.2
  • 66
    • 80053467272 scopus 로고    scopus 로고
    • Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase
    • Minnihan, E. C.; Young, D. D.; Schultz, P. G.; Stubbe, J. Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase J. Am. Chem. Soc. 2011, 133, 15942-15945 10.1021/ja207719f
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15942-15945
    • Minnihan, E.C.1    Young, D.D.2    Schultz, P.G.3    Stubbe, J.4
  • 67
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L.; Engelman, D. M. Helical membrane protein folding, stability, and evolution Annu. Rev. Biochem. 2000, 69, 881-922 10.1146/annurev.biochem.69.1.881
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 69
    • 0025341339 scopus 로고
    • A novel approach for sequential assignment of H-1, C-13, and N-15 spectra of larger proteins-heteronuclear triple resonance 3-dimensional NMR spectroscopy application to calmodulin
    • Ikura, M.; Kay, L. E.; Bax, A. A novel approach for sequential assignment of H-1, C-13, and N-15 spectra of larger proteins-heteronuclear triple resonance 3-dimensional NMR spectroscopy application to calmodulin Biochemistry 1990, 29, 4659-4667 10.1021/bi00471a022
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 70
    • 67849121879 scopus 로고    scopus 로고
    • A mutagenesis-free approach to assignment of F-19 NMR resonances in biosynthetically labeled proteins
    • Kitevski-LeBlanc, J. L.; Al-Abdul-Wahid, M. S.; Prosser, R. S. A mutagenesis-free approach to assignment of F-19 NMR resonances in biosynthetically labeled proteins J. Am. Chem. Soc. 2009, 131, 2054-2055 10.1021/ja8085752
    • (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
  • 71
    • 77954690041 scopus 로고    scopus 로고
    • Approaches to the assignment of F-19 resonances from 3-fluorophenylalanine labeled calmodulin using solution state NMR
    • Kitevski-LeBlanc, J. L.; Evanics, F.; Prosser, R. S. Approaches to the assignment of F-19 resonances from 3-fluorophenylalanine labeled calmodulin using solution state NMR J. Biomol. NMR 2010, 47, 113-123 10.1007/s10858-010-9415-y
    • (2010) J. Biomol. NMR , vol.47 , pp. 113-123
    • Kitevski-LeBlanc, J.L.1    Evanics, F.2    Prosser, R.S.3
  • 72
    • 14144255521 scopus 로고    scopus 로고
    • Interaction of the eukaryotic pore-forming cytolysin equinatoxin II with model membranes: F-19 NMR studies
    • Anderluh, G.; Razpotnik, A.; Podlesek, Z.; Macek, P.; Separovic, F.; Norton, R. S. Interaction of the eukaryotic pore-forming cytolysin equinatoxin II with model membranes: F-19 NMR studies J. Mol. Biol. 2005, 347, 27-39 10.1016/j.jmb.2004.12.058
    • (2005) J. Mol. Biol. , vol.347 , pp. 27-39
    • Anderluh, G.1    Razpotnik, A.2    Podlesek, Z.3    Macek, P.4    Separovic, F.5    Norton, R.S.6
  • 73
    • 0027519332 scopus 로고
    • Activation of the phosphosignaling protein Chey. 1. Analysis of the phosphorylated conformation by F-19 NMR and protien engineering
    • Drake, S. K.; Bourret, R. B.; Luck, L. A.; Simon, M. I.; Falke, J. J. Activation of the phosphosignaling protein Chey. 1. Analysis of the phosphorylated conformation by F-19 NMR and protien engineering J. Biol. Chem. 1993, 268, 13081-13088
    • (1993) J. Biol. Chem. , vol.268 , pp. 13081-13088
    • Drake, S.K.1    Bourret, R.B.2    Luck, L.A.3    Simon, M.I.4    Falke, J.J.5
  • 75
    • 14044269529 scopus 로고    scopus 로고
    • NMR studies of 4-F-19-phenylalanine-labeled intestinal fatty acid binding protein: Evidence for conformational heterogeneity in the native state
    • Li, H.; Frieden, C. NMR studies of 4-F-19-phenylalanine-labeled intestinal fatty acid binding protein: Evidence for conformational heterogeneity in the native state Biochemistry 2005, 44, 2369-2377 10.1021/bi047600l
    • (2005) Biochemistry , vol.44 , pp. 2369-2377
    • Li, H.1    Frieden, C.2
  • 76
    • 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 1996, 274, 1531-1534 10.1126/science.274.5292.1531
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 78
    • 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 2012, 51, 4990-5003 10.1021/bi3005126
    • (2012) Biochemistry , vol.51 , pp. 4990-5003
    • Scott, D.E.1    Coyne, A.G.2    Hudson, S.A.3    Abell, C.4
  • 79
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • Mittermaier, A. K.; Kay, L. E. Observing biological dynamics at atomic resolution using NMR Trends Biochem. Sci. 2009, 34, 601-611 10.1016/j.tibs.2009.07.004
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.E.2
  • 80
    • 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. 2005, 48, 2518-2525 10.1021/jm049131r
    • (2005) J. Med. Chem. , vol.48 , pp. 2518-2525
    • Hajduk, P.J.1    Huth, J.R.2    Fesik, S.W.3
  • 81
    • 84906254338 scopus 로고    scopus 로고
    • Anatomy of beta-strands at protein-protein interfaces
    • Watkins, A. M.; Arora, P. S. Anatomy of beta-strands at protein-protein interfaces ACS Chem. Biol. 2014, 9, 1747-1754 10.1021/cb500241y
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1747-1754
    • Watkins, A.M.1    Arora, P.S.2
  • 82
    • 33947420470 scopus 로고    scopus 로고
    • New method for fast and accurate binding-site identification and analysis
    • Halgren, T. New method for fast and accurate binding-site identification and analysis Chem. Biol. Drug Des. 2007, 69, 146-148 10.1111/j.1747-0285.2007.00483.x
    • (2007) Chem. Biol. Drug Des. , vol.69 , pp. 146-148
    • Halgren, T.1
  • 83
    • 84903152777 scopus 로고    scopus 로고
    • Using F-19 NMR to probe biological interactions of proteins and peptides
    • Marsh, E. N. G.; Suzuki, Y. Using F-19 NMR to probe biological interactions of proteins and peptides ACS Chem. Biol. 2014, 9, 1242-1250 10.1021/cb500111u
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1242-1250
    • Marsh, E.N.G.1    Suzuki, Y.2
  • 84
    • 0028175779 scopus 로고
    • F-19 NMR spectroscopy of 6-F-19 tryptophan-labeled Eschericia-coli dihydrofolate reductase-equilibrium folding and ligand-binding studies
    • Hoeltzli, S. D.; Frieden, C. F-19 NMR spectroscopy of 6-F-19 tryptophan-labeled Eschericia-coli dihydrofolate reductase-equilibrium folding and ligand-binding studies Biochemistry 1994, 33, 5502-5509 10.1021/bi00184a019
    • (1994) Biochemistry , vol.33 , pp. 5502-5509
    • Hoeltzli, S.D.1    Frieden, C.2
  • 85
    • 0025922013 scopus 로고
    • F-19 NMR-studies of the D-galactose chemosensory receptor. 1. Sugar binding yields a global structural change
    • Luck, L. A.; Falke, J. J. F-19 NMR-studies of the D-galactose chemosensory receptor. 1. sugar binding yields a global structural change Biochemistry 1991, 30, 4248-4256 10.1021/bi00231a021
    • (1991) Biochemistry , vol.30 , pp. 4248-4256
    • Luck, L.A.1    Falke, J.J.2
  • 86
    • 0025821340 scopus 로고
    • Open conformation of a substrate-binding cleft F-19 NMR studies of cleft angle in the D-galactose chemosensory receptor
    • Luck, L. A.; Falke, J. J. Open conformation of a substrate-binding cleft F-19 NMR studies of cleft angle in the D-galactose chemosensory receptor Biochemistry 1991, 30, 6484-6490 10.1021/bi00240a019
    • (1991) Biochemistry , vol.30 , pp. 6484-6490
    • Luck, L.A.1    Falke, J.J.2
  • 87
    • 0028260372 scopus 로고
    • Attract-induced and disulfide conformational-changes in the ligand-binding domain of the chemotaxis aspartate receptor-a F-19 NMR-Study
    • Danielson, M. A.; Biemann, H. P.; Koshland, D. E.; Falke, J. J. Attract-induced and disulfide conformational-changes in the ligand-binding domain of the chemotaxis aspartate receptor-a F-19 NMR-Study Biochemistry 1994, 33, 6100-6109 10.1021/bi00186a009
    • (1994) Biochemistry , vol.33 , pp. 6100-6109
    • Danielson, M.A.1    Biemann, H.P.2    Koshland, D.E.3    Falke, J.J.4
  • 88
    • 0037044756 scopus 로고    scopus 로고
    • Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP) - The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain
    • Goto, N. K.; Zor, T.; Martinez-Yamout, M.; Dyson, H. J.; Wright, P. E. Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP)-The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain J. Biol. Chem. 2002, 277, 43168-43174 10.1074/jbc.M207660200
    • (2002) J. Biol. Chem. , vol.277 , pp. 43168-43174
    • Goto, N.K.1    Zor, T.2    Martinez-Yamout, M.3    Dyson, H.J.4    Wright, P.E.5
  • 89
    • 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. 2006, 128, 1569-1579 10.1021/ja055926r
    • (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
  • 91
    • 33646160625 scopus 로고    scopus 로고
    • Structural studies of Bcl-xL/ligand complexes using F-19 NMR
    • Yu, L. P.; Hajduk, P. J.; Mack, J.; Olejniczak, E. T. Structural studies of Bcl-xL/ligand complexes using F-19 NMR J. Biomol. NMR 2006, 34, 221-227 10.1007/s10858-006-0005-y
    • (2006) J. Biomol. NMR , vol.34 , pp. 221-227
    • Yu, L.P.1    Hajduk, P.J.2    Mack, J.3    Olejniczak, E.T.4
  • 94
    • 84899973908 scopus 로고    scopus 로고
    • Targeting bromodomains: Epigenetic readers of lysine acetylation
    • Filippakopoulos, P.; Knapp, S. Targeting bromodomains: epigenetic readers of lysine acetylation Nat. Rev. Drug Discovery 2014, 13, 337-356 10.1038/nrd4286
    • (2014) Nat. Rev. Drug Discovery , vol.13 , pp. 337-356
    • Filippakopoulos, P.1    Knapp, S.2
  • 95
    • 84899936534 scopus 로고    scopus 로고
    • Acetyl-lysine binding site of bromodomain-containing protein 4 (BRD4) interacts with diverse kinase inhibitors
    • Ember, S. W. J.; Zhu, J.-Y.; Olesen, S. H.; Martin, M. P.; Becker, A.; Berndt, N.; Georg, G. I.; Schoenbrunn, E. Acetyl-lysine binding site of bromodomain-containing protein 4 (BRD4) interacts with diverse kinase inhibitors ACS Chem. Biol. 2014, 9, 1160-1171 10.1021/cb500072z
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1160-1171
    • Ember, S.W.J.1    Zhu, J.-Y.2    Olesen, S.H.3    Martin, M.P.4    Becker, A.5    Berndt, N.6    Georg, G.I.7    Schoenbrunn, E.8
  • 97
    • 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.; Schoenbrunn, E. Cyclin-dependent kinase inhibitor dinaciclib interacts with the acetyl-lysine recognition site of bromodomains ACS Chem. Biol. 2013, 8, 2360-2365 10.1021/cb4003283
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2360-2365
    • Martin, M.P.1    Olesen, S.H.2    Georg, G.I.3    Schoenbrunn, E.4
  • 98
    • 84856397832 scopus 로고    scopus 로고
    • Fragment-based discovery of bromodomain inhibitors Part 1: Inhibitor binding modes and implications for lead discovery
    • Chung, C. W.; Dean, A. W.; Woolven, J. M.; Bamborough, P. Fragment-based discovery of bromodomain inhibitors Part 1: Inhibitor binding modes and implications for lead discovery J. Med. Chem. 2012, 55, 576-586 10.1021/jm201320w
    • (2012) J. Med. Chem. , vol.55 , pp. 576-586
    • Chung, C.W.1    Dean, A.W.2    Woolven, J.M.3    Bamborough, P.4
  • 99
    • 0030614424 scopus 로고    scopus 로고
    • F-19 NMR measurements of the rotational mobility of proteins in vivo
    • Williams, S. P.; Haggie, P. M.; Brindle, K. M. F-19 NMR measurements of the rotational mobility of proteins in vivo Biophys. J. 1997, 72, 490-498 10.1016/S0006-3495(97)78690-9
    • (1997) Biophys. J. , vol.72 , pp. 490-498
    • Williams, S.P.1    Haggie, P.M.2    Brindle, K.M.3
  • 101
    • 84867807912 scopus 로고    scopus 로고
    • Nuclear magnetic resonance of hyperpolarized fluorine for characterization of protein-ligand interactions
    • Lee, Y.; Zeng, H. F.; Ruedisser, S.; Gossert, A. D.; Hilty, C. Nuclear magnetic resonance of hyperpolarized fluorine for characterization of protein-ligand interactions J. Am. Chem. Soc. 2012, 134, 17448-17451 10.1021/ja308437h
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 17448-17451
    • Lee, Y.1    Zeng, H.F.2    Ruedisser, S.3    Gossert, A.D.4    Hilty, C.5
  • 102
    • 10144227798 scopus 로고    scopus 로고
    • F-19 nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine
    • Feeney, J.; McCormick, J. E.; Bauer, C. J.; Birdsall, B.; Moody, C. M.; Starkmann, B. A.; Young, D. W.; Francis, P.; Havlin, R. H.; Arnold, W. D.; Oldfield, E. F-19 nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine J. Am. Chem. Soc. 1996, 118, 8700-8706 10.1021/ja960465i
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8700-8706
    • Feeney, J.1    McCormick, J.E.2    Bauer, C.J.3    Birdsall, B.4    Moody, C.M.5    Starkmann, B.A.6    Young, D.W.7    Francis, P.8    Havlin, R.H.9    Arnold, W.D.10    Oldfield, E.11
  • 103
    • 33846618363 scopus 로고    scopus 로고
    • Biosynthetic incorporation of fluorohistidine into proteins in E-coli: A new probe of macromolecular structure
    • Eichler, J. F.; Cramer, J. C.; Kirk, K. L.; Bann, J. G. Biosynthetic incorporation of fluorohistidine into proteins in E-coli: A new probe of macromolecular structure ChemBioChem 2005, 6, 2170-2173 10.1002/cbic.200500249
    • (2005) ChemBioChem , vol.6 , pp. 2170-2173
    • Eichler, J.F.1    Cramer, J.C.2    Kirk, K.L.3    Bann, J.G.4
  • 104
    • 0037154219 scopus 로고    scopus 로고
    • Real-time and equilibrium F-19-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD
    • Bann, J. G.; Pinkner, J.; Hultgren, S. J.; Frieden, C. Real-time and equilibrium F-19-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 709-714 10.1073/pnas.022649599
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 709-714
    • Bann, J.G.1    Pinkner, J.2    Hultgren, S.J.3    Frieden, C.4
  • 107
    • 0141454913 scopus 로고    scopus 로고
    • F-19 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. F-19 NMR studies of the leucine-isoleucine-valine binding protein: Evidence that a closed conformation exists in solution J. Biomol. Struct. Dyn. 2003, 21, 235-246 10.1080/07391102.2003.10506919
    • (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
  • 108
    • 0026612027 scopus 로고
    • F-19 nuclear magnetic resonance studies of aqeuous and transmembrane receptors-examples from the Escherichia coli chemosensory pathway
    • Falke, J. J.; Luck, L. A.; Scherrer, J. F-19 nuclear magnetic resonance studies of aqeuous and transmembrane receptors-examples from the Escherichia coli chemosensory pathway Biophys. J. 1992, 62, 82-86 10.1016/S0006-3495(92)81787-3
    • (1992) Biophys. J. , vol.62 , pp. 82-86
    • Falke, J.J.1    Luck, L.A.2    Scherrer, J.3
  • 109
    • 0035820526 scopus 로고    scopus 로고
    • Phenoxypyrimidine inhibitors of p38 alpha kinase: Synthesis and statistical evaluation of the p38 inhibitory potencies of a series of 1-(piperidin-4-yl)-4-(4-fluorophenyl)-5-2-phenoxypyrimidin-4-yl) imidazoles
    • Boehm, J. C.; Bower, M. J.; Gallagher, T. F.; Kassis, S.; Johnson, S. R.; Adams, J. L. Phenoxypyrimidine inhibitors of p38 alpha kinase: Synthesis and statistical evaluation of the p38 inhibitory potencies of a series of 1-(piperidin-4-yl)-4-(4-fluorophenyl)-5-2-phenoxypyrimidin-4-yl) imidazoles Bioorg. Med. Chem. Lett. 2001, 11, 1123-1126 10.1016/S0960-894X(01)00163-9
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 1123-1126
    • Boehm, J.C.1    Bower, M.J.2    Gallagher, T.F.3    Kassis, S.4    Johnson, S.R.5    Adams, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.