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Virology|February 1, 1987
The herpes simplex virus type 1 ribonucleotide reductase is a tight complex of the type alpha 2 beta 2 composed of 40K and 140K proteins, of which the latter shows multiple forms due to proteolysisR Ingemarson, H Lankinen
Biochemistry|July 2, 1996
A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductaseR Ingemarson, 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 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.
Virus Genes|April 1, 1990
Herpes simplex virus-encoded ribonucleotide reductase: evidence for the dissociation/reassociation of the holoenzymeA J Darling, E M McKay, R Ingemarson, et al.
Virus Genes|March 1, 1989
Reconstitution of herpes simplex virus type 1 ribonucleotide reductase activity from the large and small subunitsA J Darling, E M McKay, R Ingemarson, 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.
Biochemistry|February 19, 1991
Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunitG J Mann, A Gräslund, E Ochiai, et al.
International Journal of Peptide and Protein Research|December 1, 1994
The critical C-terminus of the small subunit of herpes simplex virus ribonucleotide reductase is mobile and conformationally similar to C-terminal peptidesS R Laplante, N Aubry, M Liuzzi, et al.
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