Publicaciones en colaboración con investigadores/as de Universidad Complutense de Madrid (22)

2008

  1. Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen

    Protein Science, Vol. 17, Núm. 2, pp. 371-376

2006

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

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

2004

  1. NMR solution structure of Ole e 6, a major allergen from olive tree pollen

    Journal of Biological Chemistry, Vol. 279, Núm. 37, pp. 39035-39041

  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. Solution structure and stability against digestion of rproBnIb, a recombinant 2S albumin from rapeseed: Relationship to its allergenic properties

    Biochemistry, Vol. 43, Núm. 51, pp. 16036-16045

2003

  1. 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

  2. Tautomeric state of α-sarcin histidines. Nδ tautomers are a common feature in the active site of extracellular microbial ribonucleases

    FEBS Letters, Vol. 534, Núm. 1-3, pp. 197-201

2002

  1. Backbone dynamics of the cytotoxic ribonuclease α-sarchin by 15N NMR relaxation methods

    Journal of Biomolecular NMR, Vol. 24, Núm. 4, pp. 301-316

  2. Solution structure of allergenic 2 S albumins

    Biochemical Society Transactions

2000

  1. Folding kinetics of phage 434 CRO protein

    Biochemistry, Vol. 39, Núm. 45, pp. 13963-13973

  2. The highly refined solution structure of the cytotoxic ribonuclease α-Sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity

    Journal of Molecular Biology, Vol. 299, Núm. 4, pp. 1061-1073

1999

  1. Hydrogen exchange in ribonuclease A and ribonuclease S: Evidence for residual structure in the unfolded state under native conditions

    Journal of Molecular Biology, Vol. 285, Núm. 2, pp. 627-643

1998

  1. Characterization of pK(a) values and titration shifts in the cytotoxic ribonuclease α-sarcin by NMR. Relationship between electrostatic interactions, structure, and catalytic function

    Biochemistry, Vol. 37, Núm. 45, pp. 15865-15876

1996

  1. 1H and 15N nuclear magnetic resonance assignment and secondary structure of the cytotoxic ribonuclease α-Sarcin

    Protein Science, Vol. 5, Núm. 5, pp. 969-972

  2. 1H NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein

    Biochemistry, Vol. 35, Núm. 49, pp. 15672-15682

  3. Structural basis for the catalytic mechanism and substrate specificity of the ribonuclease α-sarcin

    FEBS Letters, Vol. 399, Núm. 1-2, pp. 163-165

1995

  1. NMR Solution Structure of the Antifungal Protein from Aspergillus giganteus: Evidence for Cysteine Pairing Isomerism

    Biochemistry, Vol. 34, Núm. 9, pp. 3009-3021

1993

  1. Three-Dimensional Structure of ω-Conotoxin GVIA Determined by 1H-NMR

    Biochemical and Biophysical Research Communications, Vol. 192, Núm. 3, pp. 1238-1244

1986

  1. Reaction of α-diketones with ethanolamine

    Tetrahedron Letters, Vol. 27, Núm. 12, pp. 1381-1384