Evidence map›Paper›PMID 31734537›Full record

ReviewCurrent opinion in chemical biology2020

The more the merrier: how homo-oligomerization alters the interactome and function of ribonucleotide reductase.

Marcus J C Long, Alexandra Van Hall-Beauvais, Yimon Aye

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. 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.

Marcus J C LongBeverley, East Riding of Yorkshire, HU17 8QH, UK.
Alexandra Van Hall-BeauvaisSwiss Federal Institute of Technology Lausanne (EPFL), Institute of Chemical Sciences and Engineering, 1015, Lausanne, Switzerland.
Yimon AyeSwiss Federal Institute of Technology Lausanne (EPFL), Institute of Chemical Sciences and Engineering, 1015, Lausanne, Switzerland. Electronic address: yimon.aye@epfl.ch.

Funding

Deconvoluting Redox Biology with Targeted ChemistryDP2GM114850 · NIGMS · CORNELL UNIVERSITY · PI AYE, YIMON · 2014 to 2014
$2.3M
NIGMS NIH HHS DP2 GM114850
6 · The paper itself

Abstract

Stereotyped as a nexus of dNTP synthesis, the dual-subunit enzyme - ribonucleotide reductase (RNR) - is coming into view as a paradigm of oligomerization and moonlighting behavior. In the present issue of 'omics', we discuss what makes the larger subunit of this enzyme (RNR-α) so interesting, highlighting its emerging cellular interactome based on its unique oligomeric dynamism that dictates its compartment-specific occupations. Linking the history of the field with the multivariable nature of this exceedingly sophisticated enzyme, we further discuss implications of new data pertaining to DNA-damage response, S-phase checkpoints, and ultimately tumor suppression. We hereby hope to provide ideas for those interested in these fields and exemplify conceptual frameworks and tools that are useful to study RNR's broader roles in biology.

Indexed as

AnimalsDeoxyadenosinesDNA DamageDNA HelicasesHumansModels, MolecularProtein Interaction MapsProtein Structure, QuaternaryRibonucleotide ReductasesDeoxyadenosinesDNA HelicasesRibonucleotide ReductasesZRANB3 protein, humanChemotherapeuticsDNA damageMoonlightingProtein-protein associationsTumor suppressionZRANB3

Identifiers

PMID31734537
PMCPMC7131891

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.