Cargando…
Confirmation of covalently-linked structure and cell-death inducing activity in site-specific chemical conjugates of human Fas ligand extracellular domain
OBJECTIVE: In this study, we aimed to identify the structural components and to clarify the biological activity in the site-specific conjugates of human Fas ligand extracellular domain (hFasLECD) with either fluorescein moiety (FL) or chicken egg-white avidin (Avi). The conjugates were characterized...
Autores principales: | Muraki, Michiro, Hirota, Kiyonori |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6003068/ https://www.ncbi.nlm.nih.gov/pubmed/29907131 http://dx.doi.org/10.1186/s13104-018-3501-8 |
Ejemplares similares
-
Site-specific chemical conjugation of human Fas ligand extracellular domain using trans-cyclooctene – methyltetrazine reactions
por: Muraki, Michiro, et al.
Publicado: (2017) -
Preparation of a functional fluorescent human Fas ligand extracellular domain derivative using a three-dimensional structure guided site-specific fluorochrome conjugation
por: Muraki, Michiro
Publicado: (2016) -
Improved production of recombinant human Fas ligand extracellular domain in Pichia pastoris: yield enhancement using disposable culture-bag and its application to site-specific chemical modifications
por: Muraki, Michiro
Publicado: (2014) -
Impairment of Fas-ligand–caveolin-1 interaction inhibits Fas-ligand translocation to rafts and Fas-ligand-induced cell death
por: Glukhova, Xenia A., et al.
Publicado: (2018) -
The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability
por: Henkler, Frank, et al.
Publicado: (2005)