Publicaciones en las que colabora con José Luis Neira Faleiro (17)

2020

  1. Human importin α3 and its N-terminal truncated form, without the importin-β-binding domain, are oligomeric species with a low conformational stability in solution

    Biochimica et Biophysica Acta - General Subjects, Vol. 1864, Núm. 7

2016

  1. The Monomeric Species of the Regulatory Domain of Tyrosine Hydroxylase Has a Low Conformational Stability

    Biochemistry, Vol. 55, Núm. 24, pp. 3418-3431

2012

  1. Mutation of Ser-50 and Cys-66 in Snapin modulates protein structure and stability

    Biochemistry, Vol. 51, Núm. 16, pp. 3470-3484

2011

  1. Larger helical populations in peptides derived from the dimerization helix of the capsid protein of HIV-1 results in peptide binding toward regions other than the "hotspot" interface

    Biomacromolecules, Vol. 12, Núm. 9, pp. 3252-3264

  2. Nucleotide-induced conformational transitions in the CBS domain protein MJ0729 of Methanocaldococcus jannaschii

    Protein Engineering, Design and Selection, Vol. 24, Núm. 1-2, pp. 161-169

  3. Rationally designed interfacial peptides are efficient in vitro inhibitors of HIV-1 capsid assembly with antiviral activity

    PLoS ONE, Vol. 6, Núm. 9

  4. The conformational stability and biophysical properties of the eukaryotic thioredoxins of Pisum sativum are not family-conserved

    PLoS ONE, Vol. 6, Núm. 2

2010

  1. The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state

    Protein Engineering, Design and Selection, Vol. 23, Núm. 9, pp. 729-742

  2. The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a "fuzzy" complex upon DNA binding

    Biochemistry, Vol. 49, Núm. 8, pp. 1577-1589

2009

  1. The CBS domain protein MJ0729 of Methanocaldococcus jannaschii is a thermostable protein with a pH-dependent self-oligomerization

    Biochemistry, Vol. 48, Núm. 12, pp. 2760-2776

2008

  1. The family 52 β-xylosidase from Geobacillus stearothermophilus is a dimer: Structural and biophysical characterization of a glycoside hydrolase

    Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1784, Núm. 12, pp. 1924-1934

2007

  1. The isolated C-terminal domain of ring 1B is a dimer made of stable, well-structured monomers

    Biochemistry, Vol. 46, Núm. 44, pp. 12764-12776

2006

  1. Biophysical characterization of the enzyme I of the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system

    Biophysical Journal, Vol. 90, Núm. 12, pp. 4592-4604

2004

  1. The conformational stability of the Streptomyces coelicolor histidine-phosphocarrier protein: Characterization of cold denaturation and urea-protein interactions

    European Journal of Biochemistry, Vol. 271, Núm. 11, pp. 2165-2181

  2. The dimerization domain of the HIV-1 capsid protein binds a capsid protein-derived peptide: A biophysical characterization

    Protein Science, Vol. 13, Núm. 6, pp. 1512-1523

2003

  1. The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH

    European Journal of Biochemistry, Vol. 270, Núm. 10, pp. 2254-2267

2002

  1. Equilibrium unfolding of the C-terminal SAM domain of p73

    Biochemistry, Vol. 41, Núm. 18, pp. 5743-5753