Ignet

Gene Information

Gene symbol: TRHR

Gene name: thyrotropin-releasing hormone receptor

HGNC ID: 12299

Related Genes

#	Gene Symbol	Number of hits
1	EGF	1 hits
2	EGFR	1 hits
3	GNAQ	1 hits
4	GPBAR1	1 hits
5	LRSAM1	1 hits
6	PLCB1	1 hits
7	PRKCA	1 hits
8	TRH	1 hits
9	TSHB	1 hits

Related Sentences

#	PMID	Sentence
1	8772588	Screening of candidate oncogenes in human thyrotroph tumors: absence of activating mutations of the G alpha q, G alpha 11, G alpha s, or thyrotropin-releasing hormone receptor genes.
2	8772588	We hypothesized that a subset of thyrotroph tumors might be caused by dominant somatic mutations that lead to inappropriate activation of the Gq/phospholipase C beta/Ca2+/protein kinase C. pathway normally triggered by occupancy of the TRH receptor (TRHR).
3	8772588	Screening of candidate oncogenes in human thyrotroph tumors: absence of activating mutations of the G alpha q, G alpha 11, G alpha s, or thyrotropin-releasing hormone receptor genes.
4	8772588	We hypothesized that a subset of thyrotroph tumors might be caused by dominant somatic mutations that lead to inappropriate activation of the Gq/phospholipase C beta/Ca2+/protein kinase C. pathway normally triggered by occupancy of the TRH receptor (TRHR).
5	9628246	Thyrotropin-releasing hormone and somatostatin inhibit each others release in vitro in the rat retina.
6	9628246	The effect of thyrotropin-releasing hormone (TRH), somatostatin (SS) or octreotide, an analogue of SS, on release of TRH or SS from the rat retina was studied in vitro.
7	9628246	The SS release from the retina was inhibited by TRH, and the inhibitory effect of TRH on SS release from the rat retina was blocked by the addition of anti-TRH receptor antiserum immunoglobulin fraction.
8	11964021	In the former case, alterations of only two genes, TSHbeta and the TRH receptor, have so far been described as responsible for the disorder.
9	11964021	In hereditary CH associated with CPHD, inactivating mutations of different pituitary transcription factors (HESX1, PROP-1, POU1F1) have been found involved in the pathogenesis of the disease.
10	12683933	Two G protein-coupled receptors for TRH, TRH receptor type 1 (TRH-R1) and TRH receptor type 2 (TRH-R2), have been cloned from mammals.
11	12697690	Pharmacological studies of thyrotropin-releasing hormone (TRH) receptors from Xenopus laevis: is xTRHR3 a TRH receptor?
12	12697690	Previously, three receptors, xTRHR1, xTRHR2, and xTRHR3, were cloned from brain tissue of Xenopus laevis with primers designed using sequences from the mammalian TRH receptor (TRHR) subtype 1.
13	12697690	Pharmacological studies of thyrotropin-releasing hormone (TRH) receptors from Xenopus laevis: is xTRHR3 a TRH receptor?
14	12697690	Previously, three receptors, xTRHR1, xTRHR2, and xTRHR3, were cloned from brain tissue of Xenopus laevis with primers designed using sequences from the mammalian TRH receptor (TRHR) subtype 1.
15	15171688	Expression of thyrotropin-releasing hormone receptor in immortalized beta-cell lines and rat pancreas.
16	15171688	TRH increases insulin production in cultured beta-cells, suggesting that it might play a role in regulating pancreatic beta-cell function.
17	15171688	However, there is limited information on TRH receptor expression in the pancreas.
18	15171688	The aim of the present study was to explore the distribution of the TRH receptor in the pancreas and its function in pancreatic beta-cells.
19	15171688	TRH receptor type 1 (TRHR1) gene expression was detected by RT-PCR and verified by Northern blotting and immunoblotting in the beta-cell lines, INS-1 and betaTC-6, and the rat pancreatic organ.
20	15171688	The absence of TRH receptor type 2 expression in the tissue and cells indicated the tissue specificity of TRH receptor expression in the pancreas.
21	15171688	In addition, TRH induced epidermal growth factor (EGF) receptor phosphorylation with a half-maximum concentration of approximately 50 nM, whereas the high affinity analogue of TRH, MeTRH, was 1 nM.
22	15171688	This suggested that the affinity of TRH ligands for the TRH receptor influences the activation of EGF receptor phosphorylation in betaTC-6 cells.
23	15171688	Expression of thyrotropin-releasing hormone receptor in immortalized beta-cell lines and rat pancreas.
24	15171688	TRH increases insulin production in cultured beta-cells, suggesting that it might play a role in regulating pancreatic beta-cell function.
25	15171688	However, there is limited information on TRH receptor expression in the pancreas.
26	15171688	The aim of the present study was to explore the distribution of the TRH receptor in the pancreas and its function in pancreatic beta-cells.
27	15171688	TRH receptor type 1 (TRHR1) gene expression was detected by RT-PCR and verified by Northern blotting and immunoblotting in the beta-cell lines, INS-1 and betaTC-6, and the rat pancreatic organ.
28	15171688	The absence of TRH receptor type 2 expression in the tissue and cells indicated the tissue specificity of TRH receptor expression in the pancreas.
29	15171688	In addition, TRH induced epidermal growth factor (EGF) receptor phosphorylation with a half-maximum concentration of approximately 50 nM, whereas the high affinity analogue of TRH, MeTRH, was 1 nM.
30	15171688	This suggested that the affinity of TRH ligands for the TRH receptor influences the activation of EGF receptor phosphorylation in betaTC-6 cells.
31	15171688	Expression of thyrotropin-releasing hormone receptor in immortalized beta-cell lines and rat pancreas.
32	15171688	TRH increases insulin production in cultured beta-cells, suggesting that it might play a role in regulating pancreatic beta-cell function.
33	15171688	However, there is limited information on TRH receptor expression in the pancreas.
34	15171688	The aim of the present study was to explore the distribution of the TRH receptor in the pancreas and its function in pancreatic beta-cells.
35	15171688	TRH receptor type 1 (TRHR1) gene expression was detected by RT-PCR and verified by Northern blotting and immunoblotting in the beta-cell lines, INS-1 and betaTC-6, and the rat pancreatic organ.
36	15171688	The absence of TRH receptor type 2 expression in the tissue and cells indicated the tissue specificity of TRH receptor expression in the pancreas.
37	15171688	In addition, TRH induced epidermal growth factor (EGF) receptor phosphorylation with a half-maximum concentration of approximately 50 nM, whereas the high affinity analogue of TRH, MeTRH, was 1 nM.
38	15171688	This suggested that the affinity of TRH ligands for the TRH receptor influences the activation of EGF receptor phosphorylation in betaTC-6 cells.
39	15171688	Expression of thyrotropin-releasing hormone receptor in immortalized beta-cell lines and rat pancreas.
40	15171688	TRH increases insulin production in cultured beta-cells, suggesting that it might play a role in regulating pancreatic beta-cell function.
41	15171688	However, there is limited information on TRH receptor expression in the pancreas.
42	15171688	The aim of the present study was to explore the distribution of the TRH receptor in the pancreas and its function in pancreatic beta-cells.
43	15171688	TRH receptor type 1 (TRHR1) gene expression was detected by RT-PCR and verified by Northern blotting and immunoblotting in the beta-cell lines, INS-1 and betaTC-6, and the rat pancreatic organ.
44	15171688	The absence of TRH receptor type 2 expression in the tissue and cells indicated the tissue specificity of TRH receptor expression in the pancreas.
45	15171688	In addition, TRH induced epidermal growth factor (EGF) receptor phosphorylation with a half-maximum concentration of approximately 50 nM, whereas the high affinity analogue of TRH, MeTRH, was 1 nM.
46	15171688	This suggested that the affinity of TRH ligands for the TRH receptor influences the activation of EGF receptor phosphorylation in betaTC-6 cells.
47	15171688	Expression of thyrotropin-releasing hormone receptor in immortalized beta-cell lines and rat pancreas.
48	15171688	TRH increases insulin production in cultured beta-cells, suggesting that it might play a role in regulating pancreatic beta-cell function.
49	15171688	However, there is limited information on TRH receptor expression in the pancreas.
50	15171688	The aim of the present study was to explore the distribution of the TRH receptor in the pancreas and its function in pancreatic beta-cells.
51	15171688	TRH receptor type 1 (TRHR1) gene expression was detected by RT-PCR and verified by Northern blotting and immunoblotting in the beta-cell lines, INS-1 and betaTC-6, and the rat pancreatic organ.
52	15171688	The absence of TRH receptor type 2 expression in the tissue and cells indicated the tissue specificity of TRH receptor expression in the pancreas.
53	15171688	In addition, TRH induced epidermal growth factor (EGF) receptor phosphorylation with a half-maximum concentration of approximately 50 nM, whereas the high affinity analogue of TRH, MeTRH, was 1 nM.
54	15171688	This suggested that the affinity of TRH ligands for the TRH receptor influences the activation of EGF receptor phosphorylation in betaTC-6 cells.
55	15171688	Expression of thyrotropin-releasing hormone receptor in immortalized beta-cell lines and rat pancreas.
56	15171688	TRH increases insulin production in cultured beta-cells, suggesting that it might play a role in regulating pancreatic beta-cell function.
57	15171688	However, there is limited information on TRH receptor expression in the pancreas.
58	15171688	The aim of the present study was to explore the distribution of the TRH receptor in the pancreas and its function in pancreatic beta-cells.
59	15171688	TRH receptor type 1 (TRHR1) gene expression was detected by RT-PCR and verified by Northern blotting and immunoblotting in the beta-cell lines, INS-1 and betaTC-6, and the rat pancreatic organ.
60	15171688	The absence of TRH receptor type 2 expression in the tissue and cells indicated the tissue specificity of TRH receptor expression in the pancreas.
61	15171688	In addition, TRH induced epidermal growth factor (EGF) receptor phosphorylation with a half-maximum concentration of approximately 50 nM, whereas the high affinity analogue of TRH, MeTRH, was 1 nM.
62	15171688	This suggested that the affinity of TRH ligands for the TRH receptor influences the activation of EGF receptor phosphorylation in betaTC-6 cells.
63	15709754	Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: disulfide cross-linking and molecular modeling approaches.
64	15709754	The conformational changes at the cytoplasmic ends of transmembrane helices 5 and 6 (TMH5 and TMH6) of thyrotropin-releasing hormone (TRH) receptor type I (TRH-R1) during activation were analyzed by cysteine-scanning mutagenesis followed by disulfide cross-linking and molecular modeling.
65	15709754	Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: disulfide cross-linking and molecular modeling approaches.
66	15709754	The conformational changes at the cytoplasmic ends of transmembrane helices 5 and 6 (TMH5 and TMH6) of thyrotropin-releasing hormone (TRH) receptor type I (TRH-R1) during activation were analyzed by cysteine-scanning mutagenesis followed by disulfide cross-linking and molecular modeling.
67	17123625	Thyrotropin-releasing hormone (TRH), a tripeptide, exerts its biological effects through stimulation of cell-surface receptors, TRH-R, belonging to the superfamily of G protein-coupled receptors (GPCR).
68	17123625	Because of the intermediate size of TRH, it is smaller than polypeptide ligands that interact at GPCR ectodomains and larger than biogenic amines, which interact within GPCR transmembrane domains (TMD), the TRH/TRH-R complex probably shares properties of these 2 extremes, representing a unique system to study GPCR/ligand interactions.
69	17123625	In this review, we summarize the current knowledge of the structure-activity relationships in the TRH/TRH-R system.
70	17123625	Based on experimental data and the structural information acquired from computer simulations, we formulate a working hypothesis to describe the molecular events underlying the processes of TRH binding and TRH-R activation.
71	17123625	This hypothesis represents a starting point for understanding the biology of the TRH/TRH-R system on a molecular level and provides a basis for potential design of new potent and selective modulators of TRH-R's activity.
72	17123625	Thyrotropin-releasing hormone (TRH), a tripeptide, exerts its biological effects through stimulation of cell-surface receptors, TRH-R, belonging to the superfamily of G protein-coupled receptors (GPCR).
73	17123625	Because of the intermediate size of TRH, it is smaller than polypeptide ligands that interact at GPCR ectodomains and larger than biogenic amines, which interact within GPCR transmembrane domains (TMD), the TRH/TRH-R complex probably shares properties of these 2 extremes, representing a unique system to study GPCR/ligand interactions.
74	17123625	In this review, we summarize the current knowledge of the structure-activity relationships in the TRH/TRH-R system.
75	17123625	Based on experimental data and the structural information acquired from computer simulations, we formulate a working hypothesis to describe the molecular events underlying the processes of TRH binding and TRH-R activation.
76	17123625	This hypothesis represents a starting point for understanding the biology of the TRH/TRH-R system on a molecular level and provides a basis for potential design of new potent and selective modulators of TRH-R's activity.
77	17123625	Thyrotropin-releasing hormone (TRH), a tripeptide, exerts its biological effects through stimulation of cell-surface receptors, TRH-R, belonging to the superfamily of G protein-coupled receptors (GPCR).
78	17123625	Because of the intermediate size of TRH, it is smaller than polypeptide ligands that interact at GPCR ectodomains and larger than biogenic amines, which interact within GPCR transmembrane domains (TMD), the TRH/TRH-R complex probably shares properties of these 2 extremes, representing a unique system to study GPCR/ligand interactions.
79	17123625	In this review, we summarize the current knowledge of the structure-activity relationships in the TRH/TRH-R system.
80	17123625	Based on experimental data and the structural information acquired from computer simulations, we formulate a working hypothesis to describe the molecular events underlying the processes of TRH binding and TRH-R activation.
81	17123625	This hypothesis represents a starting point for understanding the biology of the TRH/TRH-R system on a molecular level and provides a basis for potential design of new potent and selective modulators of TRH-R's activity.
82	17123625	Thyrotropin-releasing hormone (TRH), a tripeptide, exerts its biological effects through stimulation of cell-surface receptors, TRH-R, belonging to the superfamily of G protein-coupled receptors (GPCR).
83	17123625	Because of the intermediate size of TRH, it is smaller than polypeptide ligands that interact at GPCR ectodomains and larger than biogenic amines, which interact within GPCR transmembrane domains (TMD), the TRH/TRH-R complex probably shares properties of these 2 extremes, representing a unique system to study GPCR/ligand interactions.
84	17123625	In this review, we summarize the current knowledge of the structure-activity relationships in the TRH/TRH-R system.
85	17123625	Based on experimental data and the structural information acquired from computer simulations, we formulate a working hypothesis to describe the molecular events underlying the processes of TRH binding and TRH-R activation.
86	17123625	This hypothesis represents a starting point for understanding the biology of the TRH/TRH-R system on a molecular level and provides a basis for potential design of new potent and selective modulators of TRH-R's activity.
87	17123625	Thyrotropin-releasing hormone (TRH), a tripeptide, exerts its biological effects through stimulation of cell-surface receptors, TRH-R, belonging to the superfamily of G protein-coupled receptors (GPCR).
88	17123625	Because of the intermediate size of TRH, it is smaller than polypeptide ligands that interact at GPCR ectodomains and larger than biogenic amines, which interact within GPCR transmembrane domains (TMD), the TRH/TRH-R complex probably shares properties of these 2 extremes, representing a unique system to study GPCR/ligand interactions.
89	17123625	In this review, we summarize the current knowledge of the structure-activity relationships in the TRH/TRH-R system.
90	17123625	Based on experimental data and the structural information acquired from computer simulations, we formulate a working hypothesis to describe the molecular events underlying the processes of TRH binding and TRH-R activation.
91	17123625	This hypothesis represents a starting point for understanding the biology of the TRH/TRH-R system on a molecular level and provides a basis for potential design of new potent and selective modulators of TRH-R's activity.
92	23087672	Taltirelin is a superagonist at the human thyrotropin-releasing hormone receptor.
93	23087672	In this study, we characterized TAL binding to and signaling by the human TRH receptor (TRH-R) in a model cell system.
94	23087672	We found that TAL exhibited lower binding affinities than TRH and lower signaling potency via the inositol-1,4,5-trisphosphate/calcium pathway than TRH.
95	23087672	However, TAL exhibited higher intrinsic efficacy than TRH in stimulating inositol-1,4,5-trisphosphate second messenger generation.
96	23087672	This is the first study that elucidates the pharmacology of TAL at TRH-R and shows that TAL is a superagonist at TRH-R.
97	23087672	Taltirelin is a superagonist at the human thyrotropin-releasing hormone receptor.
98	23087672	In this study, we characterized TAL binding to and signaling by the human TRH receptor (TRH-R) in a model cell system.
99	23087672	We found that TAL exhibited lower binding affinities than TRH and lower signaling potency via the inositol-1,4,5-trisphosphate/calcium pathway than TRH.
100	23087672	However, TAL exhibited higher intrinsic efficacy than TRH in stimulating inositol-1,4,5-trisphosphate second messenger generation.
101	23087672	This is the first study that elucidates the pharmacology of TAL at TRH-R and shows that TAL is a superagonist at TRH-R.
102	23087672	Taltirelin is a superagonist at the human thyrotropin-releasing hormone receptor.
103	23087672	In this study, we characterized TAL binding to and signaling by the human TRH receptor (TRH-R) in a model cell system.
104	23087672	We found that TAL exhibited lower binding affinities than TRH and lower signaling potency via the inositol-1,4,5-trisphosphate/calcium pathway than TRH.
105	23087672	However, TAL exhibited higher intrinsic efficacy than TRH in stimulating inositol-1,4,5-trisphosphate second messenger generation.
106	23087672	This is the first study that elucidates the pharmacology of TAL at TRH-R and shows that TAL is a superagonist at TRH-R.
107	15306657	A model of inverse agonist action at thyrotropin-releasing hormone receptor type 1: role of a conserved tryptophan in helix 6.
108	15306657	A binding pocket for thyrotropin-releasing hormone (TRH) within the transmembrane helices of the TRH receptor type 1 (TRH-R1) has been identified based on experimental evidence and computer simulations.
109	15306657	A model of inverse agonist action at thyrotropin-releasing hormone receptor type 1: role of a conserved tryptophan in helix 6.
110	15306657	A binding pocket for thyrotropin-releasing hormone (TRH) within the transmembrane helices of the TRH receptor type 1 (TRH-R1) has been identified based on experimental evidence and computer simulations.
111	15833733	Carboxyl tail cysteine mutants of the thyrotropin-releasing hormone receptor type 1 exhibit constitutive signaling: role of palmitoylation.
112	15833733	We studied the role of carboxyl tail cysteine residues and their palmitoylation in constitutive signaling by the thyrotropin-releasing hormone (TRH) receptor type 1 (TRH-R1) in transfected mammalian cells and in Xenopus laevis oocytes.
113	15833733	Carboxyl tail cysteine mutants of the thyrotropin-releasing hormone receptor type 1 exhibit constitutive signaling: role of palmitoylation.
114	15833733	We studied the role of carboxyl tail cysteine residues and their palmitoylation in constitutive signaling by the thyrotropin-releasing hormone (TRH) receptor type 1 (TRH-R1) in transfected mammalian cells and in Xenopus laevis oocytes.