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Canonical or noncanonical? Structural plasticity of serine protease-binding loops in Kunitz-STI protease inhibitors
ArticleAbstract: The Kunitz-Soybean Trypsin Inhibitor (Kunitz-STI) family is a large family of proteins with most ofPalabras claves:canonical inhibitors, Kunitz, noncanonical inhibitors, protease inhibitors, serine proteaseAutores:Berry C., Eduardo Tejera, Pons T., Vinicio Danilo Armijos-Jaramillo, Yasel GuerraFuentes:googlescopusPbkp_redicting functional residues of the Solanum lycopersicum aspartic protease inhibitor (SLAPI) by combining sequence and structural analysis with molecular docking
ArticleAbstract: The Solanum lycopersicum aspartic protease inhibitor (SLAPI), which belongs to the STI-Kunitz familyPalabras claves:Aspartic protease inhibitor, Comparative 3D modeling, Functional residue identification, Protein-protein docking, Protein-protein interface, STI-Kunitz inhibitorAutores:Berry C., Pons T., Valiente P.A., Yasel GuerraFuentes:googlescopusStructures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases: Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop?
ArticleAbstract: Bi-functional inhibitors from the Kunitz-type soybean trypsin inhibitor (STI) family are glycosylatePalabras claves:Aspartic protease inhibitors, Bi-functional inhibitors, Kunitz-type STI family inhibitors, Plant protease inhibitors, β-Trefoil foldAutores:Berry C., Pons T., Rudino-Pinera E., Valiente P.A., Yasel GuerraFuentes:googlescopus