Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Steven C. Koerber"'
Autor:
Charleen Miller, Glenn Croston, Manoj P. Samant, Jean Rivier, Doley J. Hong, Steven C. Koerber, Catherine Rivier
Publikováno v:
The Journal of Peptide Research. 65:284-291
Degarelix is a potent very long-acting GnRH antagonist after subcutaneous administration. In this paper, we describe the synthesis of two analogs of degarelix incorporating racemic 3-(2-methoxy-5-pyridyl)-alanine (2-OMe-5Pal, 5) at position 3. The tw
Autor:
Jean Rivier, Jean Claude Reubi, Christy R. Grace, Roland Riek, Steven C. Koerber, Judit Erchegyi
Publikováno v:
Journal of Medicinal Chemistry. 49:4487-4496
The three-dimensional NMR structures of six octapeptide agonist analogues of somatostatin (SRIF) in the free form are described. These analogues, with the basic sequence H-DPhe/Phe2-c[Cys3-Xxx7-DTrp8-Lys9-Thr10-Cys14]-Thr-NH2 (the numbering refers to
Autor:
Ernest Giralt, Margarida Gairí, Sergio Madurga, Judit Erchegyi, Jean Rivier, Jean Claude Reubi, Xavier Roig, Steven C. Koerber, Pilar Saiz
Publikováno v:
Journal of Peptide Science. 12:82-91
The three-dimensional structure of a potent SSTR3-selective analogue of somatostatin, cyclo(3-14)H-Cys(3)-Phe(6)-Tyr(7)-D-Agl(8)(N(beta) Me, 2-naphthoyl)-Lys(9)-Thr(10)-Phe(11)-Cys(14)-OH (des-AA(1, 2, 4, 5, 12, 13)[Tyr(7), D-Agl(8)(N(beta) Me, 2-nap
Publikováno v:
Journal of Biological Chemistry. 278:21129-21135
Activins, like other members of the transforming growth factor-beta (TGF-beta) superfamily, initiate signaling by assembling a complex of two types of transmembrane serine/threonine receptor kinases classified as type II (ActRII or ActRIIB) and type
Autor:
Wylie Vale, Jean Claude Reubi, J. Gulyas, Lei Wang, Dean A. Kirby, V Martinez, Marilyn H. Perrin, Steven C. Koerber, Jean Rivier, William Low, Koichi S. Kunitake, Beatrice Waser, Michael R. DiGruccio, Yvette Taché, Joan Vaughan
Publikováno v:
Journal of Medicinal Chemistry. 45:4737-4747
We present evidence that members of the corticotropin releasing factor (CRF) family assume distinct structures when interacting with the CRF(1) and CRF(2) receptors. Predictive methods, physicochemical measurements, and structure-activity relationshi
Publikováno v:
European Journal of Mass Spectrometry. 7:259-266
We report the electrospray mass spectra and tandem mass (MS/MS) spectra of a series of chemically-stable somatostatin (SRIF) and gonadotropin-releasing hormone (GnRH) analogs which incorporate acylated or alkylated/acylated aminoglycine residues (bet
Publikováno v:
Journal of Medicinal Chemistry. 43:819-828
Little is known of the conformation of peptide hormones as they interact with their receptors for a number of reasons: peptide hormones are notoriously flexible in solution, their receptors are particularly complex, and there is strong evidence that
Autor:
J. Gulyas, Anne Z. Corrigan, Jean Rivier, S L Lahrichi, Wylie Vale, A. G. Craig, Steven C. Koerber, Catherine Rivier
Publikováno v:
Journal of Medicinal Chemistry. 41:5002-5011
We hypothesized that covalent constraints such as side-chain to side-chain lactam rings would stabilize an alpha-helical conformation shown to be important for the recognition and binding of the human corticotropin-releasing factor (hCRF) C-terminal
Autor:
Arnold T. Hagler, John S. Porter, Anne Z. Corrigan, Jean Rivier, Guangcheng Jiang, S L Lahrichi, Lila M. Gierasch, Steven C. Koerber, Catherine Rivier, Josep Rizo, Wylie Vale
Publikováno v:
Human Reproduction. 11:133-147
To whom correspondence should be addressedWhile the clinical significance of gonadotrophin-releasing hormone (GnRH)agonists is well recognized, the potential use of GnRH antagonists in humansawaits the availability of potent analogues with no untowar
Autor:
Jean Rivier, Guangcheng Jiang, Carl A. Hoeger, John B. Porter, A. G. Craig, Steven C. Koerber, L. Simon
Publikováno v:
Proceedings of the National Academy of Sciences. 93:2031-2036
Betidamino acids (a contraction of "beta" position and "amide") are N'-monoacylated (optionally, N'-monoacylated and N-mono- or N,N'-dialkylated) aminoglycine derivatives in which each N'acyl/alkyl group may mimic naturally occurring amino acid side