Cargando…
One single method to produce native and Tat-fused recombinant human α-synuclein in Escherichia coli
BACKGROUND: Human α-synuclein is a small-sized, natively unfolded protein that in fibrillar form is the primary component of Lewy bodies, the pathological hallmark of Parkinson’s disease. Experimental evidence suggests that α-synuclein aggregation is the key event that triggers neurotoxicity althoug...
Autores principales: | Caldinelli, Laura, Albani, Diego, Pollegioni, Loredano |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3621789/ https://www.ncbi.nlm.nih.gov/pubmed/23557146 http://dx.doi.org/10.1186/1472-6750-13-32 |
Ejemplares similares
-
Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli
por: Volontè, Federica, et al.
Publicado: (2010) -
Optimizing HIV-1 protease production in Escherichia coli as fusion protein
por: Volontè, Federica, et al.
Publicado: (2011) -
Optimizing Escherichia coli as a protein expression platform to produce Mycobacterium tuberculosis immunogenic proteins
por: Piubelli, Luciano, et al.
Publicado: (2013) -
The D-amino acid oxidase-carbon nanotubes: evaluation of cytotoxicity and biocompatibility of a potential anticancer nanosystem
por: Rosini, Elena, et al.
Publicado: (2023) -
Substrate-triggered position switching of TatA and TatB during Tat transport in Escherichia coli
por: Habersetzer, Johann, et al.
Publicado: (2017)