PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2497688-4 1989 To identify the TRH precursor in the rat hypothalamus, an antiserum was raised against the synthetic decapeptide sequence, Cys-Lys-Arg-Gln-His-Pro-Gly-Lys-Arg-Cys. Proline 143-146 thyrotropin releasing hormone Rattus norvegicus 16-19 2500333-2 1989 Within secretory granules, TRH-Gly is converted to TRH through alpha-amidation of the C-terminal proline residue, using Gly as the NH2 donor. Proline 97-104 thyrotropin releasing hormone Rattus norvegicus 27-30 2500352-0 1989 Radioimmunoassay for thyrotropin-releasing hormone precursor peptide, Lys-Arg-Gln-His-Pro-Gly-Arg-Arg. Proline 86-89 thyrotropin releasing hormone Rattus norvegicus 21-50 2500352-1 1989 A radioimmunoassay for thyrotropin-releasing hormone (TRH) precursor peptide Lys-Arg-Gln-His-Pro-Gly-Arg-Arg (pro-TRH), has been developed. Proline 93-96 thyrotropin releasing hormone Rattus norvegicus 23-52 2500352-1 1989 A radioimmunoassay for thyrotropin-releasing hormone (TRH) precursor peptide Lys-Arg-Gln-His-Pro-Gly-Arg-Arg (pro-TRH), has been developed. Proline 93-96 thyrotropin releasing hormone Rattus norvegicus 110-117 2500352-2 1989 Anti-pro-TRH antibody was raised in rabbits immunized with a conjugate of synthetic pro-TRH analog, Cys-Lys-Arg-Gln-His-Pro-Gly-Arg-Arg-Cys (pCC10) to bovine serum albumin. Proline 120-123 thyrotropin releasing hormone Rattus norvegicus 5-12 2500352-2 1989 Anti-pro-TRH antibody was raised in rabbits immunized with a conjugate of synthetic pro-TRH analog, Cys-Lys-Arg-Gln-His-Pro-Gly-Arg-Arg-Cys (pCC10) to bovine serum albumin. Proline 120-123 thyrotropin releasing hormone Rattus norvegicus 84-91 2493964-2 1989 In the present study, microinjection of 10 ng to 5 micrograms of TRH into the anterior hypothalamus (AHy) dose-dependently suppressed heat production in interscapular brown adipose tissue (BAT) in chloral hydrate-anaesthetized rats tested at a room temperature of 23 +/- 2 degrees C. This effect of TRH was mimicked by the structurally related peptides acid-TRH and luteinizing hormone releasing hormone (LH-RH), and by the TRH analog CG 3509, but not by the TRH fragments pGlu-His and His-Pro. Proline 490-493 thyrotropin releasing hormone Rattus norvegicus 65-68 3141416-2 1988 Rat thyrotropin-releasing hormone prohormone (pro-TRH) contains five separate copies of the TRH progenitor sequence: Gln-His-Pro-Gly. Proline 125-128 thyrotropin releasing hormone Rattus norvegicus 46-53 3141416-2 1988 Rat thyrotropin-releasing hormone prohormone (pro-TRH) contains five separate copies of the TRH progenitor sequence: Gln-His-Pro-Gly. Proline 125-128 thyrotropin releasing hormone Rattus norvegicus 50-53 3109876-1 1987 The sequence of rat hypothalamic pro-TRH, deduced by sequencing of cDNA, contains five copies of the TRH progenitor sequence Gln-His-Pro-Gly flanked by paired basic amino acid sequences. Proline 133-136 thyrotropin releasing hormone Rattus norvegicus 33-40 3109876-1 1987 The sequence of rat hypothalamic pro-TRH, deduced by sequencing of cDNA, contains five copies of the TRH progenitor sequence Gln-His-Pro-Gly flanked by paired basic amino acid sequences. Proline 133-136 thyrotropin releasing hormone Rattus norvegicus 37-40 3109909-2 1987 Peptides related to TRH were detected by trypsin digestion and radioimmunoassay with an antibody to TRH or an antibody raised against the pentapeptide Glp-His-Pro-Gly-Lys. Proline 159-162 thyrotropin releasing hormone Rattus norvegicus 20-23 3929378-1 1985 A rabbit antiserum to a peptide sequence present in the precursor for thyrotropin-releasing hormone (proTRH), deduced from cloned amphibian-skin complementary DNA, was raised by immunization with the synthetic decapeptide Cys-Lys-Arg-Gln-His-Pro-Gly-Lys-Arg-Cys (proTRH-SH). Proline 242-245 thyrotropin releasing hormone Rattus norvegicus 70-99 3099113-2 1986 A species specific protein with repetitive -Gln-His-Pro-Gly- sequences, which are flanked on the N- and C-terminus by paired basic residues, has been shown to be the source of TRH in frog skin and rat hypothalamus. Proline 52-55 thyrotropin releasing hormone Rattus norvegicus 176-179 3079917-3 1986 This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. Proline 59-62 thyrotropin releasing hormone Rattus norvegicus 137-140 3935272-5 1985 The unidirectional transport of TRH could not be saturated with unlabelled TRH at a concentration as high as 10 mM, but was markedly reduced by 10 mM proline and by the inhibitor of amidase and aminopeptidase activity, bacitracin (2 mM). Proline 150-157 thyrotropin releasing hormone Rattus norvegicus 32-35 3002750-10 1985 It was concluded that the substitution of proline amide, for proline thioamide group in TRH molecule did not change binding affinity to receptors in the central nervous system, but decreased biological effectiveness in CNS and substantially decreased the resistance to degradation in human and rat plasma. Proline 42-49 thyrotropin releasing hormone Rattus norvegicus 88-91 3103364-6 1987 The biological activity of TRH appears to be more effectively increased by replacing an H atom by an amyl group in the C-terminal amide function of the proline residue of TRH than by a tyramyl group in the same residue. Proline 152-159 thyrotropin releasing hormone Rattus norvegicus 27-30 3103364-6 1987 The biological activity of TRH appears to be more effectively increased by replacing an H atom by an amyl group in the C-terminal amide function of the proline residue of TRH than by a tyramyl group in the same residue. Proline 152-159 thyrotropin releasing hormone Rattus norvegicus 171-174 3104816-5 1987 The results are discussed with reference to the lack of specific binding sites in brain for the proposed neuropeptide and TRH metabolite cyclo(His-Pro). Proline 147-150 thyrotropin releasing hormone Rattus norvegicus 122-125 6799149-3 1982 These results suggest that factors in addition to TRH concentrations are important in determining the unique concentration pattern of cyclo-(His--Pro) in the brain. Proline 146-149 thyrotropin releasing hormone Rattus norvegicus 50-53 6424064-0 1983 Protein-energy malnutrition alters brain thyrotropin-releasing hormone and cyclo (His-Pro) in the neonatal rat. Proline 0-3 thyrotropin releasing hormone Rattus norvegicus 41-70 3920663-0 1985 Intraventricular administration of cyclo(His-Pro), a metabolite of thyrotropin-releasing hormone (TRH), decreases water intake in the rat. Proline 45-48 thyrotropin releasing hormone Rattus norvegicus 67-96 3920663-0 1985 Intraventricular administration of cyclo(His-Pro), a metabolite of thyrotropin-releasing hormone (TRH), decreases water intake in the rat. Proline 45-48 thyrotropin releasing hormone Rattus norvegicus 98-101 4995924-4 1971 With the use of synthetic thyrotropin-releasing hormone, detected by the Pauly reagent or with (125)1-labeled thyrotropin-releasing hormone as a marker, thin-layer chromatograms, paper electrophoresis, and carboxymethyl cellulose ion exchange chromatography revealed that only proline, histidine, and glutamic acid were consistently incorporated into peptides associated with the thyrotropin-releasing hormone region. Proline 277-284 thyrotropin releasing hormone Rattus norvegicus 26-55 169122-5 1975 In cultures treated with cycloheximide (10 mug/ml) or proline (6.3 mM) the initial binding of [2,3-3H-Pro]TRH to receptors, measured after 1 h, was 97% or 102% of control. Proline 54-61 thyrotropin releasing hormone Rattus norvegicus 106-109 169122-6 1975 However, the incorporation of label from [2,3-3H-Pro]TRH into an acid-precipitable product after 22 h was inhibited by 81 and 74% by cycloheximide (1 mug/ml) and proline (2.5 mM). Proline 162-169 thyrotropin releasing hormone Rattus norvegicus 53-56 169122-7 1975 Formation of [2,3-3H] proline from [2,3-?3H-Pro] TRH was demonstrated by thin layer chromatography; the percentage of non-protein radioactivity with an Rf of proline increased from 20 to 80% in GH3 cells incubated 1 or 24 h with [2,3-3H-Pro]TRH. Proline 22-29 thyrotropin releasing hormone Rattus norvegicus 49-52 169122-7 1975 Formation of [2,3-3H] proline from [2,3-?3H-Pro] TRH was demonstrated by thin layer chromatography; the percentage of non-protein radioactivity with an Rf of proline increased from 20 to 80% in GH3 cells incubated 1 or 24 h with [2,3-3H-Pro]TRH. Proline 22-29 thyrotropin releasing hormone Rattus norvegicus 241-244 169122-8 1975 We conclude that after binding to receptors on GH3 cells, TRH is slowly metabolized to its constituent amino acids, and the products [2,3-3H]proline or [14C]histidine are incorporated into newly synthesized proteins. Proline 141-148 thyrotropin releasing hormone Rattus norvegicus 58-61 107022-3 1978 The increase in rate of formation of proline, a major plasma degradation product, was in very good agreement with the increase in rate of TRH degradation. Proline 37-44 thyrotropin releasing hormone Rattus norvegicus 138-141 15907950-2 2005 We have previously shown that a diketopiperazine structurally related to the TRH metabolite cyclo-his-pro reduces neuronal cell death in vitro and in vivo. Proline 102-105 thyrotropin releasing hormone Rattus norvegicus 77-80 18354249-2 2008 We, and others, have previously reported that thyrotropin-releasing hormone (TRH, pGlu-His-Pro-NH(2)) and TRH-like peptides with the general structure pGlu-X-Pro-NH(2), where "X" can be any amino acid residue, have neuroprotective, antidepressant, analeptic, arousal, and anti-epileptic effects that could mediate the neuropsychiatric and therapeutic effects of a variety of neurotropic agents. Proline 91-94 thyrotropin releasing hormone Rattus norvegicus 46-75 18354249-2 2008 We, and others, have previously reported that thyrotropin-releasing hormone (TRH, pGlu-His-Pro-NH(2)) and TRH-like peptides with the general structure pGlu-X-Pro-NH(2), where "X" can be any amino acid residue, have neuroprotective, antidepressant, analeptic, arousal, and anti-epileptic effects that could mediate the neuropsychiatric and therapeutic effects of a variety of neurotropic agents. Proline 91-94 thyrotropin releasing hormone Rattus norvegicus 77-80 15665420-2 2004 The metabolic product of TRH (cyclo-his-pro) retains physiological activity. Proline 14-17 thyrotropin releasing hormone Rattus norvegicus 25-28 12186408-1 2002 Prolyl endopeptidase (PEP, EC 3.4.21.26) has been proposed to play a role in degradation of proline-containing neuropeptides involved in the processes of learning and memory, e.g., vasopressin, substance P, and thyrotropin-releasing hormone (TRH). Proline 92-99 thyrotropin releasing hormone Rattus norvegicus 211-240 7577928-3 1995 In contrast, Pro1TRH, which has a protonated proline in place of the pGlu of TRH, was 10 times more potent for the N289D receptor than for the wild-type. Proline 45-52 thyrotropin releasing hormone Rattus norvegicus 17-20 9435528-4 1997 Enzymatic degradation of TRH in vivo produces other bioactive peptides such as cyclo(His-Pro). Proline 89-92 thyrotropin releasing hormone Rattus norvegicus 25-28 9435528-7 1997 TRH and its metabolite cyclo(His-Pro) dose dependently inhibited 2-deoxy-D-glucose (2-DG)-stimulated pancreatic secretion. Proline 33-36 thyrotropin releasing hormone Rattus norvegicus 0-3 7595540-2 1995 Five copies of the TRH progenitor sequence (Gln-His-Pro-Gly) and seven cryptic peptides are formed following posttranslational proteolytic cleavage of the 26-kDa rat proTRH precursor. Proline 52-55 thyrotropin releasing hormone Rattus norvegicus 19-22 7664666-2 1995 Rat pro-TRH contains five copies of the TRH progenitor sequence (Gln-His-Pro-Gly) and seven other cryptic peptides. Proline 73-76 thyrotropin releasing hormone Rattus norvegicus 4-11 21554653-8 1992 The in vitro GH-releasing bioactivities of synthetic TRH and a milk extract purified in C(18) reversed-phase chromatography were abolished by proline-specific endopeptidase. Proline 142-149 thyrotropin releasing hormone Rattus norvegicus 53-56 1314591-1 1992 Analogs of thyrotropin-releasing hormone (Glp-His-Pro-NH2, TRH) have been prepared which contain thioamide moieties in the pyroglutamic acid ring, the carboxyamide proline terminus, and in both positions (dithio). Proline 164-171 thyrotropin releasing hormone Rattus norvegicus 11-40 1314591-1 1992 Analogs of thyrotropin-releasing hormone (Glp-His-Pro-NH2, TRH) have been prepared which contain thioamide moieties in the pyroglutamic acid ring, the carboxyamide proline terminus, and in both positions (dithio). Proline 50-53 thyrotropin releasing hormone Rattus norvegicus 11-40 2162041-1 1990 Rat thyrotropin-releasing hormone (TRH) prohormone contains five copies of the TRH progenitor sequence Gln-His-Pro-Gly linked together by connecting sequences whose biological activity is unknown. Proline 111-114 thyrotropin releasing hormone Rattus norvegicus 4-33 1681421-5 1991 Further investigations on these two cytosolic enzymes show that pyroglutamyl- and proline-containing peptides are inhibitors of each TRH-degrading enzyme. Proline 82-89 thyrotropin releasing hormone Rattus norvegicus 133-136 2113484-2 1990 TRH-extended peptides have been detected in the rat olfactory lobe: these peptides accounted for approximately 11% of the total TRH immunoreactivity present in the tissue and contained the sequence pGlu-His-Pro-Gly-Arg exclusively at their N-termini. Proline 207-210 thyrotropin releasing hormone Rattus norvegicus 0-3 1421205-0 1992 Effects of dexamethasone on TRH and TRH precursor peptide (Lys-Arg-Gln-His-Pro-Gly-Arg-Arg) levels in various rat organs. Proline 75-78 thyrotropin releasing hormone Rattus norvegicus 36-39 1421205-1 1992 The effect of an acute dexamethasone administration on thyrotropin-releasing hormone (TRH) and TRH precursor peptide (Lys-Arg-Gln-His-Pro-Gly-Arg-Arg) (p-8) levels in various rat organs has been studied. Proline 134-137 thyrotropin releasing hormone Rattus norvegicus 95-98 1905410-0 1991 The effects of the TRH metabolite cyclo(His-Pro) and its analogs on feeding. Proline 44-47 thyrotropin releasing hormone Rattus norvegicus 19-22 1905410-1 1991 Cyclo(His-Pro), or cHP, is a putative metabolite of thyrotropin-releasing hormone (TRH), and, like TRH, can inhibit food intake but requires higher doses. Proline 10-13 thyrotropin releasing hormone Rattus norvegicus 52-81 1905410-1 1991 Cyclo(His-Pro), or cHP, is a putative metabolite of thyrotropin-releasing hormone (TRH), and, like TRH, can inhibit food intake but requires higher doses. Proline 10-13 thyrotropin releasing hormone Rattus norvegicus 83-86 1905410-1 1991 Cyclo(His-Pro), or cHP, is a putative metabolite of thyrotropin-releasing hormone (TRH), and, like TRH, can inhibit food intake but requires higher doses. Proline 10-13 thyrotropin releasing hormone Rattus norvegicus 99-102 2121465-1 1990 TRH (pGlu-His-Pro-NH2) arises from the post-translational processing of a larger precursor peptide containing multiple copies of the TRH progenitor sequence, Gln-His-Pro-Gly. Proline 14-17 thyrotropin releasing hormone Rattus norvegicus 0-3 2121465-1 1990 TRH (pGlu-His-Pro-NH2) arises from the post-translational processing of a larger precursor peptide containing multiple copies of the TRH progenitor sequence, Gln-His-Pro-Gly. Proline 14-17 thyrotropin releasing hormone Rattus norvegicus 133-136 2121465-1 1990 TRH (pGlu-His-Pro-NH2) arises from the post-translational processing of a larger precursor peptide containing multiple copies of the TRH progenitor sequence, Gln-His-Pro-Gly. Proline 166-169 thyrotropin releasing hormone Rattus norvegicus 0-3 2121465-1 1990 TRH (pGlu-His-Pro-NH2) arises from the post-translational processing of a larger precursor peptide containing multiple copies of the TRH progenitor sequence, Gln-His-Pro-Gly. Proline 166-169 thyrotropin releasing hormone Rattus norvegicus 133-136 2162041-1 1990 Rat thyrotropin-releasing hormone (TRH) prohormone contains five copies of the TRH progenitor sequence Gln-His-Pro-Gly linked together by connecting sequences whose biological activity is unknown. Proline 111-114 thyrotropin releasing hormone Rattus norvegicus 35-38 2162041-1 1990 Rat thyrotropin-releasing hormone (TRH) prohormone contains five copies of the TRH progenitor sequence Gln-His-Pro-Gly linked together by connecting sequences whose biological activity is unknown. Proline 111-114 thyrotropin releasing hormone Rattus norvegicus 79-82