Cargando…
Cooperative Activity of SARS Coronavirus Nsp13 Helicase Characterized by Single Molecule FRET
Autores principales: | Im, Hyeryeon, Jee, Sangmi, Lee, Gwangrog |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biophysical Society. Published by Elsevier Inc.
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111059/ http://dx.doi.org/10.1016/j.bpj.2014.11.426 |
Ejemplares similares
-
Unwinding mechanism of SARS-CoV helicase (nsp13) in the presence of Ca(2+), elucidated by biochemical and single-molecular studies
por: Yu, Jeongmin, et al.
Publicado: (2023) -
Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13
por: Lee, Na-Ra, et al.
Publicado: (2010) -
Identification of myricetin and scutellarein as novel chemical inhibitors of the SARS coronavirus helicase, nsP13
por: Yu, Mi-Sun, et al.
Publicado: (2012) -
A high ATP concentration enhances the cooperative translocation of the SARS coronavirus helicase nsP13 in the unwinding of duplex RNA
por: Jang, Kyoung-Jin, et al.
Publicado: (2020) -
Z-RNA and the Flipside of the SARS Nsp13 Helicase: Is There a Role for Flipons in Coronavirus-Induced Pathology?
por: Herbert, Alan, et al.
Publicado: (2022)