Matches in Nanopublications for { ?s ?p "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" ?g. }
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- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.
- _5 value "Phosphotyrosine at site 960 of the b subunit just inside the membrane creates an NPXpY-recognition motif for the PTB domain of the IRS proteins. Modification of this tyrosine completely inhibits subsequent phosphorylation of IRS-1 and other insulin receptor substrates and leads to loss of most insulin-dependent biological actions" provenance.