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Survival of DNA Damage in Yeast Directly Depends on Increased dNTP Levels Allowed by Relaxed Feedback Inhibition of Ribonucleotide Reductase

Cell, 2003-02, Vol.112 (3), p.391-401

2003

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Yeast Sml1, a Protein Inhibitor of Ribonucleotide Reductase

The Journal of biological chemistry, 1999-12, Vol.274 (51), p.36679-36683

1999

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The Schizosaccharomyces pombe Replication Inhibitor Spd1 Regulates Ribonucleotide Reductase Activity and dNTPs by Binding to the Large Cdc22 Subunit

The Journal of biological chemistry, 2006-01, Vol.281 (3), p.1778-1783

2006

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Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins

Scientific reports, 2017-04, Vol.7, p.45880-45880

2017

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Correction: Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins

Scientific reports, 2017-04, Vol.7 (1), Article 45880

2017

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Yeast DNA Damage-inducible Rnr3 Has a Very Low Catalytic Activity Strongly Stimulated after the Formation of a Cross-talking Rnr1/Rnr3 Complex

The Journal of biological chemistry, 2002-05, Vol.277 (21), p.18574-18578

2002

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Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins

Scientific reports, 2014-07, Vol.4 (1), p.5539-5539, Article 5539

2014

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Yeast Ribonucleotide Reductase has a Heterodimeric Iron-Radical-Containing Subunit

Proceedings of the National Academy of Sciences - PNAS, 2000-03, Vol.97 (6), p.2474-2479

2000

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The ribonucleotide reductase inhibitor Sml1 is a new target of the Mec1/Rad53 kinase cascade during growth and in response to DNA damage

The EMBO journal, 2001-07, Vol.20 (13), p.3544-3553

2001

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The First Holocomplex Structure of Ribonucleotide Reductase Gives New Insight into its Mechanism of Action

Journal of molecular biology, 2006-06, Vol.359 (2), p.365-377

2006

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Mutational and Structural Analyses of the Ribonucleotide Reductase Inhibitor Sml1 Define Its Rnr1 Interaction Domain Whose Inactivation Allows Suppression of mec1 andrad53 Lethality

Molecular and Cellular Biology, 2000-12, Vol.20 (23), p.9076-9083

2000

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Metal Binding and Activity of Ribonucleotide Reductase Protein R2 Mutants: Conditions for Formation of the Mixed Manganese−Iron Cofactor

Biochemistry (Easton), 2009-07, Vol.48 (27), p.6532-6539

2009

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Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality

Molecular and cellular biology, 2000-12, Vol.20 (23), p.9076-9083

2000

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Ribosylurea Accumulates in Yeast urc4 Mutants

Nucleosides, nucleotides & nucleic acids, 2010-06, Vol.29 (4-6), p.433-437

2010

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Chlamydial ribonucleotide reductase: Tyrosyl radical function in catalysis replaced by the FeIII-FeIV cluster

Proceedings of the National Academy of Sciences - PNAS, 2006-06, Vol.103 (26), p.9850-9854

2006

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Survival of DNA Damage in Yeast Directly Depends on Increased dNTP Levels Allowed by Relaxed Feedback Inhibition of Ribonucleotide Reductase

Yeast Sml1, a Protein Inhibitor of Ribonucleotide Reductase

The Schizosaccharomyces pombe Replication Inhibitor Spd1 Regulates Ribonucleotide Reductase Activity and dNTPs by Binding to the Large Cdc22 Subunit

Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins

Correction: Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins

Yeast DNA Damage-inducible Rnr3 Has a Very Low Catalytic Activity Strongly Stimulated after the Formation of a Cross-talking Rnr1/Rnr3 Complex

Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins

Yeast Ribonucleotide Reductase has a Heterodimeric Iron-Radical-Containing Subunit

The ribonucleotide reductase inhibitor Sml1 is a new target of the Mec1/Rad53 kinase cascade during growth and in response to DNA damage

The First Holocomplex Structure of Ribonucleotide Reductase Gives New Insight into its Mechanism of Action

Mutational and Structural Analyses of the Ribonucleotide Reductase Inhibitor Sml1 Define Its Rnr1 Interaction Domain Whose Inactivation Allows Suppression of mec1 andrad53 Lethality

Metal Binding and Activity of Ribonucleotide Reductase Protein R2 Mutants: Conditions for Formation of the Mixed Manganese−Iron Cofactor

Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality

Ribosylurea Accumulates in Yeast urc4 Mutants

Chlamydial ribonucleotide reductase: Tyrosyl radical function in catalysis replaced by the FeIII-FeIV cluster

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