• Conformational control of integrin subtype selectivity in isoDGR peptide motifs: A biological switch 

      Frank, A.O.; Otto, E.; Mas Moruno, Carlos; Schiller, H.; Marinelli, L.; Cosconati, S.; Bochen, A.; Vossmeyer, D.; Zahn, G.; Stragies, R.; Novellino, E.; Kessler, H. (2010)
      Article
      Accés restringit per política de l'editorial
      Thumbnail image of graphical abstract The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a ...
    • Increasing avß3 selectivity of the anti-angiogenic drug cilengitide by N-methylation 

      Mas Moruno, Carlos; Beck, J.G.; Doedens, L.; Frank, A.O.; Marinelli, L.; Cosconati, S.; Novellino, E.; Kessler, H. (2011)
      Article
      Accés restringit per política de l'editorial
      Thumbnail image of graphical abstract A subtle change: Structural changes upon amide bond methylation improve the selectivity of the anti-angiogenic drug Cilengitide, which after N-methylation at distinct positions ...
    • The impact of amino acid side chain mutations in conformational design of peptides and proteins 

      Laufer, B.; Frank, A.O.; Chatterjee, J.; Neubauer, T.; Mas Moruno, Carlos; Kummerlöwe, G.; Kessler, H. (2010)
      Article
      Accés restringit per política de l'editorial
      Realitzat a/amb:   Technische Universität München
      Local energetic effects of amino acid replacements are often considered to have only a moderate influence on the backbone conformation of proteins or peptides. As these effects are difficult to determine experimentally, ...