Mostrando 3 resultados de: 3
Filtros aplicados
Subtipo de publicación
Article(3)
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:googlescopusTwo aspartate residues at the putative p10 subunit of a type II metacaspase from Nicotiana tabacum L. may contribute to the substrate-binding pocket
ArticleAbstract: Metacaspases are cysteine proteases present in plants, fungi, prokaryotes, and early branching eukarPalabras claves:Autoprocessing, Cell death, protein modeling, Transient expressionAutores:Acosta-Maspons A., Lien González-Pérez, Marrero-Gutiérrez J., Pons T., Rocha-Sosa M., Sánchez-Baldoquín L., Sepúlveda-García E.Fuentes:scopusStructures 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