Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "FAK may be recruited to nascent focal adhesions because it interacts, either directly or through the cytoskeletal proteins talin and paxillin, with the cytoplasmic tail of integrin b subunits (8). Upon activation, FAK autophosphorylates Tyr397, creating a binding site for the Src homology 2 (SH2) domain of Src or Fyn (9, 10). The Src kinase then phosphorylates a number of focal adhesion components. The major targets include paxillin and tensin, two cytoskeletal proteins that may also have signaling functions, and p130CAS, a docking protein that recruits the adapter proteins Crk and Nck (11, 12)." ?g. }

• _5 value "FAK may be recruited to nascent focal adhesions because it interacts, either directly or through the cytoskeletal proteins talin and paxillin, with the cytoplasmic tail of integrin b subunits (8). Upon activation, FAK autophosphorylates Tyr397, creating a binding site for the Src homology 2 (SH2) domain of Src or Fyn (9, 10). The Src kinase then phosphorylates a number of focal adhesion components. The major targets include paxillin and tensin, two cytoskeletal proteins that may also have signaling functions, and p130CAS, a docking protein that recruits the adapter proteins Crk and Nck (11, 12)." provenance.
• _7 value "FAK may be recruited to nascent focal adhesions because it interacts, either directly or through the cytoskeletal proteins talin and paxillin, with the cytoplasmic tail of integrin b subunits (8). Upon activation, FAK autophosphorylates Tyr397, creating a binding site for the Src homology 2 (SH2) domain of Src or Fyn (9, 10). The Src kinase then phosphorylates a number of focal adhesion components. The major targets include paxillin and tensin, two cytoskeletal proteins that may also have signaling functions, and p130CAS, a docking protein that recruits the adapter proteins Crk and Nck (11, 12)." provenance.
• _7 value "FAK may be recruited to nascent focal adhesions because it interacts, either directly or through the cytoskeletal proteins talin and paxillin, with the cytoplasmic tail of integrin b subunits (8). Upon activation, FAK autophosphorylates Tyr397, creating a binding site for the Src homology 2 (SH2) domain of Src or Fyn (9, 10). The Src kinase then phosphorylates a number of focal adhesion components. The major targets include paxillin and tensin, two cytoskeletal proteins that may also have signaling functions, and p130CAS, a docking protein that recruits the adapter proteins Crk and Nck (11, 12)." provenance.
• _5 value "FAK may be recruited to nascent focal adhesions because it interacts, either directly or through the cytoskeletal proteins talin and paxillin, with the cytoplasmic tail of integrin b subunits (8). Upon activation, FAK autophosphorylates Tyr397, creating a binding site for the Src homology 2 (SH2) domain of Src or Fyn (9, 10). The Src kinase then phosphorylates a number of focal adhesion components. The major targets include paxillin and tensin, two cytoskeletal proteins that may also have signaling functions, and p130CAS, a docking protein that recruits the adapter proteins Crk and Nck (11, 12)." provenance.