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Volumn 385, Issue 2, 2009, Pages 380-382

Saturation transfer difference nuclear magnetic resonance study on the specific binding of ligand to protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DISSOCIATION; LIGANDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

EID: 58149396562     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.11.022     Document Type: Article
Times cited : (34)

References (15)
  • 1
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer M., and Meyer B. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem. Intl. Ed. 38 (1999) 1784-1788
    • (1999) Angew. Chem. Intl. Ed. , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 2
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • Meyer B., and Peters T. NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angew. Chem. Intl. Ed. 42 (2003) 864-890
    • (2003) Angew. Chem. Intl. Ed. , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 3
    • 2942550654 scopus 로고    scopus 로고
    • NMR experiments for lead generation in drug discovery
    • Peng J.W., Moore J., and Abdul-Manan N. NMR experiments for lead generation in drug discovery. Prog. NMR Spectrosc. 44 (2004) 225-256
    • (2004) Prog. NMR Spectrosc. , vol.44 , pp. 225-256
    • Peng, J.W.1    Moore, J.2    Abdul-Manan, N.3
  • 4
    • 0027145125 scopus 로고
    • Two-dimensional transferred nuclear overhauser effect spectroscopy (TRNOESY) studies of nucleotide conformations in creatine kinase complexes: effects due to weak nonspecific binding
    • Murali N., Jarori G.K., Landy S.B., and Rao B.D.N. Two-dimensional transferred nuclear overhauser effect spectroscopy (TRNOESY) studies of nucleotide conformations in creatine kinase complexes: effects due to weak nonspecific binding. Biochemistry 32 (1993) 12941-12948
    • (1993) Biochemistry , vol.32 , pp. 12941-12948
    • Murali, N.1    Jarori, G.K.2    Landy, S.B.3    Rao, B.D.N.4
  • 5
    • 0008007492 scopus 로고
    • Conformation of acetylcholine bound to the nicotinic acetylcholine receptor
    • Behling R.W., Yamane T., Navon G., and Jelinski L.W. Conformation of acetylcholine bound to the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. USA 85 (1988) 6721-6725
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6721-6725
    • Behling, R.W.1    Yamane, T.2    Navon, G.3    Jelinski, L.W.4
  • 6
    • 20444446596 scopus 로고    scopus 로고
    • Determination of protein-ligand binding affinity by NMR: observations from serum albumin model systems
    • Fielding L., Rutherford S., and Fletcher D. Determination of protein-ligand binding affinity by NMR: observations from serum albumin model systems. Magn. Reson. Chem. 43 (2005) 463-470
    • (2005) Magn. Reson. Chem. , vol.43 , pp. 463-470
    • Fielding, L.1    Rutherford, S.2    Fletcher, D.3
  • 7
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M., and Meyer B. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J. Am. Chem. Soc. 123 (2001) 6108-6117
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 8
    • 0001909564 scopus 로고    scopus 로고
    • Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy
    • Liu M.L., Mao X.A., Ye C.H., Huang H., Nicholson J.K., and Lindon J.C. Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy. J. Magn. Reson. 132 (1998) 125-129
    • (1998) J. Magn. Reson. , vol.132 , pp. 125-129
    • Liu, M.L.1    Mao, X.A.2    Ye, C.H.3    Huang, H.4    Nicholson, J.K.5    Lindon, J.C.6
  • 9
    • 0000172799 scopus 로고
    • The specific binding of l-tryptophan to serum albumin
    • McMenamy R.H., and Oncley J.L. The specific binding of l-tryptophan to serum albumin. J. Biol. Chem. 233 (1958) 1436-1446
    • (1958) J. Biol. Chem. , vol.233 , pp. 1436-1446
    • McMenamy, R.H.1    Oncley, J.L.2
  • 10
    • 0347928719 scopus 로고    scopus 로고
    • Transferred nuclear overhauser effect in nuclear magnetic resonance diffusion measurements of ligand-protein binding
    • Lucas L.H., Yan J., Larive C.K., Zartler E.R., and Shapiro M.J. Transferred nuclear overhauser effect in nuclear magnetic resonance diffusion measurements of ligand-protein binding. Anal. Chem. 75 (2003) 627-634
    • (2003) Anal. Chem. , vol.75 , pp. 627-634
    • Lucas, L.H.1    Yan, J.2    Larive, C.K.3    Zartler, E.R.4    Shapiro, M.J.5
  • 12
    • 10944256235 scopus 로고    scopus 로고
    • Competition STD NMR for the detection of high-affinity ligands and NMR-based screening
    • Wang Y.S., Liu D., and Wyss D.F. Competition STD NMR for the detection of high-affinity ligands and NMR-based screening. Magn. Reson. Chem. 42 (2004) 485-489
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 485-489
    • Wang, Y.S.1    Liu, D.2    Wyss, D.F.3
  • 13
    • 0026021941 scopus 로고
    • Octanoate binding to the indole- and benzodiazepine-binding region of human serum albumin
    • Kragh-Hansen U. Octanoate binding to the indole- and benzodiazepine-binding region of human serum albumin. Biochem. J. 273 (1991) 641-644
    • (1991) Biochem. J. , vol.273 , pp. 641-644
    • Kragh-Hansen, U.1
  • 14
    • 0037030693 scopus 로고    scopus 로고
    • NMR-based screening with competition water-ligand observed via gradient spectroscopy experiments: detection of high-affinity ligands
    • Dalvit C., Fasolini M., Flocco M., Knapp S., Pevarello P., and Veronesi M. NMR-based screening with competition water-ligand observed via gradient spectroscopy experiments: detection of high-affinity ligands. J. Med. Chem. 45 (2002) 2610-2614
    • (2002) J. Med. Chem. , vol.45 , pp. 2610-2614
    • Dalvit, C.1    Fasolini, M.2    Flocco, M.3    Knapp, S.4    Pevarello, P.5    Veronesi, M.6
  • 15
    • 42049098451 scopus 로고    scopus 로고
    • Multivalent drug design and inhibition of cholera toxin by specific and transient protein-ligand interactions
    • Liu J., Begley D., Mitchell D.D., Verlinde C.L.M.J., Varani G., and Fan E. Multivalent drug design and inhibition of cholera toxin by specific and transient protein-ligand interactions. Chem. Biol. Drug Des. 71 (2008) 408-419
    • (2008) Chem. Biol. Drug Des. , vol.71 , pp. 408-419
    • Liu, J.1    Begley, D.2    Mitchell, D.D.3    Verlinde, C.L.M.J.4    Varani, G.5    Fan, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.