Pages that link to "Q41082395"
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The following pages link to Reduction of the small subunit of Escherichia coli ribonucleotide reductase by hydrazines and hydroxylamines (Q41082395):
Displaying 16 items.
- Methyl-hydroxylamine as an efficacious antibacterial agent that targets the ribonucleotide reductase enzyme (Q28544447) (← links)
- Nanoparticle delivery of transition-metal chelators to the brain: Oxidative stress will never see it coming! (Q33957213) (← links)
- Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: implications for the protein gating of intersubunit electron transfer (Q34092078) (← links)
- Role of metal dyshomeostasis in Alzheimer's disease (Q35051952) (← links)
- An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. (Q35307893) (← links)
- Redox intermediates of the Mn-Fe Site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study (Q37855926) (← links)
- Redox-linked changes to the hydrogen-bonding network of ribonucleotide reductase β2. (Q41549682) (← links)
- Antitumor activity of 2,2'-bipyridyl-6-carbothioamide: a ribonucleotide reductase inhibitor. (Q41623715) (← links)
- Escherichia coli and herpes-simplex-virus ribonucleotide reductase R2 subunit. Compared reactivities of the redox centres (Q42167519) (← links)
- Redox-linked conformational control of proton-coupled electron transfer: Y122 in the ribonucleotide reductase β2 subunit (Q42577110) (← links)
- Structure-function investigation of the interaction of 1- and 2-substituted 3-hydroxypyridin-4-ones with 5-lipoxygenase and ribonucleotide reductase (Q43767961) (← links)
- Redox studies of subunit interactivity in aerobic ribonucleotide reductase from Escherichia coli (Q44765715) (← links)
- Reduction of the tyrosyl radical and the iron center in protein R2 of ribonucleotide reductase from mouse, herpes simplex virus and E. coli by p‐alkoxyphenols (Q45788369) (← links)
- Chemical reduction of the diferric/radical center in protein R2 from mouse ribonucleotide reductase is independent of the proposed radical transfer pathway (Q57867894) (← links)
- Kinetic studies on the reduction of the tyrosyl radical of the R2 subunit of E. coli ribonucleotide reductase (Q72109627) (← links)
- New mechanistic insights into the reactivity of the R2 protein of E. coli ribonucleotide reductase (RNR) (Q73833179) (← links)