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Journal Abstract Search

135 related items for PubMed ID: 3322391

  • 1. Location of the redox-active thiols of ribonucleotide reductase: sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes.
    Lin AN, Ashley GW, Stubbe J.
    Biochemistry; 1987 Nov 03; 26(22):6905-9. PubMed ID: 3322391
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  • 6. Lactobacillus leichmannii and Escherichia coli ribonucleotide reductases: chemical and structural similarities.
    Lin AI, Ashley GW, Stubbe J.
    Cold Spring Harb Symp Quant Biol; 1987 Nov 03; 52():587-96. PubMed ID: 3331345
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  • 7. Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii.
    Booker S, Stubbe J.
    Proc Natl Acad Sci U S A; 1993 Sep 15; 90(18):8352-6. PubMed ID: 8397403
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  • 8. Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli.
    Aberg A, Hahne S, Karlsson M, Larsson A, Ormö M, Ahgren A, Sjöberg BM.
    J Biol Chem; 1989 Jul 25; 264(21):12249-52. PubMed ID: 2663852
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  • 9. Adenosylcobalamin-dependent ribonucleoside triphosphate reductase from Lactobacillus leichmannii. Rapid, improved purification involving dGTP-based affinity chromatography plus biophysical characterization studies demonstrating enhanced, "crystallographic level" purity.
    Suto RK, Whalen MA, Finke RG.
    Prep Biochem Biotechnol; 1999 Aug 25; 29(3):273-309. PubMed ID: 10431931
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  • 10. Gemcitabine 5'-triphosphate is a stoichiometric mechanism-based inhibitor of Lactobacillus leichmannii ribonucleoside triphosphate reductase: evidence for thiyl radical-mediated nucleotide radical formation.
    Silva DJ, Stubbe J, Samano V, Robins MJ.
    Biochemistry; 1998 Apr 21; 37(16):5528-35. PubMed ID: 9548936
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  • 11. Thiyl radicals in ribonucleotide reductases.
    Licht S, Gerfen GJ, Stubbe J.
    Science; 1996 Jan 26; 271(5248):477-81. PubMed ID: 8560260
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  • 12. Inactivation of the Lactobacillus leichmannii ribonucleoside triphosphate reductase by 2'-chloro-2'-deoxyuridine 5'-triphosphate: stoichiometry of inactivation, site of inactivation, and mechanism of the protein chromophore formation.
    Ashley GW, Harris G, Stubbe J.
    Biochemistry; 1988 Jun 14; 27(12):4305-10. PubMed ID: 3048383
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  • 17. Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.
    Mulliez E, Ollagnier S, Fontecave M, Eliasson R, Reichard P.
    Proc Natl Acad Sci U S A; 1995 Sep 12; 92(19):8759-62. PubMed ID: 7568012
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  • 18. Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction: kinetic analysis of inhibition studies.
    Climent I, Sjöberg BM, Huang CY.
    Biochemistry; 1991 May 28; 30(21):5164-71. PubMed ID: 2036382
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  • 19. Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2',2'-difluoro-2'-deoxycytidine 5'-triphosphate: adenosylcobalamin destruction and formation of a nucleotide-based radical.
    Lohman GJ, Gerfen GJ, Stubbe J.
    Biochemistry; 2010 Feb 23; 49(7):1396-403. PubMed ID: 20088568
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  • 20. Hydrogen abstraction from thiols by adenosyl radicals: chemical precedent for thiyl radical formation, the first catalytic step in ribonucleoside triphosphate reductase from Lactobacillus leichmannii.
    Sirovatka JM, Finke RG.
    J Inorg Biochem; 2000 Jan 30; 78(2):149-60. PubMed ID: 10766338
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