| URN | urn:agi-ProtModification:inout-urn:agi-llid:3643:out-urn:agi-llid:3667::positive:phosphorylation |
|---|---|
| References | 64 |
| Connectivity | 2 |
| Effect | positive |
| Mechanism | phosphorylation |
| Original # of References | 64 |
| TextRef | info:pmid/9468537#abs:1 |
|---|---|
| PubYear | 1998 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 9468537:0 |
| Sentence | Insulin receptor substrate-1 (IRS-1) is phosphorylated on multiple tyrosine residues by ligand-activated insulin receptors. |
| TextRef | info:pmid/7588273#abs:1 |
|---|---|
| PubYear | 1995 |
| MedlineTA | Endocrinology |
| MedLine Reference | 7588273:0 |
| Sentence | The insulin receptor substrate-1 (IRS-1) is rapidly phosphorylated on several tyrosine residues by the activated insulin receptor. |
| TextRef | info:pmid/1385403#abs:8 |
|---|---|
| PubYear | 1992 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 1385403:7 |
| Sentence | Purified insulin receptors directly phosphorylated baculovirus-produced IRS-1 exclusively on tyrosine residues. |
| Organ | Ovary |
| Organism | Mesocricetus auratus |
| TextRef | info:pmid/17905199#abs:2 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Biochem Biophys Res Commun |
| MedLine Reference | 17905199:1 |
| Sentence | The activated insulin receptor phosphorylates insulin receptor substrate-1 (IRS1), which acts as a docking protein for downstream signal mediators. |
| CellType | Adipocytes |
| TextRef | info:pmid/9486163#abs:1 |
|---|---|
| PubYear | 1998 |
| MedlineTA | Am J Physiol |
| MedLine Reference | 9486163:0 |
| Sentence | After insulin binding, insulin receptors phosphorylate the insulin receptor substrate 1 (IRS-1) on specific motifs and thereby initiate insulin action. |
| TextMods | 41: '(IR) ' -> '' |
| TextRef | info:pmid/9346913#abs:6 |
|---|---|
| PubYear | 1997 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 9346913:5 |
| Sentence | Thus, tyrosine phosphorylation of IRS-1 by the insulin receptor specifically requires a Pleckstrin homology domain derived from IRS proteins. |
| TextMods | 88: 'PH ' -> 'Pleckstrin homology ' |
| TextRef | info:pmid/11018022#abs:2 |
|---|---|
| PubYear | 2000 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 11018022:1 |
| Sentence | The N terminus of IRS-1 contains a pleckstrin homology domain that is critical for recognition and subsequent phosphorylation of IRS-1 by the activated insulin receptor. |
| TextMods | 55: '(PH) ' -> '' |
| TextRef | info:pmid/8387037#abs:4 |
|---|---|
| PubYear | 1993 |
| MedlineTA | Diabetes |
| MedLine Reference | 8387037:3 |
| Sentence | We suspect that insulin signals are enabled when the activated insulin receptor kinase phosphorylates specific tyrosine residues in IRS-1. |
| CellType | Oocytes |
| Organ | Ovary |
| Organism | Mesocricetus auratus |
| TextRef | info:pmid/15522123#abs:11 |
|---|---|
| PubYear | 2004 |
| MedlineTA | BMC Biol |
| MedLine Reference | 15522123:10 |
| Sentence | These effects were confirmed using RNA interference against HDAC2, indicating that HDAC2 specifically prevents phosphorylation of IRS-1 by the insulin receptor. |
| Organ | Liver |
| TextRef | info:pmid/8297340#abs:9 |
|---|---|
| PubYear | 1994 |
| MedlineTA | Biochem J |
| MedLine Reference | 8297340:8 |
| Sentence | However, the addition of ATP, which allows phosphorylation of IRS-1 by the insulin receptor, also enhances the coupling of PtdIns 3-kinase to the insulin receptor. |
| TextRef | info:pmid/7651388#abs:1 |
|---|---|
| PubYear | 1995 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 7651388:0 |
| Sentence | Insulin signals are mediated through tyrosine phosphorylation of specific proteins such as insulin receptor substrate 1 (IRS-1) and Shc by the activated insulin receptor . |
| TextMods | 170: '(IR)' -> '' |
| TextRef | info:pmid/11287630#abs:1 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Proc Natl Acad Sci U S A |
| MedLine Reference | 11287630:0 |
| Sentence | Tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) by the insulin receptor permits this docking protein to interact with signaling proteins that promote insulin action. |
| TextRef | info:pmid/9210235#abs:2 |
|---|---|
| PubYear | 1997 |
| MedlineTA | Soc Gen Physiol Ser |
| MedLine Reference | 9210235:1 |
| Sentence | The active insulin receptor phosphorylates tyrosine residues of intracellular proteins such as the insulin receptor substrate-1 (IRS-1) which acts as docking sites for molecules containing Src homology 2 domains. |
| TextMods | 204: '(SH2) ' -> '' |
| TextRef | info:pmid/9609110#abs:2 |
|---|---|
| PubYear | 1998 |
| MedlineTA | Mol Cell Biochem |
| MedLine Reference | 9609110:1 |
| Sentence | The activated insulin receptor phosphorylates the intracellular substrate IRS-1, which then binds various signalling molecules that contain SRC homology 2 domains, thereby propagating the insulin signal. |
| TextRef | info:pmid/8282127#abs:1 |
|---|---|
| PubYear | 1993 |
| MedlineTA | Nippon Naibunpi Gakkai Zasshi |
| MedLine Reference | 8282127:0 |
| Sentence | Insulin binds to the alpha subunit of the insulin receptor which activates the tyrosine kinase in the beta subunit and tyrosine-phosphorylates the insulin receptor substrates-1 (IRS-1). |
| TextRef | info:pmid/7592659#abs:8 |
|---|---|
| PubYear | 1995 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 7592659:7 |
| Sentence | Taken together, these data indicate that insulin receptors phosphorylate IRS-1 at the cell surface, perhaps in coated pits which are included in the low density microsome fraction. |
| CellType | Adipocytes |
| TextRef | info:pmid/7543044#abs:1 |
|---|---|
| PubYear | 1995 |
| MedlineTA | Endocrinology |
| MedLine Reference | 7543044:0 |
| Sentence | The insulin receptor phosphorylates insulin receptor substrate-1 (IRS-1) and Shc on tyrosine residues, both of which associate with the protein-abundant Src homology/growth factor receptor-bound protein 2 leading to p21ras activation. |
| TextMods | 204: '(ASH/GRB2) ' -> ' ' |
| TextRef | info:pmid/8119950#abs:6 |
|---|---|
| PubYear | 1994 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 8119950:5 |
| Sentence | Taken together these data suggest that serine/threonine phosphorylation of IRS 1 induced by okadaic acid reduces the ability of the insulin receptor to phosphorylate IRS 1 and to dock one of its interacting molecules, i.e. |
| CellType | Adipocytes |
| TextRef | info:pmid/9271396#abs:1 |
|---|---|
| PubYear | 1997 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 9271396:0 |
| Sentence | The ability of insulin to stimulate protein synthesis and cellular growth is mediated through the insulin receptor , which phosphorylates Tyr residues in the insulin receptor substrate-signaling proteins (IRS-1 and IRS-2), Gab-1, and Shc. |
| TextMods | 115: '(IR)' -> '' |
| TextRef | info:pmid/9492017#body:59 |
|---|---|
| PubYear | 1998 |
| MedlineTA | Endocrinology |
| MedLine Reference | 9492017:1058 |
| Sentence | We also have compared the tryptic maps of IRS-1 phosphorylated by the insulin receptor vs. |
| TextRef | info:pmid/9128728#title:1 |
|---|---|
| PubYear | 1997 |
| MedLine Reference | 9128728:100 |
| Sentence | In vitro binding and phosphorylation of insulin receptor substrate 1 by the insulin receptor. |
| TextRef | info:pmid/9374521#body:200 |
|---|---|
| PubYear | 1997 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 9374521:1199 |
| Sentence | Therefore, we consider that Trks as well as the insulin receptor directly phosphorylate IRS-1 and -2. |
| TextRef | info:pmid/11916925#body:192 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Diabetes |
| MedLine Reference | 11916925:1191 |
| Sentence | IRS-1 and IRS-2 are phosphorylated on tyrosine residues by the insulin receptor after insulin stimulation. |
| TextRef | info:pmid/16269459#body:62 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Endocrinology |
| MedLine Reference | 16269459:1061 |
| Sentence | The activated insulin receptor phosphorylates insulin receptor substrate-1 (IRS-1) at tyrosine residues (11, 12, 13). |
| CellType | Adipocytes |
| TextRef | info:pmid/11739394#body:36 |
|---|---|
| PubYear | 2002 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 11739394:1035 |
| Sentence | The pleckstrin homology domain is required for efficient phosphorylation of IRS-1 by the insulin receptor (13-15). |
| TextMods | 4: 'PH ' -> 'pleckstrin homology ' |
| Tissue | Muscle, Smooth, Vascular |
| TextRef | info:pmid/19542202#body:279 |
|---|---|
| PubYear | 2009 |
| MedlineTA | Diabetes |
| MedLine Reference | 19542202:1278 |
| Sentence | We showed that bacteria-derived SH2B1 markedly increased the ability of purified insulin receptor to tyrosyl phosphorylate IRS-1 in vitro. |
| TextRef | info:pmid/11875115#body:189 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 11875115:1188 |
| Sentence | It is suggested that upon insulin stimulation, only a small portion of IRS-1 is phosphorylated on tyrosine residues by the insulin receptor. |
| TextRef | info:pmid/16492903#body:450 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Endocr Rev |
| MedLine Reference | 16492903:1449 |
| Sentence | The insulin receptor then phosphorylates tyrosine residues on the insulin receptor substrates (IRS-1-IRS-4). |
| Tissue | Muscle, Smooth, Vascular |
| CellType | Endothelial Cells |
| TextRef | info:pmid/10077007#body:147 |
|---|---|
| PubYear | 1999 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 10077007:1146 |
| Sentence | It is likely that mIRS-3-F4 exerts its inhibitory action by competing with the ability of the insulin receptor to phosphorylate endogenous IRS-1, -2, and -3. |
| TextRef | info:pmid/17560336#body:264 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Cancer Cell |
| MedLine Reference | 17560336:1263 |
| Sentence | Activated insulin receptor phosphorylates insulin receptor substrate-1 at tyrosine residues inducing downstream activation of PI3K. |
| TextMods | 42: 'IRS' -> 'insulin receptor substrate' |
| CellType | Lymphocytes, Null |
| TextRef | info:pmid/11375341#body:158 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Diabetes |
| MedLine Reference | 11375341:1157 |
| Sentence | The activated insulin receptor phosphorylates the insulin receptor substrates, IRS-1 and IRS-2, on multiple tyrosines. |
| Tissue | Serum |
| Organ | Abdomen |
| TextRef | info:pmid/8530404#body:113 |
|---|---|
| PubYear | 1995 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 8530404:1112 |
| Sentence | In addition, the insulin receptor phosphorylates IRS-1, a docking protein with multiple Tyr-Xaa-Xaa-Met motifs that also provide binding sites for the SH2 domains of p85(14). |
| TextRef | info:pmid/17332155#body:201 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Am J Physiol Regul Integr Comp Physiol |
| MedLine Reference | 17332155:1200 |
| Sentence | Upon activation, the insulin receptor catalyzes the tyrosine phosphorylation of several intracellular substrates, including the IRS1 and IRS2. |
| Organ | Soleus muscle |
| TextRef | info:pmid/9275179#body:113 |
|---|---|
| PubYear | 1997 |
| MedlineTA | Proc Natl Acad Sci U S A |
| MedLine Reference | 9275179:1112 |
| Sentence | To detect insulin receptor-catalyzed tyrosine phosphorylation of the substrate IRS-1, immunoblot analysis was performed using monoclonal antibodies to phosphotyrosine. |
| TextMods | 10: 'IR' -> 'insulin receptor' |
| TextRef | info:pmid/11245597#body:176 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Am J Physiol Cell Physiol |
| MedLine Reference | 11245597:1175 |
| Sentence | Both the IGF-I receptor and insulin receptor undergo autophosphorylation in response to ligand binding and subsequently phosphorylate tyrosine residues on a common substrate, IRS-1. |
| TextRef | info:pmid/12907755#body:240 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 12907755:1239 |
| Sentence | Similarly, the insulin receptor and insulin receptor substrate-1 are both phosphorylated by the insulin receptor kinase at similar sites, both of which are good substrates for PTP1B. |
| TextRef | info:pmid/10614641#body:331 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Endocrinology |
| MedLine Reference | 10614641:1330 |
| Sentence | Thus, reduced temperature did not further inhibit the ability of the activated insulin receptor kinase to phosphorylate IRS-1 in Rab4DeltaCT-infected cells, but did inhibit this process in control infected cells. |
| TextRef | info:pmid/15372106#body:108 |
|---|---|
| PubYear | 2004 |
| MedlineTA | J Clin Invest |
| MedLine Reference | 15372106:1107 |
| Sentence | This may in turn interfere with IRS-1 tyrosine phosphorylation by the insulin receptor, as occurs upon treatment with TNF-α and okadaic acid, leading to decreased activation of PI3K (24, 25). |
| TextRef | info:pmid/11544268#body:71 |
|---|---|
| PubYear | 2001 |
| MedlineTA | J Clin Invest |
| MedLine Reference | 11544268:1070 |
| Sentence | Whereas purified insulin receptor phosphorylates IRS-1 exclusively on tyrosine residues, treatment of the intact cell with hormone leads to extensive phosphorylation on serine and threonine. |
| TextRef | info:pmid/12799319#body:347 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Am J Physiol Endocrinol Metab |
| MedLine Reference | 12799319:1346 |
| Sentence | Insulin rapidly induces Insulin receptorbeta phosphorylation in explant retinas, and the Insulin receptor preferentially phosphorylates IRS-2 to a greater extent than IRS-1. |
| TextMods | 24: 'IR' -> 'Insulin receptor' 89: 'IR ' -> 'Insulin receptor ' |
| Organ | Retina |
| TextRef | info:pmid/18567823#body:230 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Diabetes |
| MedLine Reference | 18567823:1229 |
| Sentence | The activated c-Jun NH2-terminal kinase phosphorylates serine residues of IRS-1/2 and consequently prevents tyrosine phosphorylation of IRS-1/2 by insulin receptor (16). |
| TextMods | 14: 'c-JNK ' -> 'c-Jun NH2-terminal kinase ' |
| CellType | Hepatocytes |
| TextRef | info:pmid/10517679#body:211 |
|---|---|
| PubYear | 1999 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 10517679:1210 |
| Sentence | This apparent delayed effect of IRS-1 on insulin receptor phosphorylation suggests that IRS-1 first needs to be phosphorylated by the insulin receptor before affecting insulin receptor phosphorylation. |
| TextRef | info:pmid/9408743#body:257 |
|---|---|
| PubYear | 1997 |
| MedlineTA | Endocr Rev |
| MedLine Reference | 9408743:1256 |
| Sentence | The tyrosine-phosphorylated insulin receptor phosphorylates intracellular substrates, such as insulin receptor substrate -1 and IRS-2, initiating signal transduction and the plieotropic actions of insulin. |
| TextMods | 121: '(IRS)' -> '' |
| TextRef | info:pmid/15314154#body:35 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 15314154:1034 |
| Sentence | Upon activation, Insulin receptor tyrosyl phosphorylates and activates multiple signaling molecules, including Insulin receptor substrate 1 (IRS1), IRS2, IRS3, IRS4, Shc, APS, and SH2-B (4, 27, 30, 40, 41, 43). |
| TextMods | 17: 'IR ' -> 'Insulin receptor ' 111: 'IR ' -> 'Insulin receptor ' |
| TextRef | info:pmid/16567515#body:247 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Diabetes |
| MedLine Reference | 16567515:1246 |
| Sentence | Even though the insulin receptor and JAK2 phosphorylate IRS-1 on distinct tyrosine residues (15), it appears that IRS1/2 phosphorylation by JAK2 is not necessary for insulin-induced responses. |
| CellType | Muscle Fibers, Skeletal |
| TextRef | info:pmid/15994203#body:59 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 15994203:1058 |
| Sentence | The insulin receptor, on the other hand, is a receptor tyrosine kinase, which activates its signaling cascade by phosphorylating various intracellular substrates, including IRS-1, IRS-2, Shc, and Gαq/11. |
| CellType | Adipocytes |
| TextRef | info:pmid/15302844#body:163 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Hypertension |
| MedLine Reference | 15302844:1162 |
| Sentence | These findings suggest that phosphorylation at serine 307 may be capable of inhibiting not only tyrosine phosphorylation of IRS-1 by insulin receptor but also tyrosine kinase activity of insulin receptor. |
| TextMods | 133: 'IR ' -> 'insulin receptor ' 187: 'IR' -> 'insulin receptor' |
| Organ | Aorta |
| TextRef | info:pmid/10449437#body:78 |
|---|---|
| PubYear | 1999 |
| MedlineTA | J Clin Invest |
| MedLine Reference | 10449437:1077 |
| Sentence | Once bound and phosphorylated, insulin receptor will phosphorylate IRS-1, IRS-2, and Shc and activate phosphatidylinositol 3-kinase and Raf-mitogen-activated protein kinase pathways (1, 30). |
| TextMods | 31: 'IR ' -> 'insulin receptor ' 102: 'PI 3-kinase ' -> 'phosphatidylinositol 3-kinase ' 140: 'MAP ' -> 'mitogen-activated protein ' |
| Tissue | Muscle, Smooth, Vascular |
| CellType | Endothelial Cells |
| TextRef | info:pmid/10809663#body:144 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Genes Dev |
| MedLine Reference | 10809663:1143 |
| Sentence | Phosphorylation of IRS-1 by the insulin receptor creates multiple binding sites for phosphatidylinositol 3′-kinase, whereas Shc and FRS2 primarily engage Grb2, and thus are principally involved in activating the MAP kinase pathway. |
| TextMods | 84: 'PI3K' -> 'phosphatidylinositol 3′-kinase' 214: 'MAPK ' -> 'MAP kinase ' |
| TextRef | info:pmid/11248703#body:239 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Eur J Biochem |
| MedLine Reference | 11248703:1238 |
| Sentence | The activated insulin receptor kinase phosphorylates IRS-1 and Shc, which both associate with the adaptor proteins Grb-2-SOS, leading to p21ras, raf, MEK and mitogen-activated protein kinase activation. |
| TextMods | 14: 'IRK ' -> 'insulin receptor kinase ' 158: 'MAPK ' -> 'mitogen-activated protein kinase ' |
| CellType | Adipocytes |
| Organ | Liver |
| Organism | Rattus norvegicus |
| TextRef | info:pmid/11147799#body:46 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Diabetes |
| MedLine Reference | 11147799:1045 |
| Sentence | Subsequently, the activated insulin receptor phosphorylates a number of protein substrates on tyrosine such as insulin receptor substrate -1/IRS-2 and Shc (4,5) which can then interact with multiple targets to mediate the pleiotropic actions of insulin (6,7,8). |
| TextMods | 28: 'IR ' -> 'insulin receptor ' 94: 'tyr ' -> 'tyrosine ' 138: '(IRS)' -> '' |
| TextRef | info:pmid/20332342#body:247 |
|---|---|
| PubYear | 2010 |
| MedlineTA | Diabetes |
| MedLine Reference | 20332342:1246 |
| Sentence | All of these kinases can phosphorylate IRS1 on critical serine residues, thereby blocking phosphorylation of IRS1 by insulin receptor kinase on tyrosine sites that are required for phosphatidylinositol-3-kinase association and activation (40). |
| TextMods | 117: 'IR ' -> 'insulin receptor ' 181: 'PI3K ' -> 'phosphatidylinositol-3-kinase ' |
| Tissue | Skeletal muscle |
| TextRef | info:pmid/9813005#body:54 |
|---|---|
| PubYear | 1998 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 9813005:1053 |
| Sentence | The Pleckstrin homology domain in the IRS proteins may have a common function that mediates receptor coupling, because chimeric IRS-1 proteins bearing the Pleckstrin homology domains from IRS-2 or Gab-1 are phosphorylated normally by the insulin receptor (24). |
| TextMods | 4: 'PH ' -> 'Pleckstrin homology ' 155: 'PH ' -> 'Pleckstrin homology ' |
| TextRef | info:pmid/18252807#body:59 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Mol Pharmacol |
| MedLine Reference | 18252807:1058 |
| Sentence | Ligand-activated insulin receptor and tyrosine-phosphorylated IRS1 relay signal transmission to the phosphoinositide 3-kinase-Akt pathway, and activation of this pathway then enhances mammalian target of rapamycin (mTOR)-p70S6 kinase (S6K) 1 activity. |
| TextMods | 17: 'IR ' -> 'insulin receptor ' |
| TextRef | info:pmid/11316748#body:130 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Endocrinology |
| MedLine Reference | 11316748:1129 |
| Sentence | While a direct interaction between the pleckstrin homology domain of the insulin receptor substrate molecules and the insulin or IGF-I receptors has not been demonstrated, its presence is essential for efficient tyrosine phosphorylation of IRS-1 by the insulin receptor. |
| TextMods | 39: 'PH ' -> 'pleckstrin homology ' 73: 'IRS ' -> 'insulin receptor substrate ' |
| TextRef | info:pmid/17652184#body:157 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 17652184:1156 |
| Sentence | E, Densitometry data were obtained using Genetools software and expressed as the bar graph of phosphorylated-Akt (473), phosphorylated-insulin receptor (Tyr 1162/1163), Tyr-phosphorylated-IRS-1, and IRS-1-associated p85 in insulin-stimulated and adenovirus comprising enhanced green fluorescent protein- or Ad-miR-29-infected cells. |
| TextMods | 135: 'IR ' -> 'insulin receptor ' 246: 'Ad-eGFP' -> 'adenovirus comprising enhanced green fluorescent protein' |
| CellType | Adipocytes |
| TextRef | info:pmid/10098842#body:188 |
|---|---|
| PubYear | 1999 |
| MedlineTA | J Neurochem |
| MedLine Reference | 10098842:1187 |
| Sentence | The in vitro kinase assay using intracellular kinase domain-TrkB and GST-BIT indicated that BIT-TAM can be a good substrate for Trk receptor kinase, and sequences around the tyrosine phosphorylation sites of BIT-TAM are similar to those of insulin receptor substrate-1, which is known to be phosphorylated by the insulin receptor. |
| TextMods | 32: 'ICD' -> 'intracellular kinase domain' |
| Organ | Cerebral cortex |
| TextRef | info:pmid/15590636#body:117 |
|---|---|
| PubYear | 2005 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 15590636:1116 |
| Sentence | RESULTS TOP ABSTRACT INTRODUCTION EXPERIMENTAL PROCEDURES RESULTS DISCUSSION REFERENCES In Vitro Phosphorylation of the IRS-1-(925-1008) Fragment Is Reduced by the G972R Polymorphism-In vivo association of IRS-1 via the PTB domain (Fig. 1) with Tyr960 of the insulin receptor is normally required for optimal phosphorylation of IRS-1 by the insulin receptor (20, 21). |
| TextRef | info:pmid/11313945#body:119 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Oncogene |
| MedLine Reference | 11313945:1118 |
| Sentence | Indeed, in the insulin signaling system, it has been shown that the inhibition of tyrosine phosphorylation of the docking protein IRS1 by insulin receptor in response to okadaic acid is due to the disruption of the IRS-1/insulin receptor complex by the binding of 14-3-3 to serine phosphorylated IRS-1 (Ogihara et al., 1997). |
| TextRef | info:pmid/9415395#body:231 |
|---|---|
| PubYear | 1997 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 9415395:1230 |
| Sentence | The activated insulin receptor kinase tyrosine phosphorylates IRS-1 (35, 36) and, in certain cell lines Shc (27, 36), each of which associates with Grb-2-Sos leading to the exchange of GDP for GTP on p21ras, resulting in p21ras activation and the sequential activation, by serine/threonine phosphorylation, of Raf and MEK. |
| TextMods | 14: 'IRK ' -> 'insulin receptor kinase ' |
| TextRef | info:pmid/11163213#body:74 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Mol Cell |
| MedLine Reference | 11163213:1073 |
| Sentence | insulin receptor kinase-catalyzed phosphorylation of proteins, such as IRS-1 and IRS-2, creates high-affinity binding sites for proteins that contain Src homology 2 domains, such as phosphatidylinositol 3-kinase , resulting in the assembly of the multiprotein signaling complexes that mediate the effects of insulin on cellular metabolism, growth, and glucose homeostasis (reviewed by Patti and Kahn 1998). |
| TextMods | 0: 'IRK' -> 'insulin receptor kinase' 165: '(SH2) ' -> '' 212: '(PI3-K)' -> '' |
| TextRef | info:pmid/16020478#body:58 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Endocrinology |
| MedLine Reference | 16020478:1057 |
| Sentence | The insulin receptor in turn phosphorylates IRS-1 on tyrosine residues that serve as recognition sites for proteins with Src homology 2 (Src homology domain 2) domains, such as the regulatory subunits of phosphatidylinositol -3-kinase, Grb2/Sos, and SH protein tyrosine phosphatase-2 (SHP-2), a protein tyrosine phosphatase that dampens insulin-stimulated tyrosine phosphorylation of IRS-1 (2). |
| TextMods | 137: 'SH2' -> 'Src homology domain 2' 225: '(PI)' -> '' |
| TextRef | info:pmid/15504931#body:241 |
|---|---|
| PubYear | 2004 |
| MedlineTA | J Am Soc Nephrol |
| MedLine Reference | 15504931:1240 |
| Sentence | As in the hepatocyte, increase in intramyocellular FA in skeletal muscle has been shown to impair insulin receptor signaling by PKC-dependent serine phosphorylation of IRS-1; this leads to reduced IRS-1 availability for tyrosine phosphorylation, reducing Glut 4 translocation to the myocyte plasma membrane with consequent reduction in glucose uptake (6). |
| Tissue | Skeletal muscle |
| CellType | Hepatocytes |
| TextRef | info:pmid/15182363#body:199 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Eur J Biochem |
| MedLine Reference | 15182363:1198 |
| Sentence | Localization of IRS1 in the plasma membrane and caveolae of human adipocytes As IRS1 phosphorylation by the insulin receptor was not dependent on plasma membrane cholesterol/caveolae integrity, as has been found to be the case in rat adipocytes [22], we examined if IRS1 was localized in the plasma membrane and caveolae in human adipocytes. |
| CellType | Adipocytes |
| Organism | Homo sapiens |