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The Journal of Biological Chemistry|August 5, 1992
The role of herpes simplex virus ribonucleotide reductase small subunit carboxyl terminus in subunit interaction and formation of iron-tyrosyl center structureD Filatov, R Ingemarson, A Gräslund, et al.
Biochemistry|April 4, 1995
Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductaseU Rova, K Goodtzova, R Ingemarson, et al.
The Journal of Biological Chemistry|September 27, 1996
Induction of the mouse ribonucleotide reductase R1 and R2 genes in response to DNA damage by UV lightD Filatov, S Björklund, E Johansson, et al.
Biochemistry|July 2, 1996
A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductaseR Ingemarson, L Thelander
The Journal of Biological Chemistry|October 20, 1995
Role of a proximal NF-Y binding promoter element in S phase-specific expression of mouse ribonucleotide reductase R2 geneD Filatov, L Thelander
Journal of Virology|September 1, 1989
Herpes simplex virus ribonucleotide reductase: expression in Escherichia coli and purification to homogeneity of a tyrosyl free radical-containing, enzymatically active form of the 38-kilodalton subunitR Ingemarson, A Gräslund, A Darling, et al.
The Journal of Biological Chemistry|July 8, 2000
Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductaseP Reichard, R Eliasson, R Ingemarson, et al.
The Journal of Biological Chemistry|August 14, 1999
Evidence by mutagenesis that Tyr(370) of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathwayU Rova, A Adrait, S Pötsch, et al.
The Journal of Biological Chemistry|August 15, 1998
Kinetic evidence that a radical transfer pathway in protein R2 of mouse ribonucleotide reductase is involved in generation of the tyrosyl free radicalP P Schmidt, U Rova, B Katterle, et al.
Biochemistry|March 15, 1994
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1P O Lycksell, R Ingemarson, R Davis, et al.
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