| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-178 |
Sentence |
denotes |
Evidence for a differential interaction of SHC and the insulin receptor substrate-1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system. |
| T2 |
179-487 |
Sentence |
denotes |
Using the yeast two-hybrid system, a genetic assay for studying protein-protein interactions, we have examined and compared the interaction of the insulin-like growth factor-I receptor (IGF-IR) and the insulin receptor (IR) with their two known substrates p52Shc and the insulin receptor substrate-1 (IRS-1). |
| T3 |
488-585 |
Sentence |
denotes |
We also mapped the specific domains of the IGF-IR and p52Shc participating in these interactions. |
| T4 |
586-1036 |
Sentence |
denotes |
Our findings can be summarized as follows: (i) the tyrosine kinase activity of the IGF-IR is essential for the interaction with p52Shc and IRS-1, (ii) p52Shc and IRS-1 bind to the IGF-IR in the NPEY-juxtamembrane motif, (iii) contrary to p52Shc, IRS-1 binds also to the major autophosphorylation sites (Tyr-1131, -1135, and -1136) of the IGF-IR, and (iv) the amino-terminal domain of p52Shc is required for its association with the IR and the IGF-IR. |
| T5 |
1037-1300 |
Sentence |
denotes |
We propose that (i) the IGF-IR and the IR share at least in part the same molecular mechanism underlying their interplay with their two substrates, p52Shc and IRS-1, and (ii) IRS-1 interacts with the IGF-IR in a fashion that is different from that used by p52Shc. |
| T6 |
1301-1417 |
Sentence |
denotes |
Finally, our data highlight the crucial role of the juxtamembrane domain in signaling by both the IR and the IGF-IR. |
| T1 |
0-178 |
Sentence |
denotes |
Evidence for a differential interaction of SHC and the insulin receptor substrate-1 (IRS-1) with the insulin-like growth factor-I (IGF-I) receptor in the yeast two-hybrid system. |
| T2 |
179-487 |
Sentence |
denotes |
Using the yeast two-hybrid system, a genetic assay for studying protein-protein interactions, we have examined and compared the interaction of the insulin-like growth factor-I receptor (IGF-IR) and the insulin receptor (IR) with their two known substrates p52Shc and the insulin receptor substrate-1 (IRS-1). |
| T3 |
488-585 |
Sentence |
denotes |
We also mapped the specific domains of the IGF-IR and p52Shc participating in these interactions. |
| T4 |
586-1036 |
Sentence |
denotes |
Our findings can be summarized as follows: (i) the tyrosine kinase activity of the IGF-IR is essential for the interaction with p52Shc and IRS-1, (ii) p52Shc and IRS-1 bind to the IGF-IR in the NPEY-juxtamembrane motif, (iii) contrary to p52Shc, IRS-1 binds also to the major autophosphorylation sites (Tyr-1131, -1135, and -1136) of the IGF-IR, and (iv) the amino-terminal domain of p52Shc is required for its association with the IR and the IGF-IR. |
| T5 |
1037-1300 |
Sentence |
denotes |
We propose that (i) the IGF-IR and the IR share at least in part the same molecular mechanism underlying their interplay with their two substrates, p52Shc and IRS-1, and (ii) IRS-1 interacts with the IGF-IR in a fashion that is different from that used by p52Shc. |
| T6 |
1301-1417 |
Sentence |
denotes |
Finally, our data highlight the crucial role of the juxtamembrane domain in signaling by both the IR and the IGF-IR. |