Isoserine-based biotinylated photoaffinity probes that interact with penicillin-binding protein 1b.
暂无分享,去创建一个
D. Volke | Y. Hatanaka | T. Rühl | F. Schumer | H. Hennig | P. Welzel | K. Stembera
[1] S J Tendler,et al. Surface plasmon resonance analysis of dynamic biological interactions with biomaterials. , 2000, Biomaterials.
[2] Y. Hatanaka,et al. A trifunctional reagent for photoaffinity labeling , 2000 .
[3] G. Prestwich,et al. Using photolabile ligands in drug discovery and development. , 2000, Trends in biotechnology.
[4] J. Ghuysen,et al. The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan‐polymerizing penicillin‐binding protein 1b of Escherichia coli , 1999, Molecular microbiology.
[5] S. Jockusch,et al. A Bifunctional Photoaffinity Probe for Ligand/ Receptor Interaction Studies , 1998 .
[6] S. Fleming. Chemical reagents in photoaffinity labeling , 1995 .
[7] R. Rando,et al. Modular Design of Biotinylated Photoaffinity Probes: Synthesis and Utilization of a Biotinylated Pepstatin Photoprobe , 1995 .
[8] F. Kotzyba-Hibert,et al. Neue Entwicklungen bei der Photoaffinitätsmarkierung , 1995 .
[9] J. Heijenoort,et al. Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: possible roles of PBP 1b and PBP 3 , 1992, Journal of bacteriology.
[10] M. de Pedro,et al. Cloning and expression of the ponB gene, encoding penicillin-binding protein 1B of Escherichia coli, in heterologous systems , 1990, Journal of bacteriology.