Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
about
Solution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix ProteinJuxtamembrane contribution to transmembrane signaling.FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.Selectins in Liver Ischemia and Reperfusion Injury.Molecular Dynamics of the Association of L-Selectin and FERM Regulated by PIP2.Sequential binding of ezrin and moesin to L-selectin regulates monocyte protrusive behaviour during transendothelial migration
P2860
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
description
2013 nî lūn-bûn
@nan
2013 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@ast
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@en
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@nl
type
label
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@ast
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@en
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@nl
prefLabel
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@ast
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@en
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.
@nl
P2860
P1433
P1476
Calmodulin adopts an extended conformation when interacting with L-selectin in membranes
@en
P2093
John A Putkey
P2860
P304
P356
10.1371/JOURNAL.PONE.0062861
P407
P50
P577
2013-05-02T00:00:00Z