[1] Thiols in redox mechanism of ribonucleotide reductase
Author:
Publisher
Elsevier
Reference68 articles.
1. RIBONUCLEOTIDE REDUCTASES
2. Electron Spin Resonance of the Iron-containing Protein B2 from Ribonucleotide Reductase
3. The tyrosine free radical in ribonucleotide reductase from Escherichia coli.
4. Mechanism of Lactobacillus leichmannii ribonucleotide reductase studied with Co.alpha.[.alpha.-(aden-9-yl)]-Co.beta.-adenosylcobamide (pseudocoenzyme B12)
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1. Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins;Scientific Reports;2014-07-02
2. The use of thiols by ribonucleotide reductase;Free Radical Biology and Medicine;2010-12
3. Unraveling the Hydroxypropionaldehyde (HPA) System: An Active Antimicrobial Agent against Human Pathogens;Journal of Agricultural and Food Chemistry;2010-09-16
4. Molecular Mechanisms of Thioredoxin and Glutaredoxin as Hydrogen Donors for Mammalian S Phase Ribonucleotide Reductase;Journal of Biological Chemistry;2009-03
5. Mechanism of inhibition of ribonucleotide reductase with motexafin gadolinium (MGd);Biochemical and Biophysical Research Communications;2009-02
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