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Volumn 79, Issue 4, 2000, Pages 2155-2161

Radiation inactivation of ribonucleotide reductase, an enzyme with a stable free radical

Author keywords

[No Author keywords available]

Indexed keywords

FREE RADICAL; HOLOENZYME; RECOMBINANT ENZYME; RIBONUCLEOTIDE REDUCTASE;

EID: 0033803487     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76463-0     Document Type: Article
Times cited : (4)

References (10)
  • 1
    • 0026347398 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase
    • Bollinger, Jr., J. M., D. E. Edmondson, B. H. Huynh, J. Filley, J. R. Norton, and J. Stubbe. 1991. Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science. 253:292-298.
    • (1991) Science , vol.253 , pp. 292-298
    • Bollinger Jr., J.M.1    Edmondson, D.E.2    Huynh, B.H.3    Filley, J.4    Norton, J.R.5    Stubbe, J.6
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0021979324 scopus 로고
    • Herpes simplex virus ribonucleotide reductase induced in infected BHK-21/C13 cells: Biochemical evidence for the existence of two non-identical subunits, H1 and H2
    • Cohen, E. A., J. Charron, J. Perret, and Y. Langelier. 1985. Herpes simplex virus ribonucleotide reductase induced in infected BHK-21/C13 cells: biochemical evidence for the existence of two non-identical subunits, H1 and H2. J. Gen. Virol 66:733-745.
    • (1985) J. Gen. Virol , vol.66 , pp. 733-745
    • Cohen, E.A.1    Charron, J.2    Perret, J.3    Langelier, Y.4
  • 4
    • 0027714774 scopus 로고
    • Herpes simplex virus type 1 ribonucleotide reductase large subunit: Regions of the protein essential for subunit interaction and dimerization
    • Conner, J., J. Furlong, J. Murray, M. Meighan, A. Cross, H. Marsden, and J. B. Clements. 1993. Herpes simplex virus type 1 ribonucleotide reductase large subunit: regions of the protein essential for subunit interaction and dimerization. Biochemistry. 32:13673-13680.
    • (1993) Biochemistry , vol.32 , pp. 13673-13680
    • Conner, J.1    Furlong, J.2    Murray, J.3    Meighan, M.4    Cross, A.5    Marsden, H.6    Clements, J.B.7
  • 5
    • 0030057695 scopus 로고    scopus 로고
    • Structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis
    • Davis, M. D., M. A. Parniak, S. Kaufman, and E. Kempner. 1996. Structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis. Arch. Biochem. Biophys. 325:235-241.
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 235-241
    • Davis, M.D.1    Parniak, M.A.2    Kaufman, S.3    Kempner, E.4
  • 6
    • 0031037146 scopus 로고    scopus 로고
    • The role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis
    • Davis, M. D., M. A. Parniak, S. Kaufman, and E. Kempner. 1997. The role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis. Proc. Natl. Acad. Sci. USA. 94:491-495.
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 491-495
    • Davis, M.D.1    Parniak, M.A.2    Kaufman, S.3    Kempner, E.4
  • 7
    • 0029865405 scopus 로고    scopus 로고
    • Effect of the tyrosyl radical on the reduction and structure of the Escherichia coli ribonucleotide reductase protein R2 diferric site as probed by EPR on the mixed-valent state
    • Davydov, R., M. Sahlin, S. Kuprin, A. Graslund, and A. Ehrenberg. 1996. Effect of the tyrosyl radical on the reduction and structure of the Escherichia coli ribonucleotide reductase protein R2 diferric site as probed by EPR on the mixed-valent state. Biochemistry. 35:5571-5576.
    • (1996) Biochemistry , vol.35 , pp. 5571-5576
    • Davydov, R.1    Sahlin, M.2    Kuprin, S.3    Graslund, A.4    Ehrenberg, A.5
  • 8
    • 0002144264 scopus 로고
    • Ribonucleotide reductase
    • G. Herve, editor. CRC Press, Boca Raton, FL
    • Erikson, S., and B.-M. Sjoberg. 1989. Ribonucleotide reductase. In Allosteric Enzymes. G. Herve, editor. CRC Press, Boca Raton, FL. 189-215.
    • (1989) Allosteric Enzymes , pp. 189-215
    • Erikson, S.1    Sjoberg, B.-M.2
  • 9
    • 0026704225 scopus 로고
    • The role of herpes simplex virus ribonucleotide reductase small subunit carboxyl terminus in subunit interaction and formation of iron-tyrosyl center structure
    • Filatov, D., R. Ingemarson, A. Graslund, and L. Thelander. 1992. The role of herpes simplex virus ribonucleotide reductase small subunit carboxyl terminus in subunit interaction and formation of iron-tyrosyl center structure. J. Biol. Chem. 267:15816-15822.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15816-15822
    • Filatov, D.1    Ingemarson, R.2    Graslund, A.3    Thelander, L.4
  • 10
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U., and H. Eklund. 1994. Structure of ribonucleotide reductase protein R1. Nature. 370:533-539.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.