D. A. Fernández‐Velasco

发表

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.

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.

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 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.

The Contribution of the Ankyrin Repeat Domain of TRPV1 as a Thermal Module.

A. Torres-Larios, D. A. Fernández‐Velasco, L. Domínguez, 2019, Biophysical journal.

Potential Site to Direct Selective Compounds in the Triosephosphate Isomerase for the Development of New Drugs

D. A. Fernández‐Velasco, C. Benítez-Cardoza, A. Jiménez-Pineda, 2020 .

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.

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.

Structural basis for the modulation of plant cytosolic triosephosphate isomerase activity by mimicry of redox-based modifications.

A. Torres-Larios, S. Romero-Romero, D. A. Fernández‐Velasco, 2019, The Plant journal : for cell and molecular biology.

The contribution of the ankyrin repeat domain of TRPV1 as a thermal module

A. Torres-Larios, D. A. Fernández‐Velasco, L. Islas, 2019, bioRxiv.

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

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

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..

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.

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.

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.

ENZYME BEHAVIOR IN NONCONVENTIONAL SYSTEMS

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

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.

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.

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.

The Stability Landscape of de novo TIM Barrels Explored by a Modular Design Approach

B. Höcker, A. Rodríguez‐Romero, S. Romero-Romero, 2021, Journal of molecular biology.

Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica.

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

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.

Massively parallel de novo protein design for targeted therapeutics

Lu Zhang, Xuhui Huang, David Baker, 2017, Nature.

Influence of the germline sequence on the thermodynamic stability and fibrillogenicity of human lambda 6 light chains

D. A. Fernández‐Velasco, A. Solomon, C. Murphy, 2008, Proteins.

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.

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.

Water requirements in monomer folding and dimerization of triosephosphate isomerase in reverse micelles. Intrinsic fluorescence of conformers related to reactivation.

D. A. Fernández‐Velasco, A. Darszon, A. Galina, 1995, Biochemistry.

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

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

Engineering Concanavalin B to Release Bioactive Peptides against Metabolic Syndrome

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

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

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

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.

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.

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.

Stabilizing an amyloidogenic λ6 light chain variable domain

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

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.

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.

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.

Mutational and genetic determinants of λ6 light chain amyloidogenesis

D. A. Fernández‐Velasco, J. Pérez-Carreón, R. Sánchez-López, 2013, The FEBS journal.

The N-terminal strand modulates immunoglobulin light chain fibrillogenesis.

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

Triosephosphate Isomerase Inhibitors as Potential Drugs against Clostridium perfringens

D. A. Fernández‐Velasco, C. Benítez-Cardoza, J. L. Vique‐Sánchez, 2020 .