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Volumn 12, Issue 7, 2007, Pages 983-993

Small-molecule inhibitors of the Rce1p CaaX protease

Author keywords

CaaX protein; Isoprenylation; Posttranslational modification; Protease; Ras

Indexed keywords

ENZYME INHIBITOR; PHEROMONE; PROTEIN S ISOPRENYLCYSTEINE O METHYLTRANSFERASE; PROTEINASE; RAS PROTEIN; RCE1P CAAX PROTEIN; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 35148833800     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057107307226     Document Type: Article
Times cited : (53)

References (50)
  • 1
    • 77956670866 scopus 로고    scopus 로고
    • Postisoprenylation Protein Processing: CXXX (CaaX) Endoproteases and Isoprenylcysteine Carboxyl Methyltransferase
    • Tamanoi F, Sigman DS (eds): New York: Academic Press
    • Young SG, Ambroziak P., Kim E., Clarke S.: Postisoprenylation protein processing: CXXX (CaaX) endoproteases and isoprenylcysteine carboxyl methyltransferase. In Tamanoi F, Sigman DS (eds): The Enzymes. New York: Academic Press, 2001.
    • (2001) The Enzymes
    • Young, S.G.1    Ambroziak, P.2    Kim, E.3    Clarke, S.4
  • 2
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann AM, Casey PJ: Post-prenylation-processing enzymes as new targets in oncogenesis. Nat Rev Cancer 2005 ; 5: 405-412.
    • (2005) Nat Rev Cancer , vol.5 , pp. 405-412
    • Winter-Vann, A.M.1    Casey, P.J.2
  • 3
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk VL, Ashby MN, Rine J.: Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 1997 ; 275: 1796-1800.
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 4
    • 0031874938 scopus 로고    scopus 로고
    • Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing
    • Tam A., Nouvet F., Fujimura-Kamada K., Slunt H., Sisodia SS, Michaelis S.: Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing. J Cell Biol 1998 ; 142: 635-649.
    • (1998) J Cell Biol , vol.142 , pp. 635-649
    • Tam, A.1    Nouvet, F.2    Fujimura-Kamada, K.3    Slunt, H.4    Sisodia, S.S.5    Michaelis, S.6
  • 6
    • 0031858844 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae prenylcysteine carboxyl methltransferase Ste14p is in the endoplasmic reticulum membrane
    • Romano JD, Schmidt WK, Michaelis S.: The Saccharomyces cerevisiae prenylcysteine carboxyl methltransferase Ste14p is in the endoplasmic reticulum membrane. Mol Biol Cell 1998 ; 9: 2231-2247.
    • (1998) Mol Biol Cell , vol.9 , pp. 2231-2247
    • Romano, J.D.1    Schmidt, W.K.2    Michaelis, S.3
  • 7
    • 0032530150 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
    • Schmidt WK, Tam A., Fujimura-Kamada K., Michaelis S.: Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proc Natl Acad Sci U S A 1998 ; 95: 11175-11180.
    • (1998) Proc Natl Acad Sci U S a , vol.95 , pp. 11175-11180
    • Schmidt, W.K.1    Tam, A.2    Fujimura-Kamada, K.3    Michaelis, S.4
  • 8
    • 0036667388 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: Promises and realities
    • Cox A., Der C.: Farnesyltransferase inhibitors: promises and realities. Curr Opin Pharmacol 2002 ; 2: 388-393.
    • (2002) Curr Opin Pharmacol , vol.2 , pp. 388-393
    • Cox, A.1    Der, C.2
  • 9
    • 1642477902 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors as anticancer agents: Current status
    • Zhu K., Hamilton AD, Sebti SM: Farnesyltransferase inhibitors as anticancer agents: current status. Curr Opin Investig Drugs 2003 ; 4: 1428-1435.
    • (2003) Curr Opin Investig Drugs , vol.4 , pp. 1428-1435
    • Zhu, K.1    Hamilton, A.D.2    Sebti, S.M.3
  • 10
    • 0034263198 scopus 로고    scopus 로고
    • Solid-phase synthesis of a farnesylated CaaX peptide library: Inhibitors of the Ras CaaX endoprotease
    • Dolence EK, Dolence JM, Poulter CD: Solid-phase synthesis of a farnesylated CaaX peptide library: inhibitors of the Ras CaaX endoprotease. J Comb Chem 2000 ; 2: 522-536.
    • (2000) J Comb Chem , vol.2 , pp. 522-536
    • Dolence, E.K.1    Dolence, J.M.2    Poulter, C.D.3
  • 11
    • 0035847663 scopus 로고    scopus 로고
    • Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1
    • Schlitzer M., Winter-Vann A., Casey PJ: Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1. Bioorg Med Chem Lett 2001 ; 11: 425-427.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 425-427
    • Schlitzer, M.1    Winter-Vann, A.2    Casey, P.J.3
  • 12
    • 23844534430 scopus 로고    scopus 로고
    • The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: Development of novel inhibitors
    • Anderson JL, Henriksen BS, Gibbs RA, Hrycyna CA: The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: development of novel inhibitors. J Biol Chem 2005 ; 280: 29454-29461.
    • (2005) J Biol Chem , vol.280 , pp. 29454-29461
    • Anderson, J.L.1    Henriksen, B.S.2    Gibbs, R.A.3    Hrycyna, C.A.4
  • 13
    • 20144365360 scopus 로고    scopus 로고
    • A small-molecule inhibitor of isoprenylcysteine carboxyl methyltransferase with antitumor activity in cancer cells
    • Winter-Vann AM, Baron RA, Wong W., de la Cruz J., York JD, Gooden DM,, et al. A small-molecule inhibitor of isoprenylcysteine carboxyl methyltransferase with antitumor activity in cancer cells. Proc Natl Acad Sci U S A 2005 ; 102: 4336-4341.
    • (2005) Proc Natl Acad Sci U S a , vol.102 , pp. 4336-4341
    • Winter-Vann, A.M.1    Baron, R.A.2    Wong, W.3    De La Cruz, J.4    York, J.D.5    Gooden, D.M.6
  • 14
    • 0041919374 scopus 로고    scopus 로고
    • Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia
    • Agarwal AK, Fryns JP, Auchus RJ, Garg A.: Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia. Hum Mol Genet 2003 ; 12: 1995 -2001.
    • (2001) Hum Mol Genet , vol.12 , pp. 1995
    • Agarwal, A.K.1    Fryns, J.P.2    Auchus, R.J.3    Garg, A.4
  • 15
    • 30844434561 scopus 로고    scopus 로고
    • Prelamin A, Zmpste24, misshapen cell nuclei, and progeria-new evidence suggesting that protein farnesylation could be important for disease pathogenesis
    • Young SG, Fong LG, Michaelis S.: Prelamin A, Zmpste24, misshapen cell nuclei, and progeria-new evidence suggesting that protein farnesylation could be important for disease pathogenesis. J Lipid Res 2005 ; 46: 2531-2558.
    • (2005) J Lipid Res , vol.46 , pp. 2531-2558
    • Young, S.G.1    Fong, L.G.2    Michaelis, S.3
  • 16
    • 0028916399 scopus 로고
    • Farnesylation and proteolysis are sequential, but distinct steps in the CaaX box modifcation pathway
    • Farh L., Mitchell D., Deschenes R.: Farnesylation and proteolysis are sequential, but distinct steps in the CaaX box modifcation pathway. Arch Biochem Biophys 1995 ; 318: 113-121.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 113-121
    • Farh, L.1    Mitchell, D.2    Deschenes, R.3
  • 17
    • 0033605743 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian prenyl protein-specific protease
    • Otto JC, Kim E., Young SG, Casey PJ: Cloning and characterization of a mammalian prenyl protein-specific protease. J Biol Chem 1999 ; 274: 8379-8382.
    • (1999) J Biol Chem , vol.274 , pp. 8379-8382
    • Otto, J.C.1    Kim, E.2    Young, S.G.3    Casey, P.J.4
  • 18
    • 0035861547 scopus 로고    scopus 로고
    • The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor
    • Tam A., Schmidt WK, Michaelis S.: The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor. J Biol Chem 2001 ; 276: 46798-46806.
    • (2001) J Biol Chem , vol.276 , pp. 46798-46806
    • Tam, A.1    Schmidt, W.K.2    Michaelis, S.3
  • 19
    • 0026521412 scopus 로고
    • Endoproteolytic processing of a farnesylated peptide in vitro
    • Ashby M., King D., Rine J.: Endoproteolytic processing of a farnesylated peptide in vitro. Proc Natl Acad Sci U S A 1992 ; 89: 4613-4617.
    • (1992) Proc Natl Acad Sci U S a , vol.89 , pp. 4613-4617
    • Ashby, M.1    King, D.2    Rine, J.3
  • 20
    • 0034636066 scopus 로고    scopus 로고
    • Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p
    • Dolence JM, Steward LE, Dolence EK, Wong DH, Poulter CD: Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p. Biochemistry 2000 ; 39: 4096-4104.
    • (2000) Biochemistry , vol.39 , pp. 4096-4104
    • Dolence, J.M.1    Le, S.2    Dolence, E.K.3    Wong, D.H.4    Poulter, C.D.5
  • 21
    • 0034327206 scopus 로고    scopus 로고
    • Human ras-converting enzyme (hRCE1) endoproteolytic activity on K-ras-derived peptides
    • Hollander I., Frommer E., Mallon R.: Human ras-converting enzyme (hRCE1) endoproteolytic activity on K-ras-derived peptides. Anal Biochem 2000 ; 286: 129-137.
    • (2000) Anal Biochem , vol.286 , pp. 129-137
    • Hollander, I.1    Frommer, E.2    Mallon, R.3
  • 22
    • 1942422761 scopus 로고    scopus 로고
    • Update on NCI in vitro drug screen utilities
    • Holbeck SL: Update on NCI in vitro drug screen utilities. Eur J Cancer 2004 ; 40: 785-793.
    • (2004) Eur J Cancer , vol.40 , pp. 785-793
    • Holbeck, S.L.1
  • 23
    • 0035935711 scopus 로고    scopus 로고
    • Discovery and biological evaluation of a new family of potent inhibitors of the dual specificity protein phosphatase Cdc25
    • Lazo JS, Aslan DC, Southwick EC, Cooley KA, Ducruet AP, Joo B.,, et al. Discovery and biological evaluation of a new family of potent inhibitors of the dual specificity protein phosphatase Cdc25. J Med Chem 2001 ; 44: 4042-4049.
    • (2001) J Med Chem , vol.44 , pp. 4042-4049
    • Lazo, J.S.1    Aslan, D.C.2    Southwick, E.C.3    Cooley, K.A.4    Ducruet, A.P.5    Joo, B.6
  • 24
    • 0036682284 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors of hypoxia-inducible factor 1 transcriptional activation pathway
    • Rapisarda A., Uranchimeg B., Scudiero DA, Selby M., Sausville EA, Shoemaker RH,, et al. Identification of small molecule inhibitors of hypoxia-inducible factor 1 transcriptional activation pathway. Cancer Res 2002 ; 62: 4316-4324.
    • (2002) Cancer Res , vol.62 , pp. 4316-4324
    • Rapisarda, A.1    Uranchimeg, B.2    Scudiero, D.A.3    Selby, M.4    Sausville, E.A.5    Shoemaker, R.H.6
  • 25
    • 12844264250 scopus 로고    scopus 로고
    • Novel IMP-1 metallo-beta-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1
    • Moloughney JG, D Thomas J., Toney JH: Novel IMP-1 metallo-beta-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1. FEMS Microbiol Lett 2005 ; 243: 65-71.
    • (2005) FEMS Microbiol Lett , vol.243 , pp. 65-71
    • Moloughney, J.G.1    Thomas, J.D.2    Toney, J.H.3
  • 26
    • 25444513779 scopus 로고    scopus 로고
    • A novel platinum compound inhibits constitutive Stat3 signaling and induces cell cycle arrest and apoptosis of malignant cells
    • Turkson J., Zhang S., Mora LB, Burns A., Sebti S., Jove R.: A novel platinum compound inhibits constitutive Stat3 signaling and induces cell cycle arrest and apoptosis of malignant cells. J Biol Chem 2005 ; 280: 32979-32988.
    • (2005) J Biol Chem , vol.280 , pp. 32979-32988
    • Turkson, J.1    Zhang, S.2    Mora, L.B.3    Burns, A.4    Sebti, S.5    Jove, R.6
  • 27
    • 29044436755 scopus 로고    scopus 로고
    • Chemical library screen for novel inhibitors of Kaposi's sarcoma-associated herpesvirus processive DNA synthesis
    • Dorjsuren D., Burnette A., Gray G., Chen X., Zhu W., Roberts P.,, et al. Chemical library screen for novel inhibitors of Kaposi's sarcoma-associated herpesvirus processive DNA synthesis. Antiviral Res 2006 ; 69: 9-23.
    • (2006) Antiviral Res , vol.69 , pp. 9-23
    • Dorjsuren, D.1    Burnette, A.2    Gray, G.3    Chen, X.4    Zhu, W.5    Roberts, P.6
  • 29
    • 33746136088 scopus 로고    scopus 로고
    • Validated high-throughput screening of drug-like small molecules for inhibitors of ErbB2 transcription
    • Marx C., Berger C., Xu F., Amend C., Scott GK, Hann B.,, et al. Validated high-throughput screening of drug-like small molecules for inhibitors of ErbB2 transcription. Assay Drug Dev Technol 2006 ; 4: 273-284.
    • (2006) Assay Drug Dev Technol , vol.4 , pp. 273-284
    • Marx, C.1    Berger, C.2    Xu, F.3    Amend, C.4    Scott, G.K.5    Hann, B.6
  • 30
    • 0021713895 scopus 로고
    • Transcription and regulatory signals at the mating type locus in yeast
    • Siliciano P., Tatchell K.: Transcription and regulatory signals at the mating type locus in yeast. Cell 1984 ; 37: 969-978.
    • (1984) Cell , vol.37 , pp. 969-978
    • Siliciano, P.1    Tatchell, K.2
  • 31
    • 0022994652 scopus 로고
    • RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor
    • Powers S., Michaelis S., Broek D., Santa Anna S., Field J., Herskowitz I.,, et al. RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor. Cell 1986 ; 47: 413-422.
    • (1986) Cell , vol.47 , pp. 413-422
    • Powers, S.1    Michaelis, S.2    Broek, D.3    Santa Anna, S.4    Field, J.5    Herskowitz, I.6
  • 32
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble R.: A simple and efficient procedure for transformation of yeasts. BioTechniques 1992 ; 13: 18-20.
    • (1992) BioTechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 33
    • 0023974052 scopus 로고
    • The a-factor pheromone of Saccharomyces cerevisiae is essential for mating
    • Michaelis S., Herskowitz I.: The a-factor pheromone of Saccharomyces cerevisiae is essential for mating. Mol Cell Biol 1988 ; 8: 1309-1318.
    • (1988) Mol Cell Biol , vol.8 , pp. 1309-1318
    • Michaelis, S.1    Herskowitz, I.2
  • 34
    • 33646192360 scopus 로고    scopus 로고
    • Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues
    • Plummer LJ, Hildebrandt ER, Porter SB, Rogers VA, McCracken J., Schmidt WK: Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues. J Biol Chem 2006 ; 281: 4596-4605.
    • (2006) J Biol Chem , vol.281 , pp. 4596-4605
    • Plummer, L.J.1    Hildebrandt, E.R.2    Porter, S.B.3    Rogers, V.A.4    McCracken, J.5    Schmidt, W.K.6
  • 35
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim R., Tsien RY: Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr Biol 1996 ; 6: 178-182.
    • (1996) Curr Biol , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 36
    • 0030873221 scopus 로고    scopus 로고
    • Recombination-mediated PCR-directed plasmid construction in vivo in yeast
    • Oldenburg KR, Vo KT, Michaelis S., Paddon C.: Recombination-mediated PCR-directed plasmid construction in vivo in yeast. Nucleic Acids Res 1997 ; 25: 451-452.
    • (1997) Nucleic Acids Res , vol.25 , pp. 451-452
    • Oldenburg, K.R.1    Vo, K.T.2    Michaelis, S.3    Paddon, C.4
  • 37
    • 34249690834 scopus 로고    scopus 로고
    • Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones
    • Porter S., Hildebrandt E., Breevoort S., Dore T., Schmidt W.: Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones. Biochim Biophys Acta 2007 ; 1773: 853-862.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 853-862
    • Porter, S.1    Hildebrandt, E.2    Breevoort, S.3    Dore, T.4    Schmidt, W.5
  • 38
    • 0034052099 scopus 로고    scopus 로고
    • Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis
    • Schmidt WK, Tam A., Michaelis S.: Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis. J Biol Chem 2000 ; 275: 6227-6233.
    • (2000) J Biol Chem , vol.275 , pp. 6227-6233
    • Schmidt, W.K.1    Tam, A.2    Michaelis, S.3
  • 39
    • 0025860189 scopus 로고
    • Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone
    • Marcus S., Caldwell GA, Miller D., Xue C-B., Naider F., Becker JM: Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone. Mol Cell Biol 1991 ; 11: 3603-3612.
    • (1991) Mol Cell Biol , vol.11 , pp. 3603-3612
    • Marcus, S.1    Caldwell, G.A.2    Miller, D.3    Xue, C.-B.4    Naider, F.5    Becker, J.M.6
  • 40
    • 0027518956 scopus 로고
    • Inhibitors of the isoprenylated protein endoprotease
    • Ma Y-T., Gilbert B., Rando R.: Inhibitors of the isoprenylated protein endoprotease. Biochemistry 1993 ; 32: 2386-2393.
    • (1993) Biochemistry , vol.32 , pp. 2386-2393
    • Ma, Y.-T.1    Gilbert, B.2    Rando, R.3
  • 42
    • 0141923641 scopus 로고    scopus 로고
    • Identification and prediction of promiscuous aggregating inhibitors among known drugs
    • Seidler J., McGovern SL, Doman TN, Shoichet BK: Identification and prediction of promiscuous aggregating inhibitors among known drugs. J Med Chem 2003 ; 46: 4477-4486.
    • (2003) J Med Chem , vol.46 , pp. 4477-4486
    • Seidler, J.1    McGovern, S.L.2    Doman, T.N.3    Shoichet, B.K.4
  • 43
    • 33847094111 scopus 로고    scopus 로고
    • Stability and equilibria of promiscuous aggregates in high protein milieus
    • Coan KE, Shoichet BK: Stability and equilibria of promiscuous aggregates in high protein milieus. Mol Biosyst 2007 ; 3: 208-213.
    • (2007) Mol Biosyst , vol.3 , pp. 208-213
    • Coan, K.E.1    Shoichet, B.K.2
  • 44
    • 0036132907 scopus 로고    scopus 로고
    • Absence of the CAAX endoprotease Rce1: Effects on cell growth and transformation
    • Bergo MO, Ambroziak P., Gregory C., George A., Otto JC, Kim E.,, et al. Absence of the CAAX endoprotease Rce1: effects on cell growth and transformation. Mol Cell Biol 2002 ; 22: 171-181.
    • (2002) Mol Cell Biol , vol.22 , pp. 171-181
    • Bergo, M.O.1    Ambroziak, P.2    Gregory, C.3    George, A.4    Otto, J.C.5    Kim, E.6
  • 45
    • 16344396081 scopus 로고    scopus 로고
    • Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases
    • Michaelson D., Ali W., Chiu VK, Bergo M., Silletti J., Wright L.,, et al. Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases. Mol Biol Cell 2005 ; 16: 1606-1616.
    • (2005) Mol Biol Cell , vol.16 , pp. 1606-1616
    • Michaelson, D.1    Ali, W.2    Chiu, V.K.3    Bergo, M.4    Silletti, J.5    Wright, L.6
  • 46
    • 33746889438 scopus 로고    scopus 로고
    • Inhibition of kinesin motor proteins by adociasulfate-2
    • Reddie KG, Roberts DR, Dore TM: Inhibition of kinesin motor proteins by adociasulfate-2. J Med Chem 2006 ; 49: 4857-4860.
    • (2006) J Med Chem , vol.49 , pp. 4857-4860
    • Reddie, K.G.1    Roberts, D.R.2    Dore, T.M.3
  • 47
    • 35148897355 scopus 로고    scopus 로고
    • Compounds and methods for inhibiting Wip1 phosphatase and treating cancer, and screening method
    • Bulavin D., Belova G., Fornace AJ: Compounds and methods for inhibiting Wip1 phosphatase and treating cancer, and screening method. US Pat Appl Publ 2004: 15.
    • (2004) US Pat Appl Publ , pp. 15
    • Bulavin, D.1    Belova, G.2    Fornace, A.J.3
  • 48
    • 6444225167 scopus 로고    scopus 로고
    • Carboxyamido-triazole (CAI), a signal transduction inhibitor, induces growth inhibition and apoptosis in bladder cancer cells by modulation of Bcl-2
    • Perabo FG, Wirger A., Kamp S., Lindner H., Schmidt DH, Muller SC,, et al. Carboxyamido-triazole (CAI), a signal transduction inhibitor, induces growth inhibition and apoptosis in bladder cancer cells by modulation of Bcl-2. Anticancer Res 2004 ; 24: 2869-2877.
    • (2004) Anticancer Res , vol.24 , pp. 2869-2877
    • Perabo, F.G.1    Wirger, A.2    Kamp, S.3    Lindner, H.4    Schmidt, D.H.5    Muller, S.C.6
  • 49
    • 33646512821 scopus 로고    scopus 로고
    • Carboxyamidotriazole inhibits proliferation of human breast cancer cells via G2/M cell cycle arrest and apoptosis
    • Guo L., Li Z-S., Wang H-L., Ye C-Y., Zhang D-C.: Carboxyamidotriazole inhibits proliferation of human breast cancer cells via G2/M cell cycle arrest and apoptosis. Eur J Pharmacol 2006 ; 538: 15-22.
    • (2006) Eur J Pharmacol , vol.538 , pp. 15-22
    • Guo, L.1    Li, Z.-S.2    Wang, H.-L.3    Ye, C.-Y.4    Zhang, D.-C.5
  • 50
    • 31044438181 scopus 로고    scopus 로고
    • Novel and specific inhibitors of a poxvirus type I topoisomerase
    • Bond A., Reichert Z., Stivers JT: Novel and specific inhibitors of a poxvirus type I topoisomerase. Mol Pharmacol 2006 ; 69: 547-557.
    • (2006) Mol Pharmacol , vol.69 , pp. 547-557
    • Bond, A.1    Reichert, Z.2    Stivers, J.T.3


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