Title : Uncoupling ligand-dependent and -independent mechanisms for mitogen-activated protein kinase activation by the murine Ron receptor tyrosine kinase.

Pub. Date : 2005 Oct 21

PMID : 16103119






6 Functional Relationships(s)
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1 Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon. Tyrosine mitogen-activated protein kinase 1 Mus musculus
2 Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon. Tyrosine mitogen-activated protein kinase 1 Mus musculus
3 Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon. Tyrosine mitogen-activated protein kinase 1 Mus musculus
4 Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon. Tyrosine mitogen-activated protein kinase 1 Mus musculus
5 Phenylalanine mutations at these three tyrosines results in a receptor that fails to constitutively activate the Erk pathway but retains the ability to induce Erk phosphorylation in response to ligand stimulation. Tyrosine mitogen-activated protein kinase 1 Mus musculus
6 Phenylalanine mutations at these three tyrosines results in a receptor that fails to constitutively activate the Erk pathway but retains the ability to induce Erk phosphorylation in response to ligand stimulation. Tyrosine mitogen-activated protein kinase 1 Mus musculus