PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16382339-3 2005 Oxidative stress and protein tyrosine nitration (PTN) are also observed in response to ammonia, inflammatory cytokines, such as TNF-alpha or interferons, and benzodiazepines with affinity to the peripheral benzodiazepine receptor (PBR). Benzodiazepines 158-173 translocator protein Rattus norvegicus 195-229 16382339-3 2005 Oxidative stress and protein tyrosine nitration (PTN) are also observed in response to ammonia, inflammatory cytokines, such as TNF-alpha or interferons, and benzodiazepines with affinity to the peripheral benzodiazepine receptor (PBR). Benzodiazepines 158-173 translocator protein Rattus norvegicus 231-234 14723961-4 2004 The compounds are aryloxyanilide derivatives, and identified with known PBR ligands such as benzodiazepine (1, Ro5-4864), isoquinoline (2, PK11195), imidazopyridine (3, Alpidem), and indole (5, FGIN-1-27) derivatives. Benzodiazepines 92-106 translocator protein Rattus norvegicus 72-75 14678758-3 2003 Because the functional role of the PBR is unknown, we confirm by immunohistochemistry and PCR (I) that this receptor is expressed on microglia in vitro and (II) that benzodiazepines modulate proliferation of microglial cells and the release of the inflammatory molecules nitric oxide (NO) and tumor necrosis factor-alpha (TNF-alpha) in cell culture supernatants of primary rat microglia. Benzodiazepines 166-181 translocator protein Rattus norvegicus 35-38 12023539-1 2002 In the present study, we have investigated the potential neuroprotective effects of a novel peripheral benzodiazepine binding site (PBR) ligand, 7-chloro-N,N,5-trimethyl-4-oxo-3-phenyl-3,5-dihydro-4H-pyridazino[4,5-b]indole-1-acetamide (SSR180575), in models of central and peripheral neurodegeneration in vivo and its effect on steroid concentrations in plasma and nervous tissue. Benzodiazepines 103-117 translocator protein Rattus norvegicus 132-135 1649940-1 1991 Diazepam binding inhibitor (DBI) is a 9-kD polypeptide that was first isolated in 1983 from rat brain by monitoring its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the extracellular domain of the type A receptor for gamma-aminobutyric acid (GABAA receptor) and from the mitochondrial BZD receptor (MBR) located on the outer mitochondrial membrane. Benzodiazepines 158-172 translocator protein Rattus norvegicus 313-339 7841044-7 1995 In contrast, both the isoquinoline carboxamide PK11195 and the benzodiazepine Ro 5-4864 ligands, displaying a high affinity for the MBR, did affect ALA-mediated phototoxicity, each markedly increasing the EC50 for cell photodestruction and thus exerting a photoprotective effect. Benzodiazepines 63-77 translocator protein Rattus norvegicus 132-135 10856895-1 2000 Peripheral benzodiazepine (BDZ) receptor (PBR) and diazepam-binding inhibitor/acyl-CoA-binding protein (DBI/ACBP) characterized as a ligand at central BDZ receptors, at PBR with involvement in the regulation of steroidogenesis, and as an intracellular acyl-CoA transporter, are both known to interact with BDZ in adult systems. Benzodiazepines 27-30 translocator protein Rattus norvegicus 42-45 10856895-1 2000 Peripheral benzodiazepine (BDZ) receptor (PBR) and diazepam-binding inhibitor/acyl-CoA-binding protein (DBI/ACBP) characterized as a ligand at central BDZ receptors, at PBR with involvement in the regulation of steroidogenesis, and as an intracellular acyl-CoA transporter, are both known to interact with BDZ in adult systems. Benzodiazepines 27-30 translocator protein Rattus norvegicus 169-172 7819126-1 1994 A recognition site for benzodiazepines structurally different from that linked to the gamma-aminobutyric acid receptor subtype A or the "central type" benzodiazepine receptor has been located mainly in the outer membranes of mitochondria and designated mitochondrial benzodiazepine receptor (MBR). Benzodiazepines 23-38 translocator protein Rattus norvegicus 253-290 7819126-1 1994 A recognition site for benzodiazepines structurally different from that linked to the gamma-aminobutyric acid receptor subtype A or the "central type" benzodiazepine receptor has been located mainly in the outer membranes of mitochondria and designated mitochondrial benzodiazepine receptor (MBR). Benzodiazepines 23-38 translocator protein Rattus norvegicus 292-295 7819126-2 1994 A putative endogenous ligand for MBR is the peptide, diazepam binding inhibitor (DBI), which inhibits benzodiazepine ligand binding in mitochondrial membranes. Benzodiazepines 102-116 translocator protein Rattus norvegicus 33-36 7990651-5 1994 Although 4"-Cl-diazepam affinity is reported to vary between tissues from different species, this is the first report of an in vivo hormone treatment induced change in the benzodiazepine type PBR affinity. Benzodiazepines 172-186 translocator protein Rattus norvegicus 192-195 8385255-1 1993 Since their first description as anomalous high affinity diazepam binding sites in rat peripheral tissues, the peripheral-type benzodiazepine receptor (PBR) has been increasingly studied to better understand nonneural effects of the benzodiazepines. Benzodiazepines 233-248 translocator protein Rattus norvegicus 152-155 1323506-1 1992 The effects of chronic benzodiazepine (BZD) treatment on rat peripheral-type benzodiazepine receptors (PBR) were studied. Benzodiazepines 39-42 translocator protein Rattus norvegicus 61-101 1323506-1 1992 The effects of chronic benzodiazepine (BZD) treatment on rat peripheral-type benzodiazepine receptors (PBR) were studied. Benzodiazepines 39-42 translocator protein Rattus norvegicus 103-106 1323506-5 1992 The results suggest that chronic BZD exposure differentially regulates PBR in peripheral organs. Benzodiazepines 33-36 translocator protein Rattus norvegicus 71-74 1649940-1 1991 Diazepam binding inhibitor (DBI) is a 9-kD polypeptide that was first isolated in 1983 from rat brain by monitoring its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the extracellular domain of the type A receptor for gamma-aminobutyric acid (GABAA receptor) and from the mitochondrial BZD receptor (MBR) located on the outer mitochondrial membrane. Benzodiazepines 158-172 translocator protein Rattus norvegicus 341-344 1649940-1 1991 Diazepam binding inhibitor (DBI) is a 9-kD polypeptide that was first isolated in 1983 from rat brain by monitoring its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the extracellular domain of the type A receptor for gamma-aminobutyric acid (GABAA receptor) and from the mitochondrial BZD receptor (MBR) located on the outer mitochondrial membrane. Benzodiazepines 174-177 translocator protein Rattus norvegicus 313-339 1649940-1 1991 Diazepam binding inhibitor (DBI) is a 9-kD polypeptide that was first isolated in 1983 from rat brain by monitoring its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the extracellular domain of the type A receptor for gamma-aminobutyric acid (GABAA receptor) and from the mitochondrial BZD receptor (MBR) located on the outer mitochondrial membrane. Benzodiazepines 174-177 translocator protein Rattus norvegicus 341-344 2167683-1 1990 To examine the relationship between PKBS, a 17-kD protein covalently photolabeled by [3H]PK 14105, and its association with peripheral-type benzodiazepine binding sites, rat adrenal mitochondrial fractions were photolabeled with [3H]PK 14105, solubilized in digitonin, and subjected to anion-exchange chromatography over Q-Sepharose. Benzodiazepines 140-154 translocator protein Rattus norvegicus 36-40 2167683-7 1990 These studies provide direct biochemical evidence that the recognition sites for benzodiazepines and isoquinoline carboxamides cofractionate in unison with the 17-kD PKBS protein, demonstrating an intimate relationship between this protein and the binding domains for peripheral-type benzodiazepine ligands. Benzodiazepines 81-96 translocator protein Rattus norvegicus 166-170 2167683-7 1990 These studies provide direct biochemical evidence that the recognition sites for benzodiazepines and isoquinoline carboxamides cofractionate in unison with the 17-kD PKBS protein, demonstrating an intimate relationship between this protein and the binding domains for peripheral-type benzodiazepine ligands. Benzodiazepines 81-95 translocator protein Rattus norvegicus 166-170 32989663-1 2021 OBJECTIVE: The activation of microglia in various brain pathologies is accompanied by an increase in the expression of peripheral benzodiazepine receptor/18 kDa translocator protein (PBR/TSPO). Benzodiazepines 130-144 translocator protein Rattus norvegicus 183-186 2555358-1 1989 This report describes the cloning of a full length cDNA encoding PKBS, a protein of approximately 17 kDa associated with peripheral-type benzodiazepine binding sites. Benzodiazepines 137-151 translocator protein Rattus norvegicus 65-69 2555358-6 1989 Northern analysis with this PKBS cDNA probe in different rat tissues revealed one RNA species of approximately 850 nucleotides exhibiting relative abundances qualitatively comparable with the densities of peripheral-type benzodiazepine binding sites in each tissue. Benzodiazepines 221-235 translocator protein Rattus norvegicus 28-32 2555358-11 1989 These studies suggest that PKBS comprises binding domains for benzodiazepines and isoquinoline carboxamides and hence is apparently responsible for the manifestation of peripheral-type benzodiazepine recognition sites. Benzodiazepines 62-77 translocator protein Rattus norvegicus 27-31 2555358-11 1989 These studies suggest that PKBS comprises binding domains for benzodiazepines and isoquinoline carboxamides and hence is apparently responsible for the manifestation of peripheral-type benzodiazepine recognition sites. Benzodiazepines 62-76 translocator protein Rattus norvegicus 27-31 32989663-1 2021 OBJECTIVE: The activation of microglia in various brain pathologies is accompanied by an increase in the expression of peripheral benzodiazepine receptor/18 kDa translocator protein (PBR/TSPO). Benzodiazepines 130-144 translocator protein Rattus norvegicus 187-191 20846531-3 2010 However, recent studies showed that BZD also act on peripheral benzodiazepine receptor sites (PBR) or translocator protein 18 kDa (TSPO). Benzodiazepines 36-39 translocator protein Rattus norvegicus 94-97 24067925-7 2014 Overall, these results indicate that YL-IPA08 is a more potent and selective TSPO ligand, which exerts antidepressant-like and anxiolytic-like effects on behaviors that are mediated by TSPO but does not cause the side effects that are typically associated with conventional benzodiazepines. Benzodiazepines 274-289 translocator protein Rattus norvegicus 77-81 21159950-2 2010 Although some BDZs also bind mitochondrial receptors [translocator protein (18 kDa) (TSPO)] and promote the synthesis of GABA-enhancing neurosteroids, the role of neurosteroids in the clinical effects of BDZs is unknown. Benzodiazepines 14-18 translocator protein Rattus norvegicus 85-89 23345228-2 2013 Recent studies have shown that the ligands of translocator protein (TSPO, 18 kDa), a peripheral receptor for benzodiazepine, modulate inflammatory pain. Benzodiazepines 109-123 translocator protein Rattus norvegicus 46-66 23345228-2 2013 Recent studies have shown that the ligands of translocator protein (TSPO, 18 kDa), a peripheral receptor for benzodiazepine, modulate inflammatory pain. Benzodiazepines 109-123 translocator protein Rattus norvegicus 68-72 32272540-1 2011 Peripheral-type benzodiazepine receptor (PBR) and central-type benzodiazepine receptor (CBR) in salivary gland play a role in the inhibitory regulation of salivary secretion in rodents. Benzodiazepines 16-30 translocator protein Rattus norvegicus 41-44 20846531-3 2010 However, recent studies showed that BZD also act on peripheral benzodiazepine receptor sites (PBR) or translocator protein 18 kDa (TSPO). Benzodiazepines 36-39 translocator protein Rattus norvegicus 131-135 19392661-7 2009 Specifically, benzodiazepine Ro5-4864 and protoporphyrin IX showed 5-13-fold lower affinity for duodenal TSPO. Benzodiazepines 14-28 translocator protein Rattus norvegicus 105-109 18333964-1 2008 The translocator protein (18 kDa; TSPO), formerly known as the peripheral benzodiazepine receptor, is an outer mitochondrial membrane protein that associates with the mitochondrial permeability transition pore to regulate both steroidogenesis and apoptosis. Benzodiazepines 74-88 translocator protein Rattus norvegicus 34-38