Publicacions en col·laboració amb investigadors/es de Instituto de Química Física Rocasolano (11)

2021

  1. DD04107-Derived neuronal exocytosis inhibitor peptides: Evidences for synaptotagmin-1 as a putative target

    Bioorganic Chemistry, Vol. 115

  2. Inter-hairpin linker sequences determine the structure of the ββ-solenoid fold: a “bottom-up” study of pneumococcal LytA choline-binding module

    International Journal of Biological Macromolecules, Vol. 190, pp. 679-692

2020

  1. Turncoat Polypeptides: We Adapt to Our Environment

    ChemBioChem, Vol. 21, Núm. 4, pp. 432-441

2018

  1. Roles of Amphipathicity and Hydrophobicity in the Micelle-Driven Structural Switch of a 14-mer Peptide Core from a Choline-Binding Repeat

    Chemistry - A European Journal, Vol. 24, Núm. 22, pp. 5825-5839

2017

  1. Insights into protein-carbohydrate recognition: A novel binding mechanism for CBM family 43

    Journal of Molecular Graphics and Modelling, Vol. 73, pp. 152-156

  2. NMR Insights into the Structure-Function Relationships in the Binding of Melanocortin Analogues to the MC1R Receptor

    Molecules (Basel, Switzerland), Vol. 22, Núm. 7

2016

  1. Alanine scan and 2H NMR analysis of the membrane-active peptide BP100 point to a distinct carpet mechanism of action

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1858, Núm. 6, pp. 1328-1338

  2. Molecular basis for the protein recognition specificity of the dynein light chain DYNLT1/Tctex1: Characterization of the interaction with activin receptor IIB

    Journal of Biological Chemistry, Vol. 291, Núm. 40, pp. 20962-20975

2015

  1. Micelle-triggered β-hairpin to α-helix transition in a 14-residue peptide from a choline-binding repeat of the pneumococcal autolysin LytA

    Chemistry - A European Journal, Vol. 21, Núm. 22, pp. 8076-8089

  2. Structural Dissection of Crotalicidin, a Rattlesnake Venom Cathelicidin, Retrieves a Fragment with Antimicrobial and Antitumor Activity

    Journal of Medicinal Chemistry, Vol. 58, Núm. 21, pp. 8553-8563

  3. The C-terminal domains of two homologous Oleaceae β-1,3-glucanases recognise carbohydrates differently: Laminarin binding by NMR

    Archives of Biochemistry and Biophysics, Vol. 580, pp. 93-101