Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Ronald C. ORLOWSKI"'
Publikováno v:
International Journal of Peptide and Protein Research. 27:501-507
According to the Chou-Fasman rules for predicting the secondary structures of proteins, the 12–20 portion of salmon calcitonin should adopt an alpha helical conformation. These residues would form an amphipathic helix and contribute to the solubili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f90cecafa3e4578cc7795214ebf2547f
https://doi.org/10.1111/j.1399-3011.1986.tb01048.x
https://doi.org/10.1111/j.1399-3011.1986.tb01048.x
Publikováno v:
International Journal of Peptide and Protein Research. 25:105-111
The conformational properties of a number of calcitonin analogs were studied by circular dichroism. The ability of dimyristoylphosphatidylglycerol, lyso-phosphatidycholine or sodium dodecyl sulfate to induce the formation of more highly ordered struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86c1958ddce923bce349f60d6eba80fb
https://doi.org/10.1111/j.1399-3011.1985.tb02152.x
https://doi.org/10.1111/j.1399-3011.1985.tb02152.x
Publikováno v:
Endocrinology. 127:163-169
Binding of the nonhelical salmon calcitonin (sCT) analog, [Gly8,Ala16]-des-Leu19-sCT to membrane preparations from rat brain could be analyzed in terms of two independent binding sites. The high and low affinity binding sites for this analog were nam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0efd5d7a5b61ae0331d78f5cda0d5ade
https://doi.org/10.1210/endo-127-1-163
https://doi.org/10.1210/endo-127-1-163
Publikováno v:
Biopolymers. 76(3)
The conformational and lipid binding properties of several calcitonin analogs were compared. These analogs were designed to have the central amphipathic helical region of salmon calcitonin and N- and C-terminal segments similar to human calcitonin. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63e66e02664000c30e2b95550e7448f0
https://pubmed.ncbi.nlm.nih.gov/15148685
https://pubmed.ncbi.nlm.nih.gov/15148685
Autor:
Claude D. Arnaud, W. Bastian, Katsumi Wakabayashi, Katsuya Uda, Takamitsu Hisada, Yujiro Kobgayashi, Ronald C. Orlowski
Publikováno v:
Biologicalpharmaceutical bulletin. 22(3)
Various derivatives of human calcitonin have been synthesized and their biological characteristics compared with those of existing calcitonins. The acute effects of these analogues in reducing serum calcium levels and suppressing appetite were assess
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08187b507fa6640789bf8fbcbba0329f
https://pubmed.ncbi.nlm.nih.gov/10220278
https://pubmed.ncbi.nlm.nih.gov/10220278
Publikováno v:
Japanese journal of pharmacology. 56(4)
Using 125I-salmon calcitonin (sCT) as a ligand, in vitro autoradiography of rat brain outlined specific anatomical localization of human calcitonin (hCT) sensitive binding sites. The results presented herein show that there are hCT sensitive binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08a435e7331c0247dae16c7949dc4f1b
https://pubmed.ncbi.nlm.nih.gov/1744996
https://pubmed.ncbi.nlm.nih.gov/1744996
Publikováno v:
European journal of biochemistry. 188(3)
Leucine residues at positions 12, 16 and 19 of salmon calcitonin were systematically replaced by alanine either one, two or three at a time. Substitution of Ala at positions 12 or 16 had the greatest effect on the structure of the peptide and on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffed25dc86d14d41c301ca0509ceda37
https://pubmed.ncbi.nlm.nih.gov/2331988
https://pubmed.ncbi.nlm.nih.gov/2331988
Publikováno v:
Japanese Journal of Pharmacology. 52:120
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83673b8eac30089a9f9730ac13d869ad
https://doi.org/10.1016/s0021-5198(19)55188-5
https://doi.org/10.1016/s0021-5198(19)55188-5
Publikováno v:
Journal of the American Chemical Society. 100:3912-3918
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e7322f404aad9f6a7069c5c3d6b92a39
https://doi.org/10.1021/ja00480a042
https://doi.org/10.1021/ja00480a042
Publikováno v:
European Journal of Biochemistry. 162:399-402
The disulfide bridge formed between the cysteine residues at positions 1 and 7 of salmon calcitonin (sCT) is not required for biological activity. The analogues [Ala1,7]sCT,[AcmCys1,7]sCT and [AmcCys1,Ala7]sCT (AcmC = S-acetamido-methylcysteine) are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2120983167f20af5b80604dc5117e21
https://doi.org/10.1111/j.1432-1033.1987.tb10615.x
https://doi.org/10.1111/j.1432-1033.1987.tb10615.x