Evidence map›Paper›PMID 34189846›Full record

ArticleThe FEBS journal2021

Analysis of ligand binding and resulting conformational changes in pyrophosphatase NUDT9.

Ellen Gattkowski, Trevor J Rutherford, Franziska Möckl, Andreas Bauche, Simon Sander, Ralf Fliegert, Henning Tidow

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.0field-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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
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

7 authors at 2 institutions in 2 countries.

Ellen GattkowskiThe Hamburg Advanced Research Center for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Germany.
Trevor J RutherfordMRC Laboratory of Molecular Biology, Cambridge, UK.
Franziska MöcklDepartment of Biochemistry and Molecular Cell Biology, University Medical Centre Hamburg-Eppendorf, Germany.
Andreas BaucheDepartment of Biochemistry and Molecular Cell Biology, University Medical Centre Hamburg-Eppendorf, Germany.
Simon SanderThe Hamburg Advanced Research Center for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Germany.
Ralf FliegertDepartment of Biochemistry and Molecular Cell Biology, University Medical Centre Hamburg-Eppendorf, Germany.
Henning TidowThe Hamburg Advanced Research Center for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Germany.ORCID 0000-0002-4702-9332
Universität Hamburg · DEMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184326
6 · The paper itself

Abstract

Nudix hydrolase 9 (NUDT9) is a member of the nucleoside linked to another moiety X (NUDIX) protein superfamily, which hydrolyses a broad spectrum of organic pyrophosphates from metabolic processes. ADP-ribose (ADPR) has been the only known endogenous substrate accepted by NUDT9 so far. The Ca

Indexed as

Molecular Docking SimulationProtein ConformationAdenosine Diphosphate RiboseBinding, CompetitiveBinding SitesHumansKineticsLigandsMagnetic Resonance SpectroscopyMutationProtein BindingPyrophosphatasesScattering, Small AngleSubstrate SpecificityX-Ray DiffractionAdenosine Diphosphate RiboseLigandsNUDT9PyrophosphatasesADPRconformational changeFRET sensorligandpyrophosphataseTRPM2

Identifiers

PMID34189846
PMCPMC7612441
OpenAlexW3175404109

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.