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Volumn 38, Issue 3, 1995, Pages 435-442

Phosphinyl Acid-Based Bisubstrate Analog Inhibitors of Ras Famesyl Protein Transferase

Author keywords

[No Author keywords available]

Indexed keywords

FARNESYL TRANS TRANSFERASE; N [N [N [3 [HYDROXY(3,7,11 TRIMETHYL 1 OXO 2,6,10 DODECATRIENYL)PHOSPHINYL] 1 OXOPROPYL]VALYL]VALYL]METHIONINE; N [N [N [[[HYDROXY(3,7,11 TRIMETHYL 2,6,10 DODECATRIENYL)PHOSPHINYL]OXY]ACETYL]VALYL]LEUCYL]SERINE; N [N [N [[[HYDROXY(3,7,11 TRIMETHYL 2,6,10 DODECATRIENYL)PHOSPHINYL]OXY]ACETYL]VALYL]VALYL]METHIONINE; UNCLASSIFIED DRUG;

EID: 0029025272     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm00003a006     Document Type: Article
Times cited : (78)

References (36)
  • 3
    • 0025940718 scopus 로고
    • Isoprenoid Modification and Plasma Membrane Association: Critical Factors for Ras Oncogenicity
    • Der, C. J.; Cox, A. D. Isoprenoid Modification and Plasma Membrane Association: Critical Factors for Ras Oncogenicity. Cancer Cells 1991, 3, 331-340.
    • (1991) Cancer Cells , vol.3 , pp. 331-340
    • Der, C.J.1    Cox, A.D.2
  • 4
    • 0027284950 scopus 로고
    • Protein Prenylation: A Mediator of ProteinProtein Interactions
    • Marshall, C. J. Protein Prenylation: A Mediator of ProteinProtein Interactions. Science 1993, 259, 1865-1866.
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marshall, C.J.1
  • 9
    • 0025877861 scopus 로고
    • Ras C-Terminal Processing Enzymes-New Drug Targets?
    • Gibbs, J. B. Ras C-Terminal Processing Enzymes-New Drug Targets? Cell 1991, 65, 1-4.
    • (1991) Cell , vol.65 , pp. 1-4
    • Gibbs, J.B.1
  • 18
    • 0026657881 scopus 로고
    • Divalent Cation and Prenyl Pyrophosphate Specificities of the Protein Famesyltransferase from Rat Brain, a Zinc Metalloenzyme
    • Reiss, Y.; Brown, M. S.; Goldstein, J. L. Divalent Cation and Prenyl Pyrophosphate Specificities of the Protein Famesyltransferase from Rat Brain, a Zinc Metalloenzyme. J. Biol. Chem. 1992, 267, 6403-6408.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6403-6408
    • Reiss, Y.1    Brown, M.S.2    Goldstein, J.L.3
  • 20
    • 0020321280 scopus 로고
    • Angiotensin-Converting Enzyme Inhibitors: Medicinal Chemistry and Biological Actions
    • Petrillo, E. W., Jr.; Ondetti, M. A. Angiotensin-Converting Enzyme Inhibitors: Medicinal Chemistry and Biological Actions. Med. Res. Rev. 1982, 2, 1-41.
    • (1982) Med. Res. Rev. , vol.2 , pp. 1-41
    • Petrillo, E.W.1    Ondetti, M.A.2
  • 21
    • 84929461948 scopus 로고
    • Angiotensin Converting Enzyme Inhibitors. Properties and Side Effects
    • Gavras, H.; Gavras, I. Angiotensin Converting Enzyme Inhibitors. Properties and Side Effects. Hypertension 1988, 11 (3), Suppl. 11, 37-41.
    • (1988) Hypertension , vol.11 , Issue.3 , pp. 37-41
    • Gavras, H.1    Gavras, I.2
  • 22
    • 0002234439 scopus 로고
    • Organophosphorous Intermediates V. Some Michael Additions of Methyl Hypophosphite. A Simple Route to Functionalized Phosphiranes
    • Gallagher, M. J.; Sussman, J. Organophosphorous Intermediates V. Some Michael Additions of Methyl Hypophosphite. A Simple Route to Functionalized Phosphiranes. Phosphorous 1975, 5, 91-95.
    • (1975) Phosphorous , vol.5 , pp. 91-95
    • Gallagher, M.J.1    Sussman, J.2
  • 23
    • 0025166075 scopus 로고
    • Prenylated proteins: Synthesis of geranylgeranylcysteine and identification of this thioether amino acid as a component of proteins in CHO cells
    • Epstein, W. W.; Lever, D. C.; Rilling, H. C. Prenylated proteins: Synthesis of geranylgeranylcysteine and identification of this thioether amino acid as a component of proteins in CHO cells. Proc. Natl. Acad. Sci. U. S. A. 1990, 87, 7352-7354.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 7352-7354
    • Epstein, W.W.1    Lever, D.C.2    Rilling, H.C.3
  • 25
    • 0025819073 scopus 로고
    • Protein Famesyltransferase and Geranyltransferase Share a Common α Subunit
    • Seabra, M. C.; Reiss, Y.; Casey, P. J.; Brown, M. S.; Goldstein, J. L., Protein Famesyltransferase and Geranyltransferase Share a Common α Subunit. Cell 1991, 65, 429-434.
    • (1991) Cell , vol.65 , pp. 429-434
    • Seabra, M.C.1    Reiss, Y.2    Casey, P.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 26
    • 0026072339 scopus 로고
    • Enzymatic modification of proteins with a geranylgeranyl isoprenoid
    • Casey, P. J.; Thissen, J. A.; Moomaw, J. F. Enzymatic modification of proteins with a geranylgeranyl isoprenoid. Proc. Natl. Acad. Sci. U. S. A. 1991, 88, 8631-8635.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8631-8635
    • Casey, P.J.1    Thissen, J.A.2    Moomaw, J.F.3
  • 27
    • 0026001936 scopus 로고
    • A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity
    • Yokoyoma, K; Goodwin, G. W.; Ghomashchi, F.; Glomset, J. A.; Gelb, M. H. A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity. Proc. Natl. Acad. Sci. U. S. A. 1991, 88, 5302-5306.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5302-5306
    • Yokoyoma, K.1    Goodwin, G.W.2    Ghomashchi, F.3    Glomset, J.A.4    Gelb, M.H.5
  • 28
    • 0025944103 scopus 로고
    • Posttranslational modification of Ha-ras p21 by famesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid
    • Kinsella, B. T.; Erdman, R. A.; Maltese, W. A. Posttranslational modification of Ha-ras p21 by famesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid. Proc. Natl. Acad. Sci. U. S. A. 1991, 88, 8934-8938.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8934-8938
    • Kinsella, B.T.1    Erdman, R.A.2    Maltese, W.A.3
  • 29
    • 0026806554 scopus 로고
    • Mammalian Protein Geranylgeranyltransferase: subunit composition and metal requirements
    • Moomaw, J. F.; Casey, P. J. Mammalian Protein Geranylgeranyltransferase: subunit composition and metal requirements. J. Biol. Chem. 1992, 267, 17438-17443.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17438-17443
    • Moomaw, J.F.1    Casey, P.J.2
  • 31
    • 85022897947 scopus 로고    scopus 로고
    • manuscript in preparation
    • Saini, S. S.; Manne, V., manuscript in preparation.
    • Saini, S.S.1    Manne, V.2
  • 32
    • 0026019858 scopus 로고
    • Preferential inhibition of the oncogenic form of Ras by mutations in the GAP binding/“effector” domain
    • Famsworth, C. L.; Marshall, M. S.; Gibbs, J. B.; Stacey, D. W.; Feig, L. A. Preferential inhibition of the oncogenic form of Ras by mutations in the GAP binding/“effector” domain. Cell 1991, 64, 625-663.
    • (1991) Cell , vol.64 , pp. 625-663
    • Famsworth, C.L.1    Marshall, M.S.2    Gibbs, J.B.3    Stacey, D.W.4    Feig, L.A.5
  • 34
    • 0023889492 scopus 로고
    • Independent molecular pathways in initiation and loss of hormone responsiveness of breast carcinomas
    • Sukumar, S.; Camey, W. P.; Barbacid, M. Independent molecular pathways in initiation and loss of hormone responsiveness of breast carcinomas. Science 1988, 240, 524-526.
    • (1988) Science , vol.240 , pp. 524-526
    • Sukumar, S.1    Camey, W.P.2    Barbacid, M.3
  • 36
    • 0027989834 scopus 로고
    • Rational design of potent carboxylic acid based bisubstrate inhibitors of ras famesyl protein transferase
    • Bhide, R. S.; Patel, D. V.; Patel, M. M.; Robinson, S. P.; Hunihan, L. W.; Gordon, E. M. Rational design of potent carboxylic acid based bisubstrate inhibitors of ras famesyl protein transferase. Bioorg. Med. Chem. Lett. 1994, 4, 2107-2112.
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 2107-2112
    • Bhide, R.S.1    Patel, D.V.2    Patel, M.M.3    Robinson, S.P.4    Hunihan, L.W.5    Gordon, E.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.