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Volumn 9, Issue 9, 2009, Pages 811-823

Spin-lattice relaxation time in drug discovery and design

Author keywords

CSP; HTS; Intermolecular interaction; NMR; Nuclear relaxation; Spin lattice relaxation time; Topology of interaction

Indexed keywords

BENDAZAC LYSINE; IBUPROFEN; NONSTEROID ANTIINFLAMMATORY AGENT; SALICYLIC ACID; TOLMETIN; LIGAND; PROTEIN;

EID: 73449136407     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802609789207082     Document Type: Review
Times cited : (20)

References (98)
  • 1
    • 0001307841 scopus 로고    scopus 로고
    • NMR spectroscopy as a tool for structure-based drug design
    • Stockman B. J. NMR spectroscopy as a tool for structure-based drug design. Prog. Nucl. Magn. Reson. Spectrosc., 1998, 33, 109-151.
    • (1998) Prog. Nucl. Magn. Reson. Spectrosc , vol.33 , pp. 109-151
    • Stockman, B.J.1
  • 2
    • 0035272888 scopus 로고    scopus 로고
    • Applications of NMR screening in the pharmaceutical industry
    • Shapiro, M. Applications of NMR screening in the pharmaceutical industry. Il Farmaco 2001, 56, 141-143.
    • (2001) Il Farmaco , vol.56 , pp. 141-143
    • Shapiro, M.1
  • 4
    • 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.
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc , vol.41 , pp. 187-231
    • Stockman, B.J.1    Dalvit, C.2
  • 8
    • 13344280929 scopus 로고    scopus 로고
    • New approaches for NMR screening in drug discovery
    • Fernandez, C.; Jahnke, W. New approaches for NMR screening in drug discovery. Drug Discov. Today. Technol., 2004, 1, 277-283.
    • (2004) Drug Discov. Today. Technol , vol.1 , pp. 277-283
    • Fernandez, C.1    Jahnke, W.2
  • 10
    • 25144456011 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions
    • Pellecchia, M. Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions. Chem. Biol., 2005, 12, 961-971.
    • (2005) Chem. Biol , vol.12 , pp. 961-971
    • Pellecchia, M.1
  • 11
    • 35948942349 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. Prog. Nucl. Magn. Reson. Spectrosc., 2007, 51, 219-242.
    • (2007) Prog. Nucl. Magn. Reson. Spectrosc , vol.51 , pp. 219-242
    • Fielding, L.1
  • 12
    • 57549085603 scopus 로고    scopus 로고
    • Estimating protein-ligand binding affinity using high-throughput screening by NMR
    • Shortridge, M. D.; Hage, D. S.; Harbison, G. S.; Powers, R. Estimating protein-ligand binding affinity using high-throughput screening by NMR. J. Comb. Chem., 2008, 10, 948-958.
    • (2008) J. Comb. Chem , vol.10 , pp. 948-958
    • Shortridge, M.D.1    Hage, D.S.2    Harbison, G.S.3    Powers, R.4
  • 15
    • 0141928674 scopus 로고    scopus 로고
    • TROSY in NMR studies of the structure and function of large biological macromolecules
    • Fernandez, C.; Wider, G. TROSY in NMR studies of the structure and function of large biological macromolecules. Curr. Opin. Struct. Biol., 2003, 13, 570-580.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 570-580
    • Fernandez, C.1    Wider, G.2
  • 16
    • 20644455768 scopus 로고    scopus 로고
    • A competitive low-affinity binding model for determining the mutual and specific sites of two ligands on protein
    • Bai, G.; Cui, Y.; Yang, Y.; Ye, C.; Liu, M. A competitive low-affinity binding model for determining the mutual and specific sites of two ligands on protein. J. Pharm. Biomed. Anal., 2005, 38, 588-593.
    • (2005) J. Pharm. Biomed. Anal , vol.38 , pp. 588-593
    • Bai, G.1    Cui, Y.2    Yang, Y.3    Ye, C.4    Liu, M.5
  • 17
    • 39149084666 scopus 로고    scopus 로고
    • The application of FAST-NMR for the identification of novel drug discovery targets
    • Powers, R.; Mercier, K. A.; Copeland, J. C. The application of FAST-NMR for the identification of novel drug discovery targets. Drug Discov. Today, 2008, 13, 172-180.
    • (2008) Drug Discov. Today , vol.13 , pp. 172-180
    • Powers, R.1    Mercier, K.A.2    Copeland, J.C.3
  • 18
    • 33845231983 scopus 로고    scopus 로고
    • Mercier, K. A.; Baran, M.; Ramanathan, V.; Revesz, P.; Xiao, R.; Montelione, G. T.; Powers, R. FAST-NMR: Functional annotation screening technology using NMR spectroscopy. J. Am. Chem. Soc., 2006, 128, 15292-152-99.
    • Mercier, K. A.; Baran, M.; Ramanathan, V.; Revesz, P.; Xiao, R.; Montelione, G. T.; Powers, R. FAST-NMR: Functional annotation screening technology using NMR spectroscopy. J. Am. Chem. Soc., 2006, 128, 15292-152-99.
  • 19
    • 18044397545 scopus 로고    scopus 로고
    • Progress of structural genomics initiatives: An analysis of solved target structures
    • Todd, A. E.; Mardsen, R. L.; Thornton, J. M.; Orengo, C. A. Progress of structural genomics initiatives: an analysis of solved target structures. J. Mol. Biol., 2005, 348, 1235-1260.
    • (2005) J. Mol. Biol , vol.348 , pp. 1235-1260
    • Todd, A.E.1    Mardsen, R.L.2    Thornton, J.M.3    Orengo, C.A.4
  • 21
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation. CABIOS
    • Livingstone, C. D.; Barton, G. J. Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation. CABIOS. Comput. Appl. Biosci., 1993, 9, 745-756.
    • (1993) Comput. Appl. Biosci , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 23
    • 19444367377 scopus 로고    scopus 로고
    • Active site identification through geometry based and sequence profile-based calculations: Burial of catalytic clefts
    • Greaves, R.; Warwicker, J. Active site identification through geometry based and sequence profile-based calculations: burial of catalytic clefts. J. Mol. Biol., 2005, 349, 547-557.
    • (2005) J. Mol. Biol , vol.349 , pp. 547-557
    • Greaves, R.1    Warwicker, J.2
  • 24
    • 0033910698 scopus 로고    scopus 로고
    • Searching databases to find protein domain organization
    • Bateman, A.; Birney, E. Searching databases to find protein domain organization. Adv. Protein Chem., 2000, 54, 137-157.
    • (2000) Adv. Protein Chem , vol.54 , pp. 137-157
    • Bateman, A.1    Birney, E.2
  • 25
    • 0000195671 scopus 로고
    • Natural abundance N-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G.; Ruben, D. J. Natural abundance N-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett., 1980, 69, 185-189.
    • (1980) Chem. Phys. Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 26
    • 33748276474 scopus 로고    scopus 로고
    • Protein-ligand docking: Current status and future challenges
    • Sousa, S. F.; Fernandes, P. A.; Ramos, M. J. Protein-ligand docking: Current status and future challenges. Proteins, 2006, 65, 15-26.
    • (2006) Proteins , vol.65 , pp. 15-26
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 27
    • 33748271948 scopus 로고    scopus 로고
    • Comparison of protein active site structures for functional annotation of proteins and drug design
    • Powers, R.; Copeland, J. C.; Germer, K.; Mercier, K. A.; Ramanathan, V.; Revesz, P. Comparison of protein active site structures for functional annotation of proteins and drug design. Proteins, 2006, 65, 124-135.
    • (2006) Proteins , vol.65 , pp. 124-135
    • Powers, R.1    Copeland, J.C.2    Germer, K.3    Mercier, K.A.4    Ramanathan, V.5    Revesz, P.6
  • 28
    • 0035167572 scopus 로고    scopus 로고
    • Dietmann, S, Park, J, Notredame, C, Heger, A, Lappe, M, Holm, L. A fully automatic evolutionary classification of protein, folds: Dali Domain Dictionary version 3. Nucleic Acids Res, 2001, 29, 55-57
    • Dietmann, S.; Park, J.; Notredame, C.; Heger, A.; Lappe, M.; Holm, L. A fully automatic evolutionary classification of protein, folds: Dali Domain Dictionary version 3. Nucleic Acids Res., 2001, 29, 55-57.
  • 29
    • 0029705324 scopus 로고    scopus 로고
    • Automated docking of flexible ligands: Applications of AutoDock
    • Goodsell, D. S.; Morris, G. M.; Olson, A. J. Automated docking of flexible ligands: Applications of AutoDock. J. Mol. Recognit., 1996, 9, 1-5.
    • (1996) J. Mol. Recognit , vol.9 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 30
    • 42449160226 scopus 로고    scopus 로고
    • Synthesis and characterization of an amphiphilic cyclodextrin, a micelle with two recognition sites
    • Silva, O. F; Fernández, M. A.; Pennie, S. L.; Gil, R. R.; de Rossi, R. H. Synthesis and characterization of an amphiphilic cyclodextrin, a micelle with two recognition sites. Langmuir 2008, 24, 3718-3726.
    • (2008) Langmuir , vol.24 , pp. 3718-3726
    • Silva, O.F.1    Fernández, M.A.2    Pennie, S.L.3    Gil, R.R.4    de Rossi, R.H.5
  • 31
    • 0031989461 scopus 로고    scopus 로고
    • H-1 NMR studies on the interaction of beta-carboline derivatives with human serum albumin
    • Veglia, G.; Delfini, M.; del Giudice, M. R.; Gaggelli, E.; Valensin, G. H-1 NMR studies on the interaction of beta-carboline derivatives with human serum albumin. J. Magn. Reson., 1998, 130, 281-286.
    • (1998) J. Magn. Reson , vol.130 , pp. 281-286
    • Veglia, G.1    Delfini, M.2    del Giudice, M.R.3    Gaggelli, E.4    Valensin, G.5
  • 32
    • 0346342723 scopus 로고    scopus 로고
    • Analysis of competitive ligands to human serum albumin using NMR relaxation measurements
    • Cui, Y. F.; Bai, G. Y.; Li, C. G.; Ye, C. H; Liu, M. L. Analysis of competitive ligands to human serum albumin using NMR relaxation measurements. J. Pharmacol. Biomed. Anal., 2004, 34, 247-254.
    • (2004) J. Pharmacol. Biomed. Anal , vol.34 , pp. 247-254
    • Cui, Y.F.1    Bai, G.Y.2    Li, C.G.3    Ye, C.H.4    Liu, M.L.5
  • 33
    • 0001070626 scopus 로고
    • Fourier transform study of the spin-lattice relaxation by "progressive-saturation
    • Freeman, R.; Hill, H. D. W., Fourier transform study of the spin-lattice relaxation by "progressive-saturation". J. Chem. Phys. 1971, 54, 3367-3377.
    • (1971) J. Chem. Phys , vol.54 , pp. 3367-3377
    • Freeman, R.1    Hill, H.D.W.2
  • 34
    • 36849099862 scopus 로고
    • Spin-lattice relaxation measurements in slowly relaxing complex spectra
    • Markley, J. L.; Horsey, W. J.; Klein M. P., Spin-lattice relaxation measurements in slowly relaxing complex spectra. J. Chem. Phys., 1971, 55, 3604-3605.
    • (1971) J. Chem. Phys , vol.55 , pp. 3604-3605
    • Markley, J.L.1    Horsey, W.J.2    Klein, M.P.3
  • 35
    • 36849104960 scopus 로고
    • Measurement of spin relaxation in complex systems
    • Vold, R. L.; Waugh, J. S.; Klein, M. P.; Phelps D. E., Measurement of spin relaxation in complex systems. J. Chem. Phys., 1968, 48, 3831-3832.
    • (1968) J. Chem. Phys , vol.48 , pp. 3831-3832
    • Vold, R.L.1    Waugh, J.S.2    Klein, M.P.3    Phelps, D.E.4
  • 36
    • 36749105124 scopus 로고
    • Dipolar contribution to NMR spin-lattice relaxation of protons
    • Freeman, R.; Hill, H. D. W.; Tomlinson, B. L.; Hall, L. D. Dipolar contribution to NMR spin-lattice relaxation of protons. J. Chem. Phys., 1974, 61, 4466-4473.
    • (1974) J. Chem. Phys , vol.61 , pp. 4466-4473
    • Freeman, R.1    Hill, H.D.W.2    Tomlinson, B.L.3    Hall, L.D.4
  • 37
    • 0141555651 scopus 로고
    • Correlation time measurements of amino acid side chains from proton selective spin-lattice relaxation rates
    • Niccolai, N.; de Miles, M. P. L.; Hehir, S. P.; Gibbons, W. A. Correlation time measurements of amino acid side chains from proton selective spin-lattice relaxation rates. J. Am. Chem. Soc., 1978, 100, 6528-6529.
    • (1978) J. Am. Chem. Soc , vol.100 , pp. 6528-6529
    • Niccolai, N.1    de Miles, M.P.L.2    Hehir, S.P.3    Gibbons, W.A.4
  • 38
    • 0002785142 scopus 로고
    • Selective and non-selective proton spin-lattice relaxation studies of enzyme-substrate interactions
    • Valensin, G.; Kushnir, T.; Navon, G. Selective and non-selective proton spin-lattice relaxation studies of enzyme-substrate interactions. J. Magn. Reson., 1982, 46, 23-29.
    • (1982) J. Magn. Reson , vol.46 , pp. 23-29
    • Valensin, G.1    Kushnir, T.2    Navon, G.3
  • 39
    • 0033258850 scopus 로고    scopus 로고
    • Determination of correlation times from selective and non-selective spin lattice relaxation rates and their use in drug-drug and drug-albumin interaction studies
    • Tinoco, L. W.; Figueroa-Villar, J. D. Determination of correlation times from selective and non-selective spin lattice relaxation rates and their use in drug-drug and drug-albumin interaction studies. J. Braz. Chem. Soc., 1999, 10, 281-286.
    • (1999) J. Braz. Chem. Soc , vol.10 , pp. 281-286
    • Tinoco, L.W.1    Figueroa-Villar, J.D.2
  • 40
    • 0342936258 scopus 로고    scopus 로고
    • DNA-ligand interactions detected by proton selective and non-selective spin-lattice relaxation rate analysis
    • Bonechi, C.; Donati, A.; Picchi, M. P.; Rossi, C.; Tiezzi, E. DNA-ligand interactions detected by proton selective and non-selective spin-lattice relaxation rate analysis. Coll. Surf. A., 1996, 115, 89-95.
    • (1996) Coll. Surf. A , vol.115 , pp. 89-95
    • Bonechi, C.1    Donati, A.2    Picchi, M.P.3    Rossi, C.4    Tiezzi, E.5
  • 41
    • 13444257561 scopus 로고    scopus 로고
    • Fast simultaneous measurement of longitudinal and transverse NMR relaxation times in a single continuous wave free precession experiment
    • Venâncio, T; Engelsberg, M.; Avevedo, R. B. V.; Alem, N. E. R.; Colnago, L. A. Fast simultaneous measurement of longitudinal and transverse NMR relaxation times in a single continuous wave free precession experiment. J. Magn. Reson., 2005, 173, 34-39.
    • (2005) J. Magn. Reson , vol.173 , pp. 34-39
    • Venâncio, T.1    Engelsberg, M.2    Avevedo, R.B.V.3    Alem, N.E.R.4    Colnago, L.A.5
  • 45
    • 0030819428 scopus 로고    scopus 로고
    • The interaction of DNA with intercalating agents probed by sodium-23 NMR relaxation rates
    • Casu , M.; Puligheddu , S.; Saba , G.; Marincola, F. C.; Orellana , G.; Lai, A. The interaction of DNA with intercalating agents probed by sodium-23 NMR relaxation rates. J. Biomol. Struct. Dyn., 1997, 15, 37-43.
    • (1997) J. Biomol. Struct. Dyn , vol.15 , pp. 37-43
    • Casu, M.1    Puligheddu, S.2    Saba, G.3    Marincola, F.C.4    Orellana, G.5    Lai, A.6
  • 46
    • 0029885769 scopus 로고    scopus 로고
    • Binding of Ru(II) polyazaaromatic complexes to DNA: A Na-23 NMR spin-lattice relaxation study
    • Casu, M.; Saba, G.; Lai, A.; Luhmer, M.; KirschDeMesmaeker, A.; Moucheron, C.; Reisse, J. Binding of Ru(II) polyazaaromatic complexes to DNA: A Na-23 NMR spin-lattice relaxation study. Biophys. Chem., 1996, 59, 133-138.
    • (1996) Biophys. Chem , vol.59 , pp. 133-138
    • Casu, M.1    Saba, G.2    Lai, A.3    Luhmer, M.4    KirschDeMesmaeker, A.5    Moucheron, C.6    Reisse, J.7
  • 47
    • 0010870019 scopus 로고
    • Nuclear-magnetic-resonance as a tool for the identification of specific DNA-ligand interaction
    • Rossi C.; Donati, A.; Sansoni, M. R. Nuclear-magnetic-resonance as a tool for the identification of specific DNA-ligand interaction. Chem. Phys. Lett., 1992, 189, 278-280.
    • (1992) Chem. Phys. Lett , vol.189 , pp. 278-280
    • Rossi, C.1    Donati, A.2    Sansoni, M.R.3
  • 49
    • 33748744861 scopus 로고    scopus 로고
    • Sega, E. M.; Tormena, C. F.; de Oliveira, P. R;, R. Rittner; Tinoco, L. W.; Figueroa-Villar, J. D.; Hoehr, N. F. Solvent effects in the (2)J(HH), (3)J(HH), (1)J(NC) and (2)J(NC) coupling constants in the NMR spectrum of acetylcholine chloride. J. Mol. Struct., 2006, 797, 44-48.
    • Sega, E. M.; Tormena, C. F.; de Oliveira, P. R;, R. Rittner; Tinoco, L. W.; Figueroa-Villar, J. D.; Hoehr, N. F. Solvent effects in the (2)J(HH), (3)J(HH), (1)J(NC) and (2)J(NC) coupling constants in the NMR spectrum of acetylcholine chloride. J. Mol. Struct., 2006, 797, 44-48.
  • 50
    • 3342896722 scopus 로고    scopus 로고
    • Investigation of microenvironmental factors influencing the longitudinal relaxation times of drugs and other compounds
    • Dzik-Jurasz; A. S. K.; Leach, M. O.; Rowland, I. J. Investigation of microenvironmental factors influencing the longitudinal relaxation times of drugs and other compounds. Magn. Reson. Imag., 2004, 22, 973-982.
    • (2004) Magn. Reson. Imag , vol.22 , pp. 973-982
    • Dzik-Jurasz, A.S.K.1    Leach, M.O.2    Rowland, I.J.3
  • 51
    • 55249086098 scopus 로고    scopus 로고
    • 1H NMR study of methotrexate-serum albumin (MTX-SA) binding in reumathoid arthritis
    • Sulkoska, A.; Maciazek-Jurczyk, M.; Bojko, B.; Równica, J.; Sulkowski, W. W. 1H NMR study of methotrexate-serum albumin (MTX-SA) binding in reumathoid arthritis. J. Mol. Struct., 2008, 891, 278-283.
    • (2008) J. Mol. Struct , vol.891 , pp. 278-283
    • Sulkoska, A.1    Maciazek-Jurczyk, M.2    Bojko, B.3    Równica, J.4    Sulkowski, W.W.5
  • 52
    • 0033237596 scopus 로고    scopus 로고
    • NMR diffusion and relaxation study of drug-protein interaction
    • Luo, R. S.; Liu, M. L.; Mao, X. A. NMR diffusion and relaxation study of drug-protein interaction. Spectrochim. Acta A, 1999, 55, 1897-1901.
    • (1999) Spectrochim. Acta A , vol.55 , pp. 1897-1901
    • Luo, R.S.1    Liu, M.L.2    Mao, X.A.3
  • 53
    • 0012317481 scopus 로고
    • 1H NMR studies of the interaction of tricyclic antidepressant drugs with dodecyl-dimethylammonium chloride micelles
    • 1H NMR studies of the interaction of tricyclic antidepressant drugs with dodecyl-dimethylammonium chloride micelles. J. Phys. Chem., 1992, 96, 3146-3151.
    • (1992) J. Phys. Chem , vol.96 , pp. 3146-3151
    • Casarotto, M.G.1    Craik, D.J.2
  • 54
    • 0141555649 scopus 로고    scopus 로고
    • Interaction of daunomycin with dipalmitoylphosphatidylcholine model membranes. A 1H NMR study
    • Calzolai, L.; Gaggelli, E.; Maccotta, A.; Valensin G., Interaction of daunomycin with dipalmitoylphosphatidylcholine model membranes. A 1H NMR study. J. Magn. Reson. B, 1996, 112, 228-235.
    • (1996) J. Magn. Reson. B , vol.112 , pp. 228-235
    • Calzolai, L.1    Gaggelli, E.2    Maccotta, A.3    Valensin, G.4
  • 55
    • 0035144987 scopus 로고    scopus 로고
    • A model for the mechanism of action of cationic antibiotics
    • Interaction of aromatic guanyl hydrazones with micelles by NMR
    • Borges, N. N.; Figueroa-Villar J. D., Interaction of aromatic guanyl hydrazones with micelles by NMR: A model for the mechanism of action of cationic antibiotics. Biopolymers, 2001, 62, 9-14.
    • (2001) Biopolymers , vol.62 , pp. 9-14
    • Borges, N.N.1    Figueroa-Villar, J.D.2
  • 56
    • 6344263717 scopus 로고    scopus 로고
    • Synthesis, trypanocidal activity and micelle interaction studies of biguanylhydrazones analogous to pentamidine
    • Borges, N. N.; Messeder, J. C.; Figueroa-Villar, J. D. Synthesis, trypanocidal activity and micelle interaction studies of biguanylhydrazones analogous to pentamidine. Eur. J. Med. Chem., 2004, 39, 925-929.
    • (2004) Eur. J. Med. Chem , vol.39 , pp. 925-929
    • Borges, N.N.1    Messeder, J.C.2    Figueroa-Villar, J.D.3
  • 57
    • 0141727693 scopus 로고    scopus 로고
    • Formation of p-cresol:piperazine complex in solution monitored by spin-lattice relaxation times and pulsed field gradient NMR diffusion measurements
    • de Carvalho, E. M.; Velloso, M. H. R.; Tinoco, L. W.; Figueroa-Villar, J. D. Formation of p-cresol:piperazine complex in solution monitored by spin-lattice relaxation times and pulsed field gradient NMR diffusion measurements. J. Magn. Reson., 2003, 164, 197-204.
    • (2003) J. Magn. Reson , vol.164 , pp. 197-204
    • de Carvalho, E.M.1    Velloso, M.H.R.2    Tinoco, L.W.3    Figueroa-Villar, J.D.4
  • 58
    • 84989052410 scopus 로고
    • Measurement of interproton distances from cross-relaxation rates determined by a selective NULL inversion-recovery NMR method
    • Liu, M.; Farant, R. D.; Lindon, J. C. Measurement of interproton distances from cross-relaxation rates determined by a selective NULL inversion-recovery NMR method. Magn. Reson. Chem., 1992, 30, 173-176.
    • (1992) Magn. Reson. Chem , vol.30 , pp. 173-176
    • Liu, M.1    Farant, R.D.2    Lindon, J.C.3
  • 61
    • 0023923826 scopus 로고
    • Measuring relative acetylcholine receptor agonist binding by selective proton nuclear magnetic resonance relaxation experiments
    • Behling, R. W.; Yamane, T.; Navon, G.; Sammon, M. J.; Jelinski, L. W. Measuring relative acetylcholine receptor agonist binding by selective proton nuclear magnetic resonance relaxation experiments. Biophys. J., 1988, 53, 947-954.
    • (1988) Biophys. J , vol.53 , pp. 947-954
    • Behling, R.W.1    Yamane, T.2    Navon, G.3    Sammon, M.J.4    Jelinski, L.W.5
  • 62
    • 36849120395 scopus 로고
    • Proton relaxation in dilute solutions of cobalt (II) and nickel (II) ions in methanol and the rate of methanol exchange of the solvent sphere
    • Luz, C.; Meiboom, G. Proton relaxation in dilute solutions of cobalt (II) and nickel (II) ions in methanol and the rate of methanol exchange of the solvent sphere. J. Chem. Phys., 1964, 40, 2686-2692.
    • (1964) J. Chem. Phys , vol.40 , pp. 2686-2692
    • Luz, C.1    Meiboom, G.2
  • 64
    • 50549098465 scopus 로고    scopus 로고
    • Use of fluorinated functionality in enzyme inhibitor development: Mechanistic and analytical advantages
    • Berkowitz, D. B.; Karukurichi, K. R.; Salud-Bea, R.; Nelson, D. L.; McCune, C. D. Use of fluorinated functionality in enzyme inhibitor development: Mechanistic and analytical advantages. J. Fluor. Chem., 2008, 129, 731-742.
    • (2008) J. Fluor. Chem , vol.129 , pp. 731-742
    • Berkowitz, D.B.1    Karukurichi, K.R.2    Salud-Bea, R.3    Nelson, D.L.4    McCune, C.D.5
  • 65
    • 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. A.; 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., 2003, 125, 7696-7703.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 7696-7703
    • Dalvit, C.1    Fagerness, P.E.2    Hadden, D.T.A.3    Sarver, R.W.4    Stockman, B.J.5
  • 66
    • 36049036606 scopus 로고    scopus 로고
    • Ligand- and substrate-based 19F NMR screening: Principles and applications to drug discovery
    • Dalvit. C. Ligand- and substrate-based 19F NMR screening: Principles and applications to drug discovery. Progr. Nucl. Magn. Reson. Spectrosc., 2007, 51, 243-271.
    • (2007) Progr. Nucl. Magn. Reson. Spectrosc , vol.51 , pp. 243-271
    • Dalvit, C.1
  • 69
  • 70
    • 55949093411 scopus 로고    scopus 로고
    • Probing the binding of propanolol enantiomers to α-acid glycoprotein with ligand-detected NMR experiments
    • Becker, B. A.; Larive, C. K. Probing the binding of propanolol enantiomers to α-acid glycoprotein with ligand-detected NMR experiments. J. Phys. Chem. B, 2008, 112, 13581-13587.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 13581-13587
    • Becker, B.A.1    Larive, C.K.2
  • 71
  • 72
    • 37849045887 scopus 로고    scopus 로고
    • Lanthanide paramagnetic probes for NMR spectroscopic studies of molecular conformational dynamics in solution: Applications to macrocyclic molecules
    • Babailov, S. P. Lanthanide paramagnetic probes for NMR spectroscopic studies of molecular conformational dynamics in solution: Applications to macrocyclic molecules. Prog. Nucl. Magn. Reson. Spectrosc., 2008, 52, 1-21.
    • (2008) Prog. Nucl. Magn. Reson. Spectrosc , vol.52 , pp. 1-21
    • Babailov, S.P.1
  • 73
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie, J. R.; Shortle, D. Characterization of long range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol., 1997, 268, 158-169.
    • (1997) J. Mol. Biol , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 74
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long range structure in the denatured state of staphylococcal nuclease II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie, J. R.; Shortle, D. Characterization of long range structure in the denatured state of staphylococcal nuclease II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 1997, 268, 170-184.
    • (1997) J. Mol. Biol , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 75
    • 0021772469 scopus 로고
    • Distance measurements in spin-labeled lysozyme
    • Schmidt, P. G., and Kuntz, I. D. Distance measurements in spin-labeled lysozyme. Biochemistry, 1984, 23, 4261-4266.
    • (1984) Biochemistry , vol.23 , pp. 4261-4266
    • Schmidt, P.G.1    Kuntz, I.D.2
  • 76
    • 0042890562 scopus 로고    scopus 로고
    • Niccolai, N.; Spiga, Bernini, O. A.; Scarselli, M.; Ciutti, A.; Fiaschi, I.; Chiellini, S.; Molinari, H.; Temussi, P. A. NMR studies of protein hydration and TEMPOL accessibility. J. Mol. Biol., 2003, 332, 437-447.
    • Niccolai, N.; Spiga, Bernini, O. A.; Scarselli, M.; Ciutti, A.; Fiaschi, I.; Chiellini, S.; Molinari, H.; Temussi, P. A. NMR studies of protein hydration and TEMPOL accessibility. J. Mol. Biol., 2003, 332, 437-447.
  • 77
    • 47249159078 scopus 로고    scopus 로고
    • A soluble oligomer of tau associated with fiber formation analyzed by NMR
    • Peterson, D. W.; Zhou, H.; Dahlquist, F. W.; Lew, J. A soluble oligomer of tau associated with fiber formation analyzed by NMR. Biochemistry, 2008, 47, 7393-7404.
    • (2008) Biochemistry , vol.47 , pp. 7393-7404
    • Peterson, D.W.1    Zhou, H.2    Dahlquist, F.W.3    Lew, J.4
  • 78
    • 55549133637 scopus 로고    scopus 로고
    • Keizers, P. H. J.; Saragliadis, A.; H, Yoshitaka; Overhand, M.; Ubbink, M. Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment. J. Am. Chem. Soc., 2008, 130, 14802-14812.
    • Keizers, P. H. J.; Saragliadis, A.; H, Yoshitaka; Overhand, M.; Ubbink, M. Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment. J. Am. Chem. Soc., 2008, 130, 14802-14812.
  • 79
    • 37549050579 scopus 로고    scopus 로고
    • Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR
    • Vlasie, M. D.; Fernández-Busnadiego, R.; Prudêncio, M.; Ubbink, M. Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR. J. Mol. Biol., 2008, 375, 1405-1415.
    • (2008) J. Mol. Biol , vol.375 , pp. 1405-1415
    • Vlasie, M.D.1    Fernández-Busnadiego, R.2    Prudêncio, M.3    Ubbink, M.4
  • 81
    • 0019003286 scopus 로고
    • Preparation and properties of chromium III adenosine 5′-triphosphate chromium III, adenosine 5′-diphosphate and related chromium III complex
    • Dunaway-Mariano, D.; Cleland, W. W. Preparation and properties of chromium III adenosine 5′-triphosphate chromium III, adenosine 5′-diphosphate and related chromium III complex. Biochemistry, 1980, 19, 1496-1505.
    • (1980) Biochemistry , vol.19 , pp. 1496-1505
    • Dunaway-Mariano, D.1    Cleland, W.W.2
  • 82
    • 53249147452 scopus 로고    scopus 로고
    • Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study
    • Abbassi, F.; Galanth, C.; Amiche, M.; Saito, K.; Piesse, C.; Zargarian, L.; Hani, K.; Nicolas, P.; Lequin, O.; Ladram, A. Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study. Biochemistry, 2008, 47, 10513-10525.
    • (2008) Biochemistry , vol.47 , pp. 10513-10525
    • Abbassi, F.1    Galanth, C.2    Amiche, M.3    Saito, K.4    Piesse, C.5    Zargarian, L.6    Hani, K.7    Nicolas, P.8    Lequin, O.9    Ladram, A.10
  • 83
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data
    • Battiste, J. L.; Wagner, G. Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data. Biochemistry, 2000, 39, 5355-5365.
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 84
    • 46949092098 scopus 로고    scopus 로고
    • Mobility of TOAC spin-labelled peptides binding to the Src SH3 domain studied by paramagnetic NMR
    • Lindfors, H. E.; de Koning, P. E.; Drijfhout, J. W.; Venezia, B.; Ubbink, M. Mobility of TOAC spin-labelled peptides binding to the Src SH3 domain studied by paramagnetic NMR. J. Biomol. NMR, 2008, 41, 157-167.
    • (2008) J. Biomol. NMR , vol.41 , pp. 157-167
    • Lindfors, H.E.1    de Koning, P.E.2    Drijfhout, J.W.3    Venezia, B.4    Ubbink, M.5
  • 85
    • 39549122002 scopus 로고    scopus 로고
    • Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex
    • Kale, S.; Ulas, G.; Song, J.; Brudvig, G. W.; Furey, W.; Jordan, F. Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex. Proc. Natl. Acad. Sci. USA, 2008, 105, 1158-1163.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1158-1163
    • Kale, S.1    Ulas, G.2    Song, J.3    Brudvig, G.W.4    Furey, W.5    Jordan, F.6
  • 87
    • 33745038205 scopus 로고    scopus 로고
    • NMR structures of paramagnetic metalloproteins
    • Banci, L.; Piccioli, M.; Arnesano, F. NMR structures of paramagnetic metalloproteins. Q Rev. Biophys., 2005, 38, 167-219.
    • (2005) Q Rev. Biophys , vol.38 , pp. 167-219
    • Banci, L.1    Piccioli, M.2    Arnesano, F.3
  • 88
    • 56749172641 scopus 로고    scopus 로고
    • Detailed structural characterization of unbound protein phosphatase 1 inhibitors
    • Dancheck, B.; Nairn, A. C. and Peti, W. Detailed structural characterization of unbound protein phosphatase 1 inhibitors. Biochemistry, 2008, 47, 12346-12356.
    • (2008) Biochemistry , vol.47 , pp. 12346-12356
    • Dancheck, B.1    Nairn, A.C.2    Peti, W.3
  • 89
    • 55849120858 scopus 로고    scopus 로고
    • Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with Its RPP29 protein partner
    • Amero, C. D.; Boomershine, W. P.; Xu, Y.; Foster, M. Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with Its RPP29 protein partner. Biochemistry, 2008, 47, 11704-11710.
    • (2008) Biochemistry , vol.47 , pp. 11704-11710
    • Amero, C.D.1    Boomershine, W.P.2    Xu, Y.3    Foster, M.4
  • 90
    • 56249124978 scopus 로고    scopus 로고
    • Solution structure of the supramolecular adduct between a liver cytosolic bile acid binding protein and a bile acid-based gadolinium(III)- chelate, a potential hepatospecific magnetic resonance imaging contrast agent
    • Tomaselli, S.; Zanzoni, S.; Ragona, L.; Gianolio, E.; Aime, S.; Assfalg, M.; Molinari, H. Solution structure of the supramolecular adduct between a liver cytosolic bile acid binding protein and a bile acid-based gadolinium(III)- chelate, a potential hepatospecific magnetic resonance imaging contrast agent. J. Med. Chem., 2008, 51, 6782-6792.
    • (2008) J. Med. Chem , vol.51 , pp. 6782-6792
    • Tomaselli, S.1    Zanzoni, S.2    Ragona, L.3    Gianolio, E.4    Aime, S.5    Assfalg, M.6    Molinari, H.7
  • 91
    • 0038515326 scopus 로고    scopus 로고
    • Orientation of 1,3-bisphosphoglycerate analogs bound to phosphoglycerate kinase
    • Jakeman, D. L.; Ivory, A. J., Blackburn, G. M.; Williamson, M. P. Orientation of 1,3-bisphosphoglycerate analogs bound to phosphoglycerate kinase. J. Biol. Chem., 2003, 278, 10957-10962.
    • (2003) J. Biol. Chem , vol.278 , pp. 10957-10962
    • Jakeman, D.L.1    Ivory, A.J.2    Blackburn, G.M.3    Williamson, M.P.4
  • 92
    • 51249097829 scopus 로고    scopus 로고
    • The affinity of ETS-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region
    • Lee, G. M.; Pufall, M. A.; Meeker, C. A.; Kang, H.S.; Graves, B. J.; McIntosh, L. P. The affinity of ETS-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region. J. Mol. Biol., 2008, 382, 1014-1030.
    • (2008) J. Mol. Biol , vol.382 , pp. 1014-1030
    • Lee, G.M.1    Pufall, M.A.2    Meeker, C.A.3    Kang, H.S.4    Graves, B.J.5    McIntosh, L.P.6
  • 94
    • 45749120849 scopus 로고    scopus 로고
    • Study of the interaction of gfg tripeptide with cesium perfluorooctanoate micelles by means of NMR Spectroscopy and MD simulations
    • Pizzanelli, S.; Forte, C.; Monti, S. Study of the interaction of gfg tripeptide with cesium perfluorooctanoate micelles by means of NMR Spectroscopy and MD simulations. Langmuir, 2008, 24, 5809-5815.
    • (2008) Langmuir , vol.24 , pp. 5809-5815
    • Pizzanelli, S.1    Forte, C.2    Monti, S.3
  • 95
    • 0037160426 scopus 로고    scopus 로고
    • Pintacuda, G.; Otting, G. Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate. J. Am. Chem. Soc., 2002, 124, 372-373.
    • Pintacuda, G.; Otting, G. Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate. J. Am. Chem. Soc., 2002, 124, 372-373.
  • 98
    • 34047156546 scopus 로고    scopus 로고
    • Discovery of ligands for NURR1 by combined use of NMR screening with different isotopic and spin-labeling strategies
    • Poppe, L.; Harvey, T. S.; Mohr, C.; Zondlo, J.; Tegley, C. M.; Nuanmanee, O.; Cheetham, J. Discovery of ligands for NURR1 by combined use of NMR screening with different isotopic and spin-labeling strategies. J. Biomol. Screen., 2007, 301-311.
    • (2007) J. Biomol. Screen , pp. 301-311
    • Poppe, L.1    Harvey, T.S.2    Mohr, C.3    Zondlo, J.4    Tegley, C.M.5    Nuanmanee, O.6    Cheetham, J.7


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