Cargando…
Autoproteolytic Activation of Bacterial Toxins
Protease domains within toxins typically act as the primary effector domain within target cells. By contrast, the primary function of the cysteine protease domain (CPD) in Multifunctional Autoprocessing RTX-like (MARTX) and Clostridium sp. glucosylating toxin families is to proteolytically cleave th...
Autor principal: | Shen, Aimee |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153235/ https://www.ncbi.nlm.nih.gov/pubmed/22069620 http://dx.doi.org/10.3390/toxins2050963 |
Ejemplares similares
-
Exploring the Role of Conformational Heterogeneity
in cis-Autoproteolytic Activation of ThnT
por: Buller, Andrew R., et al.
Publicado: (2014) -
Characterization of the potyviral HC-pro autoproteolytic cleavage site
por: Carrington, James C., et al.
Publicado: (1992) -
Autoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and Catalysis
por: Buller, Andrew R., et al.
Publicado: (2012) -
Unexpected role of the L-domain of calpastatin during the autoproteolytic activation of human erythrocyte calpain
por: De Tullio, Roberta, et al.
Publicado: (2018) -
MYRF Is a Membrane-Associated Transcription Factor That Autoproteolytically Cleaves to Directly Activate Myelin Genes
por: Bujalka, Helena, et al.
Publicado: (2013)