Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding
- 1 August 1997
- Vol. 5 (8) , 1077-1092
- https://doi.org/10.1016/s0969-2126(97)00259-1
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- The Ten-stranded β/α Barrel in Ribonucleotide Reductase Protein R1Journal of Molecular Biology, 1996
- Thiyl Radicals in Ribonucleotide ReductasesScience, 1996
- Structure of ribonucleotide reductase protein R1Nature, 1994
- From RNA to DNA, Why So Many Ribonucleotide Reductases?Science, 1993
- Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activityBiochemistry, 1992
- A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusingBiochemistry, 1992
- Three-dimensional structure of the free radical protein of ribonucleotide reductaseNature, 1990
- Location of the redox-active thiols of ribonucleotide reductase: sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymesBiochemistry, 1987
- Deoxyribonucleoside-triphosphate imbalance death: Deoxyadenosine-induced dNTP imbalance and DNA double strand breaks in mouse FM3A cells and the mechanism of cell deathBiochemical and Biophysical Research Communications, 1987
- Role of effector binding in allosteric control of ribonucleoside diphosphate reductaseJournal of Molecular Biology, 1969