Publicaciones en colaboración con investigadores/as de Universidad de Granada (17)

2019

  1. Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I

    Advances in Protein Chemistry and Structural Biology (Academic Press Inc.), pp. 119-152

2012

  1. The Peripheral Binding of 14-3-3γ to Membranes Involves Isoform-Specific Histidine Residues

    PLoS ONE, Vol. 7, Núm. 11

2010

  1. Modulation of buried ionizable groups in proteins with engineered surface charge

    Journal of the American Chemical Society, Vol. 132, Núm. 4, pp. 1218-1219

  2. Protein-protein interactions at an enzyme-substrate interface: Characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase

    Proteins: Structure, Function and Bioinformatics, Vol. 78, Núm. 1, pp. 36-51

  3. Proteolytic scanning calorimetry: A novel methodology that probes the fundamental features of protein kinetic stability

    Biophysical Journal, Vol. 98, Núm. 6

  4. Role of conservative mutations in protein multi-property adaptation

    Biochemical Journal, Vol. 429, Núm. 2, pp. 243-249

  5. Using multi-objective computational design to extend protein promiscuity

    Biophysical Chemistry, Vol. 147, Núm. 1-2, pp. 13-19

2009

  1. Between-Species Variation in the Kinetic Stability of TIM Proteins Linked to Solvation-Barrier Free Energies

    Journal of Molecular Biology, Vol. 385, Núm. 3, pp. 924-937

  2. Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy

    Nature Structural and Molecular Biology, Vol. 16, Núm. 8, pp. 890-896

  3. Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes

    Journal of Biological Chemistry, Vol. 284, Núm. 47, pp. 32758-32769

2008

  1. Beyond Lumry-Eyring: An unexpected pattern of operational reversibility/irreversibility in protein denaturation

    Proteins: Structure, Function and Genetics, Vol. 70, Núm. 1, pp. 19-24

  2. Engineering proteins with tunable thermodynamic and kinetic stabilities

    Proteins: Structure, Function and Genetics, Vol. 71, Núm. 1, pp. 165-174

  3. Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis

    Journal of Biological Chemistry, Vol. 283, Núm. 40, pp. 27121-27129

  4. Structural basis of human triosephosphate isomerase deficiency: Mutation E104D is related to alterations of a conserved water network at the dimer interface

    Journal of Biological Chemistry, Vol. 283, Núm. 34, pp. 23254-23263

2006

  1. Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates

    Biophysical Journal, Vol. 91, Núm. 5

  2. Natural Selection for Kinetic Stability Is a Likely Origin of Correlations between Mutational Effects on Protein Energetics and Frequencies of Amino Acid Occurrences in Sequence Alignments

    Journal of Molecular Biology, Vol. 362, Núm. 5, pp. 966-978

  3. Role of Solvation Barriers in Protein Kinetic Stability

    Journal of Molecular Biology, Vol. 360, Núm. 3, pp. 715-724