QUÍMICA FÍSICA
DEPARTAMENTO
Universitat Autònoma de Barcelona
Barcelona, EspañaPublicaciones en colaboración con investigadores/as de Universitat Autònoma de Barcelona (18)
2024
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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
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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
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Combining Structural Aggregation Propensity and Stability Predictions to Redesign Protein Solubility
Molecular Pharmaceutics, Vol. 15, Núm. 9, pp. 3846-3859
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Global Protein Stabilization Does Not Suffice to Prevent Amyloid Fibril Formation
ACS Chemical Biology, Vol. 13, Núm. 8, pp. 2094-2105
2017
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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
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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
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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
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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
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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
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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
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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
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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
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Scanning calorimetry and Fourier-transform infrared studies into the thermal stability of cleaved bacteriorhodopsin systems
Biochemistry, Vol. 35, Núm. 50, pp. 16328-16335
1995
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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
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The role of retinal in the thermal stability of the purple membrane
European Journal of Biochemistry, Vol. 207, Núm. 2, pp. 581-585
1991
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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
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Effect of Zn2+ on the Thermal Denaturation of Carboxypeptidase B
Biochemistry, Vol. 30, Núm. 8, pp. 2067-2072
1988
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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