JOSÉ CRISTÓBAL
MARTÍNEZ HERRERÍAS
PROFESOR TITULAR DE UNIVERSIDAD
IRENE
LUQUE FERNÁNDEZ
CATEDRÁTICA DE UNIVERSIDAD
IRENE LUQUE FERNÁNDEZ-rekin lankidetzan egindako argitalpenak (19)
2024
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Phage display identification of high-affinity ligands for human TSG101-UEV: A structural and thermodynamic study of PTAP recognition
International Journal of Biological Macromolecules, Vol. 274
2023
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A calorimetric and structural analysis of cooperativity in the thermal unfolding of the PDZ tandem of human Syntenin-1
International Journal of Biological Macromolecules, Vol. 242
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Corrigendum to “A calorimetric and structural analysis of cooperativity in the thermal unfolding of the PDZ tandem of human Syntenin-1” [Int. J. Biol. Macromol. 242 (2023) 124662] (International Journal of Biological Macromolecules (2023) 242(P1), (S0141813023015568), (10.1016/j.ijbiomac.2023.124662))
International Journal of Biological Macromolecules
2022
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Phage display identification of nanomolar ligands for human NEDD4-WW3: Energetic and dynamic implications for the development of broad-spectrum antivirals
International Journal of Biological Macromolecules, Vol. 207, pp. 308-323
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Understanding binding affinity and specificity of modular protein domains: A focus in ligand design for the polyproline-binding families
Advances in Protein Chemistry and Structural Biology (Academic Press Inc.), pp. 161-188
2020
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Stability, conformational plasticity, oligomerization behaviour and equilibrium unfolding intermediates of the Ebola virus matrix protein VP40
Journal of Biomolecular Structure and Dynamics
2019
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Ultrafast folding kinetics of WW domains reveal how the amino acid sequence determines the speed limit to protein folding
Proceedings of the National Academy of Sciences of the United States of America, Vol. 116, Núm. 17, pp. 8137-8142
2018
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Approaching the thermodynamic view of protein folding through the reproduction of Anfinsen's experiment by undergraduate physical biochemistry students
Biochemistry and Molecular Biology Education, Vol. 46, Núm. 3, pp. 262-269
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Protein Folding Cooperativity and Thermodynamic Barriers of the Simplest β-Sheet Fold: A Survey of WW Domains
Journal of Physical Chemistry B, Vol. 122, Núm. 49, pp. 11058-11071
2014
2012
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Adecuación y aplicación al área de conocimiento de química física de una metodología basada en las TIC´s para la adaptación al espacio europeo de educación superior (PID 08-173)
Innovación docente y buenas prácticas en la Universidad de Granada.: Vol. 1 (Editorial Universidad de Granada), pp. 369-384
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Thermodynamic impact of embedded water molecules in the unfolding of human CD2BP2-GYF domain
Journal of Physical Chemistry B, Vol. 116, Núm. 24, pp. 7168-7175
2011
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Differential scanning calorimetry: Thermodynamic analysis of the unfolding transitions of proteins, domains and peptidic fragments by using equilibrium models
Proteomics Research Journal, Vol. 2, Núm. 4, pp. 503-538
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Differential scanning calorimetry: Thermodynamic analysis of the unfolding transitions of proteins, domains and peptidic fragments by using equilibrium models
Protein Folding (Nova Science Publishers, Inc.), pp. 313-347
2010
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Role of interfacial water molecules in proline-rich ligand recognition by the Src homology 3 domain of Abl
Journal of Biological Chemistry, Vol. 285, Núm. 4, pp. 2823-2833
2009
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Thermodynamic characterization of the folding equilibrium of the human Nedd4-WW4 domain: At the frontiers of cooperative folding
Biochemistry, Vol. 48, Núm. 36, pp. 8712-8720
2007
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Crystallization by capillary counter-diffusion and structure determination of the N114A mutant of the SH3 domain of Abl tyrosine kinase complexed with a high-affinity peptide ligand
Acta Crystallographica Section D: Biological Crystallography, Vol. 63, Núm. 5, pp. 646-652
2006
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Structure of human TSG101 UEV domain
Acta Crystallographica Section D: Biological Crystallography, Vol. 62, Núm. 4, pp. 458-464
2004
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Thermodynamic Dissection of the Binding Energetics of Proline-rich Peptides to the Abl-SH3 Domain: Implications for Rational Ligand Design
Journal of Molecular Biology, Vol. 336, Núm. 2, pp. 527-537