Results 301 to 310 of about 38,336 (323)

The evolution of ribonucleotide reduction revisited

Trends in Biochemical Sciences, 2001
Ribonucleotide reductases (RNRs) catalyze the conversion of both purine and pyrimidine nucleotides to deoxynucleotides in all organisms and provide all the monomeric precursors essential for both DNA replication and repair. RNRs have been divided into three classes on the basis of their unique metallo-cofactors.
JoAnne Stubbe, Cyril S. Yee, Jie Ge
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Ribonucleotide Reductase—a Radical Enzyme

Science, 1983
Ribonucleotide reductases catalyze the enzymatic formation of deoxyribonucleotides, an obligatory step in DNA synthesis. The native form of the enzyme from Escherichia coli or from mammalian sources contains as part of its polypeptide structure a free tyrosyl radical, stabilized by an iron center.
Peter Reichard, Anders Ehrenberg
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Purification of glycineamide ribonucleotide transformylase

Biochemical and Biophysical Research Communications, 1978
Abstract Glycineamide ribonucleotide transformylase has been purified 240-fold from chicken liver along with formyl-methenyl-methylenetetrahydrofolate synthetase (combined), through seven purification steps including a glycineamide ribonucleotide affinity column and a 10-formyl synthetase specific MgATP elution from hydroxylapatite.
Stephen J. Benkovic, G. Chettur, L.Y. Lin, Carol A. Caperelli   +3 more
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Crystallographic investigations of ribonucleotide reductase

Biochemical Society Transactions, 1993
Introduction Ribonucleotide reductase catalyses the de novo production of deoxyribonucleotides. The enzyme reduces all the four main ribonucleotides to the corresponding deoxyribonucleotides. In higher organisms and in Eschmkhziz coli. this takes place at the diphosphate level I 1 1. Kibonucleotide reductase from E.
Anders Aberg, Ulla Uhlin, Hans Eklund, Pär Nordlund   +3 more
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Enzymatic Reduction of Ribonucleotides

1967
Publisher Summary This chapter describes the enzymatic reduction of ribonucleotides. The formation of deoxyribonucleotides from ribonucleotides in a cell-free system is discussed in this chapter. It was important to establish that the observed transfer of isotope from cytidine monophosphate (CMP) to dCMP occurred only by direct reduction of the ...
Peter Reichard, Agne Larsson
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Structural features of ribonucleotide reductase

Proteins: Structure, Function, and Bioinformatics, 1986
AbstractHerpes simplex virus type 1 (HSV‐1) encodes a ribonucleotide reductase which comprises two polypeptides with sizes of 136,000 (RR1) and 38,000 mol. wt. (RR2). We have determined the entire DNA sequence specifying HSV‐1 RR1 and have identified two adjacent open reading frames in varicella‐zoster virus (VZV) which have homology to HSV RR1 and RR2;
I Nikas, Andrew J. Davison, J B Clements, John McLauchlan, William R. Taylor   +4 more
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The nature of the isomerism in yeast ribonucleotides

Biochimica et Biophysica Acta, 1953
Abstract The isomeric nucleotides obtained upon the hydrolysis of ribose nucleic acid have been studied. The nucleotides were dephosphorylated enzymically, and the resulting nucleosides subjected to further degradation by nucleoside deaminases.
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Thin-layer electrophoresis of ribonucleotides

Analytical Biochemistry, 1969
Abstract Electrophoresis on thin layers of cellulose of an alkaline hydrolyzate of RNA provides an easy and reproducible method for base ratio determinations. Separation of a nucleotide mixture (20–40 μg) is completed in 90 min at 4°C and requires only conventional equipment.
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Transcriptional Regulation of Ribonucleotide Reductase

1991
The 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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Interaction of ribonucleotide reductase with ribonucleotide analogs

Biochemistry, 1971
Hogenkamp Hp, Follmann H
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