FAK phosphorylation sites mapped by mass spectrometry

By P. Grigera, Erin D. Jeffery, K. Martin, J. Shabanowitz, D. Hunt, J. Parsons. Journal of Cell Science, 2005

139 citations recorded by the source corpus.

The protein tyrosine kinase, focal adhesion kinase (FAK), is a central regulator of integrin-mediated signaling ([Mitra et al., 2005][1]; [Parsons, 2003][2]; [Schlaepfer and Mitra, 2004][3]). FAK is present in focal adhesions, adhesive structures that mediate attachment of cells to the extracellular

Subfields: Cancer Research, Cell Biology, Immunology and Allergy

View Paper: https://www.semanticscholar.org/paper/08628dfafd362a64e1de3ef8534e27822bbc817d

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Citations in the corpus

• Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “For example, mass spectroscopic analysis of talin isolated from activated platelets identified 30 different phosphorylation sites, three with high stochiometry (Ratnikov et al. 2005), but a biological role for talin phosphorylation has yet to be shown.”