메뉴 건너뛰기




Volumn 45, Issue 1, 2005, Pages 112-125

Peptide inhibitors of mammalian ribonucleotide reductase

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA; RHODOCOCCUS RHODOCHROUS;

EID: 28444453986     PISSN: 00652571     EISSN: None     Source Type: Book Series    
DOI: 10.1016/j.advenzreg.2005.02.012     Document Type: Article
Times cited : (12)

References (47)
  • 1
    • 0027474781 scopus 로고
    • "ensemble" iterative relaxation matrix approach: A new NMR refinement protocol applied to the solution structure of crambin
    • A.M. Bonvin, J.A. Rullmann, R.M. Lamerichs, R. Boelens, and R. Kaptein "Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin Proteins: Struct Funct Genet 15 1993 385 400
    • (1993) Proteins: Struct Funct Genet , vol.15 , pp. 385-400
    • Bonvin, A.M.1    Rullmann, J.A.2    Lamerichs, R.M.3    Boelens, R.4    Kaptein, R.5
  • 2
    • 0029927025 scopus 로고    scopus 로고
    • Evaluation of a peptidomimetic ribonucleotide reductase inhibitor with a murine model of herpes simplex virus type 1 ocular disease
    • C.R. Brandt, B. Spencer, P. Imesch, M. Garneau, and R. Deziel Evaluation of a peptidomimetic ribonucleotide reductase inhibitor with a murine model of herpes simplex virus type 1 ocular disease Antimicrob Agents Chemother 40 1996 1078 1084
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1078-1084
    • Brandt, C.R.1    Spencer, B.2    Imesch, P.3    Garneau, M.4    Deziel, R.5
  • 3
    • 0037051690 scopus 로고    scopus 로고
    • Expression and mutation analyses of P53R2, a newly identified p53 target for DNA repair in human gastric carcinoma
    • D.S. Byun, K.S. Chae, B.K. Ryu, M.G. Lee, and S.G. Chi Expression and mutation analyses of P53R2, a newly identified p53 target for DNA repair in human gastric carcinoma Int J Cancer 98 2002 718 723
    • (2002) Int J Cancer , vol.98 , pp. 718-723
    • Byun, D.S.1    Chae, K.S.2    Ryu, B.K.3    Lee, M.G.4    Chi, S.G.5
  • 4
    • 0034625375 scopus 로고    scopus 로고
    • Controlled protein degradation regulates ribonucleotide reductase activity in proliferating mammalian cells during the normal cell cycle and in response to DNA damage and replication blocks
    • A. Chabes, and L. Thelander Controlled protein degradation regulates ribonucleotide reductase activity in proliferating mammalian cells during the normal cell cycle and in response to DNA damage and replication blocks J Biol Chem 275 2000 17747 17753
    • (2000) J Biol Chem , vol.275 , pp. 17747-17753
    • Chabes, A.1    Thelander, L.2
  • 6
    • 0022455333 scopus 로고
    • Specific inhibition of herpes virus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit 2
    • E.A. Cohen, P. Gaudreau, P. Brazeau, and Y. Langelier Specific inhibition of herpes virus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit 2 Nature 321 1986 441 443
    • (1986) Nature , vol.321 , pp. 441-443
    • Cohen, E.A.1    Gaudreau, P.2    Brazeau, P.3    Langelier, Y.4
  • 7
    • 0024236511 scopus 로고
    • Ribonucleotide reductase as a chemotherapeutic target
    • J.G. Cory Ribonucleotide reductase as a chemotherapeutic target Adv Enzyme Regul 27 1988 437
    • (1988) Adv Enzyme Regul , vol.27 , pp. 437
    • Cory, J.G.1
  • 9
  • 11
    • 0022443708 scopus 로고
    • Specific inhibition of herpesvirus ribonucleotide reductase by synthetic peptides
    • B.M. Dutia, M.C. Frame, J.H. Subak-Sharpe, W.N. Clark, and H.S. Marsden Specific inhibition of herpesvirus ribonucleotide reductase by synthetic peptides Nature 321 1986 439 441
    • (1986) Nature , vol.321 , pp. 439-441
    • Dutia, B.M.1    Frame, M.C.2    Subak-Sharpe, J.H.3    Clark, W.N.4    Marsden, H.S.5
  • 13
    • 0031571616 scopus 로고    scopus 로고
    • Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding
    • M. Eriksson, U. Uhlin, S. Ramaswamy, M. Ekberg, K. Regnstrom, B.M. Sjoberg, and H. Eklund Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding Structure 5 1997 1077 1092
    • (1997) Structure , vol.5 , pp. 1077-1092
    • Eriksson, M.1    Uhlin, U.2    Ramaswamy, S.3    Ekberg, M.4    Regnstrom, K.5    Sjoberg, B.M.6    Eklund, H.7
  • 14
    • 0027131858 scopus 로고
    • R2 C-terminal peptide inhibition of mammalian and yeast ribonucleotide reductase
    • A. Fisher, F.D. Yang, H. Rubin, and B.S. Cooperman R2 C-terminal peptide inhibition of mammalian and yeast ribonucleotide reductase J Med Chem 36 1993 3859 3862
    • (1993) J Med Chem , vol.36 , pp. 3859-3862
    • Fisher, A.1    Yang, F.D.2    Rubin, H.3    Cooperman, B.S.4
  • 15
    • 0028853596 scopus 로고
    • NMR structure of an inhibitory R2 C-terminal peptide bound to mouse ribonucleotide reductase R1 subunit
    • A. Fisher, P.B. Laub, and B.S. Cooperman NMR structure of an inhibitory R2 C-terminal peptide bound to mouse ribonucleotide reductase R1 subunit Nat Struct Biol 2 1995 951 955
    • (1995) Nat Struct Biol , vol.2 , pp. 951-955
    • Fisher, A.1    Laub, P.B.2    Cooperman, B.S.3
  • 16
    • 0037169982 scopus 로고    scopus 로고
    • Affinity-driven selection of tripeptide inhibitors of ribonucleotide reductase
    • Y. Gao, S. Liehr, and B.S. Cooperman Affinity-driven selection of tripeptide inhibitors of ribonucleotide reductase Bioorg Med Chem Lett 12 2002 513 515
    • (2002) Bioorg Med Chem Lett , vol.12 , pp. 513-515
    • Gao, Y.1    Liehr, S.2    Cooperman, B.S.3
  • 17
    • 14944350032 scopus 로고    scopus 로고
    • Mechanisms of action of peptide inhibitors of mammalian ribonucleotide reductase targeting quaternary structure
    • Y. Gao, O.B. Kashlan, J. Kaur, C. Tan, and B.S. Cooperman Mechanisms of action of peptide inhibitors of mammalian ribonucleotide reductase targeting quaternary structure Biopolymers (Peptide Science) 80 2005 9 17
    • (2005) Biopolymers (Peptide Science) , vol.80 , pp. 9-17
    • Gao, Y.1    Kashlan, O.B.2    Kaur, J.3    Tan, C.4    Cooperman, B.S.5
  • 18
    • 0023656197 scopus 로고
    • Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase
    • P. Gaudreau, J. Michaud, E.A. Cohen, Y. Langelier, and P. Brazeau Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase J Biol Chem 262 1987 12413 12416
    • (1987) J Biol Chem , vol.262 , pp. 12413-12416
    • Gaudreau, P.1    Michaud, J.2    Cohen, E.A.3    Langelier, Y.4    Brazeau, P.5
  • 19
    • 0025056612 scopus 로고
    • Synthesis and inhibitory potency of peptides corresponding to the subunit 2 C-terminal region of herpes virus ribonucleotide reductases
    • P. Gaudreau, H. Paradis, Y. Langelier, and P. Brazeau Synthesis and inhibitory potency of peptides corresponding to the subunit 2 C-terminal region of herpes virus ribonucleotide reductases J Med Chem 33 1990 723 730
    • (1990) J Med Chem , vol.33 , pp. 723-730
    • Gaudreau, P.1    Paradis, H.2    Langelier, Y.3    Brazeau, P.4
  • 20
    • 0026572925 scopus 로고
    • Structure-function studies of peptides inhibiting the ribonucleotide reductase activity of herpes simplex virus type I
    • P. Gaudreau, P. Brazeau, M. Richer, J. Cormier, D. Langlois, and Y. Langelier Structure-function studies of peptides inhibiting the ribonucleotide reductase activity of herpes simplex virus type I J Med Chem 35 1992 346 350
    • (1992) J Med Chem , vol.35 , pp. 346-350
    • Gaudreau, P.1    Brazeau, P.2    Richer, M.3    Cormier, J.4    Langlois, D.5    Langelier, Y.6
  • 21
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • T.F. Havel An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance Prog Biophys Mol Biol 56 1991 43 78
    • (1991) Prog Biophys Mol Biol , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 22
    • 0037452529 scopus 로고    scopus 로고
    • A comprehensive model for the allosteric regulation of class Ia ribonucleotide reductases
    • O.B. Kashlan, and B.S. Cooperman A comprehensive model for the allosteric regulation of class Ia ribonucleotide reductases Biochemistry 42 2003 1696 1706
    • (2003) Biochemistry , vol.42 , pp. 1696-1706
    • Kashlan, O.B.1    Cooperman, B.S.2
  • 23
    • 0037080335 scopus 로고    scopus 로고
    • A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP- and dATP-induced oligomerization of the large subunit
    • O.B. Kashlan, C.P. Scott, J.D. Lear, and B.S. Cooperman A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP- and dATP-induced oligomerization of the large subunit Biochemistry 41 2002 462 474
    • (2002) Biochemistry , vol.41 , pp. 462-474
    • Kashlan, O.B.1    Scott, C.P.2    Lear, J.D.3    Cooperman, B.S.4
  • 24
    • 0033592479 scopus 로고    scopus 로고
    • Synthesis and biological activity of cyclic peptide inhibitors of ribonucleotide reductase
    • S. Liehr, J. Barbosa, A.B. Smith 3rd, and B.S. Cooperman Synthesis and biological activity of cyclic peptide inhibitors of ribonucleotide reductase Org Lett 1 1999 1201 1204
    • (1999) Org Lett , vol.1 , pp. 1201-1204
    • Liehr, S.1    Barbosa, J.2    Smith III, A.B.3    Cooperman, B.S.4
  • 26
    • 0030568122 scopus 로고    scopus 로고
    • Peptidomimetic inhibitors of Herpes virus ribonucleotide reductase. Correlation between Herpes simplex and Varicella zoster virus
    • M. Llinas-Brunet, N. Moss, E. Scouten, M. Liuzzi, and R. Deziel Peptidomimetic inhibitors of Herpes virus ribonucleotide reductase. Correlation between Herpes simplex and Varicella zoster virus Bioorg Med Chem Lett 6 1996 2881 2886
    • (1996) Bioorg Med Chem Lett , vol.6 , pp. 2881-2886
    • Llinas-Brunet, M.1    Moss, N.2    Scouten, E.3    Liuzzi, M.4    Deziel, R.5
  • 27
    • 0034671521 scopus 로고    scopus 로고
    • ATP depletion+pyrimidine depletion can markedly enhance cancer therapy: Fresh insight for a new approach
    • D.S. Martin, J.R. Bertino, and J.A. Koutcher ATP depletion+pyrimidine depletion can markedly enhance cancer therapy: fresh insight for a new approach Cancer Res 60 2000 6776 6783
    • (2000) Cancer Res , vol.60 , pp. 6776-6783
    • Martin, D.S.1    Bertino, J.R.2    Koutcher, J.A.3
  • 28
    • 0035078661 scopus 로고    scopus 로고
    • A concomitant ATP-depleting strategy markedly enhances anticancer agent activity
    • D.S. Martin, D. Spriggs, and J.A. Koutcher A concomitant ATP-depleting strategy markedly enhances anticancer agent activity Apoptosis 6 2001 125 131
    • (2001) Apoptosis , vol.6 , pp. 125-131
    • Martin, D.S.1    Spriggs, D.2    Koutcher, J.A.3
  • 30
    • 0028512334 scopus 로고
    • Herpes simplex virus ribonucleotide reductase subunit association inhibitors: The effect and conformation of beta-alkylated aspartic acid derivatives
    • N. Moss, R. Deziel, J.M. Ferland, S. Goulet, P.J. Jones, S.F. Leonard, T.P. Pitner, and R. Plante Herpes simplex virus ribonucleotide reductase subunit association inhibitors: the effect and conformation of beta-alkylated aspartic acid derivatives Bioorg Med Chem 2 1994 959 970
    • (1994) Bioorg Med Chem , vol.2 , pp. 959-970
    • Moss, N.1    Deziel, R.2    Ferland, J.M.3    Goulet, S.4    Jones, P.J.5    Leonard, S.F.6    Pitner, T.P.7    Plante, R.8
  • 33
    • 0029946035 scopus 로고    scopus 로고
    • Ribonucleotide reductase inhibitors: New strategies for cancer chemotherapy
    • G. Nocentini Ribonucleotide reductase inhibitors: new strategies for cancer chemotherapy Crit Rev Oncol Hematol 22 1996 89 126
    • (1996) Crit Rev Oncol Hematol , vol.22 , pp. 89-126
    • Nocentini, G.1
  • 34
    • 0034633877 scopus 로고    scopus 로고
    • Structure-based optimization of peptide inhibitors of mammalian ribonucleotide reductase
    • M. Pellegrini, S. Liehr, A.L. Fisher, P.B. Laub, B.S. Cooperman, and D.F. Mierke Structure-based optimization of peptide inhibitors of mammalian ribonucleotide reductase Biochemistry 39 2000 12210 12215
    • (2000) Biochemistry , vol.39 , pp. 12210-12215
    • Pellegrini, M.1    Liehr, S.2    Fisher, A.L.3    Laub, P.B.4    Cooperman, B.S.5    Mierke, D.F.6
  • 35
    • 0035804296 scopus 로고    scopus 로고
    • Toward a rational design of peptide inhibitors of ribonucleotide reductase: Structure-function and modeling studies
    • B.A. Pender, X. Wu, P.H. Axelsen, and B.S. Cooperman Toward a rational design of peptide inhibitors of ribonucleotide reductase: structure-function and modeling studies J Med Chem 44 2001 36 46
    • (2001) J Med Chem , vol.44 , pp. 36-46
    • Pender, B.A.1    Wu, X.2    Axelsen, P.H.3    Cooperman, B.S.4
  • 36
    • 0032989079 scopus 로고    scopus 로고
    • Mechanism-based inhibition of ribonucleotide reductases: New mechanistic considerations and promising biological applications
    • M.J. Robins Mechanism-based inhibition of ribonucleotide reductases: new mechanistic considerations and promising biological applications Nucleosides Nucleotides 18 1999 779
    • (1999) Nucleosides Nucleotides , vol.18 , pp. 779
    • Robins, M.J.1
  • 38
    • 0035852795 scopus 로고    scopus 로고
    • A quantitative model for allosteric control of purine reduction by murine ribonucleotide reductase
    • C.P. Scott, O.B. Kashlan, J.D. Lear, and B.S. Cooperman A quantitative model for allosteric control of purine reduction by murine ribonucleotide reductase Biochemistry 40 2001 1651 1661
    • (2001) Biochemistry , vol.40 , pp. 1651-1661
    • Scott, C.P.1    Kashlan, O.B.2    Lear, J.D.3    Cooperman, B.S.4
  • 39
    • 0029612179 scopus 로고
    • Ribonucleotide reductases: Radical enzymes with suicidal tendencies
    • J. Stubbe, and W.A. van der Donk Ribonucleotide reductases: radical enzymes with suicidal tendencies Chem Biol 2 1995 793 801
    • (1995) Chem Biol , vol.2 , pp. 793-801
    • Stubbe, J.1    Van Der Donk, W.A.2
  • 40
    • 0031464519 scopus 로고    scopus 로고
    • The enzyme ribonucleotide reductase: Target for antitumor and anti-HIV therapy
    • T. Szekeres, M. Fritzer-Szekeres, and H.L. Elford The enzyme ribonucleotide reductase: target for antitumor and anti-HIV therapy Crit Rev Clin Lab Sci 34 1997 503 528
    • (1997) Crit Rev Clin Lab Sci , vol.34 , pp. 503-528
    • Szekeres, T.1    Fritzer-Szekeres, M.2    Elford, H.L.3
  • 41
    • 5344281162 scopus 로고    scopus 로고
    • More potent linear peptide inhibitors of mammalian ribonucleotide reductase
    • C. Tan, Y. Gao, J. Kaur, and B.S. Cooperman More potent linear peptide inhibitors of mammalian ribonucleotide reductase Bioorg Med Chem Lett 14 2004 5301 5304
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 5301-5304
    • Tan, C.1    Gao, Y.2    Kaur, J.3    Cooperman, B.S.4
  • 42
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • U. Uhlin, and H. Eklund Structure of ribonucleotide reductase protein R1 Nature 370 1994 533 539
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 44
    • 0020955571 scopus 로고
    • Biochemical strategy of cancer cells and the design of chemotherapy: G.H.A. Clowes Memorial Lecture
    • G. Weber Biochemical strategy of cancer cells and the design of chemotherapy: G.H.A. Clowes Memorial Lecture Cancer Res 43 1983 3466
    • (1983) Cancer Res , vol.43 , pp. 3466
    • Weber, G.1
  • 45
    • 0037374051 scopus 로고    scopus 로고
    • Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits
    • L. Xue, B. Zhou, X. Liu, W. Qiu, Z. Jin, and Y. Yen Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits Cancer Res 63 2003 980 986
    • (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
  • 46
    • 0025107020 scopus 로고
    • The carboxyl terminus heptapeptide of the R2 subunit of mammalian ribonucleotide reductase inhibits enzyme activity and can be used to purify the R1 subunit
    • F.D. Yang, R.A. Spanevello, I. Celiker, R. Hirschmann, H. Rubin, and B.S. Cooperman The carboxyl terminus heptapeptide of the R2 subunit of mammalian ribonucleotide reductase inhibits enzyme activity and can be used to purify the R1 subunit FEBS Lett 272 1990 61 64
    • (1990) FEBS Lett , vol.272 , pp. 61-64
    • Yang, F.D.1    Spanevello, R.A.2    Celiker, I.3    Hirschmann, R.4    Rubin, H.5    Cooperman, B.S.6
  • 47
    • 0030879042 scopus 로고    scopus 로고
    • Characterization of two genes encoding the Mycobacterium tuberculosis ribonucleotide reductase small subunit
    • F. Yang, S.C. Curran, L.S. Li, D. Avarbock, J.D. Graf, M.M. Chua, G. Lu, J. Salem, and H. Rubin Characterization of two genes encoding the Mycobacterium tuberculosis ribonucleotide reductase small subunit J Bacteriol 179 1997 6408 6415
    • (1997) J Bacteriol , vol.179 , pp. 6408-6415
    • Yang, F.1    Curran, S.C.2    Li, L.S.3    Avarbock, D.4    Graf, J.D.5    Chua, M.M.6    Lu, G.7    Salem, J.8    Rubin, H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.