메뉴 건너뛰기




Volumn 203, Issue 1, 2010, Pages 1-10

Group epitope mapping considering relaxation of the ligand (GEM-CRL): Including longitudinal relaxation rates in the analysis of saturation transfer difference (STD) experiments

Author keywords

CORCEMA ST; GEM; GEM CRL; Jacalin; STD; Trehalose; TreR

Indexed keywords

CALCULATED VALUES; CORCEMA-ST; CORCEMA-ST CALCULATIONS; CROSSRELAXATION; EPITOPE MAPPING; EXPERIMENTAL CONDITIONS; JACALIN; LONGITUDINAL RELAXATION; MAGNETISATION; PROTEIN PROTONS; PROTEIN-LIGAND INTERACTIONS; RELAXATION MATRIX; SATURATION-TRANSFER DIFFERENCES; THEORETICAL MODELS;

EID: 75749110898     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2009.11.015     Document Type: Article
Times cited : (48)

References (21)
  • 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. Int. Ed. 42 (2003) 864-890
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 3
    • 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. Int. Ed. 38 (1999) 1784-1788
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 4
    • 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
  • 5
    • 0043032424 scopus 로고    scopus 로고
    • The effect of relaxation on the epitope mapping by saturation transfer difference NMR
    • Yan J., Kline A.D., Mo H., Shapiro M.J., and Zartler E.R. The effect of relaxation on the epitope mapping by saturation transfer difference NMR. J. Magn. Reson. 163 (2003) 270-276
    • (2003) J. Magn. Reson. , vol.163 , pp. 270-276
    • Yan, J.1    Kline, A.D.2    Mo, H.3    Shapiro, M.J.4    Zartler, E.R.5
  • 6
    • 33748122687 scopus 로고    scopus 로고
    • Complete relaxation and conformational exchange matrix analysis of STD-NMR spectra of ligand-receptor complexes
    • Krishna N.R., and Jayalakshmi V. Complete relaxation and conformational exchange matrix analysis of STD-NMR spectra of ligand-receptor complexes. Prog. Nucl. Magn. Reson. Spectrosc. 49 (2006) 1-25
    • (2006) Prog. Nucl. Magn. Reson. Spectrosc. , vol.49 , pp. 1-25
    • Krishna, N.R.1    Jayalakshmi, V.2
  • 7
    • 0036290185 scopus 로고    scopus 로고
    • Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes
    • Jayalakshmi V., and Krishna N.R. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes. J. Magn. Reson. 155 (2002) 106-118
    • (2002) J. Magn. Reson. , vol.155 , pp. 106-118
    • Jayalakshmi, V.1    Krishna, N.R.2
  • 8
    • 1842450536 scopus 로고    scopus 로고
    • NMR-based characterization of phenothiazines as a RNA binding scaffold
    • Mayer M., and James T.L. NMR-based characterization of phenothiazines as a RNA binding scaffold. J. Am. Chem. Soc. 126 (2004) 4453-4460
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4453-4460
    • Mayer, M.1    James, T.L.2
  • 9
    • 54349083079 scopus 로고    scopus 로고
    • Saturation transfer difference (STD) NMR spectroscopy characterization of dual binding mode of a mannose disaccharide to DC-SIGN
    • Angulo J., Díaz I., Reina J.J., Tabarani G., Fieschi F., Rojo J., and Nieto P. Saturation transfer difference (STD) NMR spectroscopy characterization of dual binding mode of a mannose disaccharide to DC-SIGN. ChemBioChem 9 (2008) 2225-2227
    • (2008) ChemBioChem , vol.9 , pp. 2225-2227
    • Angulo, J.1    Díaz, I.2    Reina, J.J.3    Tabarani, G.4    Fieschi, F.5    Rojo, J.6    Nieto, P.7
  • 10
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • Solomon I. Relaxation processes in a system of two spins. Phys. Rev. 99 (1955) 559
    • (1955) Phys. Rev. , vol.99 , pp. 559
    • Solomon, I.1
  • 13
    • 75749136202 scopus 로고    scopus 로고
    • See PDB entries: 1UGW, 1UGY.
    • See PDB entries: 1UGW, 1UGY.
  • 15
    • 0023002029 scopus 로고
    • Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-d-Gal(1-3)d-GalNAc)
    • Sastry M.V., Banarjee P., Patanjali S.R., Swamy M.J., Swarnalatha G.V., and Surolia A. Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-d-Gal(1-3)d-GalNAc). J. Biol. Chem. 261 (1986) 11726-11733
    • (1986) J. Biol. Chem. , vol.261 , pp. 11726-11733
    • Sastry, M.V.1    Banarjee, P.2    Patanjali, S.R.3    Swamy, M.J.4    Swarnalatha, G.V.5    Surolia, A.6
  • 16
    • 0025141799 scopus 로고
    • Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin (Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study
    • Mahanta S.K., Sastry M.V., and Surolia A. Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin (Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study. Biochem. J. 265 (1990) 831-840
    • (1990) Biochem. J. , vol.265 , pp. 831-840
    • Mahanta, S.K.1    Sastry, M.V.2    Surolia, A.3
  • 17
    • 0032520680 scopus 로고    scopus 로고
    • Jacalin: a jackfruit (Artocarpus heterophyllus) seed-derived lectin of versatile applications in immunobiological research
    • Kabir S. Jacalin: a jackfruit (Artocarpus heterophyllus) seed-derived lectin of versatile applications in immunobiological research. J. Immunol. Methods 212 (1998) 193-211
    • (1998) J. Immunol. Methods , vol.212 , pp. 193-211
    • Kabir, S.1
  • 18
    • 0029941757 scopus 로고    scopus 로고
    • A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold
    • Sankaranarayanan R., Sekar K., Banerjee R., Sharma V., Surolia A., and Vijayan M. A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold. Nat. Struct. Biol. 3 (1996) 596-603
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 596-603
    • Sankaranarayanan, R.1    Sekar, K.2    Banerjee, R.3    Sharma, V.4    Surolia, A.5    Vijayan, M.6
  • 19
    • 0031009431 scopus 로고    scopus 로고
    • Characterization of TreR, the major regulator of the Escherichia coli trehalose system
    • Horlacher R., and Boos W. Characterization of TreR, the major regulator of the Escherichia coli trehalose system. J. Biol. Chem. 272 (1997) 13026-13032
    • (1997) J. Biol. Chem. , vol.272 , pp. 13026-13032
    • Horlacher, R.1    Boos, W.2
  • 20
    • 0031677841 scopus 로고    scopus 로고
    • Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose
    • Hars U., Horlacher R., Boos W., Welte W., and Diederichs K. Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose. Protein Sci. 7 (1998) 2511-2521
    • (1998) Protein Sci. , vol.7 , pp. 2511-2521
    • Hars, U.1    Horlacher, R.2    Boos, W.3    Welte, W.4    Diederichs, K.5
  • 21
    • 0030958608 scopus 로고    scopus 로고
    • NMR experiments for the detection of NOEs and scalar coupling constants between equivalent protons in trehalose-containing molecules
    • Poveda A., Vicent C., Penadés S., and Jiménez-Barbero J. NMR experiments for the detection of NOEs and scalar coupling constants between equivalent protons in trehalose-containing molecules. Carbohydr. Res. 301 (1997) 5-10
    • (1997) Carbohydr. Res. , vol.301 , pp. 5-10
    • Poveda, A.1    Vicent, C.2    Penadés, S.3    Jiménez-Barbero, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.