The tail domain of lamin B1 is more strongly modulated by divalent cations than lamin A.
Nucleus
; 6(3): 203-11, 2015.
Article
en En
| MEDLINE
| ID: mdl-25807068
Palabras clave
GST, glutathione S-transferase; HFF, human foreskin fibroblasts; LA, lamin A; LA-TD, the tail domain of lamin A; LB1, lamin B1; LB1-TD, the tail domain of lamin B1; MD, molecular dynamics; PME, particle mesh Ewald; REMD, replica exchange molecular dynamics; TD, tail domain; intrinsically disordered proteins; lamin; molecular dynamics; nucleoskeleton; preLA, prelamin A; preLA-TD, the tail domain of prelamin A; trLA-TD, lamin A tail domain truncated to be the same length as lamin B tail domain; ΔI/Io, change in intensity normalized to initial intensity
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Matriz Nuclear
/
Calcio
/
Lamina Tipo A
/
Lamina Tipo B
/
Magnesio
Límite:
Humans
Idioma:
En
Revista:
Nucleus
Año:
2015
Tipo del documento:
Article
País de afiliación:
Estados Unidos