메뉴 건너뛰기




Volumn 52, Issue 24, 2009, Pages 8025-8037

Design, synthesis, and characterization of peptide-based rab geranylgeranyl transferase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

PEPTICINNAMIN E; PROTEIN FARNESYLTRANSFERASE INHIBITOR; RAB GERANYLGERANYLTRANSFERASE; RAB GERANYLGERANYLTRANSFERASE INHIBITOR; TRANSFERASE; TRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 73249143294     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm901117d     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 33644748150 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. geranylgeranylation of Rab GTPases
    • Leung, K. F.; Baron, R.; Seabra, M. C. Thematic review series: lipid posttranslational modifications. geranylgeranylation of Rab GTPases. J. Lipid Res. 2006, 47, 467-475.
    • (2006) J. Lipid Res , vol.47 , pp. 467-475
    • Leung, K.F.1    Baron, R.2    Seabra, M.C.3
  • 2
  • 4
    • 0028067898 scopus 로고
    • Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes
    • Alexandrov, K.; Horiuchi, H.; Steele-Mortimer, O.; Seabra, M. C.; Zerial, M. Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes. EMBO J. 1994, 13, 5262-5273.
    • (1994) EMBO J , vol.13 , pp. 5262-5273
    • Alexandrov, K.1    Horiuchi, H.2    Steele-Mortimer, O.3    Seabra, M.C.4    Zerial, M.5
  • 8
    • 0036419738 scopus 로고    scopus 로고
    • Identification and characterization of nine novel human small GTPases showing variable expressions in liver cancer tissues
    • He, H.; Dai, F.; Yu, L.; She, X.; Zhao, Y.; Jiang, J.; Chen, X.; Zhao, S. Identification and characterization of nine novel human small GTPases showing variable expressions in liver cancer tissues. Gene Expression 2002, 10, 231-242.
    • (2002) Gene Expression , vol.10 , pp. 231-242
    • He, H.1    Dai, F.2    Yu, L.3    She, X.4    Zhao, Y.5    Jiang, J.6    Chen, X.7    Zhao, S.8
  • 10
    • 16844384058 scopus 로고    scopus 로고
    • Emerging role of RAB GTPases in cancer and human disease
    • Cheng, K. W.; Lahad, J. P.; Gray, J. W.; Mills, G. B. Emerging role of RAB GTPases in cancer and human disease. Cancer Res. 2005, 65, 2516-2519.
    • (2005) Cancer Res , vol.65 , pp. 2516-2519
    • Cheng, K.W.1    Lahad, J.P.2    Gray, J.W.3    Mills, G.B.4
  • 13
    • 34347369084 scopus 로고    scopus 로고
    • Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets
    • Konstantinopoulos, P. A.; Karamouzis, M. V.; Papavassiliou, A. G. Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets. Nat. Rev. Drug Discovery 2007, 6, 541-555.
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 541-555
    • Konstantinopoulos, P.A.1    Karamouzis, M.V.2    Papavassiliou, A.G.3
  • 15
    • 0034722890 scopus 로고    scopus 로고
    • Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: Lessons from mechanism and bench-to-bedside translational studies
    • Sebti, S. M.; Hamilton, A. D. Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: lessons from mechanism and bench-to-bedside translational studies. Oncogene 2000, 19, 6584-6593.
    • (2000) Oncogene , vol.19 , pp. 6584-6593
    • Sebti, S.M.1    Hamilton, A.D.2
  • 16
    • 0034820134 scopus 로고    scopus 로고
    • Nonpeptidic prenyltransferase inhibitors: Diverse structural classes and surprising anti-cancer mechanisms
    • Gibbs, R. A.; Zahn, T. J.; Sebolt-Leopold, J. S. Nonpeptidic prenyltransferase inhibitors: diverse structural classes and surprising anti-cancer mechanisms. Curr. Med. Chem. 2001, 8, 1437-1465.
    • (2001) Curr. Med. Chem , vol.8 , pp. 1437-1465
    • Gibbs, R.A.1    Zahn, T.J.2    Sebolt-Leopold, J.S.3
  • 18
    • 1842450537 scopus 로고    scopus 로고
    • Inhibitors of farnesyltransferase: A rational approach to cancer chemotherapy?
    • Bell, I. M. Inhibitors of farnesyltransferase: a rational approach to cancer chemotherapy? J. Med. Chem. 2004, 47, 1869-1878.
    • (2004) J. Med. Chem , vol.47 , pp. 1869-1878
    • Bell, I.M.1
  • 20
    • 0033930168 scopus 로고    scopus 로고
    • Protein geranylgeranylation is required for osteoclast formation, function, and survival: Inhibition by bisphosphonates and GGTI-298
    • Coxon, F. P.; Helfrich, M. H.; Van't Hof, R.; Sebti, S.; Ralston, S. H.; Hamilton, A.; Rogers, M. J. Protein geranylgeranylation is required for osteoclast formation, function, and survival: inhibition by bisphosphonates and GGTI-298. J. Bone Miner. Res. 2000, 15, 1467-1476.
    • (2000) J. Bone Miner. Res , vol.15 , pp. 1467-1476
    • Coxon, F.P.1    Helfrich, M.H.2    Van't Hof, R.3    Sebti, S.4    Ralston, S.H.5    Hamilton, A.6    Rogers, M.J.7
  • 22
    • 0030757145 scopus 로고    scopus 로고
    • Inhibition of type I and type II geranylgeranyl-protein transferases by the monoterpene perillyl alcohol in NIH3T3 cells
    • Ren, Z.; Elson, C. E.; Gould, M. N. Inhibition of type I and type II geranylgeranyl-protein transferases by the monoterpene perillyl alcohol in NIH3T3 cells. Biochem. Pharmacol. 1997, 54, 113-120.
    • (1997) Biochem. Pharmacol , vol.54 , pp. 113-120
    • Ren, Z.1    Elson, C.E.2    Gould, M.N.3
  • 24
    • 44349178715 scopus 로고    scopus 로고
    • Inhibitors of protein geranylgeranyltransferase I and Rab geranylgeranyltransferase identified from a library of allenoate-derived compounds
    • Watanabe, M.; Fiji, H. D.; Guo, L.; Chan, L.; Kinderman, S. S.; Slamon, D. J.; Kwon, O.; Tamanoi, F. Inhibitors of protein geranylgeranyltransferase I and Rab geranylgeranyltransferase identified from a library of allenoate-derived compounds. J. Biol. Chem. 2008, 283, 9571-9579.
    • (2008) J. Biol. Chem , vol.283 , pp. 9571-9579
    • Watanabe, M.1    Fiji, H.D.2    Guo, L.3    Chan, L.4    Kinderman, S.S.5    Slamon, D.J.6    Kwon, O.7    Tamanoi, F.8
  • 26
    • 67649690942 scopus 로고    scopus 로고
    • Structure of the DisorderedCTerminus of Rab7 GTPase Induced by Binding to the Rab Geranylgeranyl Transferase Catalytic Complex Reveals the Mechanism of Rab Prenylation
    • Wu, Y. W.; Goody, R. S.; Abagyan, R.; Alexandrov, K. Structure of the DisorderedCTerminus of Rab7 GTPase Induced by Binding to the Rab Geranylgeranyl Transferase Catalytic Complex Reveals the Mechanism of Rab Prenylation. J. Biol. Chem. 2009, 284, 13185-13192.
    • (2009) J. Biol. Chem , vol.284 , pp. 13185-13192
    • Wu, Y.W.1    Goody, R.S.2    Abagyan, R.3    Alexandrov, K.4
  • 27
    • 0037119336 scopus 로고    scopus 로고
    • From protein domains to drug candidates;natural products as guiding principles in the design and synthesis of compound libraries
    • Breinbauer, R.; Vetter, I. R.; Waldmann, H. From protein domains to drug candidates;natural products as guiding principles in the design and synthesis of compound libraries. Angew. Chem., Int. Ed. 2002, 41, 2879-2890.
    • (2002) Angew. Chem., Int. Ed , vol.41 , pp. 2879-2890
    • Breinbauer, R.1    Vetter, I.R.2    Waldmann, H.3
  • 28
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • Newman, D. J.; Cragg, G. M. Natural products as sources of new drugs over the last 25 years. J. Nat. Prod. 2007, 70, 461-477.
    • (2007) J. Nat. Prod , vol.70 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 29
    • 0027475678 scopus 로고
    • Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. I. Producing strain, fermentation, isolation and biological activity
    • Omura, S.; Van der Pyl,D.; Inokoshi, J.; Takahashi, Y.; Takeshima, H. Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. I. Producing strain, fermentation, isolation and biological activity. J. Antibiot. 1993, 46, 222-228.
    • (1993) J. Antibiot , vol.46 , pp. 222-228
    • Omura, S.1    Van der Pyl, D.2    Inokoshi, J.3    Takahashi, Y.4    Takeshima, H.5
  • 30
    • 0027458821 scopus 로고
    • Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. II. Structural elucidation of pepticinnamin E
    • Shiomi, K.; Yang, H.; Inokoshi, J.; Van der Pyl, D.; Nakagawa, A.; Takeshima, H.; Omura, S. Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. II. Structural elucidation of pepticinnamin E. J. Antibiot. 1993, 46, 229-34.
    • (1993) J. Antibiot , vol.46 , pp. 229-234
    • Shiomi, K.1    Yang, H.2    Inokoshi, J.3    Van der Pyl, D.4    Nakagawa, A.5    Takeshima, H.6    Omura, S.7
  • 32
    • 0037696092 scopus 로고    scopus 로고
    • Solid-phase synthesis of peptide esters employing the hydrazide linker
    • Peters, C.; Waldmann, H. Solid-phase synthesis of peptide esters employing the hydrazide linker. J. Org. Chem. 2003, 68, 6053-6055.
    • (2003) J. Org. Chem , vol.68 , pp. 6053-6055
    • Peters, C.1    Waldmann, H.2
  • 35
    • 0033583545 scopus 로고    scopus 로고
    • An Oxidation-Labile Traceless Linker for Solid-Phase Synthesis
    • Stieber, F.; Grether, U.; Waldmann, H. An Oxidation-Labile Traceless Linker for Solid-Phase Synthesis. Angew. Chem., Int. Ed. Engl. 1999, 38, 1073-1077.
    • (1999) Angew. Chem., Int. Ed. Engl , vol.38 , pp. 1073-1077
    • Stieber, F.1    Grether, U.2    Waldmann, H.3
  • 36
    • 0041591464 scopus 로고    scopus 로고
    • Development of the traceless phenylhydrazide linker for solid-phase synthesis
    • Stieber, F.; Grether, U.; Waldmann, H. Development of the traceless phenylhydrazide linker for solid-phase synthesis. Chemistry 2003, 9, 3270-3281.
    • (2003) Chemistry , vol.9 , pp. 3270-3281
    • Stieber, F.1    Grether, U.2    Waldmann, H.3
  • 37
    • 0032543144 scopus 로고    scopus 로고
    • Synthesis and In Vitro Evaluation of the Ras Farnesyltransferase Inhibitor Pepticinnamin E
    • Hinterding, K.; Hagenbuch, P.; Rétey, J.;Waldmann, H. Synthesis and In Vitro Evaluation of the Ras Farnesyltransferase Inhibitor Pepticinnamin E. Angew. Chem., Int. Ed. Engl. 1998, 37, 1236-1239.
    • (1998) Angew. Chem., Int. Ed. Engl , vol.37 , pp. 1236-1239
    • Hinterding, K.1    Hagenbuch, P.2    Rétey, J.3    Waldmann, H.4
  • 38
    • 0038334904 scopus 로고    scopus 로고
    • Identification of mono- and bisubstrate inhibitors of protein farnesyltransferase and inducers of apoptosis from a pepticinnamin E library
    • Thutewohl, M.; Kissau, L.; Popkirova, B.; Karaguni, I. M.; Nowak, T.; Bate, M.; Kuhlmann, J.; Muller, O.; Waldmann, H. Identification of mono- and bisubstrate inhibitors of protein farnesyltransferase and inducers of apoptosis from a pepticinnamin E library. Bioorg. Med. Chem. 2003, 11, 2617-2626.
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 2617-2626
    • Thutewohl, M.1    Kissau, L.2    Popkirova, B.3    Karaguni, I.M.4    Nowak, T.5    Bate, M.6    Kuhlmann, J.7    Muller, O.8    Waldmann, H.9
  • 39
    • 0037020391 scopus 로고    scopus 로고
    • Thutewohl,M.;Kissau, L.; Popkirova, B.; Karaguni, I.M.;Nowak, T.; Bate, M.; Kuhlmann, J.; Muller, O.; Waldmann, H. Solid-phase synthesis and biological evaluation of a pepticinnamin E library. Angew. Chem., Int. Ed. 2002, 41, 3616-20; 3516.
    • Thutewohl,M.;Kissau, L.; Popkirova, B.; Karaguni, I.M.;Nowak, T.; Bate, M.; Kuhlmann, J.; Muller, O.; Waldmann, H. Solid-phase synthesis and biological evaluation of a pepticinnamin E library. Angew. Chem., Int. Ed. 2002, 41, 3616-20; 3516.
  • 40
    • 0037997008 scopus 로고    scopus 로고
    • Solid-phase synthesis of a pepticinnamin E library
    • Thutewohl, M.; Waldmann, H. Solid-phase synthesis of a pepticinnamin E library. Bioorg. Med. Chem. 2003, 11, 2591-2615.
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 2591-2615
    • Thutewohl, M.1    Waldmann, H.2
  • 41
    • 39149120860 scopus 로고    scopus 로고
    • Synthesis of a fluorescent analogue of geranylgeranyl pyrophosphate and its use in a high-throughput fluorometric assay for Rab geranylgeranyltransferase
    • Wu, Y. W.; Alexandrov, K.; Brunsveld, L. Synthesis of a fluorescent analogue of geranylgeranyl pyrophosphate and its use in a high-throughput fluorometric assay for Rab geranylgeranyltransferase. Nat. Protoc. 2007, 2, 2704-2711.
    • (2007) Nat. Protoc , vol.2 , pp. 2704-2711
    • Wu, Y.W.1    Alexandrov, K.2    Brunsveld, L.3
  • 42
    • 0037057707 scopus 로고    scopus 로고
    • Reaction path of protein farnesyltransferase at atomic resolution
    • Long, S. B.; Casey, P. J.; Beese, L. S. Reaction path of protein farnesyltransferase at atomic resolution. Nature 2002, 419, 645-650.
    • (2002) Nature , vol.419 , pp. 645-650
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 43
    • 0344874683 scopus 로고    scopus 로고
    • Structure of mammalian protein geranylgeranyltransferase type-I
    • Taylor, J. S.; Reid, T. S.; Terry, K. L.; Casey, P. J.; Beese, L. S. Structure of mammalian protein geranylgeranyltransferase type-I. EMBO J. 2003, 22, 5963-5974.
    • (2003) EMBO J , vol.22 , pp. 5963-5974
    • Taylor, J.S.1    Reid, T.S.2    Terry, K.L.3    Casey, P.J.4    Beese, L.S.5
  • 46
    • 33845431710 scopus 로고    scopus 로고
    • Aprotein fluorescence amplifier: Continuous fluorometric assay for rab geranylgeranyltransferase
    • Wu, Y. W.; Waldmann, H.; Reents, R.; Ebetino, F. H.; Goody, R. S.; Alexandrov, K.Aprotein fluorescence amplifier: continuous fluorometric assay for rab geranylgeranyltransferase. ChemBioChem 2006, 7, 1859-1861.
    • (2006) ChemBioChem , vol.7 , pp. 1859-1861
    • Wu, Y.W.1    Waldmann, H.2    Reents, R.3    Ebetino, F.H.4    Goody, R.S.5    Alexandrov, K.6
  • 47
    • 12344284051 scopus 로고    scopus 로고
    • Synthesis and application of fluorescent ras proteins for live-cell imaging
    • Reents, R.; Wagner, M.; Schlummer, S.; Kuhlmann, J.; Waldmann, H. Synthesis and application of fluorescent ras proteins for live-cell imaging. ChemBioChem 2005, 6, 86-94.
    • (2005) ChemBioChem , vol.6 , pp. 86-94
    • Reents, R.1    Wagner, M.2    Schlummer, S.3    Kuhlmann, J.4    Waldmann, H.5
  • 48
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 1993, 26, 795-800.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 51
    • 7544226311 scopus 로고    scopus 로고
    • Schuttelkopf,A. W.; Van Aalten, D. M.PRODRG: a tool for highthroughput crystallography of protein-ligand complexes. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60, 1355-1363.
    • Schuttelkopf,A. W.; Van Aalten, D. M.PRODRG: a tool for highthroughput crystallography of protein-ligand complexes. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60, 1355-1363.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.