Evidence map›Paper›PMID 25160629›Full record

ReviewThe Journal of biological chemistry2014

Choosing the right metal: case studies of class I ribonucleotide reductases.

Mingxia Huang, Mackenzie J Parker, JoAnne Stubbe

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  7. An Unusual Route forJournal of bacteriology · 2020
    Article
  8. The emergence of carbapenemase blaEuropean journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2020
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Mingxia HuangFrom the Department of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, Colorado 80045 and.
Mackenzie J Parkerthe Departments of Chemistry and.
JoAnne Stubbethe Departments of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 stubbe@mit.edu.
Massachusetts Institute of Technology · USUniversity of Colorado Denver · US

Funding

Ribonucleotide Reductase Regulation: Diferric Y* assembly/maintenance and Sml1R01GM081393 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STUBBE, JOANNE · 2008 to 2016
$3.9M
In Vivo Regulation and Inhibition of Ribonucleotide ReductaseR01CA125574 · NCI · UNIVERSITY OF COLORADO DENVER · PI HUANG, MINGXIA · 2008 to 2012
$1.6M
NCI NIH HHS CA125574NCI NIH HHS R01 CA125574NIGMS NIH HHS GM81393NIGMS NIH HHS R01 GM081393
6 · The paper itself

Abstract

Over one-third of all proteins require metallation for function (Waldron, K. J., Rutherford, J. C., Ford, D., and Robinson, N.J. (2009) Nature 460, 823-830). As biochemical studies of most proteins depend on their isolation subsequent to recombinant expression (i.e. they are seldom purified from their host organism), there is no gold standard to assess faithful metallocofactor assembly and associated function. The biosynthetic machinery for metallocofactor formation in the recombinant expression system may be absent, inadequately expressed, or incompatible with a heterologously expressed protein. A combination of biochemical and genetic studies has led to the identification of key proteins involved in biosynthesis and likely repair of the metallocofactor of ribonucleotide reductases in both bacteria and the budding yeast. In this minireview, we will discuss the recent progress in understanding controlled delivery of metal, oxidants, and reducing equivalents for cofactor assembly in ribonucleotide reductases and highlight issues associated with controlling Fe/Mn metallation and avoidance of mismetallation.

Indexed as

Cations, DivalentEscherichia coliEscherichia coli ProteinsGene ExpressionIronManganeseModels, MolecularRecombinant ProteinsRibonucleotide ReductasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityStructure-Activity RelationshipCations, DivalentEscherichia coli ProteinsIronManganeseRecombinant ProteinsRibonucleotide ReductasesSaccharomyces cerevisiae ProteinsBacterial PathogenesisIronIron-Sulfur ProteinManganeseMetal HomeostasisMetallationMismetallationRibonucleotide ReductaseYeast

Identifiers

PMID25160629
PMCPMC4192465
OpenAlexW2070370981

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.