Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" ?g. }

• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.
• _5 value "The functional insulin receptor is a heterotetrameric protein composed of two alpha and two beta subunits. The alpha subunits contain the insulin binding site and the binding causes conformational changes in the receptor molecule. The quaternary structure of the beta subunit then changes to allow for stimulating autophosphorylation of its tyrosine residues. Those in the catalytic domain(tyrosines 1146, 1150, 1151) are essential to promote the kinase activity of the receptor" provenance.