Výsledky vyhledávání - "B V, Clineschmidt"

1-(((7,7-Dimethyl-2(S)-(2(S)-amino-4-(methylsulfonyl)butyramido)bicyclo[2.2.1]heptan-1(S)-yl)methyl)sulfonyl)-4-(2-methylphenyl)piperazine (L-368,899): An Orally Bioavailable, Non-Peptide Oxytocin Antagonist with Potential Utility for Managing Preterm Labor

Autor: P D, Williams, P S, Anderson, R G, Ball, M G, Bock, L, Carroll, S H, Chiu, B V, Clineschmidt, J C, Culberson, J M, Erb, B E, Evans

Publikováno v: Journal of Medicinal Chemistry. 37:565-571

Modifications to the previously reported spiroindenylpiperidine camphor-sulfonamide oxytocin (OT) antagonist L-366,509 have produced a new series of o-tolylpiperazine (TP) camphor-sulfonamides. A number of analogues in the TP series that incorporate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbee35be16d415185dfe2956648b8b43
https://doi.org/10.1021/jm00031a004

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Identification of an orally active, nonpeptidyl oxytocin antagonist

Autor: D J, Pettibone, B V, Clineschmidt, M T, Kishel, E V, Lis, D R, Reiss, C J, Woyden, B E, Evans, R M, Freidinger, D F, Veber, M J, Cook

Publikováno v: The Journal of pharmacology and experimental therapeutics. 264(1)

L-366,509, a member of a novel class of nonpeptidyl compounds, has been characterized as an orally active oxytocin (OT) antagonist. L-366,509 exhibits a moderate binding affinity (K(i) values, 370-780 nM) for the rat, rhesus and human uterine OT rece

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7dbbeece56505f49c8185ebdd907b8ea
https://pubmed.ncbi.nlm.nih.gov/8423533

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In vitro pharmacology of L-158,809, a new highly potent and selective angiotensin II receptor antagonist

Autor: R S, Chang, P K, Siegl, B V, Clineschmidt, N B, Mantlo, P K, Chakravarty, W J, Greenlee, A A, Patchett, V J, Lotti

Publikováno v: The Journal of pharmacology and experimental therapeutics. 262(1)

L-158,809 interacted in a competitive manner with rabbit aortic angiotensin II (AII) receptors as determined by Scatchard analysis of the specific binding of [125I]Sar1Ile8-AII. The affinity of L-158,809 (IC50 = 0.3 nM) for AII receptors in this tiss

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2214b8ef1810edd3bbc79f230d7f2839
https://pubmed.ncbi.nlm.nih.gov/1625192

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Radioligand binding studies reveal marked species differences in the vasopressin V1 receptor of rat, rhesus and human tissues

Autor: Roger M. Freidinger, Douglas J. Pettibone, Peter D. Williams, B. V. Clineschmidt, Maribeth T. Kishel, Carla J. Woyden, Mark G. Bock, Daniel F. Veber

Publikováno v: Life sciences. 50(25)

The [ 3 H]arginine-vasopressin ([ 3 H]AVP) binding site in rat, rhesus and human liver and nonpregnant human uterus was characterized and contrasted. [ 3 H]AVP bound with high affinity (K i values, 0.2–0.6 nM) to preparations of all tissues studied

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97913d5ca52b12d86927aaaa3529b456
https://pubmed.ncbi.nlm.nih.gov/1593923

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Antagonism of oxytocin in rats and pregnant rhesus monkeys by the novel cyclic hexapeptides, L-366,682 and L-366,948

Autor: B V, Clineschmidt, D J, Pettibone, D R, Reiss, E V, Lis, G J, Haluska, M J, Novy, M J, Cook, M A, Cukierski, M J, Kaufman, M G, Bock

Publikováno v: The Journal of pharmacology and experimental therapeutics. 256(3)

Two cyclic hexapeptides unrelated in chemical structure to oxytocin (OT) were shown in vivo to be antagonists of the contractile action of OT on the uterus. In anesthetized rats challenged with OT (1 micrograms/kg) administered as an i.v. bolus, L-36

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3bc80ee4c24aa903d6788c559ded54ee
https://pubmed.ncbi.nlm.nih.gov/2005582

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Potent and Selective Oxytocin Antagonists Obtained by Chemical Modification of a Streptomyces Silvensis Derived Cyclic Hexapeptide and by Total Synthesis

Autor: Roger M. Freidinger, R. D. Tung, Jill M. Erb, Willie L. Whitter, Peter D. Williams, Daniel F. Veber, N. P. Gould, Mark G. Bock, Robert M. DiPardo, Debra S. Perlow, George F. Lundell, Douglas J. Pettibone, Richard G. Ball, B. V. Clineschmidt

Publikováno v: Chemical Aspects of Enzyme Biotechnology ISBN: 9781475796391

Oxytocin (OT) is a neurohypophyseal hormone which has an important function in parturition.1 There is considerable evidence that the uterotonic action of OT and its stimulation of uterine prostaglandin release combine to initiate labor.2,3 Additional

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ee0a89b1a195dd3cd67d09cbb1b5bd26
https://doi.org/10.1007/978-1-4757-9637-7_11

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