Focal adhesion kinase: the first ten years

By J. Parsons. Journal of Cell Science, 2003

1,397 citations recorded by the source corpus.

Subfields: Cell Biology, Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/70dec40b1ec182e45e3343350ca1c3b7ededa899

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Valerie M. Weaver
2. M. Strand
3. M. Schwartz
4. A. Horwitz
5. J. Guan
6. D. Schlaepfer
7. J. Parsons
8. Sanjay Kumar

In Immunology and Allergy

1. J. Guan
2. Valerie M. Weaver
3. M. Strand
4. M. Schwartz
5. J. Parsons
6. A. Horwitz
7. D. Schlaepfer
8. Sanjay Kumar

In Molecular Biology

1. M. Strand
2. J. Guan
3. A. Horwitz
4. D. Schlaepfer
5. J. Parsons
6. Sanjay Kumar
7. Valerie M. Weaver
8. L. Claesson‐Welsh

Citations in the corpus

• Focal adhesion kinase: in command and control of cell motility (2005, background): “Early studies found that FAK could be activated by either ECM or growth factors, and that tyrosine phosphorylation of FAK was a rapid event that was associated with the formation of focal contact”
• Non-muscle myosin II takes centre stage in cell adhesion and migration (2009, neutral): “These phosphorylations trigger the activation and recruitment to adhesions of signalling intermediates such as the p130CAS–CRK and G protein-coupled receptor kinase interacting ArfGAP (GIT)–β-Pix (also known as ARHGEF7) complexes, relaying activation signals to Rho GTPases, particularly Rac (reviewe”
• Signal transduction by vascular endothelial growth factor receptors. (2012, background): “SHB binds to FAK (Holmqvist et al. 2003), which is tyrosine phosphorylated in VEGF-treated cells (Abu-Ghazaleh et al. 2001), thereby regulating cell attachment and migration (Parsons 2003). pY1214 allows recruitment of NCK and FYN to VEGFR2.”
• The insect cellular immune response (2008, background): “Downstream, integrin-mediated adhesion and phagocytosis in mammals requires tyrosine phosphorylation of other proteins including Cas, Fak, paxillan, and Pyk2 that localize to focal adhesions and link transmembrane integrins to the actin cytoskeleton (Gelman, 2003; Parsons, 2003).”
• Mechanics, malignancy, and metastasis: The force journey of a tumor cell (2009, background): “FAK is a nonreceptor tyrosine kinase that is widely overexpressed and activated in tumor cells [139–142].”
• FAK phosphorylation sites mapped by mass spectrometry (2005, background): “In addition, the phosphorylation of specific tyrosine residues appears to be important for the recruitment of SH2-domaincontaining signaling proteins, including Src and Src family kinases, PI 3-kinase and Grb2 (Mitra et al., 2005; Parsons, 2003; Parsons et al., 2000).”
• Integrin Structure and Function (2010, neutral): “(Parsons 2003).”