Cargando…
Redox properties of Cys(2)His(2) and Cys(4) zinc fingers determined by electrospray ionization mass spectrometry
Zinc finger (ZF) protein motifs, stabilized by binding of Zn(II), typically function as interaction modules that bind nucleic acids, proteins and other molecules. The elucidation of the redox states of ZF proteins in cellular conditions, which depend on their midpoint redox potentials, is important...
Autores principales: | Smirnova, Julia, Kabin, Ekaterina, Tõugu, Vello, Palumaa, Peep |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5985984/ https://www.ncbi.nlm.nih.gov/pubmed/29928572 http://dx.doi.org/10.1002/2211-5463.12422 |
Ejemplares similares
-
Copper(I)-binding properties of de-coppering drugs for the treatment of Wilson disease. α-Lipoic acid as a potential anti-copper agent
por: Smirnova, Julia, et al.
Publicado: (2018) -
An improved predictive recognition model for Cys(2)-His(2) zinc finger proteins
por: Gupta, Ankit, et al.
Publicado: (2014) -
Cys(2)/His(2) Zinc-Finger Proteins in Transcriptional Regulation of Flower Development
por: Lyu, Tianqi, et al.
Publicado: (2018) -
The geometric influence on the Cys(2)His(2) zinc finger domain and functional plasticity
por: Mueller, April L, et al.
Publicado: (2020) -
A systematic survey of the Cys(2)His(2) zinc finger DNA-binding landscape
por: Persikov, Anton V., et al.
Publicado: (2015)