메뉴 건너뛰기




Volumn 64, Issue 1, 2004, Pages 1-6

In Vitro Characterization of Enzymatic Properties and Inhibition of the p53R2 Subunit of Human Ribonucleotide Reductase

Author keywords

[No Author keywords available]

Indexed keywords

3 AMINOPICOLINALDEHYDE THIOSEMICARBAZONE; CYTIDINE DIPHOSPHATE; DEFEROXAMINE MESYLATE; HEPTAPEPTIDE; HYDROXYUREA; IRON; IRON CHELATING AGENT; OXIDOREDUCTASE INHIBITOR; PEPTIDE; PROTEIN HRRM1; PROTEIN HRRM2; PROTEIN P53; PROTEIN P53R2; RADICAL; RIBONUCLEOTIDE REDUCTASE; SCAVENGER; TYROSINE; UNCLASSIFIED DRUG;

EID: 1642453838     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-03-3048     Document Type: Article
Times cited : (82)

References (26)
  • 2
    • 0030580112 scopus 로고    scopus 로고
    • The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2
    • Kauppi, B., Nielsen, B. B., Ramaswamy, S., Larsen, I. K., Thelander, M., Thelander, L., and Eklund, H. The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. J. Mol. Biol., 262: 706-720, 1996.
    • (1996) J. Mol. Biol. , vol.262 , pp. 706-720
    • Kauppi, B.1    Nielsen, B.B.2    Ramaswamy, S.3    Larsen, I.K.4    Thelander, M.5    Thelander, L.6    Eklund, H.7
  • 4
    • 0034738967 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene is a transcriptional target of p53 and p73
    • Nakano, K., Balint, E., Ashcroft, M., and Vousden, K. H. A ribonucleotide reductase gene is a transcriptional target of p53 and p73. Oncogene, 19: 4283-4289, 2000.
    • (2000) Oncogene , vol.19 , pp. 4283-4289
    • Nakano, K.1    Balint, E.2    Ashcroft, M.3    Vousden, K.H.4
  • 5
    • 0033588374 scopus 로고    scopus 로고
    • 370 of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway
    • 370 of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway. J. Biol. Chem., 274: 23746-23751, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23746-23751
    • Rova, U.1    Adrait, A.2    Potsch, S.3    Graslund, A.4    Thelander, L.5
  • 6
    • 0037150125 scopus 로고    scopus 로고
    • EPR studies on a stable sulfinyl radical observed in the iron-oxygen-reconstituted Y177F/1263C protein R2 double mutant of ribonucleotide reductase from mouse
    • Adrait, A., Ohrstrom, M., Barra, A. L., Thelander, L., and Graslund, A. EPR studies on a stable sulfinyl radical observed in the iron-oxygen-reconstituted Y177F/1263C protein R2 double mutant of ribonucleotide reductase from mouse. Biochemistry, 41: 6510-6516, 2002.
    • (2002) Biochemistry , vol.41 , pp. 6510-6516
    • Adrait, A.1    Ohrstrom, M.2    Barra, A.L.3    Thelander, L.4    Graslund, A.5
  • 8
    • 0242317756 scopus 로고    scopus 로고
    • Mouse ribonucleotide reductase R2 protein: A new target for anaphase-promoting complex-Cdh1-mediated proteolysis
    • Chabes, A., Pfleger, C. M., Kirschner, M. W., and Thelander, L. Mouse ribonucleotide reductase R2 protein: a new target for anaphase-promoting complex-Cdh1-mediated proteolysis. Proc. Natl. Acad. Sci. USA, 100: 3925-3929, 2003.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3925-3929
    • Chabes, A.1    Pfleger, C.M.2    Kirschner, M.W.3    Thelander, L.4
  • 9
    • 0035798630 scopus 로고    scopus 로고
    • Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells
    • Guittet, O., Hakansson, P., Voevodskaya, N., Fridd, S., Graslund, A., Arakawa, H., Nakamura, Y., and Thelander, L. Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells. J. Biol. Chem., 276: 40647-40651, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40647-40651
    • Guittet, O.1    Hakansson, P.2    Voevodskaya, N.3    Fridd, S.4    Graslund, A.5    Arakawa, H.6    Nakamura, Y.7    Thelander, L.8
  • 11
    • 0034594895 scopus 로고    scopus 로고
    • p53 sends nucleotides to repair DNA
    • Lozano, G., and Elledge, S. J. p53 sends nucleotides to repair DNA. Nature (Lond.), 404: 24-25, 2000.
    • (2000) Nature (Lond.) , vol.404 , pp. 24-25
    • Lozano, G.1    Elledge, S.J.2
  • 12
    • 0142250911 scopus 로고    scopus 로고
    • The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53
    • Zhou, B., Liu, X., Mo. X., Xue. L., Darwish, D., Qiu, W., Shih, J., Hwu, E. B., Luh, F., and Yen, Y. The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53. Cancer Res., 63: 6583-6594, 2003.
    • (2003) Cancer Res. , vol.63 , pp. 6583-6594
    • Zhou, B.1    Liu, X.2    Mo, X.3    Xue, L.4    Darwish, D.5    Qiu, W.6    Shih, J.7    Hwu, E.B.8    Luh, F.9    Yen, Y.10
  • 13
    • 0037374051 scopus 로고    scopus 로고
    • Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits
    • Xue, L., Zhou, B., Liu, X., Qiu, W., Jin, Z., and Yen, Y. Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res., 63: 980-986, 2003.
    • (2003) Cancer Res. , vol.63 , pp. 980-986
    • Xue, L.1    Zhou, B.2    Liu, X.3    Qiu, W.4    Jin, Z.5    Yen, Y.6
  • 14
    • 0032522647 scopus 로고    scopus 로고
    • The mammalian ribonucleotide reductase R2 component cooperates with a variety of oncogenes in mechanisms of cellular transformation
    • Fan, H., Villegas, C., Huang, A., and Wright, J. A. The mammalian ribonucleotide reductase R2 component cooperates with a variety of oncogenes in mechanisms of cellular transformation. Cancer Res., 58: 1650-1653, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 1650-1653
    • Fan, H.1    Villegas, C.2    Huang, A.3    Wright, J.A.4
  • 15
    • 0031938457 scopus 로고    scopus 로고
    • Overexpression of transfected human ribonucleotide reductase M2 subunit in human cancer cells enhances their invasive potential
    • Zhou, B. S., Tsai, P., Ker, R., Tsai, J., Ho, R., Yu, J., Shih, J., and Yen, Y. Overexpression of transfected human ribonucleotide reductase M2 subunit in human cancer cells enhances their invasive potential. Clin. Exp. Metastasis, 16: 43-49, 1998.
    • (1998) Clin. Exp. Metastasis , vol.16 , pp. 43-49
    • Zhou, B.S.1    Tsai, P.2    Ker, R.3    Tsai, J.4    Ho, R.5    Yu, J.6    Shih, J.7    Yen, Y.8
  • 16
    • 0042166135 scopus 로고    scopus 로고
    • Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools
    • Kimura, T., Takeda, S., Sagiya, Y., Gotoh, M., Nakamura, Y., and Arakawa, H. Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools. Nat. Genet., 34: 440-4445, 2003.
    • (2003) Nat. Genet. , vol.34 , pp. 440-4445
    • Kimura, T.1    Takeda, S.2    Sagiya, Y.3    Gotoh, M.4    Nakamura, Y.5    Arakawa, H.6
  • 17
    • 0028107848 scopus 로고
    • Characterization of a hydroxyurea-resistant human KB cell line with supersensitivity to 6-thioguanine
    • Yen, Y., Grill, S. P., Dutschman, G. E., Chang, C. N., Zhou, B. S., and Cheng, Y. C. Characterization of a hydroxyurea-resistant human KB cell line with supersensitivity to 6-thioguanine. Cancer Res., 54: 3686-3691, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 3686-3691
    • Yen, Y.1    Grill, S.P.2    Dutschman, G.E.3    Chang, C.N.4    Zhou, B.S.5    Cheng, Y.C.6
  • 18
    • 0036269005 scopus 로고    scopus 로고
    • Iron chelators as therapeutic agents for the treatment of cancer
    • Richardson, D. R. Iron chelators as therapeutic agents for the treatment of cancer. Crit. Rev. Oncol. Hematol., 42: 267-281, 2002.
    • (2002) Crit. Rev. Oncol. Hematol. , vol.42 , pp. 267-281
    • Richardson, D.R.1
  • 19
    • 0033198464 scopus 로고    scopus 로고
    • Overexpression of ribonucleotide reductase as a mechanism of resistance to 2,2-difluorodeoxycytidine in the human KB cancer cell line
    • Goan, Y. G., Zhou, B., Hu, E., Mi, S., and Yen, Y. Overexpression of ribonucleotide reductase as a mechanism of resistance to 2,2-difluorodeoxycytidine in the human KB cancer cell line. Cancer Res., 59: 4204-4207, 1999.
    • (1999) Cancer Res. , vol.59 , pp. 4204-4207
    • Goan, Y.G.1    Zhou, B.2    Hu, E.3    Mi, S.4    Yen, Y.5
  • 20
    • 0038796547 scopus 로고    scopus 로고
    • Oligopeptide inhibition of class I ribonucleotide reductases
    • Cooperman, B. S. Oligopeptide inhibition of class I ribonucleotide reductases. Biopolymers, 71: 117-131, 2003.
    • (2003) Biopolymers , vol.71 , pp. 117-131
    • Cooperman, B.S.1
  • 21
    • 0025829053 scopus 로고
    • Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunit
    • Mann, G. J., Graslund, A., Ochiai, E., Ingemarson, R., and Thelander, L. Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunit. Biochemistry, 30: 1939-1947, 1991.
    • (1991) Biochemistry , vol.30 , pp. 1939-1947
    • Mann, G.J.1    Graslund, A.2    Ochiai, E.3    Ingemarson, R.4    Thelander, L.5
  • 22
    • 0027521831 scopus 로고
    • Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators
    • Nyholm, S., Mann, G. J., Johansson, A. G., Bergeron, R. J., Graslund, A., and Thelander, L. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J. Biol. Chem., 268: 26200-26205, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26200-26205
    • Nyholm, S.1    Mann, G.J.2    Johansson, A.G.3    Bergeron, R.J.4    Graslund, A.5    Thelander, L.6
  • 23
    • 0028928261 scopus 로고
    • Overexpression of ribonucleotide reductase in transfected human KB cells increases their resistance to hydroxyurea: M2 but not M1 is sufficient to increase resistance to hydroxyurea in transfected cells
    • Zhou, B. S., Hsu, N. Y., Pan, B. C., Doroshow, J. H., and Yen, Y. Overexpression of ribonucleotide reductase in transfected human KB cells increases their resistance to hydroxyurea: M2 but not M1 is sufficient to increase resistance to hydroxyurea in transfected cells. Cancer Res., 55: 1328-1333, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 1328-1333
    • Zhou, B.S.1    Hsu, N.Y.2    Pan, B.C.3    Doroshow, J.H.4    Yen, Y.5
  • 24
    • 0032832996 scopus 로고    scopus 로고
    • Triapine (3-aminopyridine-2-carboxaldehyde thiosemicarbazone; 3-AP): An inhibitor of ribonucleotide reductase with antineoplastic activity
    • Finch, R. A., Liu, M. C., Cory, A. H., Cory, J. G., and Sartorelli, A. C. Triapine (3-aminopyridine-2-carboxaldehyde thiosemicarbazone; 3-AP): an inhibitor of ribonucleotide reductase with antineoplastic activity. Adv. Enzyme Regul., 39: 3-12, 1999.
    • (1999) Adv. Enzyme Regul. , vol.39 , pp. 3-12
    • Finch, R.A.1    Liu, M.C.2    Cory, A.H.3    Cory, J.G.4    Sartorelli, A.C.5
  • 25
    • 0037237032 scopus 로고    scopus 로고
    • Examination of the antiproliferative activity of iron chelators: Multiple cellular targets and the different mechanism of action of triapine compared with desferrioxamine and the potent pyridoxal isonicotinoyl hydrazone analogue 311
    • Chaston, T. B., Lovejoy, D. B., Watts, R. N., and Richardson, D. R. Examination of the antiproliferative activity of iron chelators: multiple cellular targets and the different mechanism of action of triapine compared with desferrioxamine and the potent pyridoxal isonicotinoyl hydrazone analogue 311. Clin. Cancer Res., 9: 402-414, 2003.
    • (2003) Clin Cancer Res. , vol.9 , pp. 402-414
    • Chaston, T.B.1    Lovejoy, D.B.2    Watts, R.N.3    Richardson, D.R.4
  • 26
    • 0037122708 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and quantitative structure-activity relationship analysis of new Schiff bases of hydroxysemicarbazide as potential antitumor agents
    • Ren, S., Wang, R., Komatsu, K., Bonaz-Krause, P., Zyrianov, Y., McKenna. C. E., Csipke, C., Tokes, Z. A., and Lien, E. J. Synthesis, biological evaluation, and quantitative structure-activity relationship analysis of new Schiff bases of hydroxysemicarbazide as potential antitumor agents. J. Med. Chem., 45: 410-419, 2002.
    • (2002) J. Med. Chem. , vol.45 , pp. 410-419
    • Ren, S.1    Wang, R.2    Komatsu, K.3    Bonaz-Krause, P.4    Zyrianov, Y.5    McKenna, C.E.6    Csipke, C.7    Tokes, Z.A.8    Lien, E.J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.