Evidence map›Paper›PMID 28071757›Full record

ArticleScientific reports2017

New insights into the GINS complex explain the controversy between existing structural models.

Marta Carroni, Matteo De March, Barbara Medagli, Ivet Krastanova, Ian A Taylor, Heinz Amenitsch, Hiroyuchi Araki, Francesca M Pisani, Ardan Patwardhan, Silvia Onesti

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

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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

10 authors at 7 institutions in 4 countries.

Marta CarroniDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Matteo De MarchStructural Biology Laboratory, Elettra - Sincrotrone Trieste, Trieste 34149, Italy.
Barbara MedagliDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Ivet KrastanovaStructural Biology Laboratory, Elettra - Sincrotrone Trieste, Trieste 34149, Italy.
Ian A TaylorMill Hill Laboratory, The Francis Crick Institute, The Ridgeway, Mill Hill, London NW7 1AA, UK.
Heinz AmenitschInstitute of Inorganic Chemistry, Graz University of Technology, Stremayerg. 6/IV, 8010 Graz, Austria.
Hiroyuchi ArakiDivision of Microbial Genetics, National Institute of Genetics, Shizuoka, Japan.
Francesca M PisaniIstituto di Biochimica delle Proteine, Consiglio Nazionale delle Ricerche, Napoli, Italy.
Ardan PatwardhanDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Silvia OnestiDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Elettra-Sincrotrone Trieste S.C.p.A. · ITEuropean Bioinformatics Institute · GBGraz University of Technology · ATImperial College London · GBInstitute of Protein Biochemistry · ITNational Institute of Genetics · JPThe Francis Crick Institute · GB

Funding

Medical Research Council U117565647
6 · The paper itself

Abstract

GINS is a key component of eukaryotic replicative forks and is composed of four subunits (Sld5, Psf1, Psf2, Psf3). To explain the discrepancy between structural data from crystallography and electron microscopy (EM), we show that GINS is a compact tetramer in solution as observed in crystal structures, but also forms a double-tetrameric population, detectable by EM. This may represent an intermediate step towards the assembly of two replicative helicase complexes at origins, moving in opposite directions within the replication bubble. Reconstruction of the double-tetrameric form, combined with small-angle X-ray scattering data, allows the localisation of the B domain of the Psf1 subunit in the free GINS complex, which was not visible in previous studies and is essential for the formation of a functional replication fork.

Indexed as

Chromosomal Proteins, Non-HistoneCrystallography, X-RayDNA-Binding ProteinsHumansMicroscopy, ElectronModels, MolecularProtein MultimerizationScattering, Small AngleChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGINS1 protein, humanGINS2 protein, humanGINS3 protein, humanGINS4 protein, human

Identifiers

PMID28071757
PMCPMC5223209
OpenAlexW2569646136

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.