PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11406592-0 2001 The distal region and receptor tyrosines of the Epo receptor are non-essential for in vivo erythropoiesis. Tyrosine 31-40 erythropoietin Mus musculus 48-51 11443118-1 2001 The erythropoietin (Epo) receptor transduces its signals by activating physically associated tyrosine kinases, mainly Jak2 and Lyn, and thereby inducing tyrosine phosphorylation of various substrates including the Epo receptor (EpoR) itself. Tyrosine 93-101 erythropoietin Mus musculus 4-18 11443118-1 2001 The erythropoietin (Epo) receptor transduces its signals by activating physically associated tyrosine kinases, mainly Jak2 and Lyn, and thereby inducing tyrosine phosphorylation of various substrates including the Epo receptor (EpoR) itself. Tyrosine 93-101 erythropoietin Mus musculus 20-23 11443118-2 2001 We previously demonstrated that, in Epo-stimulated cells, an adapter protein, CrkL, becomes tyrosine-phosphorylated, physically associates with Shc, SHP-2, and Cbl, and plays a role in activation of the Ras/Erk signaling pathway. Tyrosine 92-100 erythropoietin Mus musculus 36-39 11443118-8 2001 Together, the present study suggests that, upon Epo stimulation, CrkL is recruited to the EpoR through interaction between the CrkL SH2 domain and phosphorylated Tyr(460) in the EpoR cytoplasmic domain and undergoes tyrosine phosphorylation by receptor-associated Lyn to activate the downstream signaling pathway leading to the activation of Erk and Elk-1. Tyrosine 162-165 erythropoietin Mus musculus 48-51 11443118-8 2001 Together, the present study suggests that, upon Epo stimulation, CrkL is recruited to the EpoR through interaction between the CrkL SH2 domain and phosphorylated Tyr(460) in the EpoR cytoplasmic domain and undergoes tyrosine phosphorylation by receptor-associated Lyn to activate the downstream signaling pathway leading to the activation of Erk and Elk-1. Tyrosine 216-224 erythropoietin Mus musculus 48-51 10960479-6 2000 In T-ER transformants expressing JAK2 (T-JER), EPO induced tyrosine phosphorylation of the EPOR, JAK2, and STAT5, and consequently STAT5-responsive genes including bcl-X and cis1 were normally induced. Tyrosine 59-67 erythropoietin Mus musculus 47-50 10995753-5 2000 We also observed that Epo stimulation activates Jak2/Stat5 signal transduction and increases cytoplasmic calcium, which is dependent on tyrosine phosphorylation. Tyrosine 136-144 erythropoietin Mus musculus 22-25 9488432-4 1998 While the Janus protein tyrosine kinase JAK2 and the transcription factor STAT5 became tyrosine phosphorylated with the EPO stimulation in EPO-responsive erythroblastoid cells from anemic mice, JAK1 and STAT5 were constitutively tyrosine phosphorylated in all of these FVp gp55-induced erythroblastoid or erythroleukemic cells. Tyrosine 24-32 erythropoietin Mus musculus 120-123 10979952-2 2000 Treatment of the EPO-dependent HCD57 murine cell line with 70 micromol/L orthovanadate, a tyrosine phosphatase inhibitor, resulted in both increased tyrosine protein phosphorylation and prevention of apoptosis in the absence of EPO without promoting proliferation. Tyrosine 90-98 erythropoietin Mus musculus 17-20 10880228-1 2000 Recent studies of erythropoietin (Epo) receptor signalling suggest that signals for mitogenesis, survival and differentiation are relayed efficiently by receptor forms lacking at least seven of eight cytoplasmic (phospho)tyrosine [(P)Y] sites for effector recruitment. Tyrosine 221-229 erythropoietin Mus musculus 34-37 9657741-4 1998 In fact, long-term proliferation studies performed in the absence of serum show that even at saturating concentrations of Epo, Ba/F3 cells expressing these truncated receptors die via apoptosis, while cells bearing WT EpoRs do not, and this programmed cell death correlates with an inability of Epo-stimulated Ba/F3 cells expressing truncated EpoRs to induce the tyrosine phosphorylation of MAPK and the activation of p70(S6K). Tyrosine 363-371 erythropoietin Mus musculus 122-125 10567359-2 1999 We showed that erythropoietin induced rapid glycosylphosphatidylinositol (GPI) hydrolysis and tyrosine phosphorylation of phospholipase C (PLC)-gamma(2) in FDC-P1 cells transfected with the wild-type erythropoietin-receptor. Tyrosine 94-102 erythropoietin Mus musculus 15-29 10567359-3 1999 Erythropoietin-induced tyrosine phosphorylation of PLC-gamma(2) was time- and dose-dependent. Tyrosine 23-31 erythropoietin Mus musculus 0-14 10567359-4 1999 By using FDC-P1 cells transfected with an erythropoietin receptor devoid of tyrosine residues, we showed that both effects required the tyrosine residues of intracellular domain on the erythropoietin receptor. Tyrosine 76-84 erythropoietin Mus musculus 42-56 10567359-4 1999 By using FDC-P1 cells transfected with an erythropoietin receptor devoid of tyrosine residues, we showed that both effects required the tyrosine residues of intracellular domain on the erythropoietin receptor. Tyrosine 136-144 erythropoietin Mus musculus 42-56 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 85-93 erythropoietin Mus musculus 50-64 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 85-93 erythropoietin Mus musculus 168-182 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 116-125 erythropoietin Mus musculus 50-64 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 116-125 erythropoietin Mus musculus 168-182 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 116-124 erythropoietin Mus musculus 50-64 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 116-124 erythropoietin Mus musculus 168-182 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 260-269 erythropoietin Mus musculus 50-64 10567359-6 1999 Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-gamma(2), whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Tyrosine 260-269 erythropoietin Mus musculus 168-182 10567359-7 1999 Thus, our results suggest that erythropoietin regulates GPI hydrolysis via tyrosine phosphorylation of its receptor and PLC-gamma(2) activation. Tyrosine 75-83 erythropoietin Mus musculus 31-45 9488432-4 1998 While the Janus protein tyrosine kinase JAK2 and the transcription factor STAT5 became tyrosine phosphorylated with the EPO stimulation in EPO-responsive erythroblastoid cells from anemic mice, JAK1 and STAT5 were constitutively tyrosine phosphorylated in all of these FVp gp55-induced erythroblastoid or erythroleukemic cells. Tyrosine 24-32 erythropoietin Mus musculus 139-142 9488432-4 1998 While the Janus protein tyrosine kinase JAK2 and the transcription factor STAT5 became tyrosine phosphorylated with the EPO stimulation in EPO-responsive erythroblastoid cells from anemic mice, JAK1 and STAT5 were constitutively tyrosine phosphorylated in all of these FVp gp55-induced erythroblastoid or erythroleukemic cells. Tyrosine 87-95 erythropoietin Mus musculus 120-123 9488432-4 1998 While the Janus protein tyrosine kinase JAK2 and the transcription factor STAT5 became tyrosine phosphorylated with the EPO stimulation in EPO-responsive erythroblastoid cells from anemic mice, JAK1 and STAT5 were constitutively tyrosine phosphorylated in all of these FVp gp55-induced erythroblastoid or erythroleukemic cells. Tyrosine 87-95 erythropoietin Mus musculus 139-142 9344843-0 1997 Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells. Tyrosine 31-39 erythropoietin Mus musculus 0-14 9524923-2 1997 Although the membrane-bound receptor for EPO has no intrinsic kinase activity, it triggers the activation of protein kinases via phospholipases A2, C, and D. A cascade of serine and threonine kinases, including Raf-1, MAP kinase and protein kinase C (PKC) is activated following tyrosine phosphorylation. Tyrosine 279-287 erythropoietin Mus musculus 41-44 9419812-3 1997 It mediates tyrosine phosphorylation through its association with nonreceptor tyrosine kinases such as JAK2 and initiates a cascade of signalling events in response to erythropoietin. Tyrosine 12-20 erythropoietin Mus musculus 168-182 9344843-1 1997 The present study demonstrates that erythropoietin (Epo) and IL-3 induce tyrosine phosphorylation of the SH2/SH3-containing adapter protein CrkL and its transient association with tyrosine-phosphorylated SHP-2, Shc, and Cbl in a murine IL-3-dependent cell line, 32D, expressing the Epo receptor (EpoR). Tyrosine 73-81 erythropoietin Mus musculus 36-50 9344843-1 1997 The present study demonstrates that erythropoietin (Epo) and IL-3 induce tyrosine phosphorylation of the SH2/SH3-containing adapter protein CrkL and its transient association with tyrosine-phosphorylated SHP-2, Shc, and Cbl in a murine IL-3-dependent cell line, 32D, expressing the Epo receptor (EpoR). Tyrosine 73-81 erythropoietin Mus musculus 52-55 9344843-1 1997 The present study demonstrates that erythropoietin (Epo) and IL-3 induce tyrosine phosphorylation of the SH2/SH3-containing adapter protein CrkL and its transient association with tyrosine-phosphorylated SHP-2, Shc, and Cbl in a murine IL-3-dependent cell line, 32D, expressing the Epo receptor (EpoR). Tyrosine 180-188 erythropoietin Mus musculus 36-50 9344843-1 1997 The present study demonstrates that erythropoietin (Epo) and IL-3 induce tyrosine phosphorylation of the SH2/SH3-containing adapter protein CrkL and its transient association with tyrosine-phosphorylated SHP-2, Shc, and Cbl in a murine IL-3-dependent cell line, 32D, expressing the Epo receptor (EpoR). Tyrosine 180-188 erythropoietin Mus musculus 52-55 9344843-3 1997 Studies using cells expressing mutant EpoRs showed that the Epo-induced tyrosine phosphorylation of CrkL is dependent on the membrane-proximal EpoR cytoplasmic region involved in the activation of Jak2 as well as the C-terminal 145 amino acid region which is required for tyrosine phosphorylation of SHP-2 and Shc. Tyrosine 72-80 erythropoietin Mus musculus 38-41 9359406-5 1997 PV-mediated Tyr phosphorylation of EPO-R occurred at several intracellular sites including the endoplasmic reticulum (ER), because both endoglycosidase H (endo H)-resistant EPO-R and the ER-retained EPO-R mutant (DeltaWS1 EPO-R) were Tyr phosphorylated in response to PV. Tyrosine 12-15 erythropoietin Mus musculus 35-38 9359406-5 1997 PV-mediated Tyr phosphorylation of EPO-R occurred at several intracellular sites including the endoplasmic reticulum (ER), because both endoglycosidase H (endo H)-resistant EPO-R and the ER-retained EPO-R mutant (DeltaWS1 EPO-R) were Tyr phosphorylated in response to PV. Tyrosine 12-15 erythropoietin Mus musculus 173-176 9359406-5 1997 PV-mediated Tyr phosphorylation of EPO-R occurred at several intracellular sites including the endoplasmic reticulum (ER), because both endoglycosidase H (endo H)-resistant EPO-R and the ER-retained EPO-R mutant (DeltaWS1 EPO-R) were Tyr phosphorylated in response to PV. Tyrosine 234-237 erythropoietin Mus musculus 35-38 9130706-3 1997 We have shown previously that intracellular signalling is disrupted in the J2E-NR cell line and that tyrosine phosphorylation is dramatically reduced after erythropoietin stimulation. Tyrosine 101-109 erythropoietin Mus musculus 156-170 9192755-0 1997 Erythropoietin induces tyrosine phosphorylation of the interleukin-3 receptor beta subunit (betaIL3) and recruitment of Stat5 to possible Stat5-docking sites in betaIL3. Tyrosine 23-31 erythropoietin Mus musculus 0-14 9192755-3 1997 In the present study, we demonstrate that Epo stimulation induces unidirectional cross-phosphorylation of the IL-3 receptor beta subunit (betaIL3) on tyrosines and its rapid and transient association with Stat5 in murine IL-3-dependent cell lines engineered to express the Epo receptor (EpoR). Tyrosine 150-159 erythropoietin Mus musculus 42-45 9192755-4 1997 Using cell lines expressing various EpoR mutants, it was demonstrated that the Epo-induced tyrosine phosphorylation of betaIL3 is dependent on the membrane-proximal EpoR cytoplasmic region involved in the activation of Jak2, but not on the extracellular and transmembrane regions or on the carboxy-terminal 145 amino acid region containing all the intracellular tyrosine residues. Tyrosine 91-99 erythropoietin Mus musculus 36-39 9168989-3 1997 Here, we describe the roles of Stat5 and of these tyrosine residues in the EPOR in the erythroid differentiation of murine hematopoietic cell line SKT6 which produces hemoglobin in response to EPO. Tyrosine 50-58 erythropoietin Mus musculus 75-78 9129019-0 1997 Erythropoietin and interleukin-3 activate tyrosine phosphorylation of CBL and association with CRK adaptor proteins. Tyrosine 42-50 erythropoietin Mus musculus 0-14 9129019-4 1997 Erythropoietin (EPO) and interleukin-3 induced a dose and time-dependent tyrosine phosphorylation of Cbl in both EPO-dependent Ba/F3 and DA-3 transfectants, and the erythroid cell line HCD-57. Tyrosine 73-81 erythropoietin Mus musculus 0-14 9129019-4 1997 Erythropoietin (EPO) and interleukin-3 induced a dose and time-dependent tyrosine phosphorylation of Cbl in both EPO-dependent Ba/F3 and DA-3 transfectants, and the erythroid cell line HCD-57. Tyrosine 73-81 erythropoietin Mus musculus 16-19 9129019-4 1997 Erythropoietin (EPO) and interleukin-3 induced a dose and time-dependent tyrosine phosphorylation of Cbl in both EPO-dependent Ba/F3 and DA-3 transfectants, and the erythroid cell line HCD-57. Tyrosine 73-81 erythropoietin Mus musculus 113-116 9209412-0 1997 The role of erythropoietin receptor tyrosine phosphorylation in erythropoietin-induced proliferation. Tyrosine 36-44 erythropoietin Mus musculus 12-26 9209412-0 1997 The role of erythropoietin receptor tyrosine phosphorylation in erythropoietin-induced proliferation. Tyrosine 36-44 erythropoietin Mus musculus 64-78 9209412-1 1997 Although studies with truncated erythropoietin receptors (EpoRs) have suggested the tyrosine phosphorylation (Yphos) of the EpoR may not play a significant role in Epo-induced proliferation, we found, using a full length EpoR mutant designed Null, in which all 8 of the intracellular tyrosines (Ys) were substituted with phenylalanines (Fs), that Null cells required 5-10 fold more Epo than wild type (WT) EpoR containing cells in order to proliferate as well. Tyrosine 84-92 erythropoietin Mus musculus 124-127 9096338-2 1997 Tyrosine phosphorylation of the EPO-R creates "docking sites" for SH2 domain(s) in signaling molecules such as the protein tyrosine phosphatases SH-PTP1 and SH-PTP2, phosphoinositide 3-kinase (PI3 kinase), and STAT5. Tyrosine 0-8 erythropoietin Mus musculus 32-35 8977232-0 1996 Physical and functional interactions between Stat5 and the tyrosine-phosphorylated receptors for erythropoietin and interleukin-3. Tyrosine 59-67 erythropoietin Mus musculus 97-111 8977232-1 1996 Erythropoietin (Epo) and interleukin-3 (IL-3) stimulate activation of the Jak2 tyrosine kinase and induce tyrosine phosphorylation and activation of Stat5. Tyrosine 79-87 erythropoietin Mus musculus 0-14 8977232-1 1996 Erythropoietin (Epo) and interleukin-3 (IL-3) stimulate activation of the Jak2 tyrosine kinase and induce tyrosine phosphorylation and activation of Stat5. Tyrosine 79-87 erythropoietin Mus musculus 16-19 8977232-2 1996 In the present study, we have shown that Epo or IL-3 stimulation induces binding of Stat5 to the tyrosine-phosphorylated Epo receptor (EpoR) or IL-3 receptor beta subunit (betaIL3), respectively, in IL-3-dependent 32D cells expressing the EpoR. Tyrosine 97-105 erythropoietin Mus musculus 41-44 8977232-2 1996 In the present study, we have shown that Epo or IL-3 stimulation induces binding of Stat5 to the tyrosine-phosphorylated Epo receptor (EpoR) or IL-3 receptor beta subunit (betaIL3), respectively, in IL-3-dependent 32D cells expressing the EpoR. Tyrosine 97-105 erythropoietin Mus musculus 121-124 8943308-8 1996 These data suggest that phosphorylation of either serine or tyrosine residues of the EPOR can enhance the association of the receptor with JAK2, possibly increasing the sensitivity to EPO. Tyrosine 60-68 erythropoietin Mus musculus 85-88 8639815-0 1996 Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis. Tyrosine 0-8 erythropoietin Mus musculus 34-48 8943354-9 1996 Interestingly, association of the SH2n domain of SHP-1 with the tyrosine phosphorylated erythropoietin receptor modestly potentiated but was not essential for SHP-1-mediated dephosphorylation of Jak2 and had no effect on c-fes phosphorylation. Tyrosine 64-72 erythropoietin Mus musculus 88-102 8695792-7 1996 Furthermore, the functional hybrid receptors showed Epo-dependent (nE beta) or constitutive (cE alpha and cE beta) tyrosine phosphorylation of the cytoplasmic kinases JAK1 and JAK2. Tyrosine 115-123 erythropoietin Mus musculus 52-55 8639815-0 1996 Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis. Tyrosine 113-121 erythropoietin Mus musculus 34-48 8639815-1 1996 Erythropoietin (Epo), the primary in vivo stimulator of erythroid proliferation and differentiation, acts, in part, by altering the tyrosine phosphorylation levels of various intracellular signaling molecules. Tyrosine 132-140 erythropoietin Mus musculus 0-14 8639815-1 1996 Erythropoietin (Epo), the primary in vivo stimulator of erythroid proliferation and differentiation, acts, in part, by altering the tyrosine phosphorylation levels of various intracellular signaling molecules. Tyrosine 132-140 erythropoietin Mus musculus 16-19 8639815-7 1996 Moreover, Y425 in the EpoR reduces the Epo requirement for Syp tyrosine phosphorylation and promotes proliferation. Tyrosine 63-71 erythropoietin Mus musculus 22-25 8665851-0 1996 Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation. Tyrosine 18-26 erythropoietin Mus musculus 75-89 8665851-4 1996 Erythropoietin-induced activation of STAT5 was strongly reduced in cells expressing mutated variants of the erythropoietin receptors in which tyrosine residues in their intracellular domain have been eliminated. Tyrosine 142-150 erythropoietin Mus musculus 0-14 8665851-4 1996 Erythropoietin-induced activation of STAT5 was strongly reduced in cells expressing mutated variants of the erythropoietin receptors in which tyrosine residues in their intracellular domain have been eliminated. Tyrosine 142-150 erythropoietin Mus musculus 108-122 8665851-5 1996 We determined that the erythropoietin receptor tyrosine residues 343 and 401 are independently necessary for STAT5 activation. Tyrosine 47-55 erythropoietin Mus musculus 23-37 8665851-8 1996 We propose that these two tyrosine residues of the erythropoietin receptor constitute docking sites for the STAT5 SH2 domain. Tyrosine 26-34 erythropoietin Mus musculus 51-65 7559499-6 1995 A comparison of erythropoietin-induced tyrosine phosphorylations and proliferation of wild-type and Y503F EpR-infected DA-3 cells revealed no differences. Tyrosine 39-47 erythropoietin Mus musculus 16-30 8537396-0 1995 Erythropoietin induces the tyrosine phosphorylation, nuclear translocation, and DNA binding of STAT1 and STAT5 in erythroid cells. Tyrosine 27-35 erythropoietin Mus musculus 0-14 7545788-6 1995 In HCD57 cells, SCF rapidly induces tyrosine phosphorylation of the EPO receptor, and KIT physically associates with the extended box 2 region in the cytoplasmic domain of the EPO receptor. Tyrosine 36-44 erythropoietin Mus musculus 68-71 7545788-7 1995 Our results indicate that KIT may activate the EPO receptor by tyrosine phosphorylation to induce further proliferation and maturation of CFU-Es. Tyrosine 63-71 erythropoietin Mus musculus 47-50 7522324-0 1994 Activated Ki-Ras complements erythropoietin signaling in CTLL-2 cells, inducing tyrosine phosphorylation of a 160-kDa protein. Tyrosine 80-88 erythropoietin Mus musculus 29-43 7781605-3 1995 Here we demonstrate that interleukin 2 (IL-2) as well as erythropoietin (EPO) stimulate STAT5 and induce tyrosine phosphorylation of STAT5. Tyrosine 105-113 erythropoietin Mus musculus 57-71 7781605-3 1995 Here we demonstrate that interleukin 2 (IL-2) as well as erythropoietin (EPO) stimulate STAT5 and induce tyrosine phosphorylation of STAT5. Tyrosine 105-113 erythropoietin Mus musculus 73-76 7538110-2 1995 FDC-P1 cells stably expressing the wild type murine EPOR supported the EPO-induced association of Shc with Jak2 and its rapid tyrosine phosphorylation. Tyrosine 126-134 erythropoietin Mus musculus 52-55 7541671-0 1995 Tyrosine phosphorylation of the erythropoietin receptor: role for differentiation and mitogenic signal transduction. Tyrosine 0-8 erythropoietin Mus musculus 32-46 7541671-3 1995 We and others have shown that Epo induces the tyrosine phosphorylation of its cognate receptor as well as phosphorylation of other proteins. Tyrosine 46-54 erythropoietin Mus musculus 30-33 7541671-5 1995 Eight tyrosine residues are located within the intracellular domain of the murine Epo receptor. Tyrosine 6-14 erythropoietin Mus musculus 82-85 7541671-12 1995 The mutated receptors all induced the tyrosine phosphorylation of several cellular proteins after Epo stimulation. Tyrosine 38-46 erythropoietin Mus musculus 98-101 7528577-0 1995 Hematopoietic cell phosphatase associates with erythropoietin (Epo) receptor after Epo-induced receptor tyrosine phosphorylation: identification of potential binding sites. Tyrosine 104-112 erythropoietin Mus musculus 47-61 7528577-0 1995 Hematopoietic cell phosphatase associates with erythropoietin (Epo) receptor after Epo-induced receptor tyrosine phosphorylation: identification of potential binding sites. Tyrosine 104-112 erythropoietin Mus musculus 63-66 7528577-0 1995 Hematopoietic cell phosphatase associates with erythropoietin (Epo) receptor after Epo-induced receptor tyrosine phosphorylation: identification of potential binding sites. Tyrosine 104-112 erythropoietin Mus musculus 83-86 7528577-1 1995 Erythropoietin (Epo) binding to its receptor (EpoR) induces tyrosine phosphorylation in responsive cells and this ability is required for a mitogenic response. Tyrosine 60-68 erythropoietin Mus musculus 0-14 7528577-1 1995 Erythropoietin (Epo) binding to its receptor (EpoR) induces tyrosine phosphorylation in responsive cells and this ability is required for a mitogenic response. Tyrosine 60-68 erythropoietin Mus musculus 16-19 7528577-5 1995 In the studies presented here, we show that HCP binds the tyrosine phosphorylated Epo receptor through the amino-terminal src-homology 2 (SH2) domain of HCP. Tyrosine 58-66 erythropoietin Mus musculus 82-85 8464516-3 1993 Interleukin-3 and erythropoietin, however, induce transient tyrosine phosphorylation of a common set of proteins as a growth signal, and interleukin-2 induces phosphorylation of an overlapping but distinct set of proteins. Tyrosine 60-68 erythropoietin Mus musculus 18-32 8034573-2 1994 Binding of EPO to its transmembrane receptor leads to the rapid tyrosine phosphorylation of several cellular targets including Shc, Raf-1, Gap120, the cloned EPO receptor (EPOR), pp100/97, and a M(r) 130,000 EPO-activated receptor-associated Janus protein tyrosine kinase, Jak2. Tyrosine 64-72 erythropoietin Mus musculus 11-14 7994062-6 1994 One of the substrates of tyrosine phosphorylation is the receptor and, in the case of the receptor for Epo, the membrane distal region of the cytoplasmic domain is phosphorylated. Tyrosine 25-33 erythropoietin Mus musculus 103-106 8005230-11 1994 These results suggest that the EPO-mediated early signal transduction pathway leading to c-fos expression involves protein-tyrosine phosphorylation, is modulated by tyrosine phosphatase activity and is positively regulated by PKC. Tyrosine 123-131 erythropoietin Mus musculus 31-34 8139531-6 1994 EPO-R(T) inhibited the EPO-dependent tyrosine phosphorylation of wild-type EPO-R, the tyrosine kinase (JAK2), and the SH2 adaptor protein (Shc). Tyrosine 37-45 erythropoietin Mus musculus 0-3 8139531-6 1994 EPO-R(T) inhibited the EPO-dependent tyrosine phosphorylation of wild-type EPO-R, the tyrosine kinase (JAK2), and the SH2 adaptor protein (Shc). Tyrosine 37-45 erythropoietin Mus musculus 23-26 1382712-0 1992 Erythropoietin-induced tyrosine phosphorylations in a high erythropoietin receptor-expressing lymphoid cell line. Tyrosine 23-31 erythropoietin Mus musculus 0-14 1467516-2 1992 EPO binding induces tyrosine kinase activity and rapid tyrosine phosphorylation of several cellular substrates. Tyrosine 20-28 erythropoietin Mus musculus 0-3 1467516-5 1992 Stimulation with IL-3 or EPO of the Ba/F3 cells expressing the recombinant EPO-R (Ba/F3-EPO-R) resulted in tyrosine phosphorylation of the same p97 substrate. Tyrosine 107-115 erythropoietin Mus musculus 25-28 1467516-5 1992 Stimulation with IL-3 or EPO of the Ba/F3 cells expressing the recombinant EPO-R (Ba/F3-EPO-R) resulted in tyrosine phosphorylation of the same p97 substrate. Tyrosine 107-115 erythropoietin Mus musculus 75-78 1467516-8 1992 In CTLL-2-EPO-R cells, a T-lymphocyte line stably transfected with the EPO-R, the 97-Kd substrate was tyrosine-phosphorylated in response to IL-2 or EPO. Tyrosine 102-110 erythropoietin Mus musculus 10-13 1467516-8 1992 In CTLL-2-EPO-R cells, a T-lymphocyte line stably transfected with the EPO-R, the 97-Kd substrate was tyrosine-phosphorylated in response to IL-2 or EPO. Tyrosine 102-110 erythropoietin Mus musculus 71-74 1587309-0 1992 Rapid protein tyrosine phosphorylation selectively induced in murine responsive ELM-I-1 cells by erythropoietin. Tyrosine 14-22 erythropoietin Mus musculus 97-111 1378622-2 1992 Epo stimulation of Ba/F3 cells transfected with the Epo receptor resulted in increases in tyrosine phosphorylation of proteins of 97, 75, and 55 kDa. Tyrosine 90-98 erythropoietin Mus musculus 0-3 1378622-2 1992 Epo stimulation of Ba/F3 cells transfected with the Epo receptor resulted in increases in tyrosine phosphorylation of proteins of 97, 75, and 55 kDa. Tyrosine 90-98 erythropoietin Mus musculus 52-55 1378622-3 1992 Epo-induced increases in tyrosine phosphorylation of a 97-kDa protein were also detected within the Epo receptor complex, suggesting that a protein tyrosine kinase is associated with the Epo receptor. Tyrosine 25-33 erythropoietin Mus musculus 0-3 1378622-3 1992 Epo-induced increases in tyrosine phosphorylation of a 97-kDa protein were also detected within the Epo receptor complex, suggesting that a protein tyrosine kinase is associated with the Epo receptor. Tyrosine 25-33 erythropoietin Mus musculus 100-103 1378622-3 1992 Epo-induced increases in tyrosine phosphorylation of a 97-kDa protein were also detected within the Epo receptor complex, suggesting that a protein tyrosine kinase is associated with the Epo receptor. Tyrosine 25-33 erythropoietin Mus musculus 100-103 1324920-0 1992 Interleukin 3, granulocyte-macrophage colony-stimulating factor, and transfected erythropoietin receptors mediate tyrosine phosphorylation of a common cytosolic protein (pp100) in FDC-ER cells. Tyrosine 114-122 erythropoietin Mus musculus 81-95 1587309-1 1992 We investigated whether protein tyrosine phosphorylation was induced by erythropoietin (Epo) in two murine Epo-responsive cell lines (ELM-I-1, which proliferates autonomously and is induced to differentiate by Epo, and DA-1ER, which grows in a manner dependent on Epo or interleukin-3 (IL-3) without differentiation). Tyrosine 32-40 erythropoietin Mus musculus 72-86 1587309-1 1992 We investigated whether protein tyrosine phosphorylation was induced by erythropoietin (Epo) in two murine Epo-responsive cell lines (ELM-I-1, which proliferates autonomously and is induced to differentiate by Epo, and DA-1ER, which grows in a manner dependent on Epo or interleukin-3 (IL-3) without differentiation). Tyrosine 32-40 erythropoietin Mus musculus 88-91 1587309-2 1992 In ELM-I-1, Epo induced the tyrosine phosphorylation of a protein of about 80-85 kDa (py80) which appeared in the Triton-X soluble fraction of the cell lysate in a time- and concentration-dependent manner. Tyrosine 28-36 erythropoietin Mus musculus 12-15 1656216-3 1991 By two-dimensional analysis of phosphotyrosine-containing proteins isolated with a monoclonal antibody (1G2) against phosphotyrosine, Epo and IL-3 were found to rapidly induce tyrosine phosphorylation of comparable substrates of 92, 70, and 56 kDa. Tyrosine 38-46 erythropoietin Mus musculus 134-137 1656216-2 1991 To extend these observations, we have examined the effects of erythropoietin (Epo) on tyrosine phosphorylation in an Epo-responsive cell that was obtained by transfecting the murine erythropoietin receptor (EpoR) into an interleukin-3 (IL-3)-dependent cell line. Tyrosine 86-94 erythropoietin Mus musculus 62-76 1656216-2 1991 To extend these observations, we have examined the effects of erythropoietin (Epo) on tyrosine phosphorylation in an Epo-responsive cell that was obtained by transfecting the murine erythropoietin receptor (EpoR) into an interleukin-3 (IL-3)-dependent cell line. Tyrosine 86-94 erythropoietin Mus musculus 78-81 1985918-0 1991 Proliferative action of erythropoietin is associated with rapid protein tyrosine phosphorylation in responsive B6SUt.EP cells. Tyrosine 72-80 erythropoietin Mus musculus 24-38 1985918-3 1991 Presently it is shown in the responsive, factor-dependent murine cell line B6SUt.EP that erythropoietin induces the tyrosine phosphorylation of six plasma membrane-associated proteins in a time- and concentration-dependent fashion (i.e. phosphoproteins PY153, PY140, PY100, PY93, PY74, and PY54). Tyrosine 116-124 erythropoietin Mus musculus 89-103 21255641-0 2011 Akt activation through the phosphorylation of erythropoietin receptor at tyrosine 479 is required for myeloproliferative disorder-associated JAK2 V617F mutant-induced cellular transformation. Tyrosine 73-81 erythropoietin Mus musculus 46-60 30252956-2 2019 We present here data indicating that Fyn, a Src-family-kinase, participates in the EPO signaling-pathway, since Fyn-/- mice exhibit reduced Tyr-phosphorylation of EPO-R and decreased STAT5-activity. Tyrosine 140-143 erythropoietin Mus musculus 83-86 22669948-2 2012 Structural-functional and murine knock-in experiments have suggested that EPO-R Tyr-343 is important in EPO-mediated mitogenesis. Tyrosine 80-83 erythropoietin Mus musculus 74-77 17950726-8 2007 Consequently, the autocrine Epo-EpoR signaling pathway was activated, as evidenced by higher p-Tyr JAK2, p-Tyr EpoR and p-Tyr STAT5B in the ANKH transfectants. Tyrosine 95-98 erythropoietin Mus musculus 28-31 19027957-9 2009 EPO stimulation of the BM-DCs led to Tyr-phosphorylation of STAT3. Tyrosine 37-40 erythropoietin Mus musculus 0-3 19187767-4 2009 A truncated receptor with only one cytosolic tyrosine (Y343) is sufficient for signaling in response to erythropoietin, regardless of the monomer on which it is located. Tyrosine 45-53 erythropoietin Mus musculus 104-118 15953601-5 2005 PLCgamma1 is rapidly tyrosine phosphorylated upon EPO stimulation and associates with EPO-R in an SH2-domain-dependent manner. Tyrosine 21-29 erythropoietin Mus musculus 50-53 15982852-1 2006 Hematopoietic cytokines, including interleukin (IL)-3 and erythropoietin (Epo), regulate hematopoiesis by stimulating their receptors coupled with the Jak2 tyrosine kinase to induce receptor tyrosine phosphorylation and activate mainly the STAT5, PI3K/Akt, and Ras/MEK/ERK signaling pathways. Tyrosine 156-164 erythropoietin Mus musculus 58-72 15982852-1 2006 Hematopoietic cytokines, including interleukin (IL)-3 and erythropoietin (Epo), regulate hematopoiesis by stimulating their receptors coupled with the Jak2 tyrosine kinase to induce receptor tyrosine phosphorylation and activate mainly the STAT5, PI3K/Akt, and Ras/MEK/ERK signaling pathways. Tyrosine 156-164 erythropoietin Mus musculus 74-77 17347485-3 2007 METHODS AND RESULTS: Here we show in C57BL/6J mice that 4-week treatment with the long-lasting EPO analogue darbepoetin-alpha (DPO) at a dose of 10 microg/kg/week induces a reduction of platelet reactivity using flow cytometry and Western blot analysis of tyrosine-specific platelet phosphorylation. Tyrosine 256-264 erythropoietin Mus musculus 95-98 15705783-11 2005 Furthermore, wild-type Lnk, but not the Lnk SH2 mutant, becomes tyrosine-phosphorylated following Epo administration and inhibits EpoR phosphorylation and JAK2 activation. Tyrosine 64-72 erythropoietin Mus musculus 98-101 15242770-7 2004 BAF3 cells expressing a mutant EPOR with no cytoplasmic tyrosine residues were capable of triggering EPO-dependent TNF-alpha synthesis and secretion, indicating that tyrosine-docking sites in the EPOR were not required for EPO-dependent TNF-alpha secretion. Tyrosine 166-174 erythropoietin Mus musculus 31-34 15242770-7 2004 BAF3 cells expressing a mutant EPOR with no cytoplasmic tyrosine residues were capable of triggering EPO-dependent TNF-alpha synthesis and secretion, indicating that tyrosine-docking sites in the EPOR were not required for EPO-dependent TNF-alpha secretion. Tyrosine 166-174 erythropoietin Mus musculus 101-104 12135708-4 2002 Wortmannin, another PtdIns 3-kinase inhibitor, also suppressed Epo-induced PLC-gamma2 tyrosine phosphorylation. Tyrosine 86-94 erythropoietin Mus musculus 63-66 12135708-6 2002 Upon Epo stimulation, the tyrosine-phosphorylated PLC-gamma2 was found to be associated with the tyrosine-phosphorylated Grb2-associated binder (GAB)2, SHC and SHP2 proteins. Tyrosine 26-34 erythropoietin Mus musculus 5-8 12135708-6 2002 Upon Epo stimulation, the tyrosine-phosphorylated PLC-gamma2 was found to be associated with the tyrosine-phosphorylated Grb2-associated binder (GAB)2, SHC and SHP2 proteins. Tyrosine 97-105 erythropoietin Mus musculus 5-8 11716471-0 2001 Erythropoietin-stimulated Raf-1 tyrosine phosphorylation is associated with the tyrosine kinase Lyn in J2E erythroleukemic cells. Tyrosine 32-40 erythropoietin Mus musculus 0-14 11716471-6 2001 Therefore, it was concluded that Lyn may be the kinase responsible for tyrosine phosphorylating Raf-1 and increasing its exokinase activity in response to erythropoietin. Tyrosine 71-79 erythropoietin Mus musculus 155-169 15078939-6 2004 Mutational analysis of sf-Stk indicated that a functional kinase domain and 8 of its 12 tyrosine residues are required for the induction of Epo-independent colonies. Tyrosine 88-96 erythropoietin Mus musculus 140-143 12135708-2 2002 Here, we analyzed the involvement of phosphatidylinositol (PtdIns) 3-kinase in GPI hydrolysis through PLC-gamma2 tyrosine phosphorylation in response to Epo in FDC-P1 cells transfected with a wild type (WT) erythropoietin-receptor (Epo-R). Tyrosine 113-121 erythropoietin Mus musculus 153-156 12135708-3 2002 We showed that phosphatidylinositol 3-kinase (PtdIns 3-kinase) inhibitor LY294002 inhibits Epo-induced hydrolysis of endogenous GPI and Epo-induced PLC-gamma2 tyrosine phosphorylation in a dose-dependent manner. Tyrosine 159-167 erythropoietin Mus musculus 91-94 12135708-3 2002 We showed that phosphatidylinositol 3-kinase (PtdIns 3-kinase) inhibitor LY294002 inhibits Epo-induced hydrolysis of endogenous GPI and Epo-induced PLC-gamma2 tyrosine phosphorylation in a dose-dependent manner. Tyrosine 159-167 erythropoietin Mus musculus 136-139 11877405-11 2002 Collectively, our results demonstrate that: 1) MPO and EPO contribute to tyrosine nitration in vivo; 2) the major reactive nitrogen species formed by leukocyte peroxidase-catalyzed oxidation of NO(2)(-) is the one-electron oxidation product, (*)NO(2); 3) as a minor reaction, peroxidases may also catalyze the two-electron oxidation of NO(2)(-), producing a ONOO(-)-like product. Tyrosine 73-81 erythropoietin Mus musculus 55-58