Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system
Abstract Protein degradation is a fundamental process in all living cells and is essential to remove both damaged proteins and intact proteins that are no longer needed by the cell. We are interested in creating synthetic genetic circuits that function in a cell-free expression system. This will req...
Guardado en:
Autores principales: | Xinying Shi, Ti Wu, Christian M. Cole, Neal K. Devaraj, Simpson Joseph |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/7864bd636f484af58fd311bfaf3f0ba4 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Regulation of Antimycin Biosynthesis Is Controlled by the ClpXP Protease
por: Bohdan Bilyk, et al.
Publicado: (2020) -
Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
por: Kamran Rizzolo, et al.
Publicado: (2021) -
A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells
por: Shengchen Wang, et al.
Publicado: (2021) -
Author Correction: Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
por: Kamran Rizzolo, et al.
Publicado: (2021) -
Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translation
por: Yuichi Matsushima, et al.
Publicado: (2017)