Publicaciones en colaboración con investigadores/as de Instituto de Química Física Rocasolano (29)

2014

  1. The sea anemone actinoporin (Arg-Gly-Asp) conserved motif is involved in maintaining the competent oligomerization state of these pore-forming toxins

    FEBS Journal, Vol. 281, Núm. 5, pp. 1465-1478

2013

  1. Three-dimensional structure of the actinoporin sticholysin i. influence of long-distance effects on protein function

    Archives of Biochemistry and Biophysics, Vol. 532, Núm. 1, pp. 39-45

2011

  1. Intrinsic local disorder and a network of charge-charge interactions are key to actinoporin membrane disruption and cytotoxicity

    FEBS Journal, Vol. 278, Núm. 12, pp. 2080-2089

  2. The behavior of sea anemone actinoporins at the water-membrane interface

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1808, Núm. 9, pp. 2275-2288

2010

  1. 1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II

    Biomolecular NMR Assignments, Vol. 4, Núm. 1, pp. 69-72

  2. Specific interactions of sticholysin I with model membranes: An NMR study

    Proteins: Structure, Function and Bioinformatics, Vol. 78, Núm. 8, pp. 1959-1970

2009

  1. 1H, 13C, and 15N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II

    Biomolecular NMR Assignments, Vol. 3, Núm. 2, pp. 239-241

  2. 1H, 13C, and 15N NMR assignments of the actinoporin Sticholysin i

    Biomolecular NMR Assignments, Vol. 3, Núm. 1, pp. 5-7

2006

  1. A complementary microscopy analysis of Sticholysin II crystals on lipid films: Atomic force and transmission electron characterizations

    Biophysical Chemistry, Vol. 119, Núm. 3, pp. 219-223

  2. The role of electrostatic interactions in the antitumor activity of dimeric RNases

    FEBS Journal, Vol. 273, Núm. 16, pp. 3687-3697

  3. Tyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of α-sarcin

    Biological Chemistry, Vol. 387, Núm. 5, pp. 535-541

  4. pH-dependent conformational stability of the ribotoxin α-sarcin and four active site charge substitution variants

    Biochemistry, Vol. 45, Núm. 46, pp. 13705-13718

2005

  1. Modeling the highly specific ribotoxin recognition of ribosomes

    FEBS Letters, Vol. 579, Núm. 30, pp. 6859-6864

  2. Refined NMR structure of α-sarcin by 15N-1H residual dipolar couplings

    European Biophysics Journal, Vol. 34, Núm. 8, pp. 1057-1065

2004

  1. Conserved asparagine residue 54 of α-sarcin plays a role in protein stability and enzyme activity

    Biological Chemistry, Vol. 385, Núm. 12, pp. 1165-1170

  2. NMR structure of the noncytotoxic α-sarcin mutant Δ(7-22): The importance of the native conformation of peripheral loops for activity

    Protein Science, Vol. 13, Núm. 4, pp. 1000-1011

  3. Phenotypic selection and characterization of randomly produced non-haemolytic mutants of the toxic sea anemone protein sticholysin II

    FEBS Letters, Vol. 575, Núm. 1-3, pp. 14-18

2003

  1. Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation

    Structure, Vol. 11, Núm. 11, pp. 1319-1328

  2. Dissecting Structural and Electrostatic Interactions of Charged Groups in α-Sarcin. An NMR Study of Some Mutants Involving the Catalytic Residues

    Biochemistry, Vol. 42, Núm. 45, pp. 13122-13133

  3. Leucine 145 of the ribotoxin α-sarcin plays a key role for determining the specificity of the ribosome-inactivating activity of the protein

    Protein Science, Vol. 12, Núm. 1, pp. 161-169