Matches in Nanopublications for { ?s ?p "DOC-2/DAB2 and DIP1/2 complex represent a negative feedback machinery for several exogenous stimuli-elicited signal cascade. PKC can phosphorylate the N-terminal domain of DOC-2/DAB2 (serine 24) that recruits DIP1/2 to inactivate Ras protein. On the other hand, shortly after the treatment of peptide growth factors, the C terminus of DOC-2/DAB2 (proline-rich domain) competes with SOS for Grb 2 binding, which leads to the inactivation of the MAP pathway. " ?g. }
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- _6 value "DOC-2/DAB2 and DIP1/2 complex represent a negative feedback machinery for several exogenous stimuli-elicited signal cascade. PKC can phosphorylate the N-terminal domain of DOC-2/DAB2 (serine 24) that recruits DIP1/2 to inactivate Ras protein. On the other hand, shortly after the treatment of peptide growth factors, the C terminus of DOC-2/DAB2 (proline-rich domain) competes with SOS for Grb 2 binding, which leads to the inactivation of the MAP pathway. " provenance.
- _6 value "DOC-2/DAB2 and DIP1/2 complex represent a negative feedback machinery for several exogenous stimuli-elicited signal cascade. PKC can phosphorylate the N-terminal domain of DOC-2/DAB2 (serine 24) that recruits DIP1/2 to inactivate Ras protein. On the other hand, shortly after the treatment of peptide growth factors, the C terminus of DOC-2/DAB2 (proline-rich domain) competes with SOS for Grb 2 binding, which leads to the inactivation of the MAP pathway. " provenance.
- _6 value "DOC-2/DAB2 and DIP1/2 complex represent a negative feedback machinery for several exogenous stimuli-elicited signal cascade. PKC can phosphorylate the N-terminal domain of DOC-2/DAB2 (serine 24) that recruits DIP1/2 to inactivate Ras protein. On the other hand, shortly after the treatment of peptide growth factors, the C terminus of DOC-2/DAB2 (proline-rich domain) competes with SOS for Grb 2 binding, which leads to the inactivation of the MAP pathway. " provenance.
- _6 value "DOC-2/DAB2 and DIP1/2 complex represent a negative feedback machinery for several exogenous stimuli-elicited signal cascade. PKC can phosphorylate the N-terminal domain of DOC-2/DAB2 (serine 24) that recruits DIP1/2 to inactivate Ras protein. On the other hand, shortly after the treatment of peptide growth factors, the C terminus of DOC-2/DAB2 (proline-rich domain) competes with SOS for Grb 2 binding, which leads to the inactivation of the MAP pathway. " provenance.
- _6 value "DOC-2/DAB2 and DIP1/2 complex represent a negative feedback machinery for several exogenous stimuli-elicited signal cascade. PKC can phosphorylate the N-terminal domain of DOC-2/DAB2 (serine 24) that recruits DIP1/2 to inactivate Ras protein. On the other hand, shortly after the treatment of peptide growth factors, the C terminus of DOC-2/DAB2 (proline-rich domain) competes with SOS for Grb 2 binding, which leads to the inactivation of the MAP pathway. " provenance.
- _6 value "DOC-2/DAB2 and DIP1/2 complex represent a negative feedback machinery for several exogenous stimuli-elicited signal cascade. PKC can phosphorylate the N-terminal domain of DOC-2/DAB2 (serine 24) that recruits DIP1/2 to inactivate Ras protein. On the other hand, shortly after the treatment of peptide growth factors, the C terminus of DOC-2/DAB2 (proline-rich domain) competes with SOS for Grb 2 binding, which leads to the inactivation of the MAP pathway. " provenance.