Directorio

Romero-Arias, J. R., Luviano, A. S., Costas, M., Hernandez-Machado, A. & Barrio, R. A.* (2022). Dynamical shapes of droplets of cyclodextrin-surfactant solutions. Scientific Reports, 12(1).
DOI:10.1038/s41598-022-09267-w

Rincón-López, J., Ramírez-Rodríguez, N. J., Luviano, A. S., Costas, M., López-Cervantes, J. L., García-Figueroa, A. A., Domínguez, H., Mendoza-Cruz, R., Guadarrama, P., López-Morales, S., & Rojas-Aguirre, Y.* (2022). Experimental and theoretical studies of pegylated-β-cyclodextrin: A step forward to understand its tunable self-aggregation abilities. Journal of Drug Delivery Science and Technology, 67, 102975.
DOI:10.1016/j.jddst.2021.102975

Romero-Romero, S., Costas, M., Silva Manzano, D. -A., Kordes, S., Rojas-Ortega, E., Tapia, C., Guerra, Y., Shanmugaratnam, S., Rodríguez-Romero, A., Baker, D., Baker, D.*, Höcker, B.*, & Fernández-Velasco, D. A.* (2021). The Stability Landscape of de novo TIM Barrels Explored by a Modular Design Approach. Journal of Molecular Biology, 433(18).
DOI:10.1016/j.jmb.2021.167153

Romero-Arias, J. R., S. Luviano, A., Costas, M., Hernández-Machado, A., & Barrio, R. A.* (2021). Dipole–dipole interactions control the interfacial rheological response of cyclodextrin/surfactant solutions. Soft Matter.
DOI:10.1039/d0sm01796e

Coyotl, E. A. P., Palacios, J. B., Muciño, G., Moreno-Blas, D., Costas, M., Montes, T. M., Diener, C., Uribe-Carvajal, S., Massieu, L., Castro-Obregón, S., Espinosa, O. R., Espinosa, D. M., Barrios-Payan, J., Contreras, J. C. L., Corzo, G., Hernández-Pando, R.*, & Del Rio, G.* (2020). Antimicrobial Peptide against Mycobacterium Tuberculosis That Activates Autophagy Is an Effective Treatment for Tuberculosis. Pharmaceutics, 12(11), 1-24.
DOI:10.3390/pharmaceutics12111071

Romero-Romero, S., Costas, M., Silva Manzano, D.-A., Kordes, S., Rojas-Ortega, E., Tapia, C., Guerra, Y., Shanmugaratnam, S., Rodríguez-Romero, A., Baker, D., Höcker, B., & Fernández-Velasco, D. A. (2020). Epistasis on the stability landscape of de novo TIM barrels explored by a modular design approach. bioRxiv.
DOI:10.1101/2020.09.29.319103

Riaño-Umbarila, L., Rojas-Trejo, V. M., Romero-Moreno, J. A., Costas, M., Utrera-Espíndola, I., Olamendi-Portugal, T., Possani, L. D., & Becerril, B. (2020). Comparative assessment of the VH-VL and VL-VH orientations of single-chain variable fragments of scorpion toxin-neutralizing antibodies. Molecular Immunology, 122, 141-147.
DOI:10.1016/j.molimm.2020.04.015

Troncoso, J., González-Salgado, D., & Costas, M. (2020). Volumetric characterization of the thermal denaturation of α-chymotrypsin at pH 2.2. The Journal of Chemical Thermodynamics, 149, 106147.
DOI:10.1016/j.jct.2020.106147

Pérez-Isidoro, R., & Costas, M. (2020). The effect of neuroleptic drugs on DPPC/sphingomyelin/cholesterol membranes. Chemistry and Physics of Lipids, 229.
DOI:10.1016/j.chemphyslip.2020.104913

Luviano, A. S., Hernández-Pascacio, J., Ondo, D., Campbell, R. A., Piñeiro, A., Campos-Terán, J., & Costas, M. (2020). Highly viscoelastic films at the water/air interface: α-Cyclodextrin with anionic surfactants. Journal of Colloid and Interface Science, 565, 601-613.
DOI:10.1016/j.jcis.2019.12.012

Piñeiro, Á., Muñoz, E., Sabín, J., Costas, M., Bastos, M., Velázquez-Campoy, A., Garrido, P. F., Dumas, P., Ennifar, E., García-Río, L., Rial, J., Pérez, D., Fraga, P., Rodríguez, A., & Cotelo, C. (2019). AFFINImeter: A software to analyze molecular recognition processes from experimental data. Analytical Biochemistry, 577, 117-134.
DOI:10.1016/j.ab.2019.02.031

Aguayo-Ortiz, R., González-Navejas, A., Palomino-Vizcaino, G., Rodriguez-Meza, O., Costas, M., Quintanar, L., & Dominguez, L. (2019). Thermodynamic stability of human γd-crystallin mutants using alchemical free-energy calculations. Journal of Physical Chemistry B, 123(27), 5671-5677.
DOI:10.1021/acs.jpcb.9b01818

Schulte-Sasse, M., Pardo-Ávila, F., Pulido-Mayoral, N. O., Vázquez-Lobo, A., Costas, M., García-Hernández, E., Rodríguez-Romero, A., & Fernández-Velasco, D. A. (2019). Structural, thermodynamic and catalytic characterization of an ancestral triosephosphate isomerase reveal early evolutionary coupling between monomer association and function. FEBS Journal, 286(5), 882-900.
DOI:10.1111/febs.14741

Romero-Romero, S., Becerril-Sesín, L. A., Costas, M., Rodríguez-Romero, A., & Fernández-Velasco, D. A. (2018). Structure and conformational stability of the triosephosphate isomerase from zea mays. comparison with the chemical unfolding pathways of other eukaryotic TIMs. Archives of Biochemistry and Biophysics, 658, 66-76.
DOI:10.1016/j.abb.2018.09.022

Quezada, A. G., Cabrera, N., Piñeiro, Á., Díaz-Salazar, A. J., Díaz-Mazariegos, S., Romero-Romero, S., Pérez-Montfort, R., & Costas, M. (2018). A strategy based on thermal flexibility to design triosephosphate isomerase proteins with increased or decreased kinetic stability. Biochemical and Biophysical Research Communications, 503(4), 3017-3022.
DOI:10.1016/j.bbrc.2018.08.087

Velázquez-López, I., Valdés-García, G., Romero Romero, S., Maya Martínez, R., Leal-Cervantes, A. I., Costas, M., Sánchez-López, R., Amero, C., Pastor, N., & Fernández Velasco, D. A. (2018). Localized conformational changes trigger the pH-induced fibrillogenesis of an amyloidogenic λ light chain protein. Biochimica Et Biophysica Acta – General Subjects, 1862(7), 1656-1666.
DOI:10.1016/j.bbagen.2018.04.014

Romero-Romero, S., Fernández-Velasco, D. A., & Costas, M. (2018). Estabilidad termodinámica de proteínas. Educación química, 29(3), 3-17.
DOI:10.22201/fq.18708404e.2018.3.64699

Romero-Romero, S., Fernández-Velasco, D. A., & Costas, M. (2018). Donde la termodinámica y las proteínas se encuentran. Educación química, 29(3), 18-21.
DOI:10.22201/fq.18708404e.2018.3.65734

Ondo, D., & Costas, M. (2017). Complexation thermodynamics of α-cyclodextrin with ionic surfactants in water. Journal of Colloid and Interface Science, 505, 445-453.
DOI:10.1016/j.jcis.2017.05.093

Olivares-Illana, V., Riveros-Rosas, H., Cabrera, N., Tuena de Gómez-Puyou, M., Pérez-Montfort, R., Costas, M., & Gómez-Puyou, A. (2017). A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease. Proteins: Structure, Function and Bioinformatics, 85(7), 1190-1211.
DOI:10.1002/prot.25299

Guzmán-Luna, V., Quezada, A. G., Díaz-Salazar, A. J., Cabrera, N., Pérez-Montfort, R., & Costas, M. (2017). The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes. Proteins: Structure, Function and Bioinformatics, 85(4), 571-579.
DOI:10.1002/prot.25231

Garay Sánchez, S. A., Rodríguez Álvarez, F. J., Zavala-Padilla, G., Mejia-Cristobal, L. M., Cruz-Rangel, A., Costas, M., Fernández Velasco, D. A., Melendez-Zajgla, J., & Del Pozo-Yauner, L. (2017). Stability and aggregation propensity do not fully account for the association of various germline variable domain gene segments with light chain amyloidosis. Biological Chemistry, 398(4), 477-489.
DOI:10.1515/hsz-2016-0178

Quezada, A. G., Díaz-Salazar, A. J., Cabrera, N., Pérez-Montfort, R., Piñeiro, Á., & Costas, M. (2017). Interplay between protein thermal flexibility and kinetic stability. Structure, 25(1), 167-179.
DOI:10.1016/j.str.2016.11.018

Vieyra-Eusebio, M. T., & Costas, M. (2016). Protein-protein interactions at high concentrations. isothermal titration calorimetry determination of human serum albumin-lysozyme interaction enthalpy at several pH values. Thermochimica Acta, 641, 39-42.
DOI:10.1016/j.tca.2016.08.011

Hernandez-Pascacio, J., Piñeiro, A., Ruso, J. M., Hassan, N., Campbell, R. A., Campos-Terán, J., & Costas, M. (2016). Complex behavior of aqueous α-cyclodextrin solutions. interfacial morphologies resulting from bulk aggregation. Langmuir, 32(26), 6682-6690.
DOI:10.1021/acs.langmuir.6b01646

Romero-Romero, S., Costas, M., Rodríguez-Romero, A., & Fernández-Velasco, D. A. (2016). Erratum: Reversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteins (phys.chem.chem.phys. (2016) 18 (10647)). Physical Chemistry Chemical Physics, 18(15), 10647.
DOI:10.1039/c6cp90084d

Raga-Carbajal, E., Carrillo-Nava, E., Costas, M., Porras-Dominguez, J., López-Munguía, A., & Olvera, C. (2016). Size product modulation by enzyme concentration reveals two distinct levan elongation mechanisms in bacillus subtilis levansucrase. Glycobiology, 26(4), 377-385.
DOI:10.1093/glycob/cwv112

Aguirre, C., Goto, Y., & Costas, M. (2016). Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. FEBS Letters, 590(2), 202-214.
DOI:10.1002/1873-3468.12041