Thomas Peters
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Thomas Peters has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
Thomas Weimar
Institute for Chemistry, University of Lübeck, 23538 Lübeck, Germany, Fax: (+49) 451-500-4241
3 shared publicationsLars Herfurth
Institut für Chemie der Medizinischen Universität zu Lübeck Ratzeburger Allee 160, 23538 Lübeck, Deutschland, Fax: (+49) 451‐500‐4241
2 shared publications- Bernd Meyer
Institute for Organic Chemistry, University of Hamburg, Martin‐Luther‐King‐Platz 6, 20146 Hamburg, Germany, Fax: (+49) 40‐42838‐2878
1 shared publication - Bernd Meyer
Department of Chemistry, University of Hamburg, Organic Chemistry, Martin‐Luther‐King‐Platz 6, 20146 Hamburg (Germany)
1 shared publication - Bernd Meyer
Institut für Organische Chemie der Universität, Martin-Luther-King-Platz 6, D-20146 Hamburg (Germany), Fax: (+49) 40-42838-2878
1 shared publication Christian Plath
Institute for Chemistry, University of Lübeck, 23538 Lübeck, Germany
1 shared publication
Latest Publications
- Open Access
- 3 February 2012
- Published by Wiley in ChemBioChem
- Vol. 13 (3) , 321
Cover Picture: A New Concept for Glycosyltransferase Inhibitors: Nonionic Mimics of the Nucleotide Donor of the Human Blood Group B Galactosyltransferase (ChemBioChem 3/2012)
- 3 February 2012
- Published by Wiley in ChemBioChem
- Vol. 13 (3) , 321
Open AccessCover Picture: A New Concept for Glycosyltransferase Inhibitors: Nonionic Mimics of the Nucleotide Donor of the Human Blood Group B Galactosyltransferase (ChemBioChem 3/2012)
- 17 July 2006
- Published by Wiley in ChemBioChem
- Vol. 7 (8) , 1226-1230
Assaying Sialyltransferase Activity with Surface Plasmon Resonance
- 17 July 2006
- Published by Wiley in ChemBioChem
- Vol. 7 (8) , 1226-1230
Assaying Sialyltransferase Activity with Surface Plasmon Resonance
- Top Cited Papers
- 21 February 2003
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 42 (8) , 864-890
NMR Spectroscopy Techniques for Screening and Identifying Ligand Binding to Protein Receptors
Binding events of ligands to receptors are the key for an understanding of biological processes. Gaining insight into protein–protein and protein–ligand interactions in solution has recently become possible on an atomic level by new NMR spectroscopic techniques. These experiments identify binding events either by looking at the resonance signals of the ligand or the protein. Ideally, both techniques together deliver a complete picture of ligand binding to a receptor. The approaches discussed in this review allow screening of compound libraries as well as a detailed identification of the groups involved in the binding events. Also, characterization of the binding strength and kinetics is possible, competitive binding as well as allosteric effects can be identified, and it has even been possible to identify ligand binding to intact viruses and membrane‐bound proteins.
- 21 February 2003
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 42 (8) , 864-890
Top Cited PapersNMR Spectroscopy Techniques for Screening and Identifying Ligand Binding to Protein Receptors
Binding events of ligands to receptors are the key for an understanding of biological processes. Gaining insight into protein–protein and protein–ligand interactions in solution has recently become possible on an atomic level by new NMR spectroscopic techniques. These experiments identify binding events either by looking at the resonance signals of the ligand or the protein. Ideally, both techniques together deliver a complete picture of ligand binding to a receptor. The approaches discussed in this review allow screening of compound libraries as well as a detailed identification of the groups involved in the binding events. Also, characterization of the binding strength and kinetics is possible, competitive binding as well as allosteric effects can be identified, and it has even been possible to identify ligand binding to intact viruses and membrane‐bound proteins.
- 21 February 2003
- Published by Wiley in Angewandte Chemie
- Vol. 115 (8) , 890-918
NMR‐Techniken zum Screening und zur Identifizierung der Bindung von Liganden an Proteinrezeptoren
- 21 February 2003
- Published by Wiley in Angewandte Chemie
- Vol. 115 (8) , 890-918
NMR‐Techniken zum Screening und zur Identifizierung der Bindung von Liganden an Proteinrezeptoren
- 16 June 2000
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 39 (12) , 2097-2099
Application of 3D-TOCSY-trNOESY for the Assignment of Bioactive Ligands from Mixtures
- 16 June 2000
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 39 (12) , 2097-2099
Application of 3D-TOCSY-trNOESY for the Assignment of Bioactive Ligands from Mixtures
- 16 June 2000
- Published by Wiley in Angewandte Chemie
- Vol. 112 (12) , 2192-2194
3D-TOCSY-trNOESY zur vollständigen Charakterisierung bioaktiver Liganden aus Mischungen
- 16 June 2000
- Published by Wiley in Angewandte Chemie
- Vol. 112 (12) , 2192-2194
3D-TOCSY-trNOESY zur vollständigen Charakterisierung bioaktiver Liganden aus Mischungen