TheQuest for Anticancer Vaccines: Deciphering theFine-Epitope Specificity of Cancer-Related Monoclonal Antibodies byCombining Microarray Screening and Saturation Transfer DifferenceNMR
TheQuest for Anticancer Vaccines: Deciphering theFine-Epitope Specificity of Cancer-Related Monoclonal Antibodies byCombining Microarray Screening and Saturation Transfer DifferenceNMR
Helena Coelho, Takahiko Matsushita, Gerard Artigas, Hiroshi Hinou, F. Javier Can?ada, Richard Lo-Man, Claude Leclerc, Eurico J. Cabrita, Jesu?s Jime?nez-Barbero, Shin-Ichiro Nishimura, Fayna Garcia-Marti?n and Filipa Marcelo
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b06787
[NMR paper] Saturation transfer difference NMR for fragment screening.
Saturation transfer difference NMR for fragment screening.
Related Articles Saturation transfer difference NMR for fragment screening.
Curr Protoc Chem Biol. 2013 Dec 1;5(4):251-68
Authors: Begley DW, Moen SO, Pierce PG, Zartler ER
Abstract
Fragment screening by saturation transfer difference nuclear magnetic resonance (STD-NMR) is a robust method for identifying small molecule binders and is well suited to a broad set of biological targets. STD-NMR is exquisitely sensitive for detecting weakly binding compounds (a common characteristic of...
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[NMR paper] Profiling Formulated Monoclonal Antibodies by 1H NMR Spectroscopy.
Profiling Formulated Monoclonal Antibodies by 1H NMR Spectroscopy.
Profiling Formulated Monoclonal Antibodies by 1H NMR Spectroscopy.
Anal Chem. 2013 Sep 5;
Authors: Poppe L, Jordan JB, Lawson K, Jerums M, Apostol I, Schnier PD
Abstract
Nuclear magnetic resonance (NMR) is arguably the most direct methodology for characterizing the higher-order structure of proteins in solution. Structural characterization of proteins by NMR typically utilizes heteronuclear experiments. However, for formulated monoclonal antibody (mAb) therapeutics, the...
[NMR paper] Precise epitope mapping of malaria parasite inhibitory antibodies by TROSY NMR cross-
Precise epitope mapping of malaria parasite inhibitory antibodies by TROSY NMR cross-saturation.
Related Articles Precise epitope mapping of malaria parasite inhibitory antibodies by TROSY NMR cross-saturation.
Biochemistry. 2005 Jan 18;44(2):518-23
Authors: Morgan WD, Frenkiel TA, Lock MJ, Grainger M, Holder AA
We have applied NMR cross-saturation with TROSY detection to the problem of precisely mapping conformational epitopes on complete protein antigen molecules. We have investigated complexes of the Fab fragments of two antibodies that...
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11-24-2010 11:14 PM
[NMR paper] Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by sa
Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy.
Related Articles Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy.
Biochem Biophys Res Commun. 2003 Aug 1;307(3):498-502
Authors: Murata T, Hemmi H, Nakajima M, Yoshida M, Yamaguchi I
Saturation transfer difference (STD) NMR spectroscopy is a promising tool for rapid screening, identifying ligands that interact with a target protein,...
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11-24-2010 09:16 PM
[NMR paper] Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer diff
Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer difference NMR experiments.
Related Articles Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer difference NMR experiments.
Glycobiology. 2003 Jun;13(6):435-43
Authors: Rinnbauer M, Ernst B, Wagner B, Magnani J, Benie AJ, Peters T
A complex between sialyl Lewisx (alpha-D-Neu5Ac-- beta-D-Gal---beta-D-GlcNAc-O-8 COOMe) and E-selectin was studied using saturation transfer difference (STD) nuclear magnetic resonance (NMR) experiments....
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11-24-2010 09:01 PM
[NMR paper] Group epitope mapping by saturation transfer difference NMR to identify segments of a
Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor.
Related Articles 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. 2001 Jun 27;123(25):6108-17
Authors: Mayer M, Meyer B
A protocol based on saturation transfer difference (STD) NMR spectra was developed to characterize the binding interactions at an atom level, termed group epitope mapping (GEM). As an example...
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[NMR paper] NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
Related Articles NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
J Mol Biol. 1998 Aug 7;281(1):61-7
Authors: Huang X, Yang X, Luft BJ, Koide S
Outer surface protein A (OspA) from the Lyme disease spirochete Borrelia burgdorferi has been a focus of vaccine development. We have identified epitopes of OspA to two monoclonal antibodies (mAbs) by comparing NMR chemical shifts of free OspA and those in Fab complexes....
TheQuest for Anticancer Vaccines: Deciphering theFine-Epitope Specificity of Cancer-Related Monoclonal Antibodies byCombining Microarray Screening and Saturation Transfer DifferenceNMR
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