Stephen P. Hendricks
Oregon State University
5 Papers
97 Citations
Stephen P. Hendricks is an academic researcher from Oregon State University. The author has contributed to research in topics: Enzyme & Nucleoside triphosphate. The author has an hindex of 5, co-authored 5 publications.
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Papers
Metabolic functions of microbial nucleoside diphosphate kinases.
Mark A. Bernard,Nancy B. Ray,Nancy B. Ray,Michael C. Olcott,Stephen P. Hendricks,Christopher K. Mathews +5 more
TL;DR: This article summarizes research from the laboratory on two aspects of the biochemistry of nucleoside diphosphate kinase from Escherichia coli—first, its interactions with several T4bacteriophage-coded enzymes, as part of a multienzyme complex for deoxyribonucleosidetriphosphate biosynthesis and phenotypes of an E. coli mutant strain carrying a targeted deletion of ndk.
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T4 phage gene 32 protein as a candidate organizing factor for the deoxyribonucleoside triphosphate synthetase complex.
Linda J. Wheeler,Nancy B. Ray,Christian Ungermann,Stephen P. Hendricks,Mark A. Bernard,Eric S. Hanson,Christopher K. Mathews +6 more
TL;DR: The data suggest a model in which dNTP synthetase complexes, probably more than one per growing DNA chain, are drawn to replication forks via their affinity for gp32 and hence are localized so as to produce dN TPs at their sites of utilization, immediately ahead of growing DNA 3′ termini.
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Allosteric Regulation of Vaccinia Virus Ribonucleotide Reductase, Analyzed by Simultaneous Monitoring of Its Four Activities *
TL;DR: Substrate saturation experiments with a “bioproportional” mixture containing the four rNDP substrates at their relative in vivoconcentrations revealed that a mixture of vaccinia virus R1 protein and mouse R2 protein is catalytically active, making this the first reported chimeric rN DP reductase to show biological activity.
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Differential Effects of Hydroxyurea upon Deoxyribonucleoside Triphosphate Pools, Analyzed with Vaccinia Virus Ribonucleotide Reductase
TL;DR: The primary determinant of radical loss is found to be not the ensemble of allosteric ligands bound but the activity of the enzyme, suggesting that the activities of rNDP reductase are differentially sensitive to hydroxyurea.
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Regulation of T4 phage aerobic ribonucleotide reductase. Simultaneous assay of the four activities.
TL;DR: Results show that ATP does act as a general activator, although the rate of purine nucleotide reduction was approximately 5% of the rate for the pyrimidine nucleotides, and addition of the allosteric effectors at their estimated physiological concentrations dramatically changed the relative rates of substrate reduction, creating a more “balanced” pool of products.
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