Matches in Nanopublications for { ?s <http://www.w3.org/ns/prov#value> ?o ?g. }
- _6 value "TAK1 is subsequently activated in the cytoplasm, leading to the activation of IKK. Inactive IKK sequesters NF-κB in the cytoplasm, but activation leads to phosphorylation and degradation of IκB and consequent release of NF-κB. Activation of TAK1 also results in the activation of MAP kinases and c-Jun NH2-terminal kinase (JNK)." provenance.
- _6 value "TAK1 is subsequently activated in the cytoplasm, leading to the activation of IKK. Inactive IKK sequesters NF-κB in the cytoplasm, but activation leads to phosphorylation and degradation of IκB and consequent release of NF-κB. Activation of TAK1 also results in the activation of MAP kinases and c-Jun NH2-terminal kinase (JNK)." provenance.
- _5 value "MyD88 was originally isolated as a myeloid differentiation primary response gene that is rapidly induced upon IL-6-stimulated differentiation of M1 myeloleukemic cells into macrophages" provenance.
- _7 value "Although the kinase activity of IRAK-1 increases strongly following IL-1 stimulation, IRAK-1 kinase activity is not required for its signaling function, because overexpression of a kinase-defective mutant of IRAK-1 is observed to strongly induce NF-κB activation in cells otherwise deficient for IRAK-1. Upon stimulation, IRAK-1 is recruited to the receptor through a homophilic interaction with the DD of MyD88." provenance.
- _4 value "IRAK-1-deficient mice and cell lines showed diminished cytokine production in response to IL-1 and LPS;" provenance.
- _3 value "IRAK-1-deficient mice and cell lines showed diminished cytokine production in response to IL-1 and LPS;" provenance.
- _6 value "IRAK-1-deficient mice and cell lines showed diminished cytokine production in response to IL-1 and LPS;" provenance.
- _5 value "IRAK-1-deficient mice and cell lines showed diminished cytokine production in response to IL-1 and LPS;" provenance.
- _5 value "TRAF6 directly interacts with CD40 and TRANCE-R" provenance.
- _5 value "It has been shown recently that ubiquitination plays an important role in TAK1 activation (26, 27). IKK activation by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex composed of Ubc13 and Uev1A as well as the TAK1·kinase complex. TRAF6 can interact through its RING finger domain with Ubc13 in the Ubc13·Uev1A complex. This Ubc·TRAF6 complex catalyzes the formation of a Lys-63-linked polyubiquitin chain, which triggers TAK1 activation through a unique proteasome-independent mechanism." provenance.
- _5 value "Tollip—Tollip (Toll-interacting protein) was originally cloned as a protein interacting with the IL-1 receptor accessory protein (28). Tollip also associates with TLR2 and TLR4. In resting cells, Tollip forms a complex with members of the IRAK family, thereby preventing NF-κB activation. Upon activation Tollip·IRAK-1 complexes are recruited to the cognate receptor, resulting in the rapid autophosphorylation of IRAK-1 and its dissociation from the receptor." provenance.
- _7 value "Pellino 1 is required for IL-1-induced NF-κB activation and IL-8 gene expression (30). Pellino 2 has also been shown to be involved in IL-1R/TLR signaling pathways (31). Following IL-1 stimulation, IRAK-1 and Pellino 2 associate to form complexes. Ectopic expression of a Pellino 2 antisense construct was shown to inhibit IL-1- and LPS-dependent but not TNF-α-dependent activation of the IL-8 promoter." provenance.
- _5 value "it is noteworthy that, compared with other TLR ligands, poly(I-C) stimulation induces the production of relatively large amounts of type I interferons and interferon-inducible genes but smaller amounts of inflammatory cytokines such as TNF-α and IL-6, further suggesting that TLR3 does not utilize the MyD88-dependent pathway for signaling." provenance.
- _5 value "TIRAP was shown to associate with TLR-4 but not with other TLRs. Overexpression of a dominant-negative form of TIRAP was shown to inhibit LPS-induced NF-κB activation and dendritic cell maturation. Blockage of TIRAP using a cell-permeable inhibitory peptide also prevented induction of IP-10 by LPS." provenance.
- _3 value "In accordance with the observed effects on phosphorylation of DDR1in HB2 cells (Fig. 2), we subsequently found that pertussis toxin, but not cholera toxin, impaired the adhesion of normal HB2 cells to collagen (Fig. 3a,b respectively)." provenance.
- _6 value "We found that treatment with 7.5 μM mastoparan enabled a marked collagen-induced phosphorylation of DDR1 after only 30 min (Fig. 5a) and a concomitant increase in adhesion after 60 and 90 min (Fig. 5b). Other investigators have previously reported that the indicated concentration of mastoparan primarily activates Gi/o-proteins, whereas a significantly higher concentration is needed to stimulate transducin and Gs-proteins.27" provenance.
- _5 value "To further ascertain whether such a link exists between Wnt-5a signaling, collagen-induced DDR1 activation, and the adhesiveness of HB2 cells, we tested the effects of PP1, a specific inhibitor of Src family tyrosine kinases. We found that PP1 abolished the collagen-induced phosphorylation of DDR1 (Fig. 6a), and that it also decreased adhesion of normal HB2 cells by about 50% (Fig. 6b)." provenance.
- _3 value "To further ascertain whether such a link exists between Wnt-5a signaling, collagen-induced DDR1 activation, and the adhesiveness of HB2 cells, we tested the effects of PP1, a specific inhibitor of Src family tyrosine kinases. We found that PP1 abolished the collagen-induced phosphorylation of DDR1 (Fig. 6a), and that it also decreased adhesion of normal HB2 cells by about 50% (Fig. 6b)." provenance.
- _7 value "Furthermore, we noted that collagen-stimulated DDR1 interacted with the p85 subunit of PI3K (Fig. 7b), and we also observed that adherence of HB2 cells to collagen caused tyrosine phosphorylation of the p85 of PI3K (Fig. 7c), a phenomenon associated with activation of this enzyme. Neither of these events was observed in cells pretreated with pertussis toxin (Fig. 7a,b,c)." provenance.
- _8 value "Furthermore, we noted that collagen-stimulated DDR1 interacted with the p85 subunit of PI3K (Fig. 7b), and we also observed that adherence of HB2 cells to collagen caused tyrosine phosphorylation of the p85 of PI3K (Fig. 7c), a phenomenon associated with activation of this enzyme. Neither of these events was observed in cells pretreated with pertussis toxin (Fig. 7a,b,c)." provenance.
- _5 value "Furthermore, we noted that collagen-stimulated DDR1 interacted with the p85 subunit of PI3K (Fig. 7b), and we also observed that adherence of HB2 cells to collagen caused tyrosine phosphorylation of the p85 of PI3K (Fig. 7c), a phenomenon associated with activation of this enzyme. Neither of these events was observed in cells pretreated with pertussis toxin (Fig. 7a,b,c)." provenance.
- _6 value "Adhesion of HT-29 cells on a monolayer of HUVEC pretreated with TNFα was dependent on E-selectin expression but was independent of SAPK2/p38 activity of both HUVEC and tumor cells. The adhesion of HT-29 cells to E-selectin-expressing HUVEC led to the activation of SAPK2/p38 in the tumor cells as reflected by the increased phosphorylation of the actin-polymerizing factor HSP27 by mitogen-activated protein kinase 2/3, a direct target of SAPK2/p38. Moreover, a recombinant E-selectin/Fc chimera quickly increased the activation of SAPK2/p38 in HT-29 cells. Blocking the increased activity of SAPK2/p38 of HT-29 cells by SB203580 or by expressing a dominant negative form of SAPK2/p38 inhibited their transendothelial migration." provenance.
- _5 value "Adhesion of HT-29 cells on a monolayer of HUVEC pretreated with TNFα was dependent on E-selectin expression but was independent of SAPK2/p38 activity of both HUVEC and tumor cells. The adhesion of HT-29 cells to E-selectin-expressing HUVEC led to the activation of SAPK2/p38 in the tumor cells as reflected by the increased phosphorylation of the actin-polymerizing factor HSP27 by mitogen-activated protein kinase 2/3, a direct target of SAPK2/p38. Moreover, a recombinant E-selectin/Fc chimera quickly increased the activation of SAPK2/p38 in HT-29 cells. Blocking the increased activity of SAPK2/p38 of HT-29 cells by SB203580 or by expressing a dominant negative form of SAPK2/p38 inhibited their transendothelial migration." provenance.
- _5 value "In primary cultures of HUVEC, TNFα induced a strong activation of the expression of endothelial adhesion proteins that include E-selectin and ICAM (Fig.1, A—D, and data not shown). This induction was maximal after 4 h and required de novo protein synthesis being inhibited by cycloheximide (Fig. 1,E and F)." provenance.
- _5 value "In primary cultures of HUVEC, TNFα induced a strong activation of the expression of endothelial adhesion proteins that include E-selectin and ICAM (Fig.1, A—D, and data not shown). This induction was maximal after 4 h and required de novo protein synthesis being inhibited by cycloheximide (Fig. 1,E and F)." provenance.
- _4 value "However, HT-29 cells migrated across an endothelial layer of HUVEC, and this migration was enhanced by pretreating HUVEC with TNFα (Fig.4A). This increase in cell migration was reduced down to control levels by pretreating HUVEC with the anti-E-selectin antibody indicating the requirement of E-selectin expression and E-selectin-dependent adhesion for HT-29 cell migration across an endothelial cell layer (Fig. 4A)." provenance.
- _3 value "Impairing E-selectin-mediated activation of SAPK2p38 and HSP27 phosphorylation of HT-29 cells with SB203580 (Fig. 4A and data not shown) or by expressing a dominant negative form of SAPK2/p38 inhibited their migration across activated HUVEC (Fig.4B)." provenance.
- _5 value "Northern analyses and RNase protection assays revealed that exposure of cultured EC to TNF-α, interleukin-1β, or Ox-LDL results in the accumulation of MT1- MMP mRNA" provenance.
- _5 value "Northern analyses and RNase protection assays revealed that exposure of cultured EC to TNF-α, interleukin-1β, or Ox-LDL results in the accumulation of MT1- MMP mRNA" provenance.
- _5 value "Stimulation of EC with TNF-α and/or Ox-LDL for 24 h increased the number of MT1-MMP-bearing cells to about 1.8-fold (Ox-LDL), 1.7-fold (TNF-α), or 2.5-fold (TNF-α and Ox-LDL together) as compared with unstimulated cells" provenance.
- _3 value "Tumors arising from TSC-treated A549 cells tended to be somewhat larger than those developing from untreated cells (364 F 333 versus 200 F 329 mg; P = 0.25, two-tailed t test; data not shown)." provenance.
- _4 value "Interestingly, Dkk-1, encoding a Wnt signaling antagonist frequently silenced by DNA methylation in cancer cells (20, 26), was down-regulated in a dose-dependent manner in both cell lines. Quantitative RT-PCR experiments (Fig. 1C) confirmed that TSC mediated dose-dependent decreases in Dkk-1 mRNA copy numbers in A549 and Calu-6cells, which exhibited relatively high Dkk-1 expression." provenance.
- _4 value "Diminished Dkk-1 expression coincided with reduced Dkk-1 protein levels in A549 and Calu-6 cells following TSC exposure (Fig. 1D)." provenance.
- _4 value "IL-6 also induces differentiation of macrophages [26], megakaryocytes [27-29], and osteoclasts [30]." provenance.
- _4 value "IL-6 also induces differentiation of macrophages [26], megakaryocytes [27-29], and osteoclasts [30]." provenance.
- _4 value "In the acute-phase reaction, this cytokine stimulates hepatocytes to produce acute-phase proteins such as C-reactive protein (CRP), fibrinogen, α1-antitrypsin, and serum amyloid A [12,13], and it simultaneously suppresses albumin production [11]." provenance.
- _4 value "It causes leukocytosis and fever when administered in vivo[31] and also acts as a growth factor for renal mesangial cells [32], epidermal keratinocytes [33,34], and various types of tumor cells, for example, in plasmacytoma[8], multiple myeloma[35], and renal cell carcinoma[36]." provenance.
- _4 value "It causes leukocytosis and fever when administered in vivo[31] and also acts as a growth factor for renal mesangial cells [32], epidermal keratinocytes [33,34], and various types of tumor cells, for example, in plasmacytoma[8], multiple myeloma[35], and renal cell carcinoma[36]." provenance.
- _6 value "We and our colleagues identified the two components of IL-6 receptor (IL-6R), an 80-kDa IL-6-binding protein (α chain) and a 130-kDa signal transducer known as gp130 (β chain), in 1988 and 1990[37-39], respectively. Although IL-6 cannot directly bind to gp130, it can bind to IL-6R to generate the high-affinity complex of IL-6/IL-6R/gp130." provenance.
- _6 value "Our group and others found that JAK1, JAK2, and Tky-2 are activated and are tyrosine-phosphorylated in response to IL-6, CNTF, LIF, and OSM[14]" provenance.
- _6 value "Our group and others found that JAK1, JAK2, and Tky-2 are activated and are tyrosine-phosphorylated in response to IL-6, CNTF, LIF, and OSM[14]" provenance.
- _6 value "Our group and others found that JAK1, JAK2, and Tky-2 are activated and are tyrosine-phosphorylated in response to IL-6, CNTF, LIF, and OSM[14]" provenance.
- _6 value "Our group and others found that JAK1, JAK2, and Tky-2 are activated and are tyrosine-phosphorylated in response to IL-6, CNTF, LIF, and OSM[14]" provenance.
- _6 value "Our group and others found that JAK1, JAK2, and Tky-2 are activated and are tyrosine-phosphorylated in response to IL-6, CNTF, LIF, and OSM[14]" provenance.
- _6 value "IL-6 activates STAT1 and STAT5 in addition to STAT3." provenance.
- _4 value "It is known that IL-6 induces growth arrest and macrophage differentiation in the murine myeloid leukemic cell line M1. The essential role of STAT3 in the IL-6-induced macrophage differentiation of M1 cells was demonstrated by using dominant negative forms of STAT3 [67], which inhibit both IL-6-induced growth arrest and macrophage differentiation in M1 transformants. Blocking STAT3 activation inhibits IL-6-induced repression of c-Myb and c-Myc, but not EGR-1 induction [68], while IL-6 enhances the growth of M1 cells when STAT3 is suppressed." provenance.
- _5 value "It is known that IL-6 induces growth arrest and macrophage differentiation in the murine myeloid leukemic cell line M1. The essential role of STAT3 in the IL-6-induced macrophage differentiation of M1 cells was demonstrated by using dominant negative forms of STAT3 [67], which inhibit both IL-6-induced growth arrest and macrophage differentiation in M1 transformants. Blocking STAT3 activation inhibits IL-6-induced repression of c-Myb and c-Myc, but not EGR-1 induction [68], while IL-6 enhances the growth of M1 cells when STAT3 is suppressed." provenance.
- _6 value "It is known that IL-6 induces growth arrest and macrophage differentiation in the murine myeloid leukemic cell line M1. The essential role of STAT3 in the IL-6-induced macrophage differentiation of M1 cells was demonstrated by using dominant negative forms of STAT3 [67], which inhibit both IL-6-induced growth arrest and macrophage differentiation in M1 transformants. Blocking STAT3 activation inhibits IL-6-induced repression of c-Myb and c-Myc, but not EGR-1 induction [68], while IL-6 enhances the growth of M1 cells when STAT3 is suppressed." provenance.
- _7 value "Furthermore, nonreceptor tyrosine kinases, such as Btk, Tec, Fes, and Hck[72,73] are activated through the IL-6 receptor, as well as through a variety of other cytokine receptors [74], although the biological significance of these signal transduction pathways remains to be clarified." provenance.
- _6 value "Overexpression studies have shown that PIAS-1 associates only with activated STAT1 dimers and inhibits their DNA-binding activity, but that no monomeric forms of STAT1 are present [99]. Similarly, PIAS-3 associates specifically with activated STAT3 but not with STAT1, resulting in the blocking of all STAT3-mediated gene transcriptions, and is especially well known as an inhibitor of IL-6 signaling in M1 cell lines [98]." provenance.
- _2 value "Excess amounts of reactive oxygen species (ROS) such as O2.- and H2O2 have deleterious effects on cells and contribute to various cardiovascular diseases including hypertension, heart failure, atherosclerosis, and diabetes (41), while physiological concentrations of ROS are involved in signaling to mediate cell migration, growth, and differentiation (32)." provenance.
- _5 value "Nox2 is a critical component of endothelial NADPH oxidase (38), and its expression and Nox2-dependent ROS production are increased by oxidized LDL, endothelin-1, angiotensin II, VEGF, and angiopoietin-2 in ECs (99). Nox1 is involved in shear stressinduced ROS production which is required for monocyte adhesion (93) and stimulates branching morphogenesis in sinusoidal ECs (55). Nox4 is most abundantly expressed in ECs, and involved in basal- (2) and Ang II-induced (109) O2- production. Moreover, p47phox is involved in cytokine, growth factor, or shear stress-stimulated ROS production in ECs (48, 67, 107)." provenance.
- _5 value "Nox2 is a critical component of endothelial NADPH oxidase (38), and its expression and Nox2-dependent ROS production are increased by oxidized LDL, endothelin-1, angiotensin II, VEGF, and angiopoietin-2 in ECs (99). Nox1 is involved in shear stressinduced ROS production which is required for monocyte adhesion (93) and stimulates branching morphogenesis in sinusoidal ECs (55). Nox4 is most abundantly expressed in ECs, and involved in basal- (2) and Ang II-induced (109) O2- production. Moreover, p47phox is involved in cytokine, growth factor, or shear stress-stimulated ROS production in ECs (48, 67, 107)." provenance.
- _3 value "Exogenous H2O2 stimulates induction of HIF1α and VEGF by various cell types including ECs, and promote cell proliferation and migration, cytoskeletal reorganization, and tube formation in ECs (99)." provenance.
- _2 value "Exogenous H2O2 stimulates induction of HIF1α and VEGF by various cell types including ECs, and promote cell proliferation and migration, cytoskeletal reorganization, and tube formation in ECs (99)." provenance.
- _6 value "VEGF and angiopoietin-1 stimulate ROS production via activation of Nox2-based NADPH oxidase and oxidase-derived ROS are involved in EC migration and/or proliferation (43, 49, 100, 111) (Fig. 1). Thus, many of angiogenic responses in ECs are dependent on ROS." provenance.
- _5 value "The mitogenic and chemotactic effects of VEGF in ECs are mediated mainly through VEGFR2 (76). VEGFR2 is activated through ligandstimulated receptor dimerization and transphosphorylation (autophosphorylation) of tyrosine residues in the cytoplasmic kinase domain. At present, tyrosine residues 951 and 996 in the kinase insert domain, and 1054 and 1059 in the kinase catalytic domain, have been identified as autophosphorylation sites for VEGFR2 in a bacterial expression system (30). This event is followed by activation of downstream signaling pathways such as Src, PI3 kinase, MAP kinases, and Akt, which is essential for VEGF-induced actin reorganization, cell migration, and proliferation of ECs." provenance.
- _5 value "The mitogenic and chemotactic effects of VEGF in ECs are mediated mainly through VEGFR2 (76). VEGFR2 is activated through ligandstimulated receptor dimerization and transphosphorylation (autophosphorylation) of tyrosine residues in the cytoplasmic kinase domain. At present, tyrosine residues 951 and 996 in the kinase insert domain, and 1054 and 1059 in the kinase catalytic domain, have been identified as autophosphorylation sites for VEGFR2 in a bacterial expression system (30). This event is followed by activation of downstream signaling pathways such as Src, PI3 kinase, MAP kinases, and Akt, which is essential for VEGF-induced actin reorganization, cell migration, and proliferation of ECs." provenance.
- _5 value "The mitogenic and chemotactic effects of VEGF in ECs are mediated mainly through VEGFR2 (76). VEGFR2 is activated through ligandstimulated receptor dimerization and transphosphorylation (autophosphorylation) of tyrosine residues in the cytoplasmic kinase domain. At present, tyrosine residues 951 and 996 in the kinase insert domain, and 1054 and 1059 in the kinase catalytic domain, have been identified as autophosphorylation sites for VEGFR2 in a bacterial expression system (30). This event is followed by activation of downstream signaling pathways such as Src, PI3 kinase, MAP kinases, and Akt, which is essential for VEGF-induced actin reorganization, cell migration, and proliferation of ECs." provenance.
- _5 value "The mitogenic and chemotactic effects of VEGF in ECs are mediated mainly through VEGFR2 (76). VEGFR2 is activated through ligandstimulated receptor dimerization and transphosphorylation (autophosphorylation) of tyrosine residues in the cytoplasmic kinase domain. At present, tyrosine residues 951 and 996 in the kinase insert domain, and 1054 and 1059 in the kinase catalytic domain, have been identified as autophosphorylation sites for VEGFR2 in a bacterial expression system (30). This event is followed by activation of downstream signaling pathways such as Src, PI3 kinase, MAP kinases, and Akt, which is essential for VEGF-induced actin reorganization, cell migration, and proliferation of ECs." provenance.
- _6 value "Several PTPs, including SHP-1, SHP-2, and LMW-PTP (HCPTPA), inducibly associate with VEGFR2 after VEGF stimulation (42, 46, 57)." provenance.
- _5 value "VEGFR2 is present in endothelial caveolae through association with Cav1 which negatively regulates receptor activity in basal state (Fig. 1)(61). Dissociation of VEGFR2 from caveolae/Cav1 seems to be essential for VEGFR2 autophosphorylation and activation of downstream signaling events(61)." provenance.
- _4 value "Cav1 is tyrosine phosphorylated by ROS (14, 17)and by various growth factors(54, 70), including VEGF(61). We have demonstrated that VEGF promotes the release of VEGFR2 from caveolae/lipid rafts, which is contemporaneous with the tyrosine phosphorylation of Cav1(Tyr14) and VEGFR2 and their colocalization at focal complexes, appearing as small-dot like structures at the edge of lamellipodia (Figs. 1 and 2)(52)." provenance.
- _6 value "Cav1 is tyrosine phosphorylated by ROS (14, 17)and by various growth factors(54, 70), including VEGF(61). We have demonstrated that VEGF promotes the release of VEGFR2 from caveolae/lipid rafts, which is contemporaneous with the tyrosine phosphorylation of Cav1(Tyr14) and VEGFR2 and their colocalization at focal complexes, appearing as small-dot like structures at the edge of lamellipodia (Figs. 1 and 2)(52)." provenance.
- _6 value "Phospho-caveolin interacts with Grb7 (63), low molecular weight protein tyrosine phosphatase (16), and Csk, a negative regulator for Src (13)." provenance.
- _6 value "Phospho-caveolin interacts with Grb7 (63), low molecular weight protein tyrosine phosphatase (16), and Csk, a negative regulator for Src (13)." provenance.
- _3 value "Of note, overexpression of mutant Cav1 (Y14F) blocks VEGF-stimulated localization of phospho-VEGFR2 at focal complexes as well as EC migration and proliferation." provenance.
- _5 value "In ECs, VEGF stimulates ARF6 association with Rac1, which is cotemporaneous with Rac1 activation. The dominant negative ARF6 (T27N),inhibits VEGF-stimulated GTP-loading of Rac1, ROS production, and VEGFR2 autophosphorylation. These results suggest that ARF6 is an upstream mediator for Rac1, which may contribute to ROS production that mediates VEGFR2 autophosphorylation in ECs (Fig. 1)." provenance.
- _4 value "IQGAP1 captures and stabilizes microtubules by interacting with CLIP-170, a microtubule plus end binding protein, near the cell cortical regions (83). Activated Rac1 promotes capture of CLIP-170-capped microtubules in lamellipodia(75)." provenance.
- _7 value "At the leading edge of cells, Rac1 also links the adenomatous polyposis coli (APC) protein to actin filaments through binding to IQGAP1, thereby regulating polarization and directional migration by forming a complex with APC and CLIP-170. Of note, Nox2 also binds to and colocalizes with IQGAP1 at the leading edge in actively migrating ECs (Fig. 2)(50)." provenance.
- _3 value "The model was appropriate for testing the effects of desaturase inhibition because, after subplantar injection of carrageenan, an acute and localized inflammatory response occurs in the footpad, characterized by increased edema and neutrophil infiltration. Inhibition of edema was obtained with aspirin and indomethacin and was comparable to that obtained in the rat model." provenance.
- _3 value "D. Dietary AA restored edema and MPO activity." provenance.
- _6 value "Phosphorylation of cytoplasmic FOXO at specific sites by JNK initiates translocation into the nucleus" provenance.
- _6 value "Phosphorylation of cytoplasmic FOXO at specific sites by JNK initiates translocation into the nucleus" provenance.
- _6 value "Akt-dependent phosphorylation reduces the DNA-binding activity of FOXO, interferes with binding to the co-activators p300/CBP, and inactivates the FOXO nuclear translocation signal" provenance.
- _7 value "The Akt-phosphorylated FOXO is exported from the nucleus in a CRM1- and 14-3-3-dependent process" provenance.
- _10 value "The Akt-phosphorylated FOXO is exported from the nucleus in a CRM1- and 14-3-3-dependent process" provenance.
- _8 value "Akt-phosphorylated FOXO interacts with the ubiquitin ligase Skp2 and is targeted for proteasomal degradation." provenance.
- _7 value "Akt-phosphorylated FOXO interacts with the ubiquitin ligase Skp2 and is targeted for proteasomal degradation." provenance.
- _6 value "They also repress transcription of cyclin D1 and D2, which results in an attenuation of CDK4 activity and reduced phosphorylation of Rb protein, and hence increased binding activity of E2F family members to Rb." provenance.
- _6 value "They also repress transcription of cyclin D1 and D2, which results in an attenuation of CDK4 activity and reduced phosphorylation of Rb protein, and hence increased binding activity of E2F family members to Rb." provenance.
- _7 value "Oxidative stress, for instance a low concentration of hydrogen peroxide (H2O2),leads to an activation of the small GTPase Ral, which in turn is instrumental in the phosphorylation and activation of the Jun N-terminal kinase JNK." provenance.
- _6 value "Acetylated and JNK-phosphorylated nuclear FOXO then recruits SIRT1, a constitutively nuclear, nicotinamide adenine dinucleotide-dependent protein deacetylase. This recruitment, like the nuclear import, is dependent on oxidative stress signals." provenance.
- _7 value "We observe that PI3K associates with ErbB-3 exclusively in gefitinib-sensitive NSCLC cell lines. Gefitinib dissociates this complex, thereby linking EGFR inhibition to decreased Akt activity." provenance.
- _6 value "Down-regulation of ErbB-3 by means of short hairpin RNA leads to decreased phospho-Akt levels in the gefitinib-sensitive NSCLC cell lines, Calu-3 (WT EGFR) and H3255 (L858R EGFR), but has no effect on Akt activation in the gefitinib-resistant cell lines, A549 and H522." provenance.
- _6 value "Therefore, the p85 IPs were probed with anti-ErbB-3 antibodies. In the gefitinib-sensitive NSCLC cell lines, there is indeed a gefitinib-labile interaction between p85 and ErbB-3 (Fig. 2A Bottom Right)." provenance.
- _8 value "As shown in Fig. 3A, EGF stimulated an association between p85 and ErbB-3 (also observed as the 210-kDa PTyr protein). This association was blocked by exposing the cells to 1 μM gefitinib. Assessment of ErbB-3 immunoprecipitations reveals that gefitinib leads to a decrease in ErbB-3 tyrosine phosphorylation (Fig. 3B Top) and the amount of coprecipitated p85 (Fig. 3B Middle)." provenance.
- _7 value "As shown in Fig. 3A, EGF stimulated an association between p85 and ErbB-3 (also observed as the 210-kDa PTyr protein). This association was blocked by exposing the cells to 1 μM gefitinib. Assessment of ErbB-3 immunoprecipitations reveals that gefitinib leads to a decrease in ErbB-3 tyrosine phosphorylation (Fig. 3B Top) and the amount of coprecipitated p85 (Fig. 3B Middle)." provenance.
- _6 value "As shown in Fig. 3A, EGF stimulated an association between p85 and ErbB-3 (also observed as the 210-kDa PTyr protein). This association was blocked by exposing the cells to 1 μM gefitinib. Assessment of ErbB-3 immunoprecipitations reveals that gefitinib leads to a decrease in ErbB-3 tyrosine phosphorylation (Fig. 3B Top) and the amount of coprecipitated p85 (Fig. 3B Middle)." provenance.
- _4 value "Vascular endothelial growth factor (VEGF) stimulates angiogenesis by activating VEGF receptor-2 (VEGFR-2)." provenance.
- _6 value "Vascular endothelial growth factor (VEGF) stimulates angiogenesis by activating VEGF receptor-2 (VEGFR-2)." provenance.
- _5 value "Both VEGF and PlGF bind to VEGF receptor-1 (VEGFR-1), but it is unknown whether VEGFR-1, which exists as a soluble or a membrane-bound type, is an inert decoy or a signaling receptor for PlGF during angiogenesis." provenance.
- _4 value "To examine the role of PlGF in angiogenesis, we inactivated the gene expressing PlGF (Pgf) in mice. Unexpectedly, the absence of PlGF—even in combination with a loss of VEGF-B—had a negligible effect on vascular development." provenance.
- _5 value "VEGF-B is another ligand of VEGFR-1 (ref. 18), but loss of VEGF-B (Vegfb–/–) does not affect vascular development19." provenance.
- _4 value "When both tumor and host expressed PlGF, tumors were large and highly vascularized (4 ± 1 g; n = 8; Fig. 1g and j). In contrast, when they both lacked PlGF, tumors remained small and poorly vascularized (1.0 ± 0.3 g; n = 8; Fig. 1h and j)," provenance.
- _4 value "Healing of skin incisions progressed more slowly in Pgf–/– mice versus wild-type (Fig. 3a–c)" provenance.
- _7 value "In pathological conditions, PlGF is upregulated and stimulates angiogenesis via displacement of VEGF from VEGF-R1 to VEGFR2 and via activation of VEGFR-1, of which a larger fraction is membraneassociated." provenance.
- _5 value "Here we tested whether the related human LRIG1 (also called Lig-1) protein can act as a negative regulator of EGF receptor and its relatives, ErbB2, ErbB3, and ErbB4. We observed that in co-transfected 293T cells, LRIG1 forms a complex with each of the ErbB receptors independent of growth factor binding. We further observed that co-expression of LRIG1 with EGF receptor suppresses cellular receptor levels, shortens receptor half-life, and enhances ligand-stimulated receptor ubiquitination." provenance.
- _5 value "Here we tested whether the related human LRIG1 (also called Lig-1) protein can act as a negative regulator of EGF receptor and its relatives, ErbB2, ErbB3, and ErbB4. We observed that in co-transfected 293T cells, LRIG1 forms a complex with each of the ErbB receptors independent of growth factor binding. We further observed that co-expression of LRIG1 with EGF receptor suppresses cellular receptor levels, shortens receptor half-life, and enhances ligand-stimulated receptor ubiquitination." provenance.
- _5 value "We observed that EGFR, ErbB2, ErbB3, and ErbB4 each co-immunoprecipitated with the 145- kDa LRIG1, but co-immunoprecipitation of endogenous insulin receptor was not observed. These observations indicate that LRIG1 is capable of forming a specific complex with each of the receptors of the ErbB family." provenance.