Publikationen, an denen er mitarbeitet Pedro Manuel Nieto Mesa (11)

2017

  1. Interactions between a heparin trisaccharide library and FGF-1 analyzed by NMR methods

    International Journal of Molecular Sciences, Vol. 18, Núm. 6

2015

  1. NMR Techniques for the Study of Transient Intermolecular Interactions

    Structure Elucidation in Organic Chemistry: The Search for the Right Tools (Wiley Blackwell), pp. 325-360

2014

  1. Importance of the polarity of the glycosaminoglycan chain on the interaction with FGF-1

    Glycobiology, Vol. 24, Núm. 11, pp. 1004-1009

2013

  1. Heparin modulates the mitogenic activity of fibroblast growth factor by inducing dimerization of its receptor. A 3D view by using NMR

    ChemBioChem, Vol. 14, Núm. 14, pp. 1732-1744

  2. Insights into the glycosaminoglycan-mediated cytotoxic mechanism of eosinophil cationic protein revealed by NMR

    ACS Chemical Biology, Vol. 8, Núm. 1, pp. 144-151

2011

  1. Conformational selection of the AGA*IA M heparin pentasaccharide when bound to the fibroblast growth factor receptor

    Chemistry - A European Journal, Vol. 17, Núm. 40, pp. 11204-11209

2008

  1. NMR structural studies of oligosaccharides related to cancer processes

    Anti-Cancer Agents in Medicinal Chemistry, Vol. 8, Núm. 1, pp. 52-63

2006

  1. Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods

    Journal of Biomolecular NMR, Vol. 35, Núm. 4, pp. 225-239

  2. Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue

    FEBS Journal, Vol. 273, Núm. 20, pp. 4716-4727

2005

  1. Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the 1C4 and 2So conformations of a bioactive heparin-like hexasaccharide

    Journal of the American Chemical Society, Vol. 127, Núm. 16, pp. 5778-5779

2000

  1. Structural basis for chitin recognition by defense proteins: GIcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains

    Chemistry and Biology, Vol. 7, Núm. 7, pp. 529-543