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Volumn 55, Issue 23, 2012, Pages 10786-10790

Rapid protein-ligand costructures from sparse NOE data

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; LIGAND;

EID: 84871005919     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm301396d     Document Type: Article
Times cited : (21)

References (29)
  • 1
    • 34447270269 scopus 로고    scopus 로고
    • Structure based drug design for HIV protease: From molecular modeling to cheminformatics
    • Volarath, P.; Harrison, R. W.; Weber, I. T. Structure based drug design for HIV protease: from molecular modeling to cheminformatics Curr. Top. Med. Chem. 2007, 7 (10) 1030-1038
    • (2007) Curr. Top. Med. Chem. , vol.7 , Issue.10 , pp. 1030-1038
    • Volarath, P.1    Harrison, R.W.2    Weber, I.T.3
  • 2
    • 0348227698 scopus 로고    scopus 로고
    • The impact of structure-guided drug design on clinical agents
    • Hardy, L. W.; Malikayil, A. The impact of structure-guided drug design on clinical agents Curr. Drug Discovery 2003, 3, 15-20
    • (2003) Curr. Drug Discovery , vol.3 , pp. 15-20
    • Hardy, L.W.1    Malikayil, A.2
  • 3
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk, P. J.; Greer, J. A decade of fragment-based drug design: strategic advances and lessons learned Nature Rev. Drug Discovery 2007, 6, 211-219
    • (2007) Nature Rev. Drug Discovery , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 5
    • 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
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 6
    • 77949523858 scopus 로고    scopus 로고
    • Auto-FACE: An NMR based binding site mapping program for fast chemical exchange protein-ligand systems
    • Krishnamoorthy, J.; Yu, V. C. K.; Mok, Y.-K. Auto-FACE: an NMR based binding site mapping program for fast chemical exchange protein-ligand systems PLoS One 2010, 5 (2) e8943
    • (2010) PLoS One , vol.5 , Issue.2 , pp. 8943
    • Krishnamoorthy, J.1    Yu, V.C.K.2    Mok, Y.-K.3
  • 8
    • 0036175914 scopus 로고    scopus 로고
    • NMR-based structural characterization of large protein-ligand interactions
    • Pellecchia, M.; Meininger, D.; Dong, Q.; Chang, E.; Jack, R.; Sem, D. S. NMR-based structural characterization of large protein-ligand interactions J. Biomol. NMR 2002, 22, 165-173
    • (2002) J. Biomol. NMR , vol.22 , pp. 165-173
    • Pellecchia, M.1    Meininger, D.2    Dong, Q.3    Chang, E.4    Jack, R.5    Sem, D.S.6
  • 9
    • 33744913530 scopus 로고    scopus 로고
    • Protein-ligand NOE matching: A high-throughput method for binding pose evaluation that does not require protein NMR resonance assignments
    • Constantine, K. L.; Davis, M. E.; Metzler, W.; Mueller, L.; Claus, B. L. Protein-ligand NOE matching: a high-throughput method for binding pose evaluation that does not require protein NMR resonance assignments J. Am. Chem. Soc. 2006, 128, 7252-7263
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7252-7263
    • Constantine, K.L.1    Davis, M.E.2    Metzler, W.3    Mueller, L.4    Claus, B.L.5
  • 10
    • 28544434796 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex
    • Yu, L.; Sun, C.; Song, D.; Shen, J.; Xu, N.; Gunasekera, A.; Hajduk, P. J.; Olejniczak, E. T. Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex Biochemistry 2005, 44, 15834-15841
    • (2005) Biochemistry , vol.44 , pp. 15834-15841
    • Yu, L.1    Sun, C.2    Song, D.3    Shen, J.4    Xu, N.5    Gunasekera, A.6    Hajduk, P.J.7    Olejniczak, E.T.8
  • 11
    • 0242407224 scopus 로고    scopus 로고
    • Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods
    • Tugarinov, V.; Kay, L. E. Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods J. Am. Chem. Soc. 2003, 125, 13868-13878
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13868-13878
    • Tugarinov, V.1    Kay, L.E.2
  • 12
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking
    • De Vries, S. J.; Van Dijk, M.; Bonvin, A. M. J. J. The HADDOCK web server for data-driven biomolecular docking Nature Protoc. 2010, 5, 883-897
    • (2010) Nature Protoc. , vol.5 , pp. 883-897
    • De Vries, S.J.1    Van Dijk, M.2    Bonvin, A.M.J.J.3
  • 13
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers, R.; Kay, L. E. Quantitative dynamics and binding studies of the 20S proteasome by NMR Nature 2007, 445, 618-622
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 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 Discovery Today 2007, 12, 1032-1039
    • (2007) Drug Discovery Today , vol.12 , pp. 1032-1039
    • Siegal, G.1    Ab, E.2    Schultz, J.3
  • 18
    • 44949276869 scopus 로고
    • Sensitivity improvement correlation NMR spectroscopy
    • Palmer, A. G., III; Cavanagh, J.; Wright, P. E.; Rance, M. Sensitivity improvement correlation NMR spectroscopy J. Magn. Reson. 1991, 93, 151-170
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Iii, G.P.A.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 22
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E.; Keifer, P.; Saarinen, T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J. Am. Chem. Soc. 1992, 114, 10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 23
    • 44049118259 scopus 로고
    • Experiments for recording pureabsorption heteronuclear correlation spectra using pulsed field gradients
    • Davis, A. L.; Keeler, J.; Laue, E. D.; Moskau, D. Experiments for recording pureabsorption heteronuclear correlation spectra using pulsed field gradients J. Magn. Reson. 1992, 98, 207-216
    • (1992) J. Magn. Reson. , vol.98 , pp. 207-216
    • Davis, A.L.1    Keeler, J.2    Laue, E.D.3    Moskau, D.4
  • 26
    • 40149093773 scopus 로고    scopus 로고
    • Rapid protein-ligand costructures using chemical shift perturbations
    • Stark, J.; Powers, R. Rapid protein-ligand costructures using chemical shift perturbations J. Am. Chem. Soc. 2008, 130, 535-545
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 535-545
    • Stark, J.1    Powers, R.2
  • 27
    • 79955574923 scopus 로고    scopus 로고
    • version 1.2r3pre; Schrödinger, LLC: Portland, OR
    • The PyMOL Molecular Graphics System, version 1.2r3pre; Schrödinger, LLC: Portland, OR.
    • The PyMOL Molecular Graphics System
  • 28
    • 77949411905 scopus 로고    scopus 로고
    • A comprehensive and cost-effective NMR spectroscopy of methyl groups in large proteins
    • Otten, R.; Chu, B.; Krewulak, K. D.; Vogel, H. J.; Mulder, F. A. A. A comprehensive and cost-effective NMR spectroscopy of methyl groups in large proteins J. Am. Chem. Soc. 2010, 132 (9) 2952-2960
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.9 , pp. 2952-2960
    • Otten, R.1    Chu, B.2    Krewulak, K.D.3    Vogel, H.J.4    Mulder, F.A.A.5
  • 29
    • 80755190088 scopus 로고    scopus 로고
    • Automated sequence- and stereospecific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy
    • Venditti, V.; Fawzi, N. L.; Clore, G. M. Automated sequence- and stereospecific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy J. Biomol. NMR 2011, 51, 319-328
    • (2011) J. Biomol. NMR , vol.51 , pp. 319-328
    • Venditti, V.1    Fawzi, N.L.2    Clore, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.