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The use of thiols by ribonucleotide reductase
Free Radical Biology and Medicine, 2010Ribonucleotide reductase (RNR) catalyzes the rate-limiting de novo synthesis of 2'-deoxyribonucleotides from the corresponding ribonucleotides and thereby provides balanced deoxyribonucleotide pools required for error-free DNA replication and repair.
Arne Holmgren, Rajib Sengupta
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The reduction of ribonucleotides catalyzed by the enzyme ribonucleotide reductase
Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta), 2002This work is devoted to the study of the radical catalytic pathway for the ribonucleotide reduction process assisted by ribonucleotide reductase. The present study is directed toward the investigation of one of the most controversial steps in the reduction pathway – the elimination of the 2′ hydroxyl group from the ribonucleotide.
Maria J. Ramos +2 more
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Transcriptional Regulation of Ribonucleotide Reductase
1991The Swiss 3T3 cell system can be used to explore the molecular mechanism of proliferation. These fibroblasts can be arrested in a quiescent homogeneous Go/G1 state by serum deprivation and then induced to proliferate by a variety of mitogenic growth factors (1). An important endeavour in determining the basis of growth factor action is to elucidate the
Daniel A. Albert, Enrique Rozengurt
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Regulation of Ribonucleotide Reductase
1981Publisher Summary This chapter discusses the regulation of ribonucleotide reductase. Ribonucleotide reductase catalyzes the first unique step of DNA synthesis by converting the four ribonucleotides to the corresponding deoxyribonucleotides. Deoxyribonucleotides are highly specialized metabolites playing only limited roles apart from their function as
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Targeting ribonucleotide reductase for cancer therapy
Expert Opinion on Therapeutic Targets, 2013Ribonucleotide reductase (RR) is a unique enzyme, because it is responsible for reducing ribonucleotides to their corresponding deoxyribonucleotides, which are the building blocks required for DNA replication and repair. Dysregulated RR activity is associated with genomic instability, malignant transformation and cancer development.
Jimin Shao +3 more
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Structure, function, and mechanism of ribonucleotide reductases
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2004Ribonucleotide reductase (RNR) is the enzyme responsible for the conversion of ribonucleotides to 2'-deoxyribonucleotides and thereby provides the precursors needed for both synthesis and repair of DNA. In the recent years, many new crystal structures have been obtained of the protein subunits of all three classes of RNR.
Pål Graff +3 more
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Ribonucleotide reductase as a chemotherapeutic target
Advances in Enzyme Regulation, 1988Ribonucleotide reductase, because of the critical role that it plays in DNA replication and the specific properties of the protein subunits, provides a unique metabolic target for chemotherapeutic approaches to cancer treatment. Combinations of ribonucleotide reductase inhibitors resulted in synergistic inhibition of cell growth with concurrent ...
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Studies on the Mechanism of Ribonucleotide Reductases
Journal of the American Chemical Society, 1997Ribonucleotide reductases are enzymes that catalyze the conversion of ribonucleotides to 2‘-deoxyribonucleotides. This important reaction is initiated by the generation of a C-3‘ nucleotide radical and subsequent loss of the 2‘-hydroxyl group. In order to model certain steps in this mechanism, selenol ester 23 was prepared and photolyzed providing the ...
Bernd Giese, Roman Lenz
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[2] Tyrosyl radicals and ribonucleotide reductase
2002Publisher Summary This chapter describes methods (light absorption and electron paramagnetic resonance (EPR) spectroscopy) for monitoring the various types of tyrosyl radicals in class I RNRs. These radicals are important targets for antiproliferative compounds.
Marl Fontecave, Catherine Gerez
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A simple method to purify ribonucleotide reductase
Analytical Biochemistry, 1983Assays of ribonucleotide reductase in extracts of Detroit 98 (human) cells were found to be complicated by the rapid depletion of the substrate (CDP) by nucleoside diphosphate kinase. Assays of either 100,000g supernatants or ammonium sulfate-fractionated extracts resulted in the conversion of greater than 90% of the substrate to CTP within 2 min.
Devron Averett, Thomas Spector
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