Crossref Cited-by Linking logo

Collect. Czech. Chem. Commun. 1967, 32, 1229-1241
https://doi.org/10.1135/cccc19671229

Amino acids and peptides. LXIX. Synthesis of two biologically active analogues of deamino-oxytocin not containing a disulphide bond

K. Jošt and J. Rudinger

Crossref Cited-by Linking

  • Pilkington-Miksa Michael A., Writer Michele J., Sarkar Supti, Meng Qing-Hai, Barker Suzie E., Shamlou Parviz Ayazi, Hailes Helen C., Hart Stephen L., Tabor Alethea B.: Targeting Lipopolyplexes Using Bifunctional Peptides Incorporating Hydrophobic Spacer Amino Acids: Synthesis, Transfection, and Biophysical Studies. Bioconjugate Chem. 2007, 18, 1800. <https://doi.org/10.1021/bc0700943>
  • Rousslang K. W., Reid P. J., Holloway D. M., Haynes D. R., Dragavon J., Ross J. B. A.: Time-Resolved Phosphorescence of Tyrosine, Tyrosine Analogs, and Tyrosyl Residues in Oxytocin and Small Peptides. J Protein Chem 2002, 21, 547. <https://doi.org/10.1023/A:1022481706721>
  • Creighton Christopher J., Reitz Allen B.: Synthesis of an Eight-Membered Cyclic Pseudo-Dipeptide Using Ring Closing Metathesis. Org. Lett. 2001, 3, 893. <https://doi.org/10.1021/ol015530u>
  • Hlaváček Jan, Marcová Renáta, Buděšínský Miloš, Slaninová Jiřina: 1-Deamino-1(15)-carba and -Dicarba Analogues of Endothelin-1. Collect. Czech. Chem. Commun. 2000, 65, 407. <https://doi.org/10.1135/cccc20000407>
  • Rivard M., Maloň P., Čeřovský V.: Resolution of DL-2-aminosuberic acid via protease-catalyzed ester hydrolysis. Amino Acids 1998, 15, 389. <https://doi.org/10.1007/BF01320903>
  • Williams Robert M., Liu Jiwen: Asymmetric Synthesis of Differentially Protected 2,7-Diaminosuberic Acid, a Ring-Closure Metathesis Approach. J. Org. Chem. 1998, 63, 2130. <https://doi.org/10.1021/jo971575q>
  • RAMASUBBU N., PARTHASARATHY R.: Crystal structure of l‐2‐oxothiazolidine‐4‐carboxylic acid. International Journal of Peptide and Protein Research 1989, 34, 153. <https://doi.org/10.1111/j.1399-3011.1989.tb01505.x>
  • Ross J. B. Alexander, Laws William R., Buku Angeliki, Sutherland John Clark, Wyssbrod Herman R.: Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics. Biochemistry 1986, 25, 607. <https://doi.org/10.1021/bi00351a014>
  • Picur B., Siemion I. Z.: Rotational isomerism about the C‐αC‐β bonds in sulphur‐containing amino acids and their non‐sulphur‐containing isoesters. Org. Magn. Reson. 1983, 21, 271. <https://doi.org/10.1002/omr.1270210410>
  • FAHRENHOLZ Falk, HUSSEINI Hussein S., MORGAT Jean Louis, THIERAUCH Karl-Heinz: Tritium-markierte reaktive Analoga des [1,6-α-Aminosuberinsäure, 8-Arginin]Vasopressins (Desamino-dicarba-[8-Arginin]vasopressin). Synthese und Eigenschaften. Hoppe-Seyler´s Zeitschrift für physiologische Chemie 1982, 363, 1415. <https://doi.org/10.1515/bchm2.1982.363.2.1415>
  • CORT J.H., FISCHMAN A.J., DODDS W. JEAN, RAND J.H., SCHWARTZ I.L.: NEW CATEGORY OF VASOPRESSIN RECEPTOR IN THE CENTRAL NERVOUS SYSTEM. Evidence that This Receptor Mediates the Release of a Humoral Factor VIII‐Mobilizing Principle. International Journal of Peptide and Protein Research 1981, 17, 14. <https://doi.org/10.1111/j.1399-3011.1981.tb01963.x>
  • Kawano Keiichi, Kobayashi Yuji, Kyogoku Yoshimasa, Morikawa Tadanori, Sakakibara Shumpei: Conformational studies of oxytocin analogues with different ring sizes. Biochimica et Biophysica Acta (BBA) - Protein Structure 1979, 578, 87. <https://doi.org/10.1016/0005-2795(79)90116-8>
  • VEBER DANIEL F., HOLLY FREDERICK W., NUTT RUTH F., BERGSTRAND SUSAN J., BRADY STEPHEN F., HISRSCHMANN RALPH, GLITZER MONROE S., SAPERSTEIN RICHARD: Highly active cyclic and bicyclic somatostatin analogues of reduced ring size. Nature 1979, 280, 512. <https://doi.org/10.1038/280512a0>
  • Cheng-San Chen, Srikrishnan T., Parthasarathy R.: Conformation of L-cystathionine, a carba analog of cystine, and stereochemistry of hormone-receptor interactions. Biochimica et Biophysica Acta (BBA) - General Subjects 1978, 538, 534. <https://doi.org/10.1016/0304-4165(78)90414-2>
  • Losse G., Schumacher K.-J., Stange H.: Synthese eines kondensationsfähigen insulin-b15-20-hexapeptidderivates. Tetrahedron 1977, 33, 1817. <https://doi.org/10.1016/0040-4020(77)84065-9>
  • Fauchère Jean‐Luc, Muthukumaraswamy Natesa, Tun‐Kyi Aung, Schwyzer Robert: Hormone‐Receptor Interactions. Synthesis and Conformational Study of cyclo‐L‐Cystathionine. Helvetica Chimica Acta 1976, 59, 2187. <https://doi.org/10.1002/hlca.19760590631>
  • Morikawa T., Munekata E., Sakakibara S., Noda T., Otani M.: Synthesis of Eel-Calcitonin and [Asu1,7]-Eel-Calcitonin: Contribution of the disulfide bond to the hormonal activity. Experientia 1976, 32, 1104. <https://doi.org/10.1007/BF01927568>
  • Bodanszky Miklos, Henes Jill B.: Synthesis and properties of the cyclopentapeptide desthiomalformin. Bioorganic Chemistry 1975, 4, 212. <https://doi.org/10.1016/0045-2068(75)90010-3>
  • Cort J. H., Albrecht I., Noväkovä J., Mulder J. L., Jošt K.: Regional and Systemic Haemodynamic Effects of Some Vasopressins: Structural Features of the Hormone which Prolong Activity. Eur J Clin Investigation 1975, 5, 165. <https://doi.org/10.1111/j.1365-2362.1975.tb00443.x>
  • Cort J. H., Albrecht I., Nováková J., Mulder J. L., Jošt K.: Regional and Systemic Haemodynamic Effects of Some Vasopressins: Structural Features of the Hormone which Prolong Activity. Eur J Clin Investigation 1975, 5, 165. <https://doi.org/10.1111/j.1365-2362.1975.tb02283.x>
  • Cort J. H., Sedláková E., Kluh I., Mulder J. L.: NEUROPHYSIN BINDING AND NATRIURETIC PEPTIDES FROM THE POSTERIOR PITUITARY. Annals of the New York Academy of Sciences 1975, 248, 336. <https://doi.org/10.1111/j.1749-6632.1975.tb34196.x>
  • OKA Taichi, NAKANISHI Akira, OKADA Tadao: STUDIES ON PHARMACOLOGICAL AND BIOCHEMICAL PROPERTIES OF DEAMINO-DICARBA-[GLY7]-OXYTOCIN (Y-5350). Japanese Journal of Pharmacology 1975, 25, 15. <https://doi.org/10.1254/jjp.25.15>
  • Keller Oskar, Rudinger Josef: Synthesis of [1, 6‐α, α′‐Diaminosuberic acid]oxytocin (‘Dicarba‐oxytocin’). Helvetica Chimica Acta 1974, 57, 1253. <https://doi.org/10.1002/hlca.19740570502>
  • Barth Tomislav, Krejčí Ivan, Vaněčková Jiřina, Jošt Karel, Rychlík Ivan: Prolonged action of deamino-carba analogues of oxytocin on the rat uterus in vivo. European Journal of Pharmacology 1974, 25, 67. <https://doi.org/10.1016/0014-2999(74)90095-8>
  • Sperling R., Steinberg I. Z.: Simultaneous reduction and mercuration of disulfide bond A6-A11 of insulin by monovalent mercury. Biochemistry 1974, 13, 2007. <https://doi.org/10.1021/bi00707a002>
  • Sperling Ruth, Gorecki Marian: Role of the internal cross-link in oxytocin. Preparation of mercury mercaptide oxytocin derivatives. Biochemistry 1974, 13, 2347. <https://doi.org/10.1021/bi00708a017>
  • Yamanaka Tsutomu, Sakakibara Shumpei: Oxytocin Analogues Containing No Disulfide Bond. III. The Synthesis of Three Analogues of 1,6-Aminosuberic Acid-Oxytocin. Bulletin of the Chemical Society of Japan 1974, 47, 1228. <https://doi.org/10.1246/bcsj.47.1228>
  • Poláček Ivo, Krejčí Ivan, Nesvadba Hans, Rudinger Josef: Action of [1,6-Di-alanine]-oxytocin and [1,6-Di-serine]-oxytocin on the rat uterus and mammary gland in vitro. European Journal of Pharmacology 1970, 9, 239. <https://doi.org/10.1016/0014-2999(70)90306-7>
  • SCHILD H. O.: Lack of antagonism between thioglycerol and an oxytocin analogue not containing a disulphide bond. British J Pharmacology 1970, 39, 69. <https://doi.org/10.1111/j.1476-5381.1970.tb09556.x>
  • Kobayashi Akiko, Hase Satoe, Kiyoi Reiko, Sakakibara Shumpei: Oxytocin Analogues Containing No Disulfide Bond. I. Synthesis of the Lactam of l-Tyrosyl-l-isoleucyl-l-glutaminyl-l-asparaginyl-l-α-aminosuberyl-l-prolyl-l-leucylglycine Amide. Bulletin of the Chemical Society of Japan 1969, 42, 3491. <https://doi.org/10.1246/bcsj.42.3491>
  • Goodman Murray, Toniolo Claudio: Conformational studies of proteins with aromatic side‐chain effects. Biopolymers 1968, 6, 1673. <https://doi.org/10.1002/bip.1968.360061202>
  • Braun T., Jošt K., Rudinger J.: ‘Insulin-like’ action of an oxytocin analogue lacking a disulphide group, and of a cystathionine peptide related to a sequence of insulin, on rat epididymal adipose tissue in vitro. Experientia 1968, 24, 1060. <https://doi.org/10.1007/BF02138749>
  • Sakakibara Shumpei, Hase Satoe: Synthesis of an Analogue of Desamino-lysine-vasopressin Containing No Disulfide Bond. Bulletin of the Chemical Society of Japan 1968, 41, 2816. <https://doi.org/10.1246/bcsj.41.2816>
  • Marglin A., Cushman S.W.: A biological activity of the A-chain of insulin and the inactivity of a synthetic analogue containing an intact intrachain disulfide bridge. Biochemical and Biophysical Research Communications 1967, 29, 710. <https://doi.org/10.1016/0006-291X(67)90275-6>