Cargando…
Structural Basis for Specificity of Propeptide-Enzyme Interaction in Barley C1A Cysteine Peptidases
C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and barley cathepsins has been characterized. Differen...
Autores principales: | Cambra, Inés, Hernández, David, Diaz, Isabel, Martinez, Manuel |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355106/ https://www.ncbi.nlm.nih.gov/pubmed/22615948 http://dx.doi.org/10.1371/journal.pone.0037234 |
Ejemplares similares
-
A cathepsin F-like peptidase involved in barley grain protein mobilization, HvPap-1, is modulated by its own propeptide and by cystatins
por: Cambra, Ines, et al.
Publicado: (2012) -
Cysteine peptidases and their inhibitors in Tetranychus urticae: a comparative genomic approach
por: Santamaría, María Estrella, et al.
Publicado: (2012) -
A cysteine-based molecular code informs collagen C-propeptide assembly
por: DiChiara, Andrew S., et al.
Publicado: (2018) -
Studies of Inhibitory Mechanisms of Propeptide-Like Cysteine Protease Inhibitors
por: Nga, Bui T. T., et al.
Publicado: (2014) -
Conformational analysis and interaction of the Staphylococcus aureus transmembrane peptidase AgrB with its AgrD propeptide substrate
por: Bardelang, Philip, et al.
Publicado: (2023)