Evidence map›Paper›PMID 29746236›Full record

ArticleMethods in enzymology2018

Iron-Sulfur Clusters in DNA Polymerases and Primases of Eukaryotes.

Andrey G Baranovskiy, Hollie M Siebler, Youri I Pavlov, Tahir H Tahirov

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
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  4. Revised mechanism of hydroxyurea-induced cell cycle arrest and an improved alternative.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  17. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
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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

4 authors at 2 institutions in 1 country.

Andrey G BaranovskiyEppley Institute for Research in Cancer, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, United States.
Hollie M SieblerCreighton University, Omaha, NE, United States.
Youri I PavlovEppley Institute for Research in Cancer, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, United States. Electronic address: ypavlov@unmc.edu.
Tahir H TahirovEppley Institute for Research in Cancer, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, United States. Electronic address: ttahirov@unmc.edu.
University of Nebraska Medical Center · USCreighton University · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Joann B. Sweasy · 1985 to 2026
$55.0M
Human DNA Replication Machines: Structure-Function of Polymerase Alpha-PrimaseR01GM101167 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI TAHIROV, TAHIR H · 2013 to 2017
$1.9M
NCI NIH HHS P30 CA036727NIGMS NIH HHS R01 GM101167
6 · The paper itself

Abstract

Research during the past decade witnessed the discovery of [4Fe-4S] clusters in several members of the eukaryotic DNA replication machinery. The presence of clusters was confirmed by UV-visible absorption, electron paramagnetic resonance spectroscopy, and metal analysis for primase and the B-family DNA polymerases δ and ζ. The crystal structure of primase revealed that the [4Fe-4S] cluster is buried inside the protein and fulfills a structural role. Although [4Fe-4S] clusters are firmly established in the C-terminal domains of catalytic subunits of DNA polymerases δ and ζ, no structures are currently available and their precise roles have not been ascertained. The [4Fe-4S] clusters in the polymerases and primase play a structural role ensuring proper protein folding and stability. In DNA polymerases δ and ζ, they can potentially play regulatory role by sensing hurdles during DNA replication and assisting with DNA polymerase switches by oscillation between oxidized-reduced states.

Indexed as

AnimalsDNA-Directed DNA PolymeraseDNA Polymerase IIIDNA Polymerase thetaDNA PrimaseDNA ReplicationHumansIronIron-Sulfur ProteinsModels, MolecularProtein ConformationSulfurDNA-Directed DNA PolymeraseDNA Polymerase IIIDNA Polymerase thetaDNA PrimaseIronIron-Sulfur ProteinsSulfurB-subunitCrystal structureDNA polymeraseDNA replicationIron–sulfur clusterPrimase

Identifiers

PMID29746236
PMCPMC5947875
OpenAlexW2771603555

What OpenQuestion holds

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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.