Acceso a usuarios
Bienvenid@

Tutores

ENRIQUE GARCÍA HERNÁNDEZ

Instituto de Química (IQ)

Contacto

Teléfono: 55 56 22 44 24
Email: egarciah@unam.mx
Sitio web: Visitar sitio web

Campos de conocimiento

Biofísica
Bioquímica
Reconocimiento Molecular y Bioestructura

Líneas de investigación

Formación de complejos de proteína. Plegamiento de proteína. Interacción proteína-proteína y proteína-ligando

Publicaciones

35. Leyva, E., † Medrano-Cerano, J.L., † Cano-Sánchez, P., López-González, I., † Gómez-Velasco, H., † del Río-Portilla, F., García-Hernández, E.* (2019) Bacterial expression, purification and biophysical characterization of wheat germ agglutinin and its four hevein-like domains. Biopolymers 110: e23242. (F.I. = 2.2, Q3(JCR)/Q2(SJR)/Q2(Scopus); issn 0006-3525; eissn: 1097-0282; doi: 10.1002/bip.23242).
36. Luviano, A., † Cruz-Castañeda, R., † Sánchez-Puig, N., García-Hernández, E.* (2019) Cooperative energetic effects elicited by the yeast Shwachman-Diamond syndrome protein (Sdo1) and guanine nucleotides modulate the complex conformational landscape of the elongation factor-like 1 (Efl1) GTPase. Biophys. Chem. 247: 13-24 (F.I. = 3.6, Q2(JCR)/Q2(SJR)/Q2(Scopus); issn 0301-4622; eissn: 1873-4200; doi: 10.1016/j.bpc.2019.02.003).
37. 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 J. 286: 882-900. (F.I. = 5.6, Q2(JCR)/Q1(SJR)/Q1(Scopus); issn 1742-464X; eissn: 1742-4658; doi: 10.1111/febs.14741).
38. Gómez-Velasco, H., † Rojo-Domínguez, A., García-Hernández, E.* (2020) Enthalpically-driven ligand recognition and cavity solvation of bovine odorant binding protein. Biophys. Chem. 257: 106315 (F.I. = 3.6, Q2(JCR)/Q2(SJR)/Q2(Scopus); issn 0301-4622; eissn: 1873-4200; doi: 10.1016/j.bpc.2019.106315).
39. Ruiz-Blanco, Y.B., † Avila-Barrientos, L.P., † Hernández-García, E., † Antunes, A., Agüero-Chapin, G.*, García-Hernández, E.* (2021) Engineering protein fragments via evolutionary and protein-protein interaction algorithms: De novo design of peptide inhibitors for FOF1-ATPsynthase. FEBS Lett. 595(2): 183-194. (F.I. = 3.9, Q2(JCR)/Q1(SJR)/Q1(Scopus); issn 0014-5793; eissn: 1873-3468; doi: 10.1002/1873-3468.13988).
40. Labra-Núñez, A., † Cofas-Vargas, L.F., † Gutiérrez-Magdaleno, G., † Gómez-Velasco, H., † Rodríguez-Hernández, A., Rodríguez-Romero, A., García-Hernández, E.* (2021) Energetic and structural effects of the Tanford transition on ligand recognition of bovine -lactoglobulin. Arch. Biochem. Biophys. 699: 108750. (F.I: = 4.1, Q2(JCR)/Q1(SJR)/Q1(Scopus); issn 0003-9861; eissn: 1096-0384; doi: 10.1016/j.abb.2020.108750).
41. Valdez-Cruz, N.A.*, García-Hernández, E., Espitia, C., Cobos-Marín, L., Altamirano, C., Bando-Campos, C.G., Cofas-Vargas, L.F.,† Coronado-Aceves, E.W., González-Hernández, R.A., Hernández-Peralta, P., Juárez-López, D., Ortega-Portilla, P.A., Restrepo-Pineda, S., Zelada-Cordero, P., Trujillo-Roldán, M.A.* (2021) Integrative overview of antibodies against SARS-CoV-2 and their possible applications in COVID-19 prophylaxis and treatment. Microb. Cell Fact. 20:88. (F.I. = 6.4, Q1(JCR)/Q1(SJR)/Q1(Scopus); eissn 1475-2859, doi: 10.1186/s12934‑021‑01576).
42. Avila-Barrientos, L.P.,† Cofas-Vargas, L.F.,† Agüero-Chapin, G., Hernández-García, E.,† Ruiz-Carmona, S., Valdez-Cruz, N.A., Trujillo-Roldán, M., Weber, J., Ruiz-Blanco, Y.B.†*, Barril, X., García-Hernández, E.* Computational design of inhibitors targeting the catalytic β subunit of Escherichia coli FOF1-ATP synthase. Antibiotics. 11(5), 557 (F.I. = 5.2, Q1(JCR)/Q1(SJR)/Q1(Scopus); eissn: 2079-6382; doi: 10.3390/antibiotics11050557).
43. Restrepo-Pineda, S., Sánchez-Puig, N., Pérez, N.O., García-Hernández, E., Valdez-Cruz, N.A., Trujillo-Roldán, M.* (2022) The pre-induction temperature affects the structural characteristics of recombinant HuGM-CSF inclusion bodies using a thermoinducible system. Appl. Microbiol. Biotechnol. 106, 2883–2902 (F.I. = 5.6, Q1(JCR)/Q1(SJR)/Q1(Scopus); issn 0175-7598; eissn: 1432-0614, doi: 10.1007/s00253-022-11908-z).
44. Restrepo-Pineda, S., Rosiles-Becerril, D., Vargas-Castillo, A.B., Avila-Barrientos, L.P., Luviano, A., Sánchez-Puig, N., García-Hernández, E., Pérez, N.O., Trujillo-Roldán, M., Valdez-Cruz, N.A. (2022) Induction temperature impacts the structure of recombinant HuGM-CSF inclusion bodies in thermoinducible E. coli. Elec. J. Biotech. 59: 94-106. (F.I. = 2.8, Q3(JCR)/Q2(SJR)/Q2(Scopus), issn: 0717-3458 , eissn: 0717-3458, doi: 10.1016/j.ejbt.2022.08.004)
45. Cofas-Vargas, L.F., † Mendoza-Espinosa, P., † Ávila-Barrientos, L.P., † Prada-Gracia, D., Riveros-Rosas, H., García-Hernández, E.* Exploring the druggability of the binding site of aurovertin, an exogenous allosteric inhibitor of FOF1-ATP synthase. Front. Pharmacol. 13:1012008 (F.I. = 6.0, Q1(JCR)/Q1(SJR)/Q1(Scopus); eissn: 1663-9812, doi: 10.3389/fphar.2022.1012008).
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