메뉴 건너뛰기




Volumn 32, Issue 10, 2008, Pages 1573-1581

Polyadenylation inhibition by the triphosphates of deoxyadenosine analogues

Author keywords

Cladribine; Clofarabine; Fludarabine; Nucleoside analogs; Polyadenylation inhibition; RNA processing; Transcription

Indexed keywords

CLADRIBINE; CLOFARABINE; FLUDARABINE TRIPHOSPHATE; POLYNUCLEOTIDE ADENYLYLTRANSFERASE;

EID: 44749088810     PISSN: 01452126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.leukres.2008.03.010     Document Type: Article
Times cited : (18)

References (51)
  • 1
    • 23844481419 scopus 로고    scopus 로고
    • Purine nucleoside analogues for the treatment of hematological malignancies: pharmacology and clinical applications
    • Robak T., Korycka A., Kasznicki M., Wrzesien-Kus A., and Smolewski P. Purine nucleoside analogues for the treatment of hematological malignancies: pharmacology and clinical applications. Curr Cancer Drug Tar 5 (2005) 421-444
    • (2005) Curr Cancer Drug Tar , vol.5 , pp. 421-444
    • Robak, T.1    Korycka, A.2    Kasznicki, M.3    Wrzesien-Kus, A.4    Smolewski, P.5
  • 3
    • 19944433802 scopus 로고    scopus 로고
    • Results of a phase 1-2 study of clofarabine in combination with cytarabine (ara-C) in relapsed and refractory acute leukemias
    • Faderl S., Gandhi V., O'Brien S., Bonate P., Cortes J., Estey E., et al. Results of a phase 1-2 study of clofarabine in combination with cytarabine (ara-C) in relapsed and refractory acute leukemias. Blood 105 (2005) 940-947
    • (2005) Blood , vol.105 , pp. 940-947
    • Faderl, S.1    Gandhi, V.2    O'Brien, S.3    Bonate, P.4    Cortes, J.5    Estey, E.6
  • 4
    • 9144222570 scopus 로고    scopus 로고
    • a novel nucleoside analog, is active in pediatric patients with advanced leukemia
    • Jeha S., Gandhi V., Chan K.W., McDonald L., Ramirez I., Madden R., et al. a novel nucleoside analog, is active in pediatric patients with advanced leukemia. Blood 103 (2004) 784-789
    • (2004) Blood , vol.103 , pp. 784-789
    • Jeha, S.1    Gandhi, V.2    Chan, K.W.3    McDonald, L.4    Ramirez, I.5    Madden, R.6
  • 5
    • 19344378925 scopus 로고    scopus 로고
    • Cell death of bioenergetically compromised and transcriptionally challenged CLL lymphocytes by chlorinated ATP
    • Balakrishnan K., Stellrecht C.M., Genini D., Ayres M., Wierda W.G., Keating M.J., et al. Cell death of bioenergetically compromised and transcriptionally challenged CLL lymphocytes by chlorinated ATP. Blood 105 (2005) 4455-4462
    • (2005) Blood , vol.105 , pp. 4455-4462
    • Balakrishnan, K.1    Stellrecht, C.M.2    Genini, D.3    Ayres, M.4    Wierda, W.G.5    Keating, M.J.6
  • 6
    • 25144507001 scopus 로고    scopus 로고
    • Mechanisms of cell death of chronic lymphocytic leukemia lymphocytes by RNA-directed agent, 8-NH2-adenosine
    • Balakrishnan K., Wierda W.G., Keating M.J., and Gandhi V. Mechanisms of cell death of chronic lymphocytic leukemia lymphocytes by RNA-directed agent, 8-NH2-adenosine. Clin Cancer Res 11 (2005) 6745-6752
    • (2005) Clin Cancer Res , vol.11 , pp. 6745-6752
    • Balakrishnan, K.1    Wierda, W.G.2    Keating, M.J.3    Gandhi, V.4
  • 7
    • 4644355516 scopus 로고    scopus 로고
    • Chain termination and inhibition of Saccharomyces cerevisiae poly(A) polymerase by C8-modified ATP analogs
    • Chen L.S., and Sheppard T.L. Chain termination and inhibition of Saccharomyces cerevisiae poly(A) polymerase by C8-modified ATP analogs. J Biol Chem 279 (2004) 40405-40411
    • (2004) J Biol Chem , vol.279 , pp. 40405-40411
    • Chen, L.S.1    Sheppard, T.L.2
  • 8
    • 0033902940 scopus 로고    scopus 로고
    • Inhibition of RNA transcription: a biochemical mechanism of action against chronic lymphocytic leukemia cells by fludarabine
    • Huang P., Sandoval A., Van Den Neste E., Keating M.J., and Plunkett W. Inhibition of RNA transcription: a biochemical mechanism of action against chronic lymphocytic leukemia cells by fludarabine. Leukemia 14 (2000) 1405-1413
    • (2000) Leukemia , vol.14 , pp. 1405-1413
    • Huang, P.1    Sandoval, A.2    Van Den Neste, E.3    Keating, M.J.4    Plunkett, W.5
  • 9
    • 39749115845 scopus 로고    scopus 로고
    • RNA-directed agent, cordycepin, induces cell death in multiple myeloma cells
    • Chen L.S., Stellrecht C.M., and Gandhi V. RNA-directed agent, cordycepin, induces cell death in multiple myeloma cells. Br J Haematol 140 (2008) 682-691
    • (2008) Br J Haematol , vol.140 , pp. 682-691
    • Chen, L.S.1    Stellrecht, C.M.2    Gandhi, V.3
  • 10
    • 27644485122 scopus 로고    scopus 로고
    • Eukaryotic mRNA 3′ processing: a common means to different ends
    • Gilmartin G.M. Eukaryotic mRNA 3′ processing: a common means to different ends. Genes Dev 19 (2005) 2517-2521
    • (2005) Genes Dev , vol.19 , pp. 2517-2521
    • Gilmartin, G.M.1
  • 11
    • 0030784958 scopus 로고    scopus 로고
    • Mechanism and regulation of mRNA polyadenylation
    • Colgan D.F., and Manley J.L. Mechanism and regulation of mRNA polyadenylation. Genes Dev 11 (1997) 2755-2766
    • (1997) Genes Dev , vol.11 , pp. 2755-2766
    • Colgan, D.F.1    Manley, J.L.2
  • 12
    • 0029883718 scopus 로고    scopus 로고
    • Role of polyadenylation in nucleocytoplasmic transport of mRNA
    • Huang Y., and Carmichael G.C. Role of polyadenylation in nucleocytoplasmic transport of mRNA. Mol Cell Biol 16 (1996) 1534-1542
    • (1996) Mol Cell Biol , vol.16 , pp. 1534-1542
    • Huang, Y.1    Carmichael, G.C.2
  • 13
    • 0030731419 scopus 로고    scopus 로고
    • Starting at the beginning, middle, and end: translation initiation in eukaryotes
    • Sachs A.B., Sarnow P., and Hentze M.W. Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell 89 (1997) 831-838
    • (1997) Cell , vol.89 , pp. 831-838
    • Sachs, A.B.1    Sarnow, P.2    Hentze, M.W.3
  • 15
    • 0029053016 scopus 로고
    • Degradation of mRNA in eukaryotes
    • Beelman C.A., and Parker R. Degradation of mRNA in eukaryotes. Cell 81 (1995) 179-183
    • (1995) Cell , vol.81 , pp. 179-183
    • Beelman, C.A.1    Parker, R.2
  • 17
    • 0034935020 scopus 로고    scopus 로고
    • Identification and functional characterization of neo-poly(A) polymerase, an RNA processing enzyme overexpressed in human tumors
    • Topalian S.L., Kaneko S., Gonzales M.I., Bond G.L., Ward Y., and Manley J.L. Identification and functional characterization of neo-poly(A) polymerase, an RNA processing enzyme overexpressed in human tumors. Mol Cell Biol 21 (2001) 5614-5623
    • (2001) Mol Cell Biol , vol.21 , pp. 5614-5623
    • Topalian, S.L.1    Kaneko, S.2    Gonzales, M.I.3    Bond, G.L.4    Ward, Y.5    Manley, J.L.6
  • 18
    • 0034306990 scopus 로고    scopus 로고
    • Polyadenylate polymerase enzymatic activity in mammary tumor cytosols: a new independent prognostic marker in primary breast cancer
    • Scorilas A., Talieri M., Ardavanis A., Courtis N., Dimitriadis E., Yotis J., et al. Polyadenylate polymerase enzymatic activity in mammary tumor cytosols: a new independent prognostic marker in primary breast cancer. Cancer Res 60 (2000) 5427-5433
    • (2000) Cancer Res , vol.60 , pp. 5427-5433
    • Scorilas, A.1    Talieri, M.2    Ardavanis, A.3    Courtis, N.4    Dimitriadis, E.5    Yotis, J.6
  • 19
    • 0016607411 scopus 로고
    • Polyadenylate polymerases from yeast
    • Haff L.A., and Keller E.B. Polyadenylate polymerases from yeast. J Biol Chem 250 (1975) 1838-1846
    • (1975) J Biol Chem , vol.250 , pp. 1838-1846
    • Haff, L.A.1    Keller, E.B.2
  • 20
    • 0035823480 scopus 로고    scopus 로고
    • A novel nuclear human poly(A) polymerase (PAP), PAP gamma
    • Kyriakopoulou C.B., Nordvarg H., and Virtanen A. A novel nuclear human poly(A) polymerase (PAP), PAP gamma. J Biol Chem 276 (2001) 33504-33511
    • (2001) J Biol Chem , vol.276 , pp. 33504-33511
    • Kyriakopoulou, C.B.1    Nordvarg, H.2    Virtanen, A.3
  • 21
    • 0031658778 scopus 로고    scopus 로고
    • Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain
    • Zhelkovsky A., Helmling S., and Moore C. Processivity of the Saccharomyces cerevisiae poly(A) polymerase requires interactions at the carboxyl-terminal RNA binding domain. Mol Cell Biol 18 (1998) 5942-5951
    • (1998) Mol Cell Biol , vol.18 , pp. 5942-5951
    • Zhelkovsky, A.1    Helmling, S.2    Moore, C.3
  • 22
    • 0017382248 scopus 로고
    • Specific inhibition of chromatin-associated poly(A) synthesis in vitro by cordycepin 5′-triphosphate
    • Rose K.M., Bell L.E., and Jacob S.T. Specific inhibition of chromatin-associated poly(A) synthesis in vitro by cordycepin 5′-triphosphate. Nature 267 (1977) 178-180
    • (1977) Nature , vol.267 , pp. 178-180
    • Rose, K.M.1    Bell, L.E.2    Jacob, S.T.3
  • 23
    • 0025787944 scopus 로고
    • Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae
    • Lingner J., Kellermann J., and Keller W. Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae. Nature 354 (1991) 496-498
    • (1991) Nature , vol.354 , pp. 496-498
    • Lingner, J.1    Kellermann, J.2    Keller, W.3
  • 24
    • 0031915525 scopus 로고    scopus 로고
    • Tailing and 3′-end labeling of RNA with yeast poly(A) polymerase and various nucleotides
    • Martin G., and Keller W. Tailing and 3′-end labeling of RNA with yeast poly(A) polymerase and various nucleotides. RNA 4 (1998) 226-230
    • (1998) RNA , vol.4 , pp. 226-230
    • Martin, G.1    Keller, W.2
  • 25
    • 0025990038 scopus 로고
    • Ara-ATP impairs 3′-end processing of pre-mRNAs by inhibiting both cleavage and polyadenylation
    • Ghoshal K., and Jacob S.T. Ara-ATP impairs 3′-end processing of pre-mRNAs by inhibiting both cleavage and polyadenylation. Nucleic Acids Res 19 (1991) 5871-5875
    • (1991) Nucleic Acids Res , vol.19 , pp. 5871-5875
    • Ghoshal, K.1    Jacob, S.T.2
  • 26
    • 3843067711 scopus 로고    scopus 로고
    • Structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase
    • Martin G., Moeglich A., Keller W., Doublie S., and Biochemical. Structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase. J Mol Biol 341 (2004) 911-925
    • (2004) J Mol Biol , vol.341 , pp. 911-925
    • Martin, G.1    Moeglich, A.2    Keller, W.3    Doublie, S.4    Biochemical5
  • 27
    • 34548382114 scopus 로고    scopus 로고
    • Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis
    • Balbo P.B., and Bohm A. Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis. Structure 15 (2007) 1117-1131
    • (2007) Structure , vol.15 , pp. 1117-1131
    • Balbo, P.B.1    Bohm, A.2
  • 28
    • 0031057250 scopus 로고    scopus 로고
    • Treatment of hairy-cell leukemia with cladribine: response, toxicity, and long-term follow-up
    • Hoffman M.A., Janson D., Rose E., and Rai K.R. Treatment of hairy-cell leukemia with cladribine: response, toxicity, and long-term follow-up. J Clin Oncol 15 (1997) 1138-1142
    • (1997) J Clin Oncol , vol.15 , pp. 1138-1142
    • Hoffman, M.A.1    Janson, D.2    Rose, E.3    Rai, K.R.4
  • 29
    • 0022003367 scopus 로고
    • Mechanism of deoxyadenosine and 2-chlorodeoxyadenosine toxicity to nondividing human lymphocytes
    • Seto S., Carrera C.J., Kubota M., Wasson D.B., and Carson D.A. Mechanism of deoxyadenosine and 2-chlorodeoxyadenosine toxicity to nondividing human lymphocytes. J Clin Invest 75 (1985) 377-383
    • (1985) J Clin Invest , vol.75 , pp. 377-383
    • Seto, S.1    Carrera, C.J.2    Kubota, M.3    Wasson, D.B.4    Carson, D.A.5
  • 30
    • 0020612685 scopus 로고
    • Specific toxicity of 2-chlorodeoxyadenosine toward resting and proliferating human lymphocytes
    • Carson D.A., Wasson D.B., Taetle R., and Yu A. Specific toxicity of 2-chlorodeoxyadenosine toward resting and proliferating human lymphocytes. Blood 62 (1983) 737-743
    • (1983) Blood , vol.62 , pp. 737-743
    • Carson, D.A.1    Wasson, D.B.2    Taetle, R.3    Yu, A.4
  • 31
    • 0025233649 scopus 로고
    • Incorporation of 2-halogeno-2′-deoxyadenosine 5-triphosphates into DNA during replication by human polymerases alpha and beta
    • Hentosh P., Koob R., and Blakley R.L. Incorporation of 2-halogeno-2′-deoxyadenosine 5-triphosphates into DNA during replication by human polymerases alpha and beta. J Biol Chem 265 (1990) 4033-4040
    • (1990) J Biol Chem , vol.265 , pp. 4033-4040
    • Hentosh, P.1    Koob, R.2    Blakley, R.L.3
  • 32
    • 0024787036 scopus 로고
    • Mechanisms of inhibition of DNA synthesis by 2-chlorodeoxyadenosine in human lymphoblastic cells
    • Griffig J., Koob R., and Blakley R.L. Mechanisms of inhibition of DNA synthesis by 2-chlorodeoxyadenosine in human lymphoblastic cells. Cancer Res 49 (1989) 6923-6928
    • (1989) Cancer Res , vol.49 , pp. 6923-6928
    • Griffig, J.1    Koob, R.2    Blakley, R.L.3
  • 33
    • 0023733094 scopus 로고
    • Interaction of 2-halogenated dATP analogs (fluoride, chloride, and bromide) with human DNA polymerases, DNA primase, and ribonucleotide reductase
    • Parker W.B., Bapat A.R., Shen J.X., Townsend A.J., and Cheng Y.C. Interaction of 2-halogenated dATP analogs (fluoride, chloride, and bromide) with human DNA polymerases, DNA primase, and ribonucleotide reductase. Mol Pharmacol 34 (1988) 485-491
    • (1988) Mol Pharmacol , vol.34 , pp. 485-491
    • Parker, W.B.1    Bapat, A.R.2    Shen, J.X.3    Townsend, A.J.4    Cheng, Y.C.5
  • 34
    • 85009865467 scopus 로고    scopus 로고
    • 2-Chloro-2′-deoxyadenosine inhibits DNA repair synthesis and potentiates UVC cytotoxicity in chronic lymphocytic leukemia B lymphocytes
    • Van Den Neste E., Cardoen S., Husson B., Rosier J.F., Delacauw A., Ferrant A., et al. 2-Chloro-2′-deoxyadenosine inhibits DNA repair synthesis and potentiates UVC cytotoxicity in chronic lymphocytic leukemia B lymphocytes. Leukemia 16 (2002) 36-43
    • (2002) Leukemia , vol.16 , pp. 36-43
    • Van Den Neste, E.1    Cardoen, S.2    Husson, B.3    Rosier, J.F.4    Delacauw, A.5    Ferrant, A.6
  • 35
    • 0033028601 scopus 로고    scopus 로고
    • Purine analogues kill resting lymphocytes by p53-dependent and -independent mechanisms
    • Pettitt A.R., Clarke A.R., Cawley J.C., and Griffiths S.D. Purine analogues kill resting lymphocytes by p53-dependent and -independent mechanisms. Brit J Haematol 105 (1999) 986-988
    • (1999) Brit J Haematol , vol.105 , pp. 986-988
    • Pettitt, A.R.1    Clarke, A.R.2    Cawley, J.C.3    Griffiths, S.D.4
  • 36
    • 0032844150 scopus 로고    scopus 로고
    • The effect of p53 dysfunction on purine analogue cytotoxicity in chronic lymphocytic leukaemia
    • Pettitt A.R., Sherrington P.D., and Cawley J.C. The effect of p53 dysfunction on purine analogue cytotoxicity in chronic lymphocytic leukaemia. Brit J Haematol 106 (1999) 1049-1051
    • (1999) Brit J Haematol , vol.106 , pp. 1049-1051
    • Pettitt, A.R.1    Sherrington, P.D.2    Cawley, J.C.3
  • 37
    • 0034669944 scopus 로고    scopus 로고
    • Deoxyadenosine analogs induce programmed cell death in chronic lymphocytic leukemia cells by damaging the DNA and by directly affecting the mitochondria
    • Genini D., Adachi S., Chao Q., Rose D.W., Carrera C.J., Cottam H.B., et al. Deoxyadenosine analogs induce programmed cell death in chronic lymphocytic leukemia cells by damaging the DNA and by directly affecting the mitochondria. Blood 96 (2000) 3537-3543
    • (2000) Blood , vol.96 , pp. 3537-3543
    • Genini, D.1    Adachi, S.2    Chao, Q.3    Rose, D.W.4    Carrera, C.J.5    Cottam, H.B.6
  • 38
    • 0034614551 scopus 로고    scopus 로고
    • Nucleotide requirements for the in vitro activation of the apoptosis protein-activating factor-1-mediated caspase pathway
    • Genini D., Budihardjo I., Plunkett W., Wang X., Carrera C.J., Cottam H.B., et al. Nucleotide requirements for the in vitro activation of the apoptosis protein-activating factor-1-mediated caspase pathway. J Biol Chem 275 (2000) 29-34
    • (2000) J Biol Chem , vol.275 , pp. 29-34
    • Genini, D.1    Budihardjo, I.2    Plunkett, W.3    Wang, X.4    Carrera, C.J.5    Cottam, H.B.6
  • 39
    • 0032483010 scopus 로고    scopus 로고
    • Induction of an apoptotic program in cell-free extracts by 2-chloro-2′-deoxyadenosine 5′-triphosphate and cytochrome c
    • Leoni L.M., Chao Q., Cottam H.B., Genini D., Rosenbach M., Carrera C.J., et al. Induction of an apoptotic program in cell-free extracts by 2-chloro-2′-deoxyadenosine 5′-triphosphate and cytochrome c. Proc Natl Acad Sci USA 95 (1998) 9567-9571
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9567-9571
    • Leoni, L.M.1    Chao, Q.2    Cottam, H.B.3    Genini, D.4    Rosenbach, M.5    Carrera, C.J.6
  • 40
    • 0028822482 scopus 로고
    • In vitro transcription of DNA containing 2-chloro-2′-deoxyadenosine monophosphate
    • Hentosh P., and Tibudan M. In vitro transcription of DNA containing 2-chloro-2′-deoxyadenosine monophosphate. Mol Pharmacol 48 (1995) 897-904
    • (1995) Mol Pharmacol , vol.48 , pp. 897-904
    • Hentosh, P.1    Tibudan, M.2
  • 41
    • 0031900744 scopus 로고    scopus 로고
    • Pharmacokinetics of cladribine in plasma and its 5′-monophosphate and 5′-triphosphate in leukemic cells of patients with chronic lymphocytic leukemia
    • Albertioni F., Lindemalm S., Reichelova V., Pettersson B., Eriksson S., Juliusson G., et al. Pharmacokinetics of cladribine in plasma and its 5′-monophosphate and 5′-triphosphate in leukemic cells of patients with chronic lymphocytic leukemia. Clin Cancer Res 4 (1998) 653-658
    • (1998) Clin Cancer Res , vol.4 , pp. 653-658
    • Albertioni, F.1    Lindemalm, S.2    Reichelova, V.3    Pettersson, B.4    Eriksson, S.5    Juliusson, G.6
  • 42
    • 0027436016 scopus 로고
    • Fludarabine: pharmacokinetics, mechanisms of action, and rationales for combination therapies
    • Plunkett W., Gandhi V., Huang P., Robertson L.E., Yang L.Y., Gregoire V., et al. Fludarabine: pharmacokinetics, mechanisms of action, and rationales for combination therapies. Semin Oncol 20 (1993) 2-12
    • (1993) Semin Oncol , vol.20 , pp. 2-12
    • Plunkett, W.1    Gandhi, V.2    Huang, P.3    Robertson, L.E.4    Yang, L.Y.5    Gregoire, V.6
  • 43
    • 0025130572 scopus 로고
    • Termination of DNA synthesis by 9-β-d-arabinofuranosyl-2-fluoroadenine. A mechanism for cytotoxicity
    • Huang P., Chubb S., and Plunkett W. Termination of DNA synthesis by 9-β-d-arabinofuranosyl-2-fluoroadenine. A mechanism for cytotoxicity. J Biol Chem 265 (1990) 16617-16625
    • (1990) J Biol Chem , vol.265 , pp. 16617-16625
    • Huang, P.1    Chubb, S.2    Plunkett, W.3
  • 44
    • 0020058465 scopus 로고
    • In vitro biological activity of 9-β-d-arabinofuranosyl-2-fluoroadenine and the biochemical actions of its triphosphate on DNA polymerases and ribonucleotide reductase from HeLa cells
    • Tseng W.C., Derse D., Cheng Y.C., Brockman R.W., and Bennett Jr. L.L. In vitro biological activity of 9-β-d-arabinofuranosyl-2-fluoroadenine and the biochemical actions of its triphosphate on DNA polymerases and ribonucleotide reductase from HeLa cells. Mol Pharmacol 21 (1982) 474-477
    • (1982) Mol Pharmacol , vol.21 , pp. 474-477
    • Tseng, W.C.1    Derse, D.2    Cheng, Y.C.3    Brockman, R.W.4    Bennett Jr., L.L.5
  • 45
    • 0025777811 scopus 로고
    • Action of 9-β-d-arabinofuranosyl-2-fluoroadenine on RNA metabolism
    • Huang P., and Plunkett W. Action of 9-β-d-arabinofuranosyl-2-fluoroadenine on RNA metabolism. Mol Pharmacol 39 (1991) 449-455
    • (1991) Mol Pharmacol , vol.39 , pp. 449-455
    • Huang, P.1    Plunkett, W.2
  • 46
    • 0022991391 scopus 로고
    • 9-Beta-d-arabinofuranosyl-2-fluoroadenine 5′-monophosphate pharmacokinetics in plasma and tumor cells of patients with relapsed leukemia and lymphoma
    • Danhauser L., Plunkett W., Keating M., and Cabanillas F. 9-Beta-d-arabinofuranosyl-2-fluoroadenine 5′-monophosphate pharmacokinetics in plasma and tumor cells of patients with relapsed leukemia and lymphoma. Cancer Chemother Pharmacol 18 (1986) 145-152
    • (1986) Cancer Chemother Pharmacol , vol.18 , pp. 145-152
    • Danhauser, L.1    Plunkett, W.2    Keating, M.3    Cabanillas, F.4
  • 47
    • 0030832602 scopus 로고    scopus 로고
    • Fludarabine ability to down-regulate Bcl-2 gene product in CD5+ leukemic B cells: in vitro/in vivo correlations
    • Gottardi D., De Leo A.M., Alfarano A., Stacchini A., Circosta P., Gregoretti M.G., et al. Fludarabine ability to down-regulate Bcl-2 gene product in CD5+ leukemic B cells: in vitro/in vivo correlations. Brit J Haematol 99 (1997) 147-157
    • (1997) Brit J Haematol , vol.99 , pp. 147-157
    • Gottardi, D.1    De Leo, A.M.2    Alfarano, A.3    Stacchini, A.4    Circosta, P.5    Gregoretti, M.G.6
  • 48
    • 0029053894 scopus 로고
    • Metabolism and actions of 2-chloro-9-(2-deoxy-2-fluoro-β-d-arabinofuranosyl)-adenine in human lymphoblastoid cells
    • Xie C., and Plunkett W. Metabolism and actions of 2-chloro-9-(2-deoxy-2-fluoro-β-d-arabinofuranosyl)-adenine in human lymphoblastoid cells. Cancer Res 55 (1995) 2847-2852
    • (1995) Cancer Res , vol.55 , pp. 2847-2852
    • Xie, C.1    Plunkett, W.2
  • 49
    • 0025811415 scopus 로고
    • Effects of 2-chloro-9-(2-deoxy-2-fluoro-β-d-arabinofuranosyl)adenine on K562 cellular metabolism and the inhibition of human ribonucleotide reductase and DNA polymerases by its 5′-triphosphate
    • Parker W.B., Shaddix S.C., Chang C.H., White E.L., Rose L.M., Brockman R.W., et al. Effects of 2-chloro-9-(2-deoxy-2-fluoro-β-d-arabinofuranosyl)adenine on K562 cellular metabolism and the inhibition of human ribonucleotide reductase and DNA polymerases by its 5′-triphosphate. Cancer Res 51 (1991) 2386-2394
    • (1991) Cancer Res , vol.51 , pp. 2386-2394
    • Parker, W.B.1    Shaddix, S.C.2    Chang, C.H.3    White, E.L.4    Rose, L.M.5    Brockman, R.W.6
  • 50
    • 0346963139 scopus 로고    scopus 로고
    • Pharmacodynamics of plasma clofarabine and cellular clofarabine triphosphate in patients with acute leukemias
    • Gandhi V., Kantarjian H., Faderl S., Bonate P., Du M., Ayres M., et al. Pharmacodynamics of plasma clofarabine and cellular clofarabine triphosphate in patients with acute leukemias. Clin Cancer Res 9 (2003) 6335-6342
    • (2003) Clin Cancer Res , vol.9 , pp. 6335-6342
    • Gandhi, V.1    Kantarjian, H.2    Faderl, S.3    Bonate, P.4    Du, M.5    Ayres, M.6
  • 51
    • 0141482004 scopus 로고    scopus 로고
    • Phase 2 clinical and pharmacologic study of clofarabine in patients with refractory or relapsed acute leukemia
    • Kantarjian H., Gandhi V., Cortes J., Verstovsek S., Du M., Garcia-Manero G., et al. Phase 2 clinical and pharmacologic study of clofarabine in patients with refractory or relapsed acute leukemia. Blood 102 (2003) 2379-2386
    • (2003) Blood , vol.102 , pp. 2379-2386
    • Kantarjian, H.1    Gandhi, V.2    Cortes, J.3    Verstovsek, S.4    Du, M.5    Garcia-Manero, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.