메뉴 건너뛰기




Volumn 534, Issue , 2009, Pages 375-386

Saturation transfer difference NMR spectroscopy as a technique to investigate protein-carbohydrate interactions in solution

Author keywords

Enzyme carbohydrate interaction; Epitope mapping; Leishmania major pyrophosphorylase; Nuclear magnetic resonance spectroscopy; Protein carbohydrate interactions; Saturation transfer difference NMR; UDP Glc; UTP

Indexed keywords

LEISHMANIA MAJOR;

EID: 66149141028     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-022-5_26     Document Type: Article
Times cited : (37)

References (14)
  • 1
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • DOI 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0. CO;2-Q
    • Mayer, M., Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angewandte Chemie, International Edition, 38, 1784-1788 (Pubitemid 29290947)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 2
    • 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
    • DOI 10.1021/ja0100120
    • Mayer, M., Meyer, B. (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. Journal of the American Chemical Society 123, 6108-6117 (Pubitemid 32888480)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.25 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 3
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • DOI 10.1002/anie.200390233
    • Meyer, B., Peters, T. (2003) NMR spectroscopy techniques for screening and identifying lig-and binding to protein receptors. Angewandte Chemie, International Edition 42, 864-890 (Pubitemid 36314024)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.8 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 4
    • 3242685827 scopus 로고    scopus 로고
    • Refinement of the conformation of UDP-galactose bound to galactosyltransferase using the STD NMR intensity-restrained CORCEMA optimization
    • DOI 10.1021/ja048703u
    • Jayalakshmi, V., Biet, T., Peters, T., Krishna, N.R. (2004) Refinement of the conformation of UDP-galactose bound to galactosyltrans-ferase using the STD NMR intensity-restrained CORCEMA optimization. Journal of the American Chemical Society 126, 8610-8611 (Pubitemid 38955699)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.28 , pp. 8610-8611
    • Jayalakshmi, V.1    Biet, T.2    Peters, T.3    Krishna, N.R.4
  • 5
    • 0037425531 scopus 로고    scopus 로고
    • Virus-ligand interactions: Identification and characterization of ligand binding by NMR spectroscopy
    • DOI 10.1021/ja027691e
    • Benie, A.J., Moser, R., Bauml, E., Blaas, D., Peters, T. (2003) Virus-ligand interactions: identification and characterization of ligand binding by NMR spectroscopy. Journal of the American Chemical Society 125, 14-15 (Pubitemid 36068625)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.1 , pp. 14-15
    • Benie, A.J.1    Moser, R.2    Bauml, E.3    Blaas, D.4    Peters, T.5
  • 7
    • 12444289530 scopus 로고    scopus 로고
    • 3 in native platelets than in liposomes
    • DOI 10.1021/ja044434w
    • Claasen, B., Axmann, M., Meinecke, M., Meyer, B. (2005) Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spec-troscopy method shows a significantly higher affinity of integrin a(IIb)b3 in native platelets than in liposomes. Journal of the American Chemical Society 127, 916-919 (Pubitemid 40144290)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.3 , pp. 916-919
    • Claasen, B.1    Axmann, M.2    Meinecke, R.3    Meyer, B.4
  • 8
    • 0034725387 scopus 로고    scopus 로고
    • Application of NMR based binding assays to identify key hydroxy groups for intermolecular recognition
    • DOI 10.1021/ja0001916
    • Vogtherr, M., Peters, T. (2000) Application of NMR based binding assays to identify key hydroxy groups for intermolecular recognition. Journal of the American Chemical Society 122, 6093-6099 (Pubitemid 30451114)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.25 , pp. 6093-6099
    • Vogtherr, M.1    Peters, T.2
  • 9
    • 33745216038 scopus 로고    scopus 로고
    • Molecular cloning of the leishmania major udp-glucose pyrophosphorylase, functional characterisation and ligand binding analyses using NMR spectroscopy
    • Lamerz, A.-C., Haselhorst, T., Bergfeld, A. K., von Itzstein, M., Gerardy-Schahn, R. (2006) Molecular cloning of the Leishmania major UDP-glucose pyrophosphorylase, functional characterisation and ligand binding analyses using NMR spectroscopy. Journal of Biological Chemistry, 281(24), 16314-16322
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.24 , pp. 16314-16322
    • Lamerz, A.-C.1    Haselhorst, T.2    Bergfeld, A.K.3    Von Itzstein, M.4    Gerardy-Schahn, R.5
  • 10
  • 11
    • 84858068030 scopus 로고    scopus 로고
    • SUGABASE http://www.boc.chem.uu.nl/sugabase/sugabase.html
    • SUGABASE
  • 12
    • 3042809541 scopus 로고    scopus 로고
    • 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase
    • DOI 10.1002/prot.20143
    • Haselhorst, T., Wilson, J.C., Thomson, R.J., McAtamney, S., Menting, J.G., von Itzstein, M. (2004) Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetyl-neuraminic acid and derivatives to Vibrio chol-erae sialidase. Proteins: Structure, Function, and Bioinformatics 56, 346-353 (Pubitemid 38850167)
    • (2004) Proteins: Structure, Function and Genetics , vol.56 , Issue.2 , pp. 346-353
    • Haselhorst, T.1    Wilson, J.C.2    Thomson, R.J.3    McAtamney, S.4    Menting, J.G.5    Coppel, R.L.6    Von Itzstein, M.7
  • 14
    • 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., Zartler, E.R. (2003) The effect of relaxation on the epitope mapping by saturation transfer difference NMR. Journal of Magnetic Resonance 163, 270-276
    • (2003) Journal of Magnetic Resonance , vol.163 , pp. 270-276
    • Yan, J.1    Kline, A.D.2    Mo, H.3    Shapiro, M.J.4    Zartler, E.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.