The evolution of ribonucleotide reduction revisited (Q31884365)

4 July 2017

title

The evolution of ribonucleotide reduction revisited (English)

1 reference

4 July 2017

Stubbe J

1

1 reference

4 July 2017

Ge J

series ordinal

2

1 reference

4 July 2017

Yee CS

series ordinal

3

1 reference

4 July 2017

publication date

1 February 2001

1 reference

4 July 2017

number of pages

7

1 reference

Trends in Biochemical Sciences

inferred from page(s)

published in

1 reference

4 July 2017

volume

26

1 reference

4 July 2017

issue

2

1 reference

4 July 2017

page(s)

93-99

1 reference

The evolution of ribonucleotide reduction

4 July 2017

cites work

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The structural basis of ribosome activity in peptide bond synthesis

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

MOLECULAR EVOLUTION:Do Proteins Predate DNA?

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Ribonucleotide reductases

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Protein Radicals in Enzyme Catalysis

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Structure of ribonucleotide reductase protein R1

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

A Glycyl Radical Site in the Crystal Structure of a Class III Ribonucleotide Reductase

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Mechanism of inactivation of Escherichia coli ribonucleotide reductase by 2'-chloro-2'-deoxyuridine 5'-diphosphate: evidence for generation of a 2'-deoxy-3'-ketonucleotide via a net 1,2 hydrogen shift

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Location of the redox-active thiols of ribonucleotide reductase: sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cysteine residues in ribonucleotide reduction

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Thiyl radicals in ribonucleotide reductases.

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The Free Radical of the Anaerobic Ribonucleotide Reductase fromEscherichia coliIs at Glycine 681

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction.

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The activating component of the anaerobic ribonucleotide reductase from Escherichia coli. An iron-sulfur center with only three cysteines

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Ribonucleotide reductases in the twenty-first century

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Glycyl radical enzymes: a conservative structural basis for radicals

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The B12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: an evolutionary solution to the ribonucleotide reductase conundrum

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The [4Fe-4S]1 Cluster of Pyruvate Formate-Lyase Activating Enzyme Generates the Glycyl Radical on Pyruvate Formate-Lyase: EPR-Detected Single Turnover

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Cysteines Involved in Radical Generation and Catalysis of Class III Anaerobic Ribonucleotide Reductase

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalyzed by cysteine 419

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Role of effector binding in allosteric control of ribonucleoside diphosphate reductase

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Allosteric control of three B12-dependent (class II) ribonucleotide reductases. Implications for the evolution of ribonucleotide reduction

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

From RNA to DNA, why so many ribonucleotide reductases?

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and allosteric regulation of the pure enzyme system.

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Allosterism, regulation and cooperativity: the case of ribonucleotide reductase of Lactobacillus leichmannii

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Allosteric Regulation of the Class III Anaerobic Ribonucleotide Reductase from Bacteriophage T4

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Regulation of T4 phage aerobic ribonucleotide reductase. Simultaneous assay of the four activities

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Allosteric regulation of vaccinia virus ribonucleotide reductase, analyzed by simultaneous monitoring of its four activities

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

The ten-stranded beta/alpha barrel in ribonucleotide reductase protein R1

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

Ribonucleotide reductases: the link between an RNA and a DNA world?

1 reference

https://api.crossref.org/works/10.1016/S0968-0004(00)01764-3

7 January 2021

10.1016/S0968-0004(00)01764-3

Identifiers

DOI

1 reference

4 July 2017

1 reference