Publicaciones en colaboración con investigadores/as de Universitat Autònoma de Barcelona (18)

2024

  1. Selective Formation of Pd-DNA Hybrids Using Tailored Palladium-Mediated Base Pairs: Towards Heteroleptic Pd-DNA Systems

    Angewandte Chemie - International Edition, Vol. 63, Núm. 11

2019

  1. Insight into the specificity and severity of pathogenic mechanisms associated with missense mutations through experimental and structural perturbation analyses

    Human Molecular Genetics, Vol. 28, Núm. 1, pp. 1-15

2018

  1. Combining Structural Aggregation Propensity and Stability Predictions to Redesign Protein Solubility

    Molecular Pharmaceutics, Vol. 15, Núm. 9, pp. 3846-3859

  2. Global Protein Stabilization Does Not Suffice to Prevent Amyloid Fibril Formation

    ACS Chemical Biology, Vol. 13, Núm. 8, pp. 2094-2105

2017

  1. Towards the improvement in stability of an anti-Aβ single-chain variable fragment, scFv-h3D6, as a way to enhance its therapeutic potential

    Amyloid, Vol. 24, Núm. 3, pp. 167-175

  2. Understanding the contribution of disulfide bridges to the folding and misfolding of an anti-Aβ scFv

    Protein Science, Vol. 26, Núm. 6, pp. 1138-1149

2016

  1. Common features in the unfolding and misfolding of PDZ domains and beyond: The modulatory effect of domain swapping and extra-elements

    Scientific Reports, Vol. 6

  2. The chondroitin sulfate/dermatan sulfate 4-O-endosulfatase from marine bacterium Vibrio sp FC509 is a dimeric species: Biophysical characterization of an endosulfatase

    Biochimie, Vol. 131, pp. 85-95

2014

  1. A thermodynamic study of the third PDZ domain of MAGUK neuronal protein PSD-95 reveals a complex three-state folding behavior

    Biophysical Chemistry, Vol. 185, pp. 1-7

  2. The impact of extra-domain structures and post-translational modifications in the folding/misfolding behaviour of the third PDZ domain of MAGUK neuronal protein PSD-95

    PLoS ONE, Vol. 9, Núm. 5

2012

  1. The interconversion between a flexible β-sheet and a fibril β-arrangement constitutes the main conformational event during misfolding of PSD95-PDZ3 domain

    Biophysical Journal, Vol. 103, Núm. 4, pp. 738-747

2000

  1. Thermodynamic analysis of helix-engineered forms of the activation domain of human procarboxypeptidase A2

    European Journal of Biochemistry, Vol. 267, Núm. 19, pp. 5891-5899

1996

  1. Scanning calorimetry and Fourier-transform infrared studies into the thermal stability of cleaved bacteriorhodopsin systems

    Biochemistry, Vol. 35, Núm. 50, pp. 16328-16335

1995

  1. Evidence for a Two-State Transition in the Folding Process of the Activation Domain of Human Procarboxypeptidase A2

    Biochemistry, Vol. 34, Núm. 46, pp. 15105-15110

1992

  1. The role of retinal in the thermal stability of the purple membrane

    European Journal of Biochemistry, Vol. 207, Núm. 2, pp. 581-585

1991

  1. Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain

    European Journal of Biochemistry, Vol. 200, Núm. 3, pp. 663-670

  2. Effect of Zn2+ on the Thermal Denaturation of Carboxypeptidase B

    Biochemistry, Vol. 30, Núm. 8, pp. 2067-2072

1988

  1. Analysis of the thermal unfolding of porcine procarboxypeptidase A and its functional pieces by differential scnning calorimetry

    European Journal of Biochemistry, Vol. 176, Núm. 1, pp. 225-230