Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
about
An update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker proteinLASP2 suppresses colorectal cancer progression through JNK/p38 MAPK pathway meditated epithelial-mesenchymal transition.Leiomodin 3 and tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis.The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2's function.Common variants at 10p12.31, 10q21.1 and 13q12.13 are associated with sporadic pituitary adenoma.New Frontiers for the Cytoskeletal Protein LASP1
P2860
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
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2013 nî lūn-bûn
@nan
2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի փետրվարին 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
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
@ast
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
@en
type
label
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
@ast
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
@en
prefLabel
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
@ast
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
@en
P2093
P2860
P356
P1476
Investigating lasp-2 in cell adhesion: new binding partners and roles in motility.
@en
P2093
Carol C Gregorio
Colin M Jones-Weinert
Katherine T Bliss
Miensheng Chu
P2860
P304
P356
10.1091/MBC.E12-10-0723
P577
2013-02-06T00:00:00Z