Integrin-linked kinase: a cancer therapeutic target unique among its ILK
By G. Hannigan, A. Troussard, S. Dedhar. Nature Reviews. Cancer, 2005
619 citations recorded by the source corpus.
Subfields: Cell Biology, Immunology and Allergy, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/99dc7bba9ce676e752b1cbec2dccdb165b05e500
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Citations in the corpus
- Signaling mechanisms of the epithelial-mesenchymal transition (2014, background): “TGF-β signaling can directly increase LEF1 expression through SMADs and inhibit glycogen synthase kinase 3β (GSK-3β) through the phosphoinositide 3-kinase (PI3K)–Akt pathway, which enables β-catenin–dependent activation of LEF-1 to induce EMT (58, 105).”
- ILK, PINCH and parvin: the tIPP of integrin signalling (2006, background): “Interestingly, ILK expression is upregulated in many human tumour”
- Integrin signalling at a glance (2009, background): “ILK contains an N-terminal ankyrin-repeat domain that mediates protein interactions with PINCH1 or PINCH2, and a Cterminal kinase domain that supports interactions with α-, β- or γ-parvin, paxillin (see below) and, possibly, βintegrin tails (Hannigan et al., 2005; Legate et al., 2006).”