Evidence map›Paper›PMID 29531348›Full record

ArticleScientific reports2018

Structural model of human dUTPase in complex with a novel proteinaceous inhibitor.

Kinga Nyíri, Haydyn D T Mertens, Borbála Tihanyi, Gergely N Nagy, Bianka Kőhegyi, Judit Matejka, Matthew J Harris, Judit E Szabó, Veronika Papp-Kádár, Veronika Németh-Pongrácz and 5 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

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  11. Detection of Genomic Uracil Patterns.International journal of molecular sciences · 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

15 authors at 5 institutions in 3 countries.

Kinga NyíriDepartment of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, 1111, Hungary. nyiri.kinga@ttk.mta.hu.
Haydyn D T MertensEuropean Molecular Biology Laboratory, Hamburg Outstation, c/o DESY, Notkestrasse 85, Hamburg, 22603, Germany.ORCID 0000-0002-5664-744X
Borbála TihanyiInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, 1117, Hungary.
Gergely N NagyDepartment of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, 1111, Hungary.
Bianka KőhegyiDepartment of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, 1111, Hungary.
Judit MatejkaDepartment of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, 1111, Hungary.
Matthew J HarrisDepartment of Chemistry, King's College London, Britannia House, London, SE1 1DB, United Kingdom.
Judit E SzabóDepartment of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, 1111, Hungary.
Veronika Papp-KádárDepartment of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, 1111, Hungary.
Veronika Németh-PongráczInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, 1117, Hungary.
Olivér OzohanicsInstitute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, 1117, Hungary.ORCID 0000-0002-2705-9921
Károly VékeyInstitute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, 1117, Hungary.
Dmitri I SvergunEuropean Molecular Biology Laboratory, Hamburg Outstation, c/o DESY, Notkestrasse 85, Hamburg, 22603, Germany.
Antoni J BorysikDepartment of Chemistry, King's College London, Britannia House, London, SE1 1DB, United Kingdom.
Beáta G VértessyDepartment of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, 1111, Hungary. vertessy@mail.bme.hu.
Budapest University of Technology and Economics · HUEuropean Molecular Biology Laboratory · DEInstitute of Molecular Life Sciences · HUInstitute of Organic Chemistry · HUKing's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase), essential for DNA integrity, acts as a survival factor for tumor cells and is a target for cancer chemotherapy. Here we report that the Staphylococcal repressor protein Stl

Indexed as

Bacterial ProteinsCatalytic DomainHumansMolecular Docking SimulationProtein BindingProtein ConformationProtein MultimerizationPyrophosphatasesRepressor ProteinsScattering, Small AngleStaphylococcal InfectionsStaphylococcus aureusX-Ray DiffractionBacterial ProteinsdUTP pyrophosphatasePyrophosphatasesRepressor Proteins

Identifiers

PMID29531348
PMCPMC5847570
OpenAlexW2807563188

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.