PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11640967-3 2001 Several lines of evidence suggest that histamine decreases food intake via H(1)-receptors (H1R) at least in the ventromedial hypothalamus or the paraventricular nucleus. Histamine 39-48 histamine receptor H1 Mus musculus 75-89 11640967-3 2001 Several lines of evidence suggest that histamine decreases food intake via H(1)-receptors (H1R) at least in the ventromedial hypothalamus or the paraventricular nucleus. Histamine 39-48 histamine receptor H1 Mus musculus 91-94 1515368-0 1992 Transcriptional control of epidermal growth factor receptor by retinoic acid. Tretinoin 63-76 epidermal growth factor receptor Homo sapiens 27-59 1515368-5 1992 There is evidence for functional interactions between RA and the EGF receptor (EGFR). Tretinoin 54-56 epidermal growth factor receptor Homo sapiens 65-77 1515368-5 1992 There is evidence for functional interactions between RA and the EGF receptor (EGFR). Tretinoin 54-56 epidermal growth factor receptor Homo sapiens 79-83 1515368-6 1992 RA enhances the proliferative response of cultured keratinocytes to EGF, increases the number of EGFRs on the surface of some cells, and induces EGFR promoter activity in most cells. Tretinoin 0-2 epidermal growth factor receptor Homo sapiens 97-101 1515368-7 1992 In contrast, immunoprecipitation, Northern blot, and nuclear run-on analysis described in this paper show that RA suppresses EGFR synthesis at the transcriptional level in human epidermoid carcinoma ME180 cells. Tretinoin 111-113 epidermal growth factor receptor Homo sapiens 125-129 1584225-1 1992 The epidermal growth factor (EGF) receptor (EGFR) promoter is negatively regulated by thyroid hormone and retinoic acid. Tretinoin 106-119 epidermal growth factor receptor Homo sapiens 44-48 2340496-0 1990 Epidermal growth factor receptor expression in a retinoic acid-treated human melanoma cell line. Tretinoin 49-62 epidermal growth factor receptor Homo sapiens 0-32 1389683-0 1992 Suppression by retinoic acid of epidermal growth factor receptor autophosphorylation and glycosylation in cultured human head and neck squamous carcinoma cells. Tretinoin 15-28 epidermal growth factor receptor Homo sapiens 32-64 1389683-3 1992 Here we examined the effects of RA on the expression and function of EGF-R in two HNSCC cell lines, 1483 and 183, which exhibit distinct states of squamous cell differentiation, EGF-R mRNA levels, and responses to the growth inhibitory effects of RA. Tretinoin 32-34 epidermal growth factor receptor Homo sapiens 69-74 1389683-4 1992 Treatment with RA (1 microM, 7 days) of the RA-sensitive 1483 cells decreased the level of EGF-R mRNA two- to four-fold and the binding of 125I-EGF to the cell surface by 30%-35%. Tretinoin 15-17 epidermal growth factor receptor Homo sapiens 91-96 1389683-6 1992 Other effects of RA on EGF-R structure and function were similar in both cell lines. Tretinoin 17-19 epidermal growth factor receptor Homo sapiens 23-28 1389683-8 1992 More important, RA treatment of both cell lines decreased EGF-R autophosphorylation activity detected in immune-complex-kinase assay by about three- and five-fold in the 1483 and 183 cells, respectively. Tretinoin 16-18 epidermal growth factor receptor Homo sapiens 58-63 1389683-9 1992 Likewise, RA decreased the glycosylation of EGF-R in both cell lines. Tretinoin 10-12 epidermal growth factor receptor Homo sapiens 44-49 1389683-11 1992 These results demonstrate that RA can modify the structure of the EGF-R by decreasing its glycosylation and suggest that these changes may suppress the autophosphorylation activity of the receptor kinase. Tretinoin 31-33 epidermal growth factor receptor Homo sapiens 66-71 1389683-12 1992 The RA-induced changes in EGF-R do not correlate with the effect of RA on the growth of the cells but may be related to the suppression of squamous cell differentiation in the 1483 cells. Tretinoin 4-6 epidermal growth factor receptor Homo sapiens 26-31 2307713-0 1990 Inhibition of epidermal growth factor receptor activity by retinoic acid in glioma cells. Tretinoin 59-72 epidermal growth factor receptor Homo sapiens 14-46 2307713-2 1990 The protein tyrosine kinase activity of epidermal growth factor receptor (EGF-receptor) appeared to parallel the cell"s growth responsiveness to RA. Tretinoin 145-147 epidermal growth factor receptor Homo sapiens 40-72 2307713-2 1990 The protein tyrosine kinase activity of epidermal growth factor receptor (EGF-receptor) appeared to parallel the cell"s growth responsiveness to RA. Tretinoin 145-147 epidermal growth factor receptor Homo sapiens 74-86 2307713-3 1990 Cells sensitive to RA-induced growth inhibition exhibited a dose-dependent decrease in EGF-receptor activity, whereas RA-resistant cells showed no alterations in EGF-receptor protein tyrosine kinase activity or expression. Tretinoin 19-21 epidermal growth factor receptor Homo sapiens 87-99 2307713-4 1990 The modulation of EGF-receptor by RA was further examined with RA-sensitive (LG) and -resistant (NG-1) cell lines. Tretinoin 34-36 epidermal growth factor receptor Homo sapiens 18-30 2307713-8 1990 These results suggest RA-induced growth inhibition in sensitive cells may arise, at least in part, through alterations in EGF-receptor and structure. Tretinoin 22-24 epidermal growth factor receptor Homo sapiens 122-134 2575317-1 1989 The effects of 13-cis retinoic acid (RA) and dexamethasone on the levels of epidermal growth factor (EGF) receptor and fibroblast derived proteoglycan core protein (PG40) mRNAs were studied in human skin fibroblasts. Tretinoin 37-39 epidermal growth factor receptor Homo sapiens 76-114 34650910-10 2021 In vitro, treatment with the EGFR inhibitor gefitinib (ZD1839) reduced cell proliferation and survival of NB4 (ATRA-sensitive) and NB4-R2 (ATRA-resistant) cells. Tretinoin 111-115 epidermal growth factor receptor Homo sapiens 29-33 35078784-0 2022 Targeting S100A9-ALDH1A1-retinoic acid signaling to suppress brain relapse in EGFR-mutant lung cancer. Tretinoin 25-38 epidermal growth factor receptor Homo sapiens 78-82 2613750-0 1989 Modulation of transforming growth factor alpha-dependent expression of epidermal growth factor receptor gene by transforming growth factor beta, triiodothyronine, and retinoic acid. Tretinoin 167-180 epidermal growth factor receptor Homo sapiens 71-103 2613750-6 1989 Similarly, retinoic acid treatment also enhanced in a time- and dose-dependent manner the TGF alpha-dependent response of EGF receptor mRNA and acted synergistically with TGF beta 1. Tretinoin 11-24 epidermal growth factor receptor Homo sapiens 122-134 2912547-0 1989 Modulation of growth and epidermal growth factor receptor activity by retinoic acid in human glioma cells. Tretinoin 70-83 epidermal growth factor receptor Homo sapiens 25-57 31810919-6 2019 Importantly, PLX4032, when used in combination with ATRA, an inhibitor of PIN1, reduced EGFR expression, and consequently reduced cell viability and anchorage-independent growth of A375R cells compared to PLX4032 alone. Tretinoin 52-56 epidermal growth factor receptor Homo sapiens 88-92 23974111-0 2013 EGFR inhibitors exacerbate differentiation and cell cycle arrest induced by retinoic acid and vitamin D3 in acute myeloid leukemia cells. Tretinoin 76-89 epidermal growth factor receptor Homo sapiens 0-4 23974111-1 2013 By means of an unbiased, automated fluorescence microscopy-based screen, we identified the epidermal growth factor receptor (EGFR) inhibitors erlotinib and gefitinib as potent enhancers of the differentiation of HL-60 acute myeloid leukemia (AML) cells exposed to suboptimal concentrations of vitamin A (all-trans retinoic acid, ATRA) or vitamin D (1alpha,25-hydroxycholecalciferol, VD). Tretinoin 314-327 epidermal growth factor receptor Homo sapiens 91-123 23974111-1 2013 By means of an unbiased, automated fluorescence microscopy-based screen, we identified the epidermal growth factor receptor (EGFR) inhibitors erlotinib and gefitinib as potent enhancers of the differentiation of HL-60 acute myeloid leukemia (AML) cells exposed to suboptimal concentrations of vitamin A (all-trans retinoic acid, ATRA) or vitamin D (1alpha,25-hydroxycholecalciferol, VD). Tretinoin 314-327 epidermal growth factor receptor Homo sapiens 125-129 23974111-1 2013 By means of an unbiased, automated fluorescence microscopy-based screen, we identified the epidermal growth factor receptor (EGFR) inhibitors erlotinib and gefitinib as potent enhancers of the differentiation of HL-60 acute myeloid leukemia (AML) cells exposed to suboptimal concentrations of vitamin A (all-trans retinoic acid, ATRA) or vitamin D (1alpha,25-hydroxycholecalciferol, VD). Tretinoin 329-333 epidermal growth factor receptor Homo sapiens 91-123 23974111-1 2013 By means of an unbiased, automated fluorescence microscopy-based screen, we identified the epidermal growth factor receptor (EGFR) inhibitors erlotinib and gefitinib as potent enhancers of the differentiation of HL-60 acute myeloid leukemia (AML) cells exposed to suboptimal concentrations of vitamin A (all-trans retinoic acid, ATRA) or vitamin D (1alpha,25-hydroxycholecalciferol, VD). Tretinoin 329-333 epidermal growth factor receptor Homo sapiens 125-129 23644172-7 2013 We found that EGFR inhibitor AG1478 prevented the increase in VEGF-A production induced by PGE2- and all-trans retinoic acid. Tretinoin 111-124 epidermal growth factor receptor Homo sapiens 14-18 23644172-9 2013 PGE2 and all-trans retinoic acid also increased EGFR phosphorylation and this effect was sensitive to antagonists of EP receptors. Tretinoin 9-32 epidermal growth factor receptor Homo sapiens 48-52 23644172-10 2013 The role of intracellular PGE2 was indicated by two facts; i) PGE2-induced EGFR phosphorylation was substantially prevented by inhibitor of prostaglandin uptake transporter bromocresol green and ii) all-trans retinoic acid treatment, which enhanced intracellular but not extracellular PGE2, had lower effect on EGFR phosphorylation upon pre-treatment with cyclooxygenase inhibitor diclofenac. Tretinoin 209-222 epidermal growth factor receptor Homo sapiens 75-79 21705183-1 2011 In the present report, we investigated the action of retinoic acid (RA) on the transactivation of the epidermal growth factor receptor (EGFR) gene promoter. Tretinoin 53-66 epidermal growth factor receptor Homo sapiens 102-134 21705183-1 2011 In the present report, we investigated the action of retinoic acid (RA) on the transactivation of the epidermal growth factor receptor (EGFR) gene promoter. Tretinoin 53-66 epidermal growth factor receptor Homo sapiens 136-140 21705183-1 2011 In the present report, we investigated the action of retinoic acid (RA) on the transactivation of the epidermal growth factor receptor (EGFR) gene promoter. Tretinoin 68-70 epidermal growth factor receptor Homo sapiens 102-134 21705183-1 2011 In the present report, we investigated the action of retinoic acid (RA) on the transactivation of the epidermal growth factor receptor (EGFR) gene promoter. Tretinoin 68-70 epidermal growth factor receptor Homo sapiens 136-140 21705183-7 2011 Our results suggest that the interference with the activity of Sp1 on the EGFR promoter could be related to the observed RA-mediated growth suppression of breast cancer cells. Tretinoin 121-123 epidermal growth factor receptor Homo sapiens 74-78 3021829-5 1986 Many studies have indicated that retinoic acid can markedly increase the number of cellular receptors for epidermal growth factor, which is partially encoded by another oncogene, erb-B. Tretinoin 33-46 epidermal growth factor receptor Homo sapiens 179-184 28684780-0 2017 Retinoic Acid affects Lung Adenocarcinoma growth by inducing differentiation via GATA6 activation and EGFR and Wnt inhibition. Tretinoin 0-13 epidermal growth factor receptor Homo sapiens 102-106 28684780-5 2017 In addition, our results demonstrate that RA inhibits EGFR and Wnt signaling activation, two pathways involved in NSCLC progression. Tretinoin 42-44 epidermal growth factor receptor Homo sapiens 54-58 28684780-6 2017 Furthermore, we uncovered a novel mechanism in NSCLC that shows how RA exerts its function; we found that RA-mediated GATA6 activation is necessary for EGFR and Wnt inhibition, thus leading to 1) increased differentiation and 2) loss of proliferation. Tretinoin 68-70 epidermal growth factor receptor Homo sapiens 152-156 28684780-6 2017 Furthermore, we uncovered a novel mechanism in NSCLC that shows how RA exerts its function; we found that RA-mediated GATA6 activation is necessary for EGFR and Wnt inhibition, thus leading to 1) increased differentiation and 2) loss of proliferation. Tretinoin 106-108 epidermal growth factor receptor Homo sapiens 152-156