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Volumn 11, Issue 1, 2005, Pages 45-52

β-Sulfonamido gonadotropin-releasing hormone analogs: Synthesis and evaluation of several parent hormone properties

Author keywords

sulfonamido surrogates; GnRH analogs

Indexed keywords

BETA SULFONAMIDO GONADORELIN DERIVATIVE; GONADORELIN DERIVATIVE; GONADORELIN[5 DETYROSINE]; GONADORELIN[BETA 6 ALANINE]; HORMONE DERIVATIVE; LUTEINIZING HORMONE; PSEUDOPEPTIDE; UNCLASSIFIED DRUG;

EID: 11944270364     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.596     Document Type: Article
Times cited : (4)

References (25)
  • 3
    • 0018168286 scopus 로고
    • Hypophysial responses to continuous and intermittent delivery of hypothalamic gonadotropin-releasing hormone
    • Belchets PE, Plant TM, Nakai Y, Keogh EJ, Knobil E. Hypophysial responses to continuous and intermittent delivery of hypothalamic gonadotropin-releasing hormone. Science 1978; 202 631-632.
    • (1978) Science , vol.202 , pp. 631-632
    • Belchets, P.E.1    Plant, T.M.2    Nakai, Y.3    Keogh, E.J.4    Knobil, E.5
  • 4
    • 0024117312 scopus 로고
    • Molecular mechanism of gonadotropin releasing hormone (GnRH) action. I. The GnRH receptors
    • Hazum E, Conn PM. Molecular mechanism of gonadotropin releasing hormone (GnRH) action. I. The GnRH receptors. Endocr Rev 1988; 9: 379-386.
    • (1988) Endocr. Rev. , vol.9 , pp. 379-386
    • Hazum, E.1    Conn, P.M.2
  • 5
    • 0032739426 scopus 로고    scopus 로고
    • Luteinizing hormone-releasing-hormone analogs: Their impact on the control of tumorigenesis
    • Schally AV. Luteinizing hormone-releasing-hormone analogs: their impact on the control of tumorigenesis. Peptides 1998; 20 1247-1262.
    • (1998) Peptides , vol.20 , pp. 1247-1262
    • Schally, A.V.1
  • 6
    • 0002493425 scopus 로고
    • Superagonists of LHRH for contraception in women
    • Labrie F, Belanger A, Dupont A (eds). Elsevier Science: Amsterdam
    • Nillius SJ, Bergquist C, Gudmundsson JA, Wide L. Superagonists of LHRH for contraception in women. In LHRH and Its Analogues, Labrie F, Belanger A, Dupont A (eds). Elsevier Science: Amsterdam, 1984;261-274.
    • (1984) LHRH and Its Analogues , pp. 261-274
    • Nillius, S.J.1    Bergquist, C.2    Gudmundsson, J.A.3    Wide, L.4
  • 7
    • 0016273916 scopus 로고
    • Enzymic degradation of luteinizing hormone-releasing hormone (LH-RH) by hypothalamic tissue
    • Koch Y, Baram T, Chobsieng, Fridkin M. Enzymic degradation of luteinizing hormone-releasing hormone (LH-RH) by hypothalamic tissue. Biochem. Biophys. Res. Commun. 1974; 61: 95-103.
    • (1974) Biochem. Biophys. Res. Commun. , vol.61 , pp. 95-103
    • Koch, Y.1    Baram, T.2    Chobsieng, A.3    Fridkin, M.4
  • 8
    • 0017327199 scopus 로고
    • Resistance of enzymatic degradation of LHRH analogues possessing increased biological activity
    • Koch Y, Baram T, Hazum E, Fridkin M. Resistance of enzymatic degradation of LHRH analogues possessing increased biological activity. Biochem. Biophys. Res. Commun. 1977; 74: 488-491.
    • (1977) Biochem. Biophys. Res. Commun. , vol.74 , pp. 488-491
    • Koch, Y.1    Baram, T.2    Hazum, E.3    Fridkin, M.4
  • 10
    • 0033775341 scopus 로고    scopus 로고
    • An efficient synthesis of N-protected β-aminoethanesulfonyl chlorides: Versatile building blocks for the synthesis of oligopeptidosulfonamides
    • Brouwer AJ, Monnee MCF, Liskamp RMJ. An efficient synthesis of N-protected β-aminoethanesulfonyl chlorides: versatile building blocks for the synthesis of oligopeptidosulfonamides. Synthesis 2000;1579-1584.
    • (2000) Synthesis , pp. 1579-1584
    • Brouwer, A.J.1    Monnee, M.C.F.2    Liskamp, R.M.J.3
  • 11
    • 0021276063 scopus 로고
    • A different effect of trypsin on pituitary gonadotropin-releasing hormone receptors from intact and ovarioctomized rats. Evidence for the existence of two distinct receptor populations
    • Liscovitch M, Ben-Aroya N, Meidan R, Koch Y. A different effect of trypsin on pituitary gonadotropin-releasing hormone receptors from intact and ovarioctomized rats. Evidence for the existence of two distinct receptor populations. Eur. J. Biochem. 1984; 140: 191-197.
    • (1984) Eur. J. Biochem. , vol.140 , pp. 191-197
    • Liscovitch, M.1    Ben-Aroya, N.2    Meidan, R.3    Koch, Y.4
  • 12
    • 0015029118 scopus 로고
    • Periovulatory patterns of rat serum follicle stimulating hormone and luteinizing hormone during the normal estrous cycle as revealed by radioimmunoassays: Effects of pentobarbital
    • Daane TA, Parlow AF. Periovulatory patterns of rat serum follicle stimulating hormone and luteinizing hormone during the normal estrous cycle as revealed by radioimmunoassays: effects of pentobarbital. Endocrinology 1971; 88: 653-667.
    • (1971) Endocrinology , vol.88 , pp. 653-667
    • Daane, T.A.1    Parlow, A.F.2
  • 13
    • 0032489414 scopus 로고    scopus 로고
    • Theoretical investigation of phosphonamidates and sulfonamides as protease transition state isosteres
    • Radikiewicz JL, McAllister MA, Goldstein E, Houk KN. Theoretical investigation of phosphonamidates and sulfonamides as protease transition state isosteres. J. Org. Chem. 1998: 63: 1419-1428.
    • (1998) J. Org. Chem. , vol.63 , pp. 1419-1428
    • Radikiewicz, J.L.1    McAllister, M.A.2    Goldstein, E.3    Houk, K.N.4
  • 14
    • 0002903441 scopus 로고
    • Analog approaches to the structure of the transition state in the enzyme reaction
    • Wolfenden R. Analog approaches to the structure of the transition state in the enzyme reaction. Acc. Chem. Res. 1972; 5 10-18.
    • (1972) Acc. Chem. Res. , vol.5 , pp. 10-18
    • Wolfenden, R.1
  • 15
    • 0015924871 scopus 로고
    • Enzymatic catalysis and transition-state theory
    • Lienhard GE. Enzymatic catalysis and transition-state theory. Science 1973; 180: 1949-1954.
    • (1973) Science , vol.180 , pp. 1949-1954
    • Lienhard, G.E.1
  • 16
    • 0033018532 scopus 로고    scopus 로고
    • Increased stability of peptidosulfonamide peptidomimetics towards protease catalyzed degradation
    • De Bont DBA, Sliedregt-Bol KM, Hofmeyer LJF, Liskamp RMJ. Increased stability of peptidosulfonamide peptidomimetics towards protease catalyzed degradation. Bioorg. Med. Chem. 1999; 7: 1043-1047.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 1043-1047
    • De Bont, D.B.A.1    Sliedregt-Bol, K.M.2    Hofmeyer, L.J.F.3    Liskamp, R.M.J.4
  • 17
    • 0022665939 scopus 로고
    • Gonadotropin-releasing hormone analog design. Structure-function studies toward the development of agonists and antagonists: Rationale and perspective
    • Karten MJ, Rivier JE. Gonadotropin-releasing hormone analog design. Structure-function studies toward the development of agonists and antagonists: rationale and perspective. Endocr. Rev. 1986; 7: 44-46.
    • (1986) Endocr. Rev. , vol.7 , pp. 44-46
    • Karten, M.J.1    Rivier, J.E.2
  • 18
    • 0027184025 scopus 로고
    • Conformation-function relationships in LHRH analogs, I. Conformations of LHRH peptide backbone
    • Nikilforovich GV, Marshall GR. Conformation-function relationships in LHRH analogs, I. Conformations of LHRH peptide backbone. Int. J. Peptide Protein Res. 1993; 42: 171- 180.
    • (1993) Int. J. Peptide Protein Res. , vol.42 , pp. 171-180
    • Nikilforovich, G.V.1    Marshall, G.R.2
  • 19
    • 0027184026 scopus 로고
    • Conformation-function relationships in LHRH analogs, II. Conformations of LHRH peptide backbone
    • Nikiforovich GV, Marshall GR. Conformation-function relationships in LHRH analogs, II. Conformations of LHRH peptide backbone. Int. J. Peptide Protein Res. 1993: 42: 181-193.
    • (1993) Int. J. Peptide Protein Res. , vol.42 , pp. 181-193
    • Nikiforovich, G.V.1    Marshall, G.R.2
  • 20
    • 0018583540 scopus 로고
    • Circular dichroism study of the solution conformation of luteinizing hormone releasing hormone
    • Cann JR, Channabasavaiah K, Stewart JM. Circular dichroism study of the solution conformation of luteinizing hormone releasing hormone. Biochemistry 1979; 18: 5776-5781.
    • (1979) Biochemistry , vol.18 , pp. 5776-5781
    • Cann, J.R.1    Channabasavaiah, K.2    Stewart, J.M.3
  • 21
    • 0017048844 scopus 로고
    • Conformational characteristics of luliberin. Circular dichroism and fluorescence studies
    • Marche P, Montenay-Garestier T, Helene C, Fromageot P. Conformational characteristics of luliberin. Circular dichroism and fluorescence studies. Biochemistry 1976; 15: 5730-5737.
    • (1976) Biochemistry , vol.15 , pp. 5730-5737
    • Marche, P.1    Montenay-Garestier, T.2    Helene, C.3    Fromageot, P.4
  • 22
    • 0029953285 scopus 로고    scopus 로고
    • β-Peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by x-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability toward pepsin
    • Seebach D, Overhand M, Kühnle FNM, Martinoni B, Oberer L, Hommel U, Widmer H. β-Peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by x-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability toward pepsin. Helv. Chim. Acta 1996; 79: 913-941.
    • (1996) Helv. Chim. Acta , vol.79 , pp. 913-941
    • Seebach, D.1    Overhand, M.2    Kühnle, F.N.M.3    Martinoni, B.4    Oberer, L.5    Hommel, U.6    Widmer, H.7
  • 23
    • 0035471135 scopus 로고    scopus 로고
    • β-Peptides: From structure to function
    • Cheng RP, Gellman SH, DeGrado WF. β-Peptides: from structure to function. Chem. Rev. 2001; 101: 3219-3232.
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    DeGrado, W.F.3
  • 25
    • 4043089374 scopus 로고    scopus 로고
    • 2-amino acids - Syntheses, occurrence in natural products, and components of β-peptides
    • 2-amino acids - syntheses, occurrence in natural products, and components of β-peptides. Biopolymers 2004; 76: 206-243.
    • (2004) Biopolymers , vol.76 , pp. 206-243
    • Lelais, G.1    Seebach, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.