메뉴 건너뛰기




Volumn 35, Issue 14, 1999, Pages 2010-2030

Discovering novel chemotherapeutic drugs for the third millennium

Author keywords

Combinatorial chemistry; Contemporary drug discovery; Drug design and screening; High throughput bioscience assays; Hypothesis testing clinical trials; Molecular pharmacodynamics and imaging; Novel molecular targets; Small molecule mechanism based drugs

Indexed keywords

ANTINEOPLASTIC AGENT; CAFFEINE; CISPLATIN; CLOTRIMAZOLE; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE INHIBITOR; DIHYDROFOLATE REDUCTASE; ENZYME INHIBITOR; EPIDERMAL GROWTH FACTOR RECEPTOR; FLAVOPIRIDOL; GELDANAMYCIN; GROWTH FACTOR RECEPTOR; GUANOSINE TRIPHOSPHATASE; METHYLXANTHINE DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN P55; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; PROTEINASE INHIBITOR; RADICICOL; RAS PROTEIN; RETINOBLASTOMA PROTEIN; STAUROSPORINE; TELOMERASE; TRANSFERASE INHIBITOR; TRASTUZUMAB; TYRPHOSTIN; UBIQUITIN; UNINDEXED DRUG;

EID: 0033402254     PISSN: 09598049     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-8049(99)00280-4     Document Type: Article
Times cited : (141)

References (247)
  • 1
    • 0343339979 scopus 로고    scopus 로고
    • From bench to bedside
    • Baring M. From bench to bedside. Science. 278:1997;1035-1039.
    • (1997) Science , vol.278 , pp. 1035-1039
    • Baring, M.1
  • 2
    • 0142050676 scopus 로고
    • The potential for molecular oncology to define new drug targets
    • In Kerr DJ, Workman P, eds. CRC Press Inc.
    • Workman P. The potential for molecular oncology to define new drug targets. In Kerr DJ, Workman P, eds. New Molecular Targets for Cancer Chemotherapy. CRC Press Inc., 1994, 1-29.
    • (1994) New Molecular Targets for Cancer Chemotherapy , pp. 1-29
    • Workman, P.1
  • 3
    • 0024505574 scopus 로고
    • Delivery of novel therapeutic agents in tumors: Physiological barriers and strategies
    • Jain R.K. Delivery of novel therapeutic agents in tumors. physiological barriers and strategies J. Natl. Cancer Inst. 81:1989;570-576.
    • (1989) J. Natl. Cancer Inst. , vol.81 , pp. 570-576
    • Jain, R.K.1
  • 4
    • 77957073610 scopus 로고
    • Is there a future for the small molecule in developmental cancer therapy?
    • M.J. Waring, & B.A.J. Ponder. Dordrecht: Kluwer
    • Stevens M.F.G. Is there a future for the small molecule in developmental cancer therapy? Waring M.J., Ponder B.A.J. The Search for New Anticancer Drugs. 1992;1-17 Kluwer, Dordrecht.
    • (1992) The Search for New Anticancer Drugs , pp. 1-17
    • Stevens, M.F.G.1
  • 5
    • 0342904984 scopus 로고    scopus 로고
    • Emerging molecular therapies: Small molecule drugs
    • M.H. Bronchud, M. Foote, W.P. Peters, & M.O. Robinson. Totowa: Humana Press
    • Workman P. Emerging molecular therapies. small molecule drugs Bronchud M.H., Foote M., Peters W.P., Robinson M.O. Principles of Molecular Oncology. 1999;413-429 Humana Press, Totowa.
    • (1999) Principles of Molecular Oncology , pp. 413-429
    • Workman, P.1
  • 7
    • 0010992283 scopus 로고    scopus 로고
    • Conventional cancer therapy: Promise broken or promise delayed?
    • Tannock I.F. Conventional cancer therapy. promise broken or promise delayed? Lancet. 351(Suppl. II):1998;9-16.
    • (1998) Lancet , vol.351 , Issue.SUPPL. II , pp. 9-16
    • Tannock, I.F.1
  • 8
    • 0032931825 scopus 로고    scopus 로고
    • Essential drugs for cancer therapy: A World Health Organisation consultation
    • Sikora K., Advani S., Koroltchouk V.et al. Essential drugs for cancer therapy. a World Health Organisation consultation Ann. Oncol. 10:1999;385-390.
    • (1999) Ann. Oncol. , vol.10 , pp. 385-390
    • Sikora, K.1    Advani, S.2    Koroltchouk, V.3
  • 11
    • 0343775700 scopus 로고
    • Oncogenes
    • Boston: Jones and Bartlett Publishers
    • Cooper G.M. Oncogenes. 2nd edn. 1995;Jones and Bartlett Publishers, Boston.
    • (1995) 2nd Edn.
    • Cooper, G.M.1
  • 14
    • 11544306035 scopus 로고    scopus 로고
    • The promise of cancer genetics
    • Haber D.A., Fearon E.R. The promise of cancer genetics. Lancet. 351(Suppl. II):1998;1-8.
    • (1998) Lancet , vol.351 , Issue.SUPPL. II , pp. 1-8
    • Haber, D.A.1    Fearon, E.R.2
  • 15
    • 0032537407 scopus 로고    scopus 로고
    • The promise of molecular oncology
    • Lane D. The promise of molecular oncology. Lancet. 351(Suppl. II):1998;17-20.
    • (1998) Lancet , vol.351 , Issue.SUPPL. II , pp. 17-20
    • Lane, D.1
  • 16
    • 0033598275 scopus 로고    scopus 로고
    • Gene estimate rises as US and U.K. discuss freedom of access
    • Dickson D. Gene estimate rises as US and U.K. discuss freedom of access. Nature. 401:1999;311.
    • (1999) Nature , vol.401 , pp. 311
    • Dickson, D.1
  • 18
    • 0030274647 scopus 로고    scopus 로고
    • Genomic sciences and the medicine of tomorrow
    • Drews J. Genomic sciences and the medicine of tomorrow. Nat. Biotechnol. 14:1996;1518-1519.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1518-1519
    • Drews, J.1
  • 19
    • 84984934048 scopus 로고    scopus 로고
    • DNA microarrays in drug discovery and development
    • Debouck C., Goodfellow P.N. DNA microarrays in drug discovery and development. Nature Genetics. 21:1999;48-51.
    • (1999) Nature Genetics , vol.21 , pp. 48-51
    • Debouck, C.1    Goodfellow, P.N.2
  • 21
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase β gene segment in T cells using cell type-specific gene targeting
    • Gu H., Marth J.D., Orban P.C., Mossmann H., Rajewsky K. Deletion of a DNA polymerase β gene segment in T cells using cell type-specific gene targeting. Science. 265:1994;103-106.
    • (1994) Science , vol.265 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 22
    • 0030962307 scopus 로고    scopus 로고
    • Gene expression profiles in normal and cancer cells
    • Zhang L., Zhou W., Velculescu V.E.et al. Gene expression profiles in normal and cancer cells. Science. 276:1997;1268-1272.
    • (1997) Science , vol.276 , pp. 1268-1272
    • Zhang, L.1    Zhou, W.2    Velculescu, V.E.3
  • 23
    • 0028915475 scopus 로고
    • Identifying small-molecule lead compounds: The screening approach to drug discovery
    • Bevan P., Ryder H., Shaw I. Identifying small-molecule lead compounds. the screening approach to drug discovery Trends in Biotechnology. 13:1995;115-121.
    • (1995) Trends in Biotechnology , vol.13 , pp. 115-121
    • Bevan, P.1    Ryder, H.2    Shaw, I.3
  • 24
    • 0032832775 scopus 로고    scopus 로고
    • Drug screening - Beyond the bottleneck
    • Dove A. Drug screening - beyond the bottleneck. Nature Biotech. 17:1999;859-862.
    • (1999) Nature Biotech. , vol.17 , pp. 859-862
    • Dove, A.1
  • 25
    • 0032880426 scopus 로고    scopus 로고
    • The drug discovery factory: An inevitable evolutionary consequence of high-throughput parallel processing
    • Archer R. The drug discovery factory. an inevitable evolutionary consequence of high-throughput parallel processing Nature Biotech. 17:1999;834.
    • (1999) Nature Biotech. , vol.17 , pp. 834
    • Archer, R.1
  • 27
    • 0029065615 scopus 로고
    • Combinatorial synthesis - The design of compound libraries and the application to drug discovery
    • Terrett N.K., Gardner M., Gordon D.W., Kobylecki R.J., Steele J. Combinatorial synthesis - the design of compound libraries and the application to drug discovery. Tetrahedron. 51:1995;8135-8173.
    • (1995) Tetrahedron , vol.51 , pp. 8135-8173
    • Terrett, N.K.1    Gardner, M.2    Gordon, D.W.3    Kobylecki, R.J.4    Steele, J.5
  • 28
    • 0030939592 scopus 로고    scopus 로고
    • Combinatorial chemistry in drug discovery
    • Hogan J.C. Combinatorial chemistry in drug discovery. Nature Biotechnology. 15:1997;328-340.
    • (1997) Nature Biotechnology , vol.15 , pp. 328-340
    • Hogan, J.C.1
  • 29
    • 0030756360 scopus 로고    scopus 로고
    • Reactive compounds and in vitro false positives in HTS
    • Rishton G.M. Reactive compounds and in vitro false positives in HTS. Drug Discovery Today. 2:1997;382-384.
    • (1997) Drug Discovery Today , vol.2 , pp. 382-384
    • Rishton, G.M.1
  • 31
    • 0030775794 scopus 로고    scopus 로고
    • Towards intelligent anticancer drug screening in the post-genome era?
    • Workman P. Towards intelligent anticancer drug screening in the post-genome era? Anti-Cancer Drug Design. 12:1997;525-531.
    • (1997) Anti-Cancer Drug Design , vol.12 , pp. 525-531
    • Workman, P.1
  • 32
    • 0032996591 scopus 로고    scopus 로고
    • A novel class of lipophilic quinazoline-based folic acid analogues: Cytotoxic agents with a folate-independent locus
    • Skelton L.A., Ormerod M.G., Titley J., Kimbell R., Brunton L.A., Jackman A.L. A novel class of lipophilic quinazoline-based folic acid analogues: cytotoxic agents with a folate-independent locus. Br. J. Cancer. 79:1999;1692-1701.
    • (1999) Br. J. Cancer , vol.79 , pp. 1692-1701
    • Skelton, L.A.1    Ormerod, M.G.2    Titley, J.3    Kimbell, R.4    Brunton, L.A.5    Jackman, A.L.6
  • 33
    • 0031933503 scopus 로고    scopus 로고
    • 2-(4-Aminophenyl) benzothiazoles: Novel agents with selective profiles of an in vitro anti-tumour activity
    • Bradshaw T.D., Wrigley S., Shi D.F., Schultz R.J., Paull K.D., Stevens M.F. 2-(4-Aminophenyl) benzothiazoles. novel agents with selective profiles of an in vitro anti-tumour activity Br. J. Cancer. 77:1998;745-752.
    • (1998) Br. J. Cancer , vol.77 , pp. 745-752
    • Bradshaw, T.D.1    Wrigley, S.2    Shi, D.F.3    Schultz, R.J.4    Paull, K.D.5    Stevens, M.F.6
  • 34
    • 0031035181 scopus 로고    scopus 로고
    • An information-intensive approach to the molecular pharmacology of cancer
    • For update of molecular target information see http://dtp.nci.nih.gov/ click on molecular targets
    • Weinstein J., Myers T., O'Connor P.M.et al. An information-intensive approach to the molecular pharmacology of cancer. Science. 275:1997;343. For update of molecular target information see http://dtp.nci.nih.gov/ click on molecular targets.
    • (1997) Science , vol.275 , pp. 343
    • Weinstein, J.1    Myers, T.2    O'Connor, P.M.3
  • 35
    • 0030667434 scopus 로고    scopus 로고
    • Integrating genetic approaches into the discovery of anticancer drugs
    • Hartwell L.H., Szankasi P., Roberts C.J., Murray A.W., Friend S.H. Integrating genetic approaches into the discovery of anticancer drugs. Science. 278:1997;1064-1086.
    • (1997) Science , vol.278 , pp. 1064-1086
    • Hartwell, L.H.1    Szankasi, P.2    Roberts, C.J.3    Murray, A.W.4    Friend, S.H.5
  • 36
    • 0030574268 scopus 로고    scopus 로고
    • Structure-based drug design
    • Blundell T.L. Structure-based drug design. Nature. 384:1996;23-25.
    • (1996) Nature , vol.384 , pp. 23-25
    • Blundell, T.L.1
  • 37
  • 38
    • 0032831070 scopus 로고    scopus 로고
    • Structural genomics: Beyond the human genome project
    • Burley S.K., Almo S.C., Bonanno J.B.et al. Structural genomics. beyond the human genome project Nature Genetics. 23:1999;151-157.
    • (1999) Nature Genetics , vol.23 , pp. 151-157
    • Burley, S.K.1    Almo, S.C.2    Bonanno, J.B.3
  • 39
    • 0033178766 scopus 로고    scopus 로고
    • Chemical genetics: exploring and controlling cellular processes with chemical probes
    • Crews CM, Splittgerber U. Chemical genetics: exploring and controlling cellular processes with chemical probes. TIBS 1999, 24, 317-320.
    • (1999) TIBS , vol.24 , pp. 317-320
    • Crews, C.M.1    Splittgerber, U.2
  • 40
    • 0032901378 scopus 로고    scopus 로고
    • Use of a drug-resistant mutant of stress-activated protein kinase 2a/p38 to validate the in vivo specificity of SB 203580
    • Eyers P.A., van den Ijssel P., Quinlan R.A., Goedert M., Cohen P. Use of a drug-resistant mutant of stress-activated protein kinase 2a/p38 to validate the in vivo specificity of SB 203580. FEBS Lett. 21:1999;191-196.
    • (1999) FEBS Lett , vol.21 , pp. 191-196
    • Eyers, P.A.1    Van Den Ijssel, P.2    Quinlan, R.A.3    Goedert, M.4    Cohen, P.5
  • 41
    • 0004099649 scopus 로고
    • F.D. King. Cambridge: Royal Society of Chemistry. 179-188
    • King F.D. Medicinal Chemistry. Principles and Practice:1994;Royal Society of Chemistry, Cambridge. 179-188.
    • (1994) Medicinal Chemistry: Principles and Practice
  • 42
    • 0027787738 scopus 로고
    • Pharmacokinetics and cancer. Successes, failures and future prospects
    • P. Workman, & M.A. Graham. New York: Cold Spring Harbor Laboratory Press
    • Workman P. Pharmacokinetics and cancer. Successes, failures and future prospects. Workman P., Graham M.A. Pharmacokinetics and Cancer Chemotherapy. Cancer Surveys, Vol. 17. 1993;1-26 Cold Spring Harbor Laboratory Press, New York.
    • (1993) Pharmacokinetics and Cancer Chemotherapy. Cancer Surveys, Vol. 17 , pp. 1-26
    • Workman, P.1
  • 44
    • 0018848562 scopus 로고
    • Partition coefficient as a guide to the development of radiosensitizers which are less toxic than misonidazole
    • Brown J.M., Workman P. Partition coefficient as a guide to the development of radiosensitizers which are less toxic than misonidazole. Radiat. Res. 82:1989;171-190.
    • (1989) Radiat. Res. , vol.82 , pp. 171-190
    • Brown, J.M.1    Workman, P.2
  • 45
    • 0019418024 scopus 로고
    • Structure-pharmacokinetic relationships for misonidazole analogues in mice
    • Workman P., Brown J.M. Structure-pharmacokinetic relationships for misonidazole analogues in mice. Cancer Chemother. Pharmacol. 6:1981;39-49.
    • (1981) Cancer Chemother. Pharmacol. , vol.6 , pp. 39-49
    • Workman, P.1    Brown, J.M.2
  • 46
    • 0343775697 scopus 로고
    • Pharmacokinetics-QSAR: Definitions, concepts and models
    • J.C. Dearden. Amsterdam: Elsevier
    • Rowland M. Pharmacokinetics-QSAR. definitions, concepts and models Dearden J.C. Quantitative Approaches to Drug Design. 1983;155-161 Elsevier, Amsterdam.
    • (1983) Quantitative Approaches to Drug Design , pp. 155-161
    • Rowland, M.1
  • 47
  • 48
    • 0031442434 scopus 로고    scopus 로고
    • Quantitative structure-pharmacokinetics relationships: I. Development of a whole-body physiologically based model to characterize changes in pharmacokinetics across a homologous series of barbiturates in the rat
    • Blakey G.M., Nestorov I.A., Arundel P.A., Aarons L.J., Rowland M. Quantitative structure-pharmacokinetics relationships. I. Development of a whole-body physiologically based model to characterize changes in pharmacokinetics across a homologous series of barbiturates in the rat J. Pharmacokinetics and Biopharmaceutics. 25:1997;277.
    • (1997) J. Pharmacokinetics and Biopharmaceutics , vol.25 , pp. 277
    • Blakey, G.M.1    Nestorov, I.A.2    Arundel, P.A.3    Aarons, L.J.4    Rowland, M.5
  • 49
    • 0032434917 scopus 로고    scopus 로고
    • Quantitative structure-pharmacokinetics relationships: II. A mechanistically based model to evaluate the relationship between tissue distribution parameters and compound lipophilcity
    • Nestorov I., Aarons L., Rowland M. Quantitative structure-pharmacokinetics relationships. II. A mechanistically based model to evaluate the relationship between tissue distribution parameters and compound lipophilcity J. Pharmacokinetics and Biopharmaceutics. 26:1998;521.
    • (1998) J. Pharmacokinetics and Biopharmaceutics , vol.26 , pp. 521
    • Nestorov, I.1    Aarons, L.2    Rowland, M.3
  • 50
    • 0031048025 scopus 로고    scopus 로고
    • The simultaneous determination of mixtures of drug candidates by liquid chromatography/atmospheric pressure chemical ionization mass spectrometry as an in vivo drug screening procedure
    • Ohah T.V., McLoughlin D.A., Gilbert J.D. The simultaneous determination of mixtures of drug candidates by liquid chromatography/atmospheric pressure chemical ionization mass spectrometry as an in vivo drug screening procedure. Rapid Communications in Mass Spectrometry. 11:1997;17-23.
    • (1997) Rapid Communications in Mass Spectrometry , vol.11 , pp. 17-23
    • Ohah, T.V.1    McLoughlin, D.A.2    Gilbert, J.D.3
  • 51
    • 0031456698 scopus 로고    scopus 로고
    • Preclinical drug metabolism in the age of high throughput screening: An industrial perspective
    • Rodrigues A.K. Preclinical drug metabolism in the age of high throughput screening. an industrial perspective Pharmaceutical Research. 14:1997;1504-1515.
    • (1997) Pharmaceutical Research , vol.14 , pp. 1504-1515
    • Rodrigues, A.K.1
  • 52
  • 54
    • 0030695955 scopus 로고    scopus 로고
    • Systems for identifying new drugs are often faulty
    • Gura T. Systems for identifying new drugs are often faulty. Science. 278:1997;1041-1042.
    • (1997) Science , vol.278 , pp. 1041-1042
    • Gura, T.1
  • 55
    • 0032424179 scopus 로고    scopus 로고
    • What is the optimal rodent model for anti-tumor drug testing?
    • Kerbel R.S. What is the optimal rodent model for anti-tumor drug testing? Cancer Metastasis Rev. 17:1998;301-304.
    • (1998) Cancer Metastasis Rev. , vol.17 , pp. 301-304
    • Kerbel, R.S.1
  • 56
    • 0032410157 scopus 로고    scopus 로고
    • Orthotopic models are necessary to predict therapy of transplantable tumors in mice
    • Killion J.J., Radinsky R., Fidler I.J. Orthotopic models are necessary to predict therapy of transplantable tumors in mice. Cancer Metastasis Rev. 17:1998;279-284.
    • (1998) Cancer Metastasis Rev. , vol.17 , pp. 279-284
    • Killion, J.J.1    Radinsky, R.2    Fidler, I.J.3
  • 57
    • 0022640309 scopus 로고
    • Role of murine tumor models in cancer treatment research
    • Martin D.S., Balis M.E., Fisher B.et al. Role of murine tumor models in cancer treatment research. Cancer Res. 46:1986;2189-2192.
    • (1986) Cancer Res. , vol.46 , pp. 2189-2192
    • Martin, D.S.1    Balis, M.E.2    Fisher, B.3
  • 58
    • 0028908050 scopus 로고
    • Revisions of general guidelines for the preclinical toxicology of new cytotoxic anticancer agents in Europe
    • Burtles S.S., Newell D.R., Henrar R.E.C., Connors T.A. Revisions of general guidelines for the preclinical toxicology of new cytotoxic anticancer agents in Europe. Eur. J. Cancer. 31A:1995;408-410.
    • (1995) Eur. J. Cancer , vol.31 , pp. 408-410
    • Burtles, S.S.1    Newell, D.R.2    Henrar, R.E.C.3    Connors, T.A.4
  • 59
    • 0342904967 scopus 로고    scopus 로고
    • Evaluation of "rodent only" preclinical toxicology for phase I trials of new cancer treatments - The Cancer Research Campaign (CRC) experience
    • Burtles S.S., Jodrell D.I., Newell D.R. Evaluation of "rodent only" preclinical toxicology for phase I trials of new cancer treatments - the Cancer Research Campaign (CRC) experience. Proc. AACR. 39:1998;363.
    • (1998) Proc. AACR , vol.39 , pp. 363
    • Burtles, S.S.1    Jodrell, D.I.2    Newell, D.R.3
  • 60
    • 0032748041 scopus 로고    scopus 로고
    • Evaluation of rodent-only toxicology for early clinical trials with novel cancer therapeutics
    • Newell D.R., Burtles S.S., Fox B.W., Jodrell D.I., Connors T.A. Evaluation of rodent-only toxicology for early clinical trials with novel cancer therapeutics. Br. J. Cancer. 81:1999;760-768.
    • (1999) Br. J. Cancer , vol.81 , pp. 760-768
    • Newell, D.R.1    Burtles, S.S.2    Fox, B.W.3    Jodrell, D.I.4    Connors, T.A.5
  • 61
    • 0027787736 scopus 로고
    • New approaches in preclinical and clinical pharmacokinetics
    • Graham M.A., Kaye S.B. New approaches in preclinical and clinical pharmacokinetics. Cancer Surv. 17:1993;27-49.
    • (1993) Cancer Surv. , vol.17 , pp. 27-49
    • Graham, M.A.1    Kaye, S.B.2
  • 63
    • 0033523233 scopus 로고    scopus 로고
    • Anticancer agents targeting signaling molecules and cancer cell environment: Challenges for drug development
    • Gelman K.A., Eisenhauer E.A., Harris A.L., Ratain M.J., Workman P. Anticancer agents targeting signaling molecules and cancer cell environment. challenges for drug development J. Natl. Cancer Inst. 91:1999;1281-1287.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1281-1287
    • Gelman, K.A.1    Eisenhauer, E.A.2    Harris, A.L.3    Ratain, M.J.4    Workman, P.5
  • 64
    • 0022569778 scopus 로고
    • Potential roles for preclinical pharmacology in phase I clinical trials
    • Collins J.M., Zaharko D.S., Dedrick E.L.et al. Potential roles for preclinical pharmacology in phase I clinical trials. Cancer Treat. Rep. 70:1986;73-80.
    • (1986) Cancer Treat. Rep. , vol.70 , pp. 73-80
    • Collins, J.M.1    Zaharko, D.S.2    Dedrick, E.L.3
  • 65
    • 0026572101 scopus 로고
    • The impact of pharmacokinetically guided dose escalation strategies in phase I clinical trials: Clinical evaluation and recommendations for future studies
    • Graham M.A., Workman P. The impact of pharmacokinetically guided dose escalation strategies in phase I clinical trials. clinical evaluation and recommendations for future studies Ann. Oncol. 3:1992;339-347.
    • (1992) Ann. Oncol. , vol.3 , pp. 339-347
    • Graham, M.A.1    Workman, P.2
  • 66
    • 0025148278 scopus 로고
    • Continual reassessment method: A practical design for phase I clinical trials in cancer
    • O'Quigley J., Pepe M., Fisher L. Continual reassessment method. a practical design for phase I clinical trials in cancer Biometrics. 46:1990;33-48.
    • (1990) Biometrics , vol.46 , pp. 33-48
    • O'Quigley, J.1    Pepe, M.2    Fisher, L.3
  • 67
    • 0027787753 scopus 로고
    • New techniques in pharmacokinetic analysis of cancer drugs III: Nuclear magnetic resonance
    • Maxwell R.J. New techniques in pharmacokinetic analysis of cancer drugs III. nuclear magnetic resonance Cancer Surv. 17:1983;415-423.
    • (1983) Cancer Surv. , vol.17 , pp. 415-423
    • Maxwell, R.J.1
  • 68
    • 0027787752 scopus 로고
    • New techniques in the pharmacokinetic analysis of cancer drugs. IV. Positron emission tomography
    • Tilsley D.W., Harte R.J., Jones T.et al. New techniques in the pharmacokinetic analysis of cancer drugs. IV. Positron emission tomography. Cancer Surv. 17:1993;425-442.
    • (1993) Cancer Surv. , vol.17 , pp. 425-442
    • Tilsley, D.W.1    Harte, R.J.2    Jones, T.3
  • 69
    • 0026920334 scopus 로고
    • Non-invasive MRS in new anticancer drug development
    • Workman P., Maxwell R.J., Griffiths J.R. Non-invasive MRS in new anticancer drug development. NMR Biomed. 5:1992;270-272.
    • (1992) NMR Biomed. , vol.5 , pp. 270-272
    • Workman, P.1    Maxwell, R.J.2    Griffiths, J.R.3
  • 70
    • 0005943108 scopus 로고
    • Bottlenecks in anticancer drug discovery and development: In vivo pharmacokinetic and pharmacodynamic issues and the potential role of PET
    • D. Komar. Dordrecht: Kluwer
    • Workman P. Bottlenecks in anticancer drug discovery and development. in vivo pharmacokinetic and pharmacodynamic issues and the potential role of PET Komar D. PET for Drug Development and Evaluation. 1995;277 Kluwer, Dordrecht.
    • (1995) PET for Drug Development and Evaluation , pp. 277
    • Workman, P.1
  • 71
    • 0032879583 scopus 로고    scopus 로고
    • Molecular imaging: Exploring the next frontier
    • Weissleder R. Molecular imaging. exploring the next frontier Radiology. 212:1999;609-614.
    • (1999) Radiology , vol.212 , pp. 609-614
    • Weissleder, R.1
  • 72
    • 0031903646 scopus 로고    scopus 로고
    • Phase II study of receptor-enhanced chemosenitivity using recombinant humanised anti-p185HER2/neu monoclonal antibody plus cisplatin in patients with HER2/neu-overexpressing metastatic breast cancer refractory to chemotherapy treatment
    • Pergram M.D., Lipton A., Hayes D.F.et al. Phase II study of receptor-enhanced chemosenitivity using recombinant humanised anti-p185HER2/neu monoclonal antibody plus cisplatin in patients with HER2/neu-overexpressing metastatic breast cancer refractory to chemotherapy treatment. J. Clin. Oncol. 16:1998;2659-2671.
    • (1998) J. Clin. Oncol. , vol.16 , pp. 2659-2671
    • Pergram, M.D.1    Lipton, A.2    Hayes, D.F.3
  • 73
    • 0342904944 scopus 로고    scopus 로고
    • Scrip No 2374 30 September
    • Scrip No 2374 30 September 1998, 20.
    • (1998) , pp. 20
  • 74
    • 0024337144 scopus 로고
    • Studies of the HER-2/neu proto-oncogene in human breast and ovarian cancer
    • Slamon D.J., Godolphil W., Jones L.A.et al. Studies of the HER-2/neu proto-oncogene in human breast and ovarian cancer. Science. 244:1989;707-712.
    • (1989) Science , vol.244 , pp. 707-712
    • Slamon, D.J.1    Godolphil, W.2    Jones, L.A.3
  • 76
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: An approach to drug development
    • Levitski A., Gazit A. Tyrosine kinase inhibition. an approach to drug development Science. 267:1995;1782-1788.
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitski, A.1    Gazit, A.2
  • 77
    • 0029850505 scopus 로고    scopus 로고
    • In vivo pharmacology and anti-tumour evaluation of the tyrphostin tyrosine kinase inhibitor RG13022
    • McLeod H.L., Brunton V.G., Eckardt N.et al. In vivo pharmacology and anti-tumour evaluation of the tyrphostin tyrosine kinase inhibitor RG13022. Br. J. Cancer. 74:1996;1714-1718.
    • (1996) Br. J. Cancer , vol.74 , pp. 1714-1718
    • McLeod, H.L.1    Brunton, V.G.2    Eckardt, N.3
  • 78
    • 0028142387 scopus 로고
    • A specific inhibitor of the epidermal growth factor receptor tyrosine kinase
    • Fry D.W., Kraker A.J., McMichael A.et al. A specific inhibitor of the epidermal growth factor receptor tyrosine kinase. Science. 265:1994;1093-1095.
    • (1994) Science , vol.265 , pp. 1093-1095
    • Fry, D.W.1    Kraker, A.J.2    McMichael, A.3
  • 80
    • 0029135109 scopus 로고
    • Opportunities for pharmacological intervention in the ras pathway
    • Marshall C.J. Opportunities for pharmacological intervention in the ras pathway. Ann. Oncol. 6(Suppl. 1):1995;S63-67.
    • (1995) Ann. Oncol. , vol.6 , Issue.SUPPL. 1 , pp. 63-67
    • Marshall, C.J.1
  • 81
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock J.F., Magee A.I., Childs J.E., Marshall C.J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 57:1989;1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 82
    • 0023898932 scopus 로고
    • The ras gene family and human carcinogenesis
    • Bos J.L. The ras gene family and human carcinogenesis. Mutat. Res. 195:1988;255-271.
    • (1988) Mutat. Res. , vol.195 , pp. 255-271
    • Bos, J.L.1
  • 83
    • 0029022018 scopus 로고
    • Mutations of ras genes in human tumours
    • Kiaris H., Spandidos D.A. Mutations of ras genes in human tumours. Intl. J. Oncol. 7:1995;413-421.
    • (1995) Intl. J. Oncol. , vol.7 , pp. 413-421
    • Kiaris, H.1    Spandidos, D.A.2
  • 85
    • 0025740753 scopus 로고
    • The structure of Ras protein: A model for a universal switch
    • Wittinghofer A., Pai E.F. The structure of Ras protein. a model for a universal switch Trends Biochem. Sci. 16:1991;382-387.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pai, E.F.2
  • 87
    • 0033614962 scopus 로고    scopus 로고
    • Essential role for oncogenic Ras in tumour maintenance
    • Chin L., Tam A., Pomerantz J.et al. Essential role for oncogenic Ras in tumour maintenance. Nature. 400:1999;468-472.
    • (1999) Nature , vol.400 , pp. 468-472
    • Chin, L.1    Tam, A.2    Pomerantz, J.3
  • 88
    • 0021970413 scopus 로고
    • Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells
    • Mulcahy L.S., Smith M.R., Stacey D.W. Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells. Nature. 313:1985;241-242.
    • (1985) Nature , vol.313 , pp. 241-242
    • Mulcahy, L.S.1    Smith, M.R.2    Stacey, D.W.3
  • 89
    • 0022472990 scopus 로고
    • Requirement for c-ras proteins during viral oncogene transformation
    • Smith M.R., DeGuidicibus S.J., Stacey D.W. Requirement for c-ras proteins during viral oncogene transformation. Nature. 320:1986;540-543.
    • (1986) Nature , vol.320 , pp. 540-543
    • Smith, M.R.1    Deguidicibus, S.J.2    Stacey, D.W.3
  • 90
    • 0028097472 scopus 로고
    • Pharmaceutical research in molecular oncology
    • Gibbs J.B., Oliff A. Pharmaceutical research in molecular oncology. Cell. 79:1994;193-198.
    • (1994) Cell , vol.79 , pp. 193-198
    • Gibbs, J.B.1    Oliff, A.2
  • 91
    • 0031007684 scopus 로고    scopus 로고
    • Inhibition of Ras prenylation: A signalling target for novel anti-cancer drug design
    • Lerner E.C., Hamilton A.D., Sebti S.M. Inhibition of Ras prenylation. a signalling target for novel anti-cancer drug design Anti-Cancer Drug Design. 12:1997;229-238.
    • (1997) Anti-Cancer Drug Design , vol.12 , pp. 229-238
    • Lerner, E.C.1    Hamilton, A.D.2    Sebti, S.M.3
  • 92
    • 0030829794 scopus 로고    scopus 로고
    • Inhibitors of prenyl transferases
    • Sebti S., Hamilton A. Inhibitors of prenyl transferases. Curr. Opin. Oncol. 9:1997;557-561.
    • (1997) Curr. Opin. Oncol. , vol.9 , pp. 557-561
    • Sebti, S.1    Hamilton, A.2
  • 93
    • 0025883047 scopus 로고
    • Dominant inhibitory Ras mutants selectively inhibit the activity of either cellular or oncogenic Ras
    • Stacey D.W., Feig L.A., Gibbs J.B. Dominant inhibitory Ras mutants selectively inhibit the activity of either cellular or oncogenic Ras. Mol. Cell Biol. 11:1991;4053-4064.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 4053-4064
    • Stacey, D.W.1    Feig, L.A.2    Gibbs, J.B.3
  • 94
    • 0033179479 scopus 로고    scopus 로고
    • Paradoxical activation of Raf by a novel Raf inhibitor
    • Hall-Jackson C.A., Eyers P.A., Cohen P.et al. Paradoxical activation of Raf by a novel Raf inhibitor. Chem. Biol. 6(8):1999;559-568.
    • (1999) Chem. Biol. , vol.6 , Issue.8 , pp. 559-568
    • Hall-Jackson, C.A.1    Eyers, P.A.2    Cohen, P.3
  • 95
    • 0005318501 scopus 로고    scopus 로고
    • Effect of SB 203580 on the activity of c-Raf in vitro and in vivo
    • Hall-Jackson C.A., Goedert M., Hedge P., Cohen P. Effect of SB 203580 on the activity of c-Raf in vitro and in vivo. Oncogene. 18(12):1999;2047-2054.
    • (1999) Oncogene , vol.18 , Issue.12 , pp. 2047-2054
    • Hall-Jackson, C.A.1    Goedert, M.2    Hedge, P.3    Cohen, P.4
  • 97
    • 0032984348 scopus 로고    scopus 로고
    • Blockade of the MAP kinase pathway suppresses growth of colon tumors in vivo
    • Sebolt-Leopold J.S., Dudley D.T., Herrera R.et al. Blockade of the MAP kinase pathway suppresses growth of colon tumors in vivo. Nat. Med. 5(7):1999;810-816.
    • (1999) Nat. Med. , vol.5 , Issue.7 , pp. 810-816
    • Sebolt-Leopold, J.S.1    Dudley, D.T.2    Herrera, R.3
  • 99
    • 0033517244 scopus 로고    scopus 로고
    • Akt is more than just a bad kinase
    • Khwaja A. Akt is more than just a bad kinase. Nature. 401:1999;33-34.
    • (1999) Nature , vol.401 , pp. 33-34
    • Khwaja, A.1
  • 100
    • 0032590011 scopus 로고    scopus 로고
    • PIK3CA is implicated as an oncogene in ovarian cancer
    • Shayesteh L., Lu Y., Kuo W.L.et al. PIK3CA is implicated as an oncogene in ovarian cancer. Nat. Genet. 21(1):1999;99-102.
    • (1999) Nat. Genet. , vol.21 , Issue.1 , pp. 99-102
    • Shayesteh, L.1    Lu, Y.2    Kuo, W.L.3
  • 101
    • 0032475861 scopus 로고    scopus 로고
    • Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
    • Stambolic V., Suzuki A., de la Pompa J.L.et al. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell. 95(1):1998;29-39.
    • (1998) Cell , vol.95 , Issue.1 , pp. 29-39
    • Stambolic, V.1    Suzuki, A.2    De La Pompa, J.L.3
  • 102
    • 0028933897 scopus 로고
    • Phosphatidylinositol 3-kinase inhibitors and their effects on cell signalling pathways
    • Vlahos C.J. Phosphatidylinositol 3-kinase inhibitors and their effects on cell signalling pathways. Drugs of the Future. 20(2):1995;165-171.
    • (1995) Drugs of the Future , vol.20 , Issue.2 , pp. 165-171
    • Vlahos, C.J.1
  • 103
    • 0031458721 scopus 로고    scopus 로고
    • Inhibition of phospholipid signalling and proliferation of Swiss 3T3 cells by the wortmannin analogue demethoxyviridin
    • Cross M.J., Hodgkin M.N., Plumb J.A.et al. Inhibition of phospholipid signalling and proliferation of Swiss 3T3 cells by the wortmannin analogue demethoxyviridin. Biochim. Biophys. Acta. 1362(1):1997;29-38.
    • (1997) Biochim. Biophys. Acta , vol.1362 , Issue.1 , pp. 29-38
    • Cross, M.J.1    Hodgkin, M.N.2    Plumb, J.A.3
  • 104
    • 0029156587 scopus 로고
    • In vitro and in vivo antitumor activity of the phosphatidylinositol-3-kinase inhibitor, wortmannin
    • Schultz R.M., Merriman R.L., Andis S.L.et al. In vitro and in vivo antitumor activity of the phosphatidylinositol-3-kinase inhibitor, wortmannin. Anticancer Res. 15(4):1995;1135-1139.
    • (1995) Anticancer Res. , vol.15 , Issue.4 , pp. 1135-1139
    • Schultz, R.M.1    Merriman, R.L.2    Andis, S.L.3
  • 105
    • 0032614379 scopus 로고    scopus 로고
    • Cellular mechanisms of wingless/Wnt signal transduction
    • Dierick H., Bejsovec A. Cellular mechanisms of wingless/Wnt signal transduction. Curr. Top. Dev. Biol. 43:1999;153-190.
    • (1999) Curr. Top. Dev. Biol. , vol.43 , pp. 153-190
    • Dierick, H.1    Bejsovec, A.2
  • 106
    • 0032406715 scopus 로고    scopus 로고
    • Mechanisms of Wnt signaling in development
    • Wodarz A., Nusse R. Mechanisms of Wnt signaling in development. Ann. Rev. Cell Dev. Biol. 14:1998;59-88.
    • (1998) Ann. Rev. Cell Dev. Biol. , vol.14 , pp. 59-88
    • Wodarz, A.1    Nusse, R.2
  • 107
    • 0031975738 scopus 로고    scopus 로고
    • The role of beta-catenin in cell adhesion, signal transduction, and cancer
    • Bullions L.C.et al. The role of beta-catenin in cell adhesion, signal transduction, and cancer. Curr. Opin. Oncol. 10(1):1998;81-87.
    • (1998) Curr. Opin. Oncol. , vol.10 , Issue.1 , pp. 81-87
    • Bullions, L.C.1
  • 108
    • 0033054464 scopus 로고    scopus 로고
    • The oncogenic activation of beta-catenin
    • Polakis P. The oncogenic activation of beta-catenin. Curr. Opin. Genet. Dev. 9(1):1999;15-21.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , Issue.1 , pp. 15-21
    • Polakis, P.1
  • 109
    • 0032614379 scopus 로고    scopus 로고
    • Cellular mechanisms of wingless/Wnt signal transduction
    • Dierick H., Bejsovec A. Cellular mechanisms of wingless/Wnt signal transduction. Curr. Top. Dev. Biol. 43:1999;153-190.
    • (1999) Curr. Top. Dev. Biol. , vol.43 , pp. 153-190
    • Dierick, H.1    Bejsovec, A.2
  • 111
    • 0032871895 scopus 로고    scopus 로고
    • APC: The plot thickens
    • Bienz M. APC. the plot thickens Curr. Opin. Genet. Dev. 9:1999;595-603.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 595-603
    • Bienz, M.1
  • 112
    • 0033565533 scopus 로고    scopus 로고
    • Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex
    • Willert K., Shibamoto S., Nusse R. Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex. Genes Dev. 13(14):1999;1768-1773.
    • (1999) Genes Dev. , vol.13 , Issue.14 , pp. 1768-1773
    • Willert, K.1    Shibamoto, S.2    Nusse, R.3
  • 113
    • 0032941717 scopus 로고    scopus 로고
    • Regulation of LEF-1/TCF transcription factors by Wnt and other signals
    • Eastman Q., Grosschedl R. Regulation of LEF-1/TCF transcription factors by Wnt and other signals. Curr. Opin. Cell Biol. 11(2):1999;233-240.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , Issue.2 , pp. 233-240
    • Eastman, Q.1    Grosschedl, R.2
  • 114
    • 0021270667 scopus 로고
    • Mode of proviral activation of a putative mammary oncogene (int-1) on mouse chromosome 15.
    • Nusse R, van Ooyen A, Cox D, Fung YK, Varmus H. Mode of proviral activation of a putative mammary oncogene (int-1) on mouse chromosome 15. Nature 1984, 307, 131-136.
    • (1984) Nature , vol.307 , pp. 131-136
    • Nusse, R.1    Van Ooyen, A.2    Cox, D.3    Fung, Y.K.4    Varmus, H.5
  • 115
    • 0022993326 scopus 로고
    • A retrovirus vector expressing the putative mammary oncogene int-1 causes partial transformation of a mammary epithelial cell line
    • Brown A.M., Wildin R.S., Prendergast T.J., Varmus H.E. A retrovirus vector expressing the putative mammary oncogene int-1 causes partial transformation of a mammary epithelial cell line. Cell. 46(7):1986;1001-1009.
    • (1986) Cell , vol.46 , Issue.7 , pp. 1001-1009
    • Brown, A.M.1    Wildin, R.S.2    Prendergast, T.J.3    Varmus, H.E.4
  • 116
    • 0026894053 scopus 로고
    • Somatic mutations of the APC gene in colorectal tumors: Mutation cluster region in the APC gene
    • Miyoshi Y., Nagase H., Ando H.et al. Somatic mutations of the APC gene in colorectal tumors. mutation cluster region in the APC gene Hum. Mol. Genet. 1(4):1992;229-233.
    • (1992) Hum. Mol. Genet. , vol.1 , Issue.4 , pp. 229-233
    • Miyoshi, Y.1    Nagase, H.2    Ando, H.3
  • 117
  • 118
    • 0032525836 scopus 로고    scopus 로고
    • Activation of the beta-catenin gene in primary hepatocellular carcinomas by somatic alterations involving exon 3
    • Miyoshi Y., Iwao K., Nagasawa Y.et al. Activation of the beta-catenin gene in primary hepatocellular carcinomas by somatic alterations involving exon 3. Cancer Res. 58:1998;2524-2527.
    • (1998) Cancer Res. , vol.58 , pp. 2524-2527
    • Miyoshi, Y.1    Iwao, K.2    Nagasawa, Y.3
  • 119
    • 0032801892 scopus 로고    scopus 로고
    • Neoplastic transformation of RK3E by mutant beta-catenin requires deregulation of Tcf/Lef transcription but not activation of c-myc expression
    • Kolligs F.T., Hu G., Dang C.V., Fearon E.R. Neoplastic transformation of RK3E by mutant beta-catenin requires deregulation of Tcf/Lef transcription but not activation of c-myc expression. Mol. Cell Biol. 19:1999;5696-5706.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5696-5706
    • Kolligs, F.T.1    Hu, G.2    Dang, C.V.3    Fearon, E.R.4
  • 120
    • 0031741386 scopus 로고    scopus 로고
    • Tissue-specific expression of beta-catenin in normal mesenchyme and uveal melanomas and its effect on invasiveness
    • Kim K., Daniels K.J., Hay E.D. Tissue-specific expression of beta-catenin in normal mesenchyme and uveal melanomas and its effect on invasiveness. Exp. Cell Res. 245(1):1998;79-90.
    • (1998) Exp. Cell Res. , vol.245 , Issue.1 , pp. 79-90
    • Kim, K.1    Daniels, K.J.2    Hay, E.D.3
  • 121
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan D.O. Principles of CDK regulation. Nature. 374:1995;131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 122
    • 0029807526 scopus 로고    scopus 로고
    • Viewpoint: Putting the cell cycle in order
    • Nasmyth K. Viewpoint. putting the cell cycle in order Science. 274:1996;1643-1645.
    • (1996) Science , vol.274 , pp. 1643-1645
    • Nasmyth, K.1
  • 123
    • 0033597816 scopus 로고    scopus 로고
    • Evolving ideas about cyclins
    • Roberts J.M. Evolving ideas about cyclins. Cell. 98(2):1999;129-132.
    • (1999) Cell , vol.98 , Issue.2 , pp. 129-132
    • Roberts, J.M.1
  • 124
    • 0031309361 scopus 로고    scopus 로고
    • Aberrations of the G1- And G1/S-regulating genes in human cancer
    • Bartkova J., Lukas J., Bartek J. Aberrations of the G1- and G1/S-regulating genes in human cancer. Prog. Cell Cycle Res. 3:1997;211-220.
    • (1997) Prog. Cell Cycle Res. , vol.3 , pp. 211-220
    • Bartkova, J.1    Lukas, J.2    Bartek, J.3
  • 125
    • 0032980308 scopus 로고    scopus 로고
    • The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer
    • Tsihlias J., Kapusta L., Slingerland J. The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer. Ann. Rev. Med. 50:1999;401-423.
    • (1999) Ann. Rev. Med. , vol.50 , pp. 401-423
    • Tsihlias, J.1    Kapusta, L.2    Slingerland, J.3
  • 126
    • 0029921317 scopus 로고    scopus 로고
    • Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer
    • Hall M., Peters G. Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer. Adv. Cancer Res. 68:1996;67-108.
    • (1996) Adv. Cancer Res. , vol.68 , pp. 67-108
    • Hall, M.1    Peters, G.2
  • 127
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr C.J. Cancer cell cycles. Science. 274:1996;1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 128
    • 0031670668 scopus 로고    scopus 로고
    • Phase I trial of continuous infusion flavopiridol, a novel cyclin-dependent kinase inhibitor, in patients with refractory neoplasms
    • Senderowicz A.M., Headlee D., Stinson S.F.et al. Phase I trial of continuous infusion flavopiridol, a novel cyclin-dependent kinase inhibitor, in patients with refractory neoplasms. Clin. Oncol. 16(9):1998;2986-2999.
    • (1998) Clin. Oncol. , vol.16 , Issue.9 , pp. 2986-2999
    • Senderowicz, A.M.1    Headlee, D.2    Stinson, S.F.3
  • 130
    • 0030271304 scopus 로고    scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer L. Chemical inhibitors of cyclin-dependent kinases. Trends in Cell Biology. 6:1996;393-397.
    • (1996) Trends in Cell Biology , vol.6 , pp. 393-397
    • Meijer, L.1
  • 131
    • 0033064532 scopus 로고    scopus 로고
    • Identification of cytosolic aldehyde dehydrogenase 1 from non-small cell lung carcinomas as a flavopiridol-binding protein
    • Schnier J.B., Kaur G., Kaiser A.et al. Identification of cytosolic aldehyde dehydrogenase 1 from non-small cell lung carcinomas as a flavopiridol-binding protein. FEBS Lett. 454:1999;100-104.
    • (1999) FEBS Lett. , vol.454 , pp. 100-104
    • Schnier, J.B.1    Kaur, G.2    Kaiser, A.3
  • 133
    • 0033128165 scopus 로고    scopus 로고
    • Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases
    • Hoessel R., Leclerc S., Endicott J.A.et al. Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases. Nat. Cell Biol. 1(1):1999;60-67.
    • (1999) Nat. Cell Biol. , vol.1 , Issue.1 , pp. 60-67
    • Hoessel, R.1    Leclerc, S.2    Endicott, J.A.3
  • 134
    • 0344809977 scopus 로고    scopus 로고
    • ATP-site directed inhibitors of cyclin-dependent kinases
    • Gray N., Detivaud L., Doerig C., Meijer L. ATP-site directed inhibitors of cyclin-dependent kinases. Curr. Med. Chem. 6(9):1999;859-875.
    • (1999) Curr. Med. Chem. , vol.6 , Issue.9 , pp. 859-875
    • Gray, N.1    Detivaud, L.2    Doerig, C.3    Meijer, L.4
  • 135
    • 0032563315 scopus 로고    scopus 로고
    • Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors
    • Gray N.S., Wodicka L., Thunnissen A.M.et al. Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors. Science. 281:1998;533-538.
    • (1998) Science , vol.281 , pp. 533-538
    • Gray, N.S.1    Wodicka, L.2    Thunnissen, A.M.3
  • 136
    • 0343339935 scopus 로고    scopus 로고
    • Synthesis and application of functionally diverse 2,6,9-trisubstituted purine libraries as CDK inhibitors
    • Chang Y.T., Gray N.S., Rosania G.R.et al. Synthesis and application of functionally diverse 2,6,9-trisubstituted purine libraries as CDK inhibitors. J. Med. Chem. 42(15):1999;2909-2919.
    • (1999) J. Med. Chem. , vol.42 , Issue.15 , pp. 2909-2919
    • Chang, Y.T.1    Gray, N.S.2    Rosania, G.R.3
  • 138
    • 0030515966 scopus 로고    scopus 로고
    • Antitumor effects of butyrolactone I, a selective cdc2 kinase inhibitor, on human lung cancer cell lines
    • Nishio K., Ishida T., Arioka H.et al. Antitumor effects of butyrolactone I, a selective cdc2 kinase inhibitor, on human lung cancer cell lines. Anticancer Res. 16(6B):1996;3387-3395.
    • (1996) Anticancer Res. , vol.16 , Issue.6 B , pp. 3387-3395
    • Nishio, K.1    Ishida, T.2    Arioka, H.3
  • 139
    • 0031847296 scopus 로고    scopus 로고
    • Cdk2/cdc2 expression in colon carcinogenesis and effects of cdk2/cdc2 inhibitor in colon cancer cells
    • Yamamoto H., Monden T., Miyoshi T.et al. Cdk2/cdc2 expression in colon carcinogenesis and effects of cdk2/cdc2 inhibitor in colon cancer cells. Int. J. Oncol. 13(2):1998;233-239.
    • (1998) Int. J. Oncol. , vol.13 , Issue.2 , pp. 233-239
    • Yamamoto, H.1    Monden, T.2    Miyoshi, T.3
  • 140
    • 0033614949 scopus 로고    scopus 로고
    • Paullones, a series of cyclin-dependent kinase inhibitors: Synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity
    • Schultz C., Link A., Leost M.et al. Paullones, a series of cyclin-dependent kinase inhibitors. synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity J. Med. Chem. 42(15):1999;2909-2919.
    • (1999) J. Med. Chem. , vol.42 , Issue.15 , pp. 2909-2919
    • Schultz, C.1    Link, A.2    Leost, M.3
  • 141
    • 0033152122 scopus 로고    scopus 로고
    • Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases
    • Zaharevitz D.W., Gussio R., Leost M.et al. Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases. Cancer Res. 59(11):1999;2566-2569.
    • (1999) Cancer Res. , vol.59 , Issue.11 , pp. 2566-2569
    • Zaharevitz, D.W.1    Gussio, R.2    Leost, M.3
  • 143
    • 0029177397 scopus 로고    scopus 로고
    • Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/INK4A
    • Fahraeus R., Paramio J.M., Ball K.L., Lain S., Lane D.P. Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/INK4A. Curr. Biol. 6(1):1996;84-91.
    • (1996) Curr. Biol. , vol.6 , Issue.1 , pp. 84-91
    • Fahraeus, R.1    Paramio, J.M.2    Ball, K.L.3    Lain, S.4    Lane, D.P.5
  • 144
    • 0031025385 scopus 로고    scopus 로고
    • Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21WAF1
    • Ball K.L., Lain S., Fahraeus R., Smythe C., Lane D.P. Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21WAF1. Curr. Biol. 7(1):1997;71-80.
    • (1997) Curr. Biol. , vol.7 , Issue.1 , pp. 71-80
    • Ball, K.L.1    Lain, S.2    Fahraeus, R.3    Smythe, C.4    Lane, D.P.5
  • 145
    • 0032485025 scopus 로고    scopus 로고
    • Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumour suppressor molecule
    • Fahraeus R., Lain S., Ball K.L., Lane D.P. Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumour suppressor molecule. Oncogene. 16(5):1998;587-596.
    • (1998) Oncogene , vol.16 , Issue.5 , pp. 587-596
    • Fahraeus, R.1    Lain, S.2    Ball, K.L.3    Lane, D.P.4
  • 146
    • 0032510327 scopus 로고    scopus 로고
    • Inhibitors of cyclin-dependent kinases induce features of replicative senescence in early passage human diploid fibroblasts
    • McConnell B.B., Starborg M., Brookes S., Peters G. Inhibitors of cyclin-dependent kinases induce features of replicative senescence in early passage human diploid fibroblasts. Curr. Biol. 8(6):1998;351-354.
    • (1998) Curr. Biol. , vol.8 , Issue.6 , pp. 351-354
    • McConnell, B.B.1    Starborg, M.2    Brookes, S.3    Peters, G.4
  • 147
    • 0032496373 scopus 로고    scopus 로고
    • Features of replicative senescence induced by direct addition of antennapedia-p16INK4A fusion protein to human diploid fibroblasts
    • Kato D., Miyazawa K., Ruas M.et al. Features of replicative senescence induced by direct addition of antennapedia-p16INK4A fusion protein to human diploid fibroblasts. FEBS Lett. 427(2):1998;203-208.
    • (1998) FEBS Lett. , vol.427 , Issue.2 , pp. 203-208
    • Kato, D.1    Miyazawa, K.2    Ruas, M.3
  • 148
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • Colas P., Cohen B., Jessen T., Grishina I., McCoy J., Brent R. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. Nature. 380:1996;548-550.
    • (1996) Nature , vol.380 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishina, I.4    McCoy, J.5    Brent, R.6
  • 149
    • 0032564350 scopus 로고    scopus 로고
    • An artificial cell-cycle inhibitor isolated from a combinatorial library
    • Cohen B.A., Colas P., Brent R. An artificial cell-cycle inhibitor isolated from a combinatorial library. Proc. Natl. Acad. Sci. USA. 95(24):1998;14272-14277.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.24 , pp. 14272-14277
    • Cohen, B.A.1    Colas, P.2    Brent, R.3
  • 150
    • 0000223931 scopus 로고    scopus 로고
    • Role of E2F in cell cycle control and cancer
    • Johnson D.G., Schneider-Broussard R. Role of E2F in cell cycle control and cancer. Front Biosci. 3:1998;d447-448.
    • (1998) Front Biosci. , vol.3 , pp. 447-448
    • Johnson, D.G.1    Schneider-Broussard, R.2
  • 151
    • 0026652346 scopus 로고
    • CDNA encoding a pRB-binding protein with properties of the transcription factor E2F
    • Helin K., Lees J.A., Vidal M., Dyson N., Harlow E., Fattaey A.A. cDNA encoding a pRB-binding protein with properties of the transcription factor E2F. Cell. 70(2):1992;337-350.
    • (1992) Cell , vol.70 , Issue.2 , pp. 337-350
    • Helin, K.1    Lees, J.A.2    Vidal, M.3    Dyson, N.4    Harlow, E.5    Fattaey, A.A.6
  • 152
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson N. The regulation of E2F by pRB-family proteins. Genes Dev. 12(15):1998;2245-2262.
    • (1998) Genes Dev. , vol.12 , Issue.15 , pp. 2245-2262
    • Dyson, N.1
  • 153
    • 0033614968 scopus 로고    scopus 로고
    • Inhibition of mammalian cell proliferation by genetically selected peptide aptamers that functionally antagonize E2F activity
    • Fabbrizio E., Le Cam L., Polanowska J.et al. Inhibition of mammalian cell proliferation by genetically selected peptide aptamers that functionally antagonize E2F activity. Oncogene. 18(30):1999;4357-4363.
    • (1999) Oncogene , vol.18 , Issue.30 , pp. 4357-4363
    • Fabbrizio, E.1    Le Cam, L.2    Polanowska, J.3
  • 154
    • 0027936686 scopus 로고
    • Differential regulation of E2F transactivation by cyclin/cdk2 complexes
    • Dynlacht B.D., Flores O., Lees J.A., Harlow E. Differential regulation of E2F transactivation by cyclin/cdk2 complexes. Genes Dev. 8(15):1994;1772-1786.
    • (1994) Genes Dev. , vol.8 , Issue.15 , pp. 1772-1786
    • Dynlacht, B.D.1    Flores, O.2    Lees, J.A.3    Harlow, E.4
  • 155
    • 0028362359 scopus 로고
    • Negative regulation of the growth-promoting transcription factor E2F-1 by a stably bound cyclin A-dependent protein kinase
    • Krek W., Ewen M.E., Shirodkar S., Arany Z., Kaelin W.G. Jr., Livingston D.M. Negative regulation of the growth-promoting transcription factor E2F-1 by a stably bound cyclin A-dependent protein kinase. Cell. 78(1):1994;161-172.
    • (1994) Cell , vol.78 , Issue.1 , pp. 161-172
    • Krek, W.1    Ewen, M.E.2    Shirodkar, S.3    Arany, Z.4    Kaelin W.G., Jr.5    Livingston, D.M.6
  • 156
    • 0029559027 scopus 로고
    • Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint
    • Krek W., Xu G., Livingston D.M. Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint. Cell. 83(7):1995;1149-1158.
    • (1995) Cell , vol.83 , Issue.7 , pp. 1149-1158
    • Krek, W.1    Xu, G.2    Livingston, D.M.3
  • 157
    • 0028960617 scopus 로고
    • E2F1 overexpression in quiescent fibroblasts leads to induction of cellular DNA synthesis and apoptosis
    • Kowalik T.F., DeGregori J., Schwarz J.K., Nevins J.R. E2F1 overexpression in quiescent fibroblasts leads to induction of cellular DNA synthesis and apoptosis. J. Virol. 69(4):1995;2491-2500.
    • (1995) J. Virol. , vol.69 , Issue.4 , pp. 2491-2500
    • Kowalik, T.F.1    Degregori, J.2    Schwarz, J.K.3    Nevins, J.R.4
  • 158
    • 0027947383 scopus 로고
    • Deregulated transcription factor E2F-1 expression leads to S-phase entry and p53-mediated apoptosis
    • Qin X.Q., Livingston D.M., Kaelin W.G. Jr., Adams P.D. Deregulated transcription factor E2F-1 expression leads to S-phase entry and p53-mediated apoptosis. Proc. Natl. Acad. Sci. USA. 91(23):1994;10918-10922.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.23 , pp. 10918-10922
    • Qin, X.Q.1    Livingston, D.M.2    Kaelin W.G., Jr.3    Adams, P.D.4
  • 159
    • 0033551066 scopus 로고    scopus 로고
    • Selective killing of transformed cells by cyclin/cyclin-dependent kinase 2 antagonists
    • Chen Y.N., Sharma S.K., Ramsey T.M.et al. Selective killing of transformed cells by cyclin/cyclin-dependent kinase 2 antagonists. Proc. Natl. Acad. Sci. USA. 96(8):1999;4325-4329.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.8 , pp. 4325-4329
    • Chen, Y.N.1    Sharma, S.K.2    Ramsey, T.M.3
  • 160
    • 0033551218 scopus 로고    scopus 로고
    • Tossing monkey wrenches into the clock: New ways of treating cancer
    • Lees J.A., Weinberg R.A. Tossing monkey wrenches into the clock. new ways of treating cancer Proc. Natl. Acad. Sci. USA. 96(8):1999;4221-4223.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.8 , pp. 4221-4223
    • Lees, J.A.1    Weinberg, R.A.2
  • 161
    • 0031743063 scopus 로고    scopus 로고
    • Polo-like kinases: Positive regulators of cell division from start to finish
    • Nigg E.A. Polo-like kinases. positive regulators of cell division from start to finish Curr. Opin. Cell Biol. 10(6):1998;776-783.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , Issue.6 , pp. 776-783
    • Nigg, E.A.1
  • 162
    • 0033231927 scopus 로고    scopus 로고
    • The Aurora/Ipl1p kinase family: Regulators of chromosome segregation and cytokinesis
    • Bischoff J.R., Plowman G.D. The Aurora/Ipl1p kinase family. regulators of chromosome segregation and cytokinesis Trends Cell Biol. 9(11):1999;454-459.
    • (1999) Trends Cell Biol. , vol.9 , Issue.11 , pp. 454-459
    • Bischoff, J.R.1    Plowman, G.D.2
  • 163
    • 0028071555 scopus 로고
    • Mutations in the p53 tumor suppressor gene: Clues to cancer etiology and molecular pathogenesis
    • Greenblatt M.S., Bennett W.P., Hollstein M., Harris C.C. Mutations in the p53 tumor suppressor gene. clues to cancer etiology and molecular pathogenesis Cancer Res. 54(18):1994;4855-4878.
    • (1994) Cancer Res. , vol.54 , Issue.18 , pp. 4855-4878
    • Greenblatt, M.S.1    Bennett, W.P.2    Hollstein, M.3    Harris, C.C.4
  • 164
    • 0029101848 scopus 로고
    • Cancer progression and p53
    • Carson D.A., Lois A. Cancer progression and p53. Lancet. 346:1995;1009-1011.
    • (1995) Lancet , vol.346 , pp. 1009-1011
    • Carson, D.A.1    Lois, A.2
  • 165
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • Lane D.P. Cancer. p53, guardian of the genome. Nature. 358:1992;15-16.
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 166
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia A.J., Kastan M.B. The complexity of p53 modulation. emerging patterns from divergent signals Genes Dev. 12(19):1998;2973-2983.
    • (1998) Genes Dev. , vol.12 , Issue.19 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 167
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives C., Hall P.A. The p53 pathway. J. Pathol. 187(1):1999;112-126.
    • (1999) J. Pathol. , vol.187 , Issue.1 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 169
    • 0029972806 scopus 로고    scopus 로고
    • P53: Puzzle and paradigm
    • Ko L.J., Prives C. p53. puzzle and paradigm Genes Dev. 10(9):1996;1054-1072.
    • (1996) Genes Dev. , vol.10 , Issue.9 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 170
    • 0033543077 scopus 로고    scopus 로고
    • A phase I/II study of hepatic artery infusion with wtp53-CMV-Ad in metastatic malignant liver tumours
    • Habib N.A., Hodgson H.J., Lemoine N., Pignatelli M. A phase I/II study of hepatic artery infusion with wtp53-CMV-Ad in metastatic malignant liver tumours. Hum. Gene Ther. 10(12):1999;2019-2034.
    • (1999) Hum. Gene Ther. , vol.10 , Issue.12 , pp. 2019-2034
    • Habib, N.A.1    Hodgson, H.J.2    Lemoine, N.3    Pignatelli, M.4
  • 171
    • 0032809839 scopus 로고    scopus 로고
    • Adenovirus-mediated wild-type p53 gene transfer, as a surgical adjuvant in advanced head and neck cancers
    • Clayman G.L., Frank D.K., Bruso P.A., Goepfert H. Adenovirus-mediated wild-type p53 gene transfer, as a surgical adjuvant in advanced head and neck cancers. Clin. Cancer Res. 5(7):1999;1715-1722.
    • (1999) Clin. Cancer Res. , vol.5 , Issue.7 , pp. 1715-1722
    • Clayman, G.L.1    Frank, D.K.2    Bruso, P.A.3    Goepfert, H.4
  • 172
    • 9544244796 scopus 로고    scopus 로고
    • Retrovirus-mediated wild-type p53 gene transfer to tumors of patients with lung cancer
    • Roth J.A., Nguyen D., Lawrence D.D.et al. Retrovirus-mediated wild-type p53 gene transfer to tumors of patients with lung cancer. Nat. Med. 2(9):1996;985-991.
    • (1996) Nat. Med. , vol.2 , Issue.9 , pp. 985-991
    • Roth, J.A.1    Nguyen, D.2    Lawrence, D.D.3
  • 173
    • 0029856243 scopus 로고    scopus 로고
    • Retrovirus-mediated p53 gene therapy
    • Estreicher A., Iggo R. Retrovirus-mediated p53 gene therapy. Nat. Med. 2(11):1996;1163.
    • (1996) Nat. Med. , vol.2 , Issue.11 , pp. 1163
    • Estreicher, A.1    Iggo, R.2
  • 174
    • 0032911047 scopus 로고    scopus 로고
    • Reactivation of mutant p53 through interaction of a C-terminal peptide with the core domain
    • Selivanova G., Ryabchenko L., Jansson E., Iotsova V., Wiman K.G. Reactivation of mutant p53 through interaction of a C-terminal peptide with the core domain. Mol. Cell Biol. 19(5):1999;3395-3402.
    • (1999) Mol. Cell Biol. , vol.19 , Issue.5 , pp. 3395-3402
    • Selivanova, G.1    Ryabchenko, L.2    Jansson, E.3    Iotsova, V.4    Wiman, K.G.5
  • 176
    • 0032448439 scopus 로고    scopus 로고
    • New p53-based anti-cancer therapeutic strategies
    • Wiman K.G. New p53-based anti-cancer therapeutic strategies. Med. Oncol. 15(4):1998;222-228.
    • (1998) Med. Oncol. , vol.15 , Issue.4 , pp. 222-228
    • Wiman, K.G.1
  • 177
    • 0030961889 scopus 로고    scopus 로고
    • Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain
    • Selivanova G., Iotsova V., Okan I.et al. Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain. Nat. Med. 3(6):1997;632-638.
    • (1997) Nat. Med. , vol.3 , Issue.6 , pp. 632-638
    • Selivanova, G.1    Iotsova, V.2    Okan, I.3
  • 178
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the MDM2-p53 circuit
    • Prives C. Signaling to p53. breaking the MDM2-p53 circuit Cell. 95(1):1998;5-8.
    • (1998) Cell , vol.95 , Issue.1 , pp. 5-8
    • Prives, C.1
  • 179
    • 0027964904 scopus 로고
    • Immunochemical analysis of the interaction of p53 with MDM2;- fine mapping of the MDM2 binding site on p53 using synthetic peptides
    • Picksley S.M., Vojtesek B., Sparks A., Lane D.P. Immunochemical analysis of the interaction of p53 with MDM2;- fine mapping of the MDM2 binding site on p53 using synthetic peptides. Oncogene. 9(9):1994;2523-2529.
    • (1994) Oncogene , vol.9 , Issue.9 , pp. 2523-2529
    • Picksley, S.M.1    Vojtesek, B.2    Sparks, A.3    Lane, D.P.4
  • 180
    • 0029818380 scopus 로고    scopus 로고
    • Identification of novel mdm2 binding peptides by phage display identification of novel mdm2 binding peptides by phage display
    • Bottger V., Bottger A., Howard S.F.et al. Identification of novel mdm2 binding peptides by phage display identification of novel mdm2 binding peptides by phage display. Oncogene. 13(10):1996;2141-2147.
    • (1996) Oncogene , vol.13 , Issue.10 , pp. 2141-2147
    • Bottger, V.1    Bottger, A.2    Howard, S.F.3
  • 181
    • 0031282325 scopus 로고    scopus 로고
    • Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo
    • Bottger A., Bottger V., Sparks A., Liu W.L., Howard S.F., Lane D.P. Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo. Curr. Biol. 7(11):1997;860-869.
    • (1997) Curr. Biol. , vol.7 , Issue.11 , pp. 860-869
    • Bottger, A.1    Bottger, V.2    Sparks, A.3    Liu, W.L.4    Howard, S.F.5    Lane, D.P.6
  • 182
    • 0038298110 scopus 로고    scopus 로고
    • An inhibitor of nuclear export activates the p53 response and induces the localization of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs
    • Lain S., Midgley C., Sparks A., Lane E.B., Lane D.P. An inhibitor of nuclear export activates the p53 response and induces the localization of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs. Exp. Cell Res. 248(2):1999;457-472.
    • (1999) Exp. Cell Res. , vol.248 , Issue.2 , pp. 457-472
    • Lain, S.1    Midgley, C.2    Sparks, A.3    Lane, E.B.4    Lane, D.P.5
  • 183
    • 0344188096 scopus 로고    scopus 로고
    • An adenovirus mutant that replicates selectively in p53-deficient human tumor cells
    • Bischoff J.R., Kirn D.H., Williams A.et al. An adenovirus mutant that replicates selectively in p53-deficient human tumor cells. Science. 274:1996;373-376.
    • (1996) Science , vol.274 , pp. 373-376
    • Bischoff, J.R.1    Kirn, D.H.2    Williams, A.3
  • 184
    • 0031759169 scopus 로고    scopus 로고
    • ONYX-015: Clinical data are encouraging
    • Kirn D., Hermiston T., McCormick F. ONYX-015. clinical data are encouraging Nat. Med. 4(12):1998;1341-1342.
    • (1998) Nat. Med , vol.4 , Issue.12 , pp. 1341-1342
    • Kirn, D.1    Hermiston, T.2    McCormick, F.3
  • 185
    • 0030612166 scopus 로고    scopus 로고
    • Mammalian G1 and G2 phase checkpoints
    • O'Connor P.M. Mammalian G1 and G2 phase checkpoints. Cancer Surv. 29:1997;151-182.
    • (1997) Cancer Surv. , vol.29 , pp. 151-182
    • O'Connor, P.M.1
  • 186
    • 0030310066 scopus 로고    scopus 로고
    • DNA damage checkpoints: Implications for cancer therapy
    • O'Connor P.M., Fan S. DNA damage checkpoints. implications for cancer therapy Prog. Cell Cycle Res. 2:1996;165-173.
    • (1996) Prog. Cell Cycle Res. , vol.2 , pp. 165-173
    • O'Connor, P.M.1    Fan, S.2
  • 188
    • 0032509403 scopus 로고    scopus 로고
    • UCN-01 abrogates G2 arrest through a Cdc2-dependent pathway that is associated with inactivation of the Wee1Hu kinase and activation of the Cdc25C phosphatase
    • Yu L., Orlandi L., Wang P.et al. UCN-01 abrogates G2 arrest through a Cdc2-dependent pathway that is associated with inactivation of the Wee1Hu kinase and activation of the Cdc25C phosphatase. J. Biol. Chem. 273(50):1998;33455-33464.
    • (1998) J. Biol. Chem. , vol.273 , Issue.50 , pp. 33455-33464
    • Yu, L.1    Orlandi, L.2    Wang, P.3
  • 189
    • 0031672099 scopus 로고    scopus 로고
    • Clinical pharmacology of UCN-01: Initial observations and comparison to preclinical models
    • Sausville E.A., Lush R.D., Headlee D.et al. Clinical pharmacology of UCN-01. initial observations and comparison to preclinical models Cancer Chemother. Pharmacol. 42(Suppl.):1998;S54-59.
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , Issue.SUPPL. , pp. 54-59
    • Sausville, E.A.1    Lush, R.D.2    Headlee, D.3
  • 190
    • 0033543728 scopus 로고    scopus 로고
    • A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy
    • Komarov P.G., Komarova E.A., Kondratov R.V.et al. A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy. Science. 285:1999;1733-1737.
    • (1999) Science , vol.285 , pp. 1733-1737
    • Komarov, P.G.1    Komarova, E.A.2    Kondratov, R.V.3
  • 191
    • 0033593316 scopus 로고    scopus 로고
    • Size control in animal development
    • Conlon I., Raff M. Size control in animal development. Cell. 96(2):1999;235-244.
    • (1999) Cell , vol.96 , Issue.2 , pp. 235-244
    • Conlon, I.1    Raff, M.2
  • 192
    • 0033600635 scopus 로고    scopus 로고
    • All Creatures Great and Small
    • Leevers S.J. All Creatures Great and Small. Science. 285:1999;2082-2083.
    • (1999) Science , vol.285 , pp. 2082-2083
    • Leevers, S.J.1
  • 193
    • 0017729820 scopus 로고
    • Continuous protein synthesis is required to maintain the probability of entry into S phase
    • Brooks R.F. Continuous protein synthesis is required to maintain the probability of entry into S phase. Cell. 12(1):1977;311-317.
    • (1977) Cell , vol.12 , Issue.1 , pp. 311-317
    • Brooks, R.F.1
  • 194
    • 0027445185 scopus 로고
    • Translation factors as effectors of cell growth and tumorigenesis
    • Sonenberg N. Translation factors as effectors of cell growth and tumorigenesis. Curr. Opin. Cell Biol. 5(6):1993;955-960.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , Issue.6 , pp. 955-960
    • Sonenberg, N.1
  • 195
  • 196
    • 0032054816 scopus 로고    scopus 로고
    • The mRNA 5′ cap-binding protein eIF4E and control of cell growth
    • Sonenberg N., Gingras A.C. The mRNA 5′ cap-binding protein eIF4E and control of cell growth. Curr. Opin. Cell Biol. 10(2):1998;268-275.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , Issue.2 , pp. 268-275
    • Sonenberg, N.1    Gingras, A.C.2
  • 198
    • 0032967120 scopus 로고    scopus 로고
    • Translational control of growth factor and proto-oncogene expression
    • Willis A.E. Translational control of growth factor and proto-oncogene expression. Int. J. Biochem. Cell Biol. 31(1):1999;73-86.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , Issue.1 , pp. 73-86
    • Willis, A.E.1
  • 199
    • 0033213918 scopus 로고    scopus 로고
    • Translation initiation: Adept at adapting
    • Dever T.E. Translation initiation. adept at adapting Trends Biochem. Sci. 24(10):1999;398-403.
    • (1999) Trends Biochem. Sci. , vol.24 , Issue.10 , pp. 398-403
    • Dever, T.E.1
  • 200
    • 0032493199 scopus 로고    scopus 로고
    • Depletion of intracellular Ca2+ stores, phosphorylation of eIF2alpha, and sustained inhibition of translation initiation mediate the anticancer effects of clotrimazole
    • Aktas H., Fluckiger R., Acosta J.A., Savage J.M., Palakurthi S.S., Halperin J.A. Depletion of intracellular Ca2+ stores, phosphorylation of eIF2alpha, and sustained inhibition of translation initiation mediate the anticancer effects of clotrimazole. Proc. Natl. Acad. Sci. USA. 95(14):1998;8280-8285.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.14 , pp. 8280-8285
    • Aktas, H.1    Fluckiger, R.2    Acosta, J.A.3    Savage, J.M.4    Palakurthi, S.S.5    Halperin, J.A.6
  • 203
    • 0033006919 scopus 로고    scopus 로고
    • EIF4E activity is regulated at multiple levels
    • Raught B., Gingras A.C. eIF4E activity is regulated at multiple levels. Int. J. Biochem. Cell Biol. 31(1):1999;43-57.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , Issue.1 , pp. 43-57
    • Raught, B.1    Gingras, A.C.2
  • 204
    • 0032718056 scopus 로고    scopus 로고
    • Signal transduction pathways that regulate eukaryotic protein synthesis
    • Rhoads R.E. Signal transduction pathways that regulate eukaryotic protein synthesis. J. Biol. Chem. 274(43):1999;30337-30340.
    • (1999) J. Biol. Chem. , vol.274 , Issue.43 , pp. 30337-30340
    • Rhoads, R.E.1
  • 205
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism
    • Gingras A.C., Gygi S.P., Raught B.et al. Regulation of 4E-BP1 phosphorylation. a novel two-step mechanism Genes Dev. 13(11):1999;1422-1437.
    • (1999) Genes Dev. , vol.13 , Issue.11 , pp. 1422-1437
    • Gingras, A.C.1    Gygi, S.P.2    Raught, B.3
  • 206
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • Minich W.B., Balasta M.L., Goss D.J., Rhoads R.E. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E. increased cap affinity of the phosphorylated form Proc. Natl. Acad. Sci. USA. 91(16):1994;7668-7672.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.16 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 207
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E
    • Pyronnet S., Imataka H., Gingras A.C., Fukunaga R., Hunter T., Sonenberg N. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J. 18(1):1999;270-279.
    • (1999) EMBO J. , vol.18 , Issue.1 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 208
    • 0029922065 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled study to determine safety, tolerance, and preliminary pharmacokinetics of ascending single doses of orally administered sirolimus (rapamycin) in stable renal transplant recipients
    • Brattstrom C., Tyden G., Sawe J., Herlenius G., Claesson K., Groth C.G. A randomized, double-blind, placebo-controlled study to determine safety, tolerance, and preliminary pharmacokinetics of ascending single doses of orally administered sirolimus (rapamycin) in stable renal transplant recipients. Transplant Proc. 28(2):1996;985-986.
    • (1996) Transplant Proc. , vol.28 , Issue.2 , pp. 985-986
    • Brattstrom, C.1    Tyden, G.2    Sawe, J.3    Herlenius, G.4    Claesson, K.5    Groth, C.G.6
  • 209
    • 0033557578 scopus 로고    scopus 로고
    • Rapamycin causes poorly reversible inhibition of mTOR and induces p53-independent apoptosis in human rhabdomyosarcoma cells
    • Hosoi H., Dilling M.B., Shikata T.et al. Rapamycin causes poorly reversible inhibition of mTOR and induces p53-independent apoptosis in human rhabdomyosarcoma cells. Cancer Res. 59(4):1999;886-894.
    • (1999) Cancer Res. , vol.59 , Issue.4 , pp. 886-894
    • Hosoi, H.1    Dilling, M.B.2    Shikata, T.3
  • 210
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway. on protein death and cell life EMBO J. 17(24):1998;7151-7160.
    • (1998) EMBO J. , vol.17 , Issue.24 , pp. 7151-7160
    • Ciechanover, A.1
  • 212
    • 0031973765 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in cancer
    • Spataro V., Norbury C., Harris A.L. The ubiquitin-proteasome pathway in cancer. Br. J. Cancer. 77(3):1998;448-455.
    • (1998) Br. J. Cancer , vol.77 , Issue.3 , pp. 448-455
    • Spataro, V.1    Norbury, C.2    Harris, A.L.3
  • 213
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz A.L., Ciechanover A. The ubiquitin-proteasome pathway and pathogenesis of human diseases. Ann. Rev. Med. 50:1999;57-74.
    • (1999) Ann. Rev. Med. , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 214
    • 0033118469 scopus 로고    scopus 로고
    • Relationships between proteasomes and viral gene products
    • Jarrousse A.S., Gautier K., Apcher S.et al. Relationships between proteasomes and viral gene products. Mol. Biol. Rep. 26(1-2):1999;113-117.
    • (1999) Mol. Biol. Rep. , vol.26 , Issue.12 , pp. 113-117
    • Jarrousse, A.S.1    Gautier, K.2    Apcher, S.3
  • 215
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M., Huibregtse J.M., Vierstra R.D., Howley P.M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell. 75(3):1993;495-505.
    • (1993) Cell , vol.75 , Issue.3 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 216
    • 0031042746 scopus 로고    scopus 로고
    • Cancer prognostics: Past, present and p27
    • Steeg P.S., Abrams J.S. Cancer prognostics. past, present and p27 Nat. Med. 3(2):1997;152-154.
    • (1997) Nat. Med. , vol.3 , Issue.2 , pp. 152-154
    • Steeg, P.S.1    Abrams, J.S.2
  • 217
    • 0031048716 scopus 로고    scopus 로고
    • Expression of cell-cycle regulators p27Kip1 and cyclin E, alone and in combination, correlate with survival in young breast cancer patients
    • Porter P.L., Malone K.E., Heagerty P.J.et al. Expression of cell-cycle regulators p27Kip1 and cyclin E, alone and in combination, correlate with survival in young breast cancer patients. Nat. Med. 3(2):1997;222-225.
    • (1997) Nat. Med. , vol.3 , Issue.2 , pp. 222-225
    • Porter, P.L.1    Malone, K.E.2    Heagerty, P.J.3
  • 218
    • 16944363001 scopus 로고    scopus 로고
    • Decreased levels of the cell-cycle inhibitor p27Kip1 protein: Prognostic implications in primary breast cancer
    • Catzavelos C., Bhattacharya N., Ung Y.C.et al. Decreased levels of the cell-cycle inhibitor p27Kip1 protein. prognostic implications in primary breast cancer Nat. Med. 3(2):1997;227-230.
    • (1997) Nat. Med. , vol.3 , Issue.2 , pp. 227-230
    • Catzavelos, C.1    Bhattacharya, N.2    Ung, Y.C.3
  • 219
    • 0031048236 scopus 로고    scopus 로고
    • Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas
    • Loda M., Cukor B., Tam S.W.et al. Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nat. Med. 3(2):1997;231-234.
    • (1997) Nat. Med. , vol.3 , Issue.2 , pp. 231-234
    • Loda, M.1    Cukor, B.2    Tam, S.W.3
  • 220
    • 0033141406 scopus 로고    scopus 로고
    • NF-kappaB to the rescue: RELs, apoptosis and cellular transformation
    • Foo S.Y., Nolan G.P. NF-kappaB to the rescue. RELs, apoptosis and cellular transformation Trends Genet. 15(6):1999;229-235.
    • (1999) Trends Genet. , vol.15 , Issue.6 , pp. 229-235
    • Foo, S.Y.1    Nolan, G.P.2
  • 221
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control
    • Chu Z.L., McKinsey T.A., Liu L., Gentry J.J., Malim M.H., Ballard D.W. Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control. Proc. Natl. Acad. Sci. USA. 94(19):1997;10057-10062.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.19 , pp. 10057-10062
    • Chu, Z.L.1    McKinsey, T.A.2    Liu, L.3    Gentry, J.J.4    Malim, M.H.5    Ballard, D.W.6
  • 222
    • 0029666234 scopus 로고    scopus 로고
    • The NF-kappaB transcription factor in oncogenesis
    • Sharma H.W., Narayanan R. The NF-kappaB transcription factor in oncogenesis. Anticancer Res. 16(2):1996;589-596.
    • (1996) Anticancer Res. , vol.16 , Issue.2 , pp. 589-596
    • Sharma, H.W.1    Narayanan, R.2
  • 223
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • Fenteany G., Schreiber S.L. Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 273(15):1998;8545-8548.
    • (1998) J. Biol. Chem. , vol.273 , Issue.15 , pp. 8545-8548
    • Fenteany, G.1    Schreiber, S.L.2
  • 224
    • 0026699379 scopus 로고
    • Inhibition of different steps of the ubiquitin system by cisplatin and aclarubicin
    • Isoe T., Naito M., Shirai A., Hirai R., Tsuruo T. Inhibition of different steps of the ubiquitin system by cisplatin and aclarubicin. Biochim. Biophys. Acta. 1117(2):1992;131-135.
    • (1992) Biochim. Biophys. Acta , vol.1117 , Issue.2 , pp. 131-135
    • Isoe, T.1    Naito, M.2    Shirai, A.3    Hirai, R.4    Tsuruo, T.5
  • 225
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee D.H., Goldberg A. Proteasome inhibitors. valuable new tools for cell biologists Trends Cell Biol. 8(10):1998;397-403.
    • (1998) Trends Cell Biol. , vol.8 , Issue.10 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.2
  • 226
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: A novel class of potent and effective antitumor agents
    • Adams J., Palombella V.J., Sausville E.A.et al. Proteasome inhibitors. a novel class of potent and effective antitumor agents Cancer Res. 59(11):1999;2615-2622.
    • (1999) Cancer Res. , vol.59 , Issue.11 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 227
    • 0031831274 scopus 로고    scopus 로고
    • Combinatorial control in ubiquitin dependent proteolysis: Don't Skp the F-box hypothesis
    • Patton E.E., Willems A.R., Tyers M. Combinatorial control in ubiquitin dependent proteolysis. don't Skp the F-box hypothesis Trends Genet. 14(6):1998;236-243.
    • (1998) Trends Genet. , vol.14 , Issue.6 , pp. 236-243
    • Patton, E.E.1    Willems, A.R.2    Tyers, M.3
  • 228
    • 0033565672 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity
    • Lisztwan J., Imbert G., Wirbelauer C., Gstaiger M., Krek W. The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity. Genes Dev. 13(14):1999;1822-1833.
    • (1999) Genes Dev. , vol.13 , Issue.14 , pp. 1822-1833
    • Lisztwan, J.1    Imbert, G.2    Wirbelauer, C.3    Gstaiger, M.4    Krek, W.5
  • 230
    • 0033523203 scopus 로고    scopus 로고
    • Chromatin remodelling and transcriptional regulation
    • Luo R.X., Dean D.C. Chromatin remodelling and transcriptional regulation. J. Natl. Cancer Inst. 91(15):1999;1288-1294.
    • (1999) J. Natl. Cancer Inst. , vol.91 , Issue.15 , pp. 1288-1294
    • Luo, R.X.1    Dean, D.C.2
  • 231
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr. Opin. Genet. Dev. 9(1):1999;40-48.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , Issue.1 , pp. 40-48
    • Kouzarides, T.1
  • 232
    • 0033551152 scopus 로고    scopus 로고
    • A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors
    • Saito A., Yamashita T., Mariko Y.et al. A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors. Proc. Natl. Acad. Sci. USA. 96(8):1999;4592-4597.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.8 , pp. 4592-4597
    • Saito, A.1    Yamashita, T.2    Mariko, Y.3
  • 233
    • 0033529033 scopus 로고    scopus 로고
    • Molecular chaperones: The busy life of Hsp90
    • Mayer M.P., Bukau B. Molecular chaperones. the busy life of Hsp90 Curr. Biol. 9(9):1999;R322-325.
    • (1999) Curr. Biol. , vol.9 , Issue.9 , pp. 322-325
    • Mayer, M.P.1    Bukau, B.2
  • 234
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte T.W., Neckers L.M. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. 42(4):1998;273-279.
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , Issue.4 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 235
    • 0033579175 scopus 로고    scopus 로고
    • DT-diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland L.R., Sharp S.Y., Rogers P.M., Myers T.G., Workman P. DT-diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J. Natl. Cancer Inst. 91(22):1999;1-10.
    • (1999) J. Natl. Cancer Inst. , vol.91 , Issue.22 , pp. 1-10
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 236
    • 0030608633 scopus 로고    scopus 로고
    • O6-benzylguanine and its role in chemotherapy
    • Dolan M.E., Pegg A.E. O6-benzylguanine and its role in chemotherapy. Clin. Cancer Res. 3(6):1997;837-847.
    • (1997) Clin. Cancer Res. , vol.3 , Issue.6 , pp. 837-847
    • Dolan, M.E.1    Pegg, A.E.2
  • 237
    • 0029080684 scopus 로고
    • The role of inhibitors of poly(ADP-ribose) polymerase as resistance-modifying agents in cancer therapy
    • Griffin R.J., Crutin N.J., Newell D.R., Golding B.T., Durkacz B.W., Calvert A.H. The role of inhibitors of poly(ADP-ribose) polymerase as resistance-modifying agents in cancer therapy. Biochimie. 77(6):1995;408-422.
    • (1995) Biochimie , vol.77 , Issue.6 , pp. 408-422
    • Griffin, R.J.1    Crutin, N.J.2    Newell, D.R.3    Golding, B.T.4    Durkacz, B.W.5    Calvert, A.H.6
  • 238
    • 0030442683 scopus 로고    scopus 로고
    • DNA damage detection by DNA dependent protein kinase and related enzymes
    • Jackson S.P. DNA damage detection by DNA dependent protein kinase and related enzymes. Cancer Surv. 28:1996;261-279.
    • (1996) Cancer Surv. , vol.28 , pp. 261-279
    • Jackson, S.P.1
  • 239
    • 0032828652 scopus 로고    scopus 로고
    • Inhibition of telomerase limits the growth of human cancer cells
    • Hahn W.C., Stewart S.A., Brooks M.W.et al. Inhibition of telomerase limits the growth of human cancer cells. Nat. Med. 5(10):1999;1164-1170.
    • (1999) Nat. Med. , vol.5 , Issue.10 , pp. 1164-1170
    • Hahn, W.C.1    Stewart, S.A.2    Brooks, M.W.3
  • 240
    • 0032825217 scopus 로고    scopus 로고
    • Telomeres: Has cancer's Achilles' heel been exposed?
    • Zumstein L.A., Lundbald V. Telomeres. has cancer's Achilles' heel been exposed? Nat. Med. 5(10):1999;1129-1130.
    • (1999) Nat. Med. , vol.5 , Issue.10 , pp. 1129-1130
    • Zumstein, L.A.1    Lundbald, V.2
  • 241
    • 0033529563 scopus 로고    scopus 로고
    • For better or worse? Telomerase inhibition and cancer
    • De Lange T., Jacks T. For better or worse? Telomerase inhibition and cancer. Cell. 98(3):1999;273-275.
    • (1999) Cell , vol.98 , Issue.3 , pp. 273-275
    • De Lange, T.1    Jacks, T.2
  • 242
    • 0031760366 scopus 로고    scopus 로고
    • Telomeres and telomerase: Targets for cancer chemotherapy
    • Perry P.J., Kelland L.R. Telomeres and telomerase. targets for cancer chemotherapy Exp. Opin. Ther. Patents. 8(12):1998;1567-1586.
    • (1998) Exp. Opin. Ther. Patents , vol.8 , Issue.12 , pp. 1567-1586
    • Perry, P.J.1    Kelland, L.R.2
  • 245
    • 0033044355 scopus 로고    scopus 로고
    • EIF4E expression in tumours: Its possible role in progression of malignancies
    • De Benedetti A., Harris A.L. EIF4E expression in tumours. its possible role in progression of malignancies Int. J. Biochem. Cell Biol. 31(1):1999;59-72.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , Issue.1 , pp. 59-72
    • De Benedetti, A.1    Harris, A.L.2
  • 246
    • 0342904899 scopus 로고    scopus 로고
    • Pharmaprojects, Richmond, PJB Publications
    • Pharmaprojects, Richmond, PJB Publications, 1999.
    • (1999)
  • 247
    • 0033585504 scopus 로고    scopus 로고
    • In vivo eradication of human bcr/abl-positive leukemia cells with an abl kinase inhibitor
    • Le Coutre P., Mologni L., Cleris L.et al. In vivo eradication of human bcr/abl-positive leukemia cells with an abl kinase inhibitor. J. Natl. Cancer Inst. 91(2):1999;163-168.
    • (1999) J. Natl. Cancer Inst. , vol.91 , Issue.2 , pp. 163-168
    • Le Coutre, P.1    Mologni, L.2    Cleris, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.