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Volumn 13, Issue 12, 2007, Pages 822-832

Design, synthesis and evaluation of peptide inhibitors of Mycobacterium tuberculosis ribonucleotide reductase

Author keywords

Alanine scan; FHDoE; Mycobacterium tuberculosis; Peptide inhibitors; Ribonucleotide reductase; Statistical molecular design; Structure activity relationships

Indexed keywords

ALANINE; HEPTAPEPTIDE; PHENYLALANINE; RIBONUCLEOTIDE REDUCTASE; RIBONUCLEOTIDE REDUCTASE INHIBITOR; SYNTHETIC PEPTIDE; TRYPTOPHAN; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

EID: 37349063385     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.906     Document Type: Article
Times cited : (27)

References (32)
  • 1
    • 37349067013 scopus 로고    scopus 로고
    • World Health Organization Home, last accessed Apr 2007
    • World Health Organization Home Page. http://www.who.int [last accessed Apr 2007].
  • 2
    • 37349043529 scopus 로고    scopus 로고
    • http://www.who.int/mediacentre/ factsheets/fs104/en/print.html [last accessed Apr 2007]
    • World Health Organization Home, March
    • World Health Organization Home Page. http://www.who.int/mediacentre/ factsheets/fs104/en/print.html [last accessed Apr 2007], Fact sheet No 104, March 2007.
    • (2007) Fact sheet , Issue.104
  • 4
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • Reichard P. From RNA to DNA, why so many ribonucleotide reductases? Science 1993; 260: 1773-1777.
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 5
    • 0031571616 scopus 로고    scopus 로고
    • Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding
    • Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnström K, Sjöberg BM, Eklund H. Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure 1997; 5: 1077-1092.
    • (1997) Structure , vol.5 , pp. 1077-1092
    • Eriksson, M.1    Uhlin, U.2    Ramaswamy, S.3    Ekberg, M.4    Regnström, K.5    Sjöberg, B.M.6    Eklund, H.7
  • 6
    • 0022763898 scopus 로고
    • Identification of the stable free radical tyrosine residue in ribonucleotide reductase
    • Larsson A, Sjöberg BM. Identification of the stable free radical tyrosine residue in ribonucleotide reductase. EMBO J. 1986; 5: 2037-2040.
    • (1986) EMBO J , vol.5 , pp. 2037-2040
    • Larsson, A.1    Sjöberg, B.M.2
  • 7
    • 19044394312 scopus 로고    scopus 로고
    • Overview of ribonucleotide reductase inhibitors: An appealing target in antitumour therapy
    • Cerqueira NM, Pereira S, Fernandes PA, Ramos MJ. Overview of ribonucleotide reductase inhibitors: an appealing target in antitumour therapy. Curr. Med. Chem. 2005; 12: 1283-1294.
    • (2005) Curr. Med. Chem , vol.12 , pp. 1283-1294
    • Cerqueira, N.M.1    Pereira, S.2    Fernandes, P.A.3    Ramos, M.J.4
  • 8
    • 33747090604 scopus 로고    scopus 로고
    • Ribonucleotide reductase inhibitors as antiherpes agents
    • Wnuk SF, Robins MJ. Ribonucleotide reductase inhibitors as antiherpes agents. Antiviral Res. 2006; 71: 122-126.
    • (2006) Antiviral Res , vol.71 , pp. 122-126
    • Wnuk, S.F.1    Robins, M.J.2
  • 9
    • 0032508046 scopus 로고    scopus 로고
    • Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE III, Tekaia F, Badcock D, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krough A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998; 393: 537-544.
    • Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE III, Tekaia F, Badcock D, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krough A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998; 393: 537-544.
  • 10
    • 0242381240 scopus 로고    scopus 로고
    • Ribonucleotide reduction in Mycobacterium tuberculosis: Function and expression of genes encoding class Ib and class II ribonucleotide reductases
    • Dawes SS, Warner DF, Tsenova L, Timm J, McKinney JD, Kaplan G, Rubin H, Mizrahi V. Ribonucleotide reduction in Mycobacterium tuberculosis: function and expression of genes encoding class Ib and class II ribonucleotide reductases. Infect. Immun. 2003; 71: 6124-6131.
    • (2003) Infect. Immun , vol.71 , pp. 6124-6131
    • Dawes, S.S.1    Warner, D.F.2    Tsenova, L.3    Timm, J.4    McKinney, J.D.5    Kaplan, G.6    Rubin, H.7    Mizrahi, V.8
  • 11
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti CM, Boyd DH, Rubin EJ. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 2003; 48: 77-84.
    • (2003) Mol. Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 12
    • 0025851264 scopus 로고
    • Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction: Kinetic analysis of inhibition studies
    • Climent I, Sjöberg BM, Huang CY. Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction: kinetic analysis of inhibition studies. Biochemistry 1991; 30: 5164-5171.
    • (1991) Biochemistry , vol.30 , pp. 5164-5171
    • Climent, I.1    Sjöberg, B.M.2    Huang, C.Y.3
  • 13
    • 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
    • Yang FD, Spanevello RA, Celiker I, Hirschmann R, Rubin H, Cooperman BS. 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. 1990; 272: 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
  • 14
    • 0023656197 scopus 로고
    • Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase
    • Gaudreau P, Michaud J, Cohen EA, Langelier Y, Brazeau P. Structure-activity studies on synthetic peptides inhibiting herpes simplex virus ribonucleotide reductase. J. Biol. Chem. 1987; 282: 12413-12416.
    • (1987) J. Biol. Chem , vol.282 , pp. 12413-12416
    • Gaudreau, P.1    Michaud, J.2    Cohen, E.A.3    Langelier, Y.4    Brazeau, P.5
  • 15
    • 0035804296 scopus 로고    scopus 로고
    • Toward a rational design of peptide inhibitors of ribonucleotide reductase: Structure-function and modeling studies
    • Pender BA, Wu X, Axelsen PH, Cooperman BS. Toward a rational design of peptide inhibitors of ribonucleotide reductase: structure-function and modeling studies. J. Med. Chem. 2001; 44: 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
  • 16
    • 0026572925 scopus 로고
    • Structure-function studies of peptides inhibiting the ribonucleotide reductase activity of herpes simplex virus type I
    • Gaudreau P, Brazeau P, Richer M, Cormier J, Langlois D, Langelier Y. Structure-function studies of peptides inhibiting the ribonucleotide reductase activity of herpes simplex virus type I. J. Med. Chem. 1992; 35: 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
  • 18
    • 0030879042 scopus 로고    scopus 로고
    • Characterization of two genes encoding the Mycobacterium tuberculosis ribonucleotide reductase small subunit
    • Yang F, Curran SC, Li IS, Avarbock D, Graf JD, Chua MM, Lu G, Salem J, Rubin H. Characterization of two genes encoding the Mycobacterium tuberculosis ribonucleotide reductase small subunit. J. Bacteriol. 1997; 179: 6408-6415.
    • (1997) J. Bacteriol , vol.179 , pp. 6408-6415
    • Yang, F.1    Curran, S.C.2    Li, I.S.3    Avarbock, D.4    Graf, J.D.5    Chua, M.M.6    Lu, G.7    Salem, J.8    Rubin, H.9
  • 20
    • 85159505007 scopus 로고    scopus 로고
    • Focused hierarchical design of peptide libraries - follow the lead
    • in press, DOI: 10.1002/cem. 1069
    • Muthas D, Lek PM, Nurbo J, Karlén A, Lundstedt T. Focused hierarchical design of peptide libraries - follow the lead. J. Chemometrics (in press). DOI: 10.1002/cem. 1069.
    • J. Chemometrics
    • Muthas, D.1    Lek, P.M.2    Nurbo, J.3    Karlén, A.4    Lundstedt, T.5
  • 21
    • 85082858512 scopus 로고    scopus 로고
    • OPLS discriminant analysis: Combining the strengths of PLS-DA and SIMCA classification
    • in press, DOI: 10.1002/cem. 1006
    • Bylesjö M, Rantalainen M, Cloarec O, Nicholson JK, Holmes E, Trygg J. OPLS discriminant analysis: combining the strengths of PLS-DA and SIMCA classification, J. Chemom. in press, DOI: 10.1002/cem. 1006.
    • J. Chemom
    • Bylesjö, M.1    Rantalainen, M.2    Cloarec, O.3    Nicholson, J.K.4    Holmes, E.5    Trygg, J.6
  • 23
    • 0036083139 scopus 로고    scopus 로고
    • Orthogonal projections to latent structures (OPLS)
    • Trygg J, Wold S. Orthogonal projections to latent structures (OPLS). J. Chemom. 2002; 16: 119-128.
    • (2002) J. Chemom , vol.16 , pp. 119-128
    • Trygg, J.1    Wold, S.2
  • 24
    • 0018786967 scopus 로고
    • Ribonucleotide reductase from calf thymus. Purification and properties
    • Engström Y, Eriksson S, Thelander L, Åkerman M. Ribonucleotide reductase from calf thymus. Purification and properties. Biochemistry 1979; 18: 2941-2948.
    • (1979) Biochemistry , vol.18 , pp. 2941-2948
    • Engström, Y.1    Eriksson, S.2    Thelander, L.3    Åkerman, M.4
  • 25
    • 0022455333 scopus 로고
    • Specific inhibition of herpesvirus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit 2
    • Cohen EA, Gaudreau PPB, Langelier Y. Specific inhibition of herpesvirus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit 2. Nature 1986; 321: 441-443.
    • (1986) Nature , vol.321 , pp. 441-443
    • Cohen, E.A.1    Gaudreau, P.P.B.2    Langelier, Y.3
  • 27
    • 0023192524 scopus 로고
    • Peptide quantitative structure-activity relationships, a multivariate approach
    • Hellberg S, Sjöström M, Skagerberg B, Wold S. Peptide quantitative structure-activity relationships, a multivariate approach. J. Med. Chem. 1987; 38: 1126-1135.
    • (1987) J. Med. Chem , vol.38 , pp. 1126-1135
    • Hellberg, S.1    Sjöström, M.2    Skagerberg, B.3    Wold, S.4
  • 28
    • 0032474777 scopus 로고    scopus 로고
    • New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids
    • Sandberg M, Eriksson L, Jonsson J, Sjöström M, Wold S. New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids. J. Med. Chem. 1998; 41: 2481-2491.
    • (1998) J. Med. Chem , vol.41 , pp. 2481-2491
    • Sandberg, M.1    Eriksson, L.2    Jonsson, J.3    Sjöström, M.4    Wold, S.5
  • 29
    • 0032248238 scopus 로고    scopus 로고
    • Statistical molecular design of peptoid libraries
    • Linusson A, Wold S, Norden B. Statistical molecular design of peptoid libraries. Mol. Divers. 1998; 4:103-114.
    • (1998) Mol. Divers , vol.4 , pp. 103-114
    • Linusson, A.1    Wold, S.2    Norden, B.3
  • 30
    • 0036685711 scopus 로고    scopus 로고
    • Hierarchical experimental design exemplified by QSAR evaluation of a chemical library directed towards the melanocortin 4 receptor
    • Andersson PM, Lundstedt T. Hierarchical experimental design exemplified by QSAR evaluation of a chemical library directed towards the melanocortin 4 receptor, J. Chemom. 2002; 16: 490-496.
    • (2002) J. Chemom , vol.16 , pp. 490-496
    • Andersson, P.M.1    Lundstedt, T.2
  • 31
    • 0000706576 scopus 로고
    • Mechanism of the racemization of amino acids. Kinetics of racemization of arylglycines
    • Smith GG, Sivakua T. Mechanism of the racemization of amino acids. Kinetics of racemization of arylglycines. J. Org. Chem. 1983; 48: 627-634.
    • (1983) J. Org. Chem , vol.48 , pp. 627-634
    • Smith, G.G.1    Sivakua, T.2
  • 32
    • 33646176383 scopus 로고    scopus 로고
    • The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action
    • Uppsten M, Färnegårdh M, Domkin V, Uhlin U. The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action. J. Mol. Biol. 2006; 359: 365-377.
    • (2006) J. Mol. Biol , vol.359 , pp. 365-377
    • Uppsten, M.1    Färnegårdh, M.2    Domkin, V.3    Uhlin, U.4


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