D. Fernández‐Velasco

发表

Human Gpn1 purified from bacteria binds guanine nucleotides and hydrolyzes GTP as a protein dimer stabilized by its C-terminal tail.

A. Hernández-Arana, S. Lara-González, M. R. Calera, 2017, Protein expression and purification.

Insights on Structure and Function of a Late Embryogenesis Abundant Protein from Amaranthus cruentus: An Intrinsically Disordered Protein Involved in Protection against Desiccation, Oxidant Conditions, and Osmotic Stress

D. A. Fernández‐Velasco, A. P. Barba de la Rosa, Á. Guevara-García, 2017, Front. Plant Sci..

Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme.

M. Costas, D. A. Fernández‐Velasco, Hugo Nájera, 2003, The Biochemical journal.

The interplay of protein–ligand and water‐mediated interactions shape affinity and selectivity in the LAO binding protein

A. Rodríguez‐Romero, S. Romero-Romero, D. A. Fernández‐Velasco, 2020, The FEBS journal.

Mapping the metal-catalytic site of a zinc-activated phytochelatin synthase

R. Moreno-Sánchez, E. Saavedra, S. Romero-Romero, 2020 .

Activity of heart and muscle lactate dehydrogenases in all-aqueous systems and in organic solvents with low amounts of water. Effect of guanidine chloride.

D. A. Fernández‐Velasco, A. Darszon, A. Gómez-Puyou, 1992, European journal of biochemistry.

Thermodynamic and kinetic characterization of a germ line human lambda6 light-chain protein: the relation between unfolding and fibrillogenesis.

D. A. Fernández‐Velasco, J. M. Sanchez-Ruiz, Luis del Pozo-Yauner, 2009, Journal of molecular biology.

Stabilizing an amyloidogenic λ6 light chain variable domain

D. A. Fernández‐Velasco, B. Becerril, O. D. Luna-Martinez, 2017, The FEBS journal.

Structural, thermodynamic and catalytic characterization of an ancestral triosephosphate isomerase reveal early evolutionary coupling between monomer association and function

A. Rodríguez‐Romero, E. García-Hernández, M. Costas, 2019, The FEBS journal.

Unfolding of triosephosphate isomerase from Trypanosoma brucei: identification of intermediates and insight into the denaturation pathway using tryptophan mutants.

G. Saab-Rincón, D. A. Fernández‐Velasco, R. Pérez-Montfort, 2002, Archives of biochemistry and biophysics.

ENZYME BEHAVIOR IN NONCONVENTIONAL SYSTEMS

D. A. Fernández‐Velasco, E. Vázquez-Contreras, H. N. Peña, 2002 .

Structure and conformational stability of the triosephosphate isomerase from Zea mays. Comparison with the chemical unfolding pathways of other eukaryotic TIMs.

A. Rodríguez‐Romero, S. Romero-Romero, M. Costas, 2018, Archives of biochemistry and biophysics.

Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica.

A. Rodríguez‐Romero, D. A. Fernández‐Velasco, A. Kornhauser, 2002, Journal of molecular biology.

Thermodynamic and kinetic analysis of the LAO binding protein and its isolated domains reveal non-additivity in stability, folding, and function

A. Rodríguez‐Romero, S. Romero-Romero, M. Costas, 2023, bioRxiv.

Insertion of antihypertensive peptides in acidic subunit from amaranth 11S induces contrasting effects in stability

D. A. Fernández‐Velasco, S. Luna-Suárez, C. Benítez-Cardoza, 2018, Applied Microbiology and Biotechnology.

The N-terminal strand modulates immunoglobulin light chain fibrillogenesis.

D. A. Fernández‐Velasco, A. Ochoa‐Leyva, J. Wall, 2014, Biochemical and biophysical research communications.

Energetics of protein homodimerization: Effects of water sequestering on the formation of β‐lactoglobulin dimer

M. Bello, E. García-Hernández, D. A. Fernández‐Velasco, 2007, Proteins.

Modification of Vegetable Proteins to Release Bioactive Peptides Able to Treat Metabolic Syndrome—In Silico Assessment

D. A. Fernández‐Velasco, S. Luna-Suárez, F. F. Rosas-Cárdenas, 2020, Applied Sciences.

Thermal unfolding of triosephosphate isomerase from Entamoeba histolytica: dimer dissociation leads to extensive unfolding.

D. A. Fernández‐Velasco, D. A. Cisneros, L. Blancas-Mejia, 2008, Biochemistry.

A COMPARATIVE STUDY OF BIOCHEMICAL AND IMMUNOLOGICAL PROPERTIES OF TRIOSEPHOSPHATE ISOMERASE FROM TAENIA SOLIUM AND SUS SCROFA

D. A. Fernández‐Velasco, K. Willms, A. Landa, 2003, The Journal of parasitology.

Sequencing, expression and properties of triosephosphate isomerase from Entamoeba histolytica.

D. A. Fernández‐Velasco, A. Landa, L. Jiménez, 1997, European journal of biochemistry.

Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution.

M. Peimbert, L. Domínguez-Ramírez, D. Fernández‐Velasco, 2008, Biochemistry.

Insertion of antihypertensive peptides in acidic subunit from amaranth 11S induces contrasting effects in stability

D. A. Fernández‐Velasco, S. Luna-Suárez, C. Benítez-Cardoza, 2018, Applied Microbiology and Biotechnology.

Swim Bladder of Farmed Totoaba macdonaldi: A Source of Value-Added Collagen

D. A. Fernández‐Velasco, T. Silva, L. Olivera-Castillo, 2021, Marine drugs.

The insertion of bioactive peptides at the C-terminal end of an 11S globulin changes the structural stability and improves the antihypertensive activity

D. A. Fernández‐Velasco, S. Luna-Suárez, F. F. Rosas-Cárdenas, 2019, Electronic Journal of Biotechnology.

Enzyme activation by denaturants in organic solvent systems with a low water content.

D. A. Fernández‐Velasco, A. Darszon, A. Gómez-Puyou, 1992, European journal of biochemistry.

Solution NMR structure of cementum protein 1 derived peptide (CEMP1‐p1) and its role in the mineralization process

H. Arzate, Enrique Romo-Arévalo, D. Fernández‐Velasco, 2023, Journal of peptide science : an official publication of the European Peptide Society.

Thermodynamic and kinetic characterization of the association of triosephosphate isomerase: the role of diffusion.

D. A. Fernández‐Velasco, L. Dagdug, Hugo Nájera, 2007, Biochimica et biophysica acta.

Crystal structure of a reconstructed ancestor of Triosephosphate isomerase from eukaryotes

Mariana Schulte‐Sasse, Nancy O. Pulido‐Mayoral, D. Fernández‐Velasco, 2019 .

Epistasis on the stability landscape of de novo TIM barrels explored by a modular design approach

D. Baker, B. Höcker, A. Rodríguez‐Romero, 2020, bioRxiv.

Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteins.

A. Rodríguez‐Romero, S. Romero-Romero, M. Costas, 2015, Physical chemistry chemical physics : PCCP.

Site-directed mutagenesis reveals regions implicated in the stability and fiber formation of human λ3r light chains.

E. Rudiño-Piñera, R. Sánchez-López, B. Becerril, 2015, The Journal of Biological Chemistry.

Site-directed Mutagenesis Reveals Regions Implicated in the Stability and Fiber Formation of Human λ3r Light Chains*

E. Rudiño-Piñera, D. A. Fernández‐Velasco, R. Sánchez-López, 2014, The Journal of Biological Chemistry.

On the molecular basis of the high affinity binding of basic amino acids to LAOBP, a periplasmic binding protein from Salmonella typhimurium

Daniel‐Adriano Silva, E. García-Hernández, D. A. Fernández‐Velasco, 2015, Journal of molecular recognition : JMR.

Engineering Concanavalin B to Release Bioactive Peptides against Metabolic Syndrome

D. A. Fernández‐Velasco, S. Luna-Suárez, F. F. Rosas-Cárdenas, 2021, Foods.