C: DGLU-ALA-ALLO-DILE-LEU-DTRP结构式
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常用名 | C: DGLU-ALA-ALLO-DILE-LEU-DTRP | 英文名 | BE-18257B |
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| CAS号 | 136553-74-7 | 分子量 | 612.71700 | |
| 密度 | 1.23g/cm3 | 沸点 | 1012.2ºC at 760 mmHg | |
| 分子式 | C31H44N6O7 | 熔点 | N/A | |
| MSDS | 美版 | 闪点 | 566ºC |
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An endothelin receptor (ETA) antagonist isolated from Streptomyces misakiensis.
Biochem. Biophys. Res. Commun. 178 , 132, (1991) A competitive endothelin (ET) antagonist, BE-18257B, was isolated from the fermentation products of Streptomyces misakiensis. It is a novel cyclic pentapeptide, cyclo(-D-Glu-L-Ala-allo-D-Ile-L-Leu-D-Trp-), and binds to ETA receptors (ET-1 selective) in cardio... |
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[Agonists and antagonists to endothelin receptors].
Tanpakushitsu Kakusan Koso. 38(11) , 1827-40, (1993)
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Effects of endothelin-1 and endothelin-A receptor antagonist on recovery after hypothermic cardioplegic ischemia in neonatal lamb hearts.
Circulation 92(9 Suppl) , II400-4, (1995) Prior studies suggest an important role for coronary endothelium in ischemia/reperfusion (I/R) injury. Decreased endothelial release of the vasodilator nitric oxide occurs after I/R, but the role of the endothelium-derived vasoconstrictor endothelin-1 (ET-1) ... |
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Involvement of ETA receptors in the facilitation by endothelin-1 of non-adrenergic non-cholinergic transmission in the rat urinary bladder.
Br. J. Pharmacol. 111(2) , 473-82, (1994) 1. Endothelin-1 (ET-1; 3-10 nM) raised the tone of rat bladders bathed in buffer containing atropine (1 microM) plus guanethidine (3.4 microM). In addition, ET-1 potentiated, in a concentration-dependent fashion (1-10 nM), the contractions evoked by both tran... |
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A conformational study by 1H NMR of a cyclic pentapeptide antagonist of endothelin.
J. Med. Chem. 36(18) , 2658-65, (1993) The selective endothelin antagonist cyclo(D-Glu-L-Ala-D-allo-Ile-L-Leu-D-Trp, BE18257B) has been synthesized via solid-phase methods and its solution conformation determined by NMR spectroscopy and simulated annealing calculations based on NOE constraints. Ad... |
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Endothelin-binding inhibitors, BE-18257A and BE-18257B. I. Taxonomy, fermentation, isolation and characterization.
J. Antibiot. 44(12) , 1342-7, (1991) Two endothelin (ET)-binding inhibitors, BE-18257A and BE-18257B, which antagonized 125I-ET-1 binding to a porcine aortic smooth muscle membrane, were isolated from the mycelium of a strain of Streptomyces misakiensis. These binding inhibitors were extracted w... |
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Endothelin-binding inhibitors, BE-18257A and BE-18257B II. Structure determination.
J. Antibiot. 44(12) , 1348-56, (1991) The structures of novel endothelin-binding inhibitors, BE-18257A and BE-18257B, were elucidated by spectral analyses and chemical studies. Both inhibitors were found to have a cyclic pentapeptide structure containing three D-form amino acid residues, namely, ... |
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WS-7338, new endothelin receptor antagonists isolated from Streptomyces sp. No. 7338. I. Taxonomy, fermentation, isolation, physico-chemical properties and biological activities.
J. Antibiot. 45 , 74-82, (1992) WS-7338 A, B, C and D, novel endothelin receptor antagonists, have been isolated from fermentation broth of Streptomyces sp. No. 7338. These antagonists were purified from the culture mycelium by extraction with acetone, followed by carbon column chromatograp... |
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Molecular modelling of the structures of endothelin antagonists. Identification of a possible structural determinant for ET-A receptor binding.
FEBS Lett. 310(1) , 83-7, (1992) Computer-aided molecular modelling of the endothelin (ET-A) receptor antagonists, BQ-123 and BE-18257B, shows that they have very similar 3D structures. Parts of their 3D structures are also shown to match closely with that reported for residues 6-8 in endoth... |
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Renal actions of endothelin-1 under endothelin receptor blockade by BE-18257B.
J. Urol. 159(2) , 563-6, (1998) Endothelin-1 (ET-1), a peptide produced by the vascular endothelium, causes profound renal vasoconstriction by binding to ET-A receptors. The present study examined the renal actions of ET-1 after ET-A receptors were blocked by BE-18257B to unmask the functio... |