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Article(3)
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Biotechnology and Applied Biochemistry(1)
Journal of Structural Biology(1)
Protein Science(1)
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:googlescopusGeneration of an affinity matrix useful in the purification of natural inhibitors of plasmepsin II, an antimalarial-drug target
ArticleAbstract: An affinity matrix containing the antimalarial drug target Plm II (plasmepsin II) as ligand was genePalabras claves:Antimalarial-drug target, Plasmepsin II inhibitor, Plasmodium (malarial parasite), Plexaura homomalla (black sea rod), Xestospongia muta (giant barrel sponge)Autores:Berry C., Chávez M.d.l.A., García B., Hernández-Zanui A., Mendiola J., Otero A.J., Ramírez A.R., 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