Evidence map›Paper›PMID 33172212›Full record

ArticleInternational journal of molecular sciences2020

Ensemble-Based Analysis of the Dynamic Allostery in the PSD-95 PDZ3 Domain in Relation to the General Variability of PDZ Structures.

Dániel Dudola, Anett Hinsenkamp, Zoltán Gáspári

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Resonance assignment of the Shank1 PDZ domain.Biomolecular NMR assignments · 2022
    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

3 authors.

Dániel DudolaFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, 1083 Budapest, Hungary.
Anett HinsenkampFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, 1083 Budapest, Hungary.
Zoltán GáspáriFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, 1083 Budapest, Hungary.ORCID 0000-0002-8692-740X

Funding

European Union and co-financed by the European Social Fund EFOP-3.6.2-16-2017-00013Hungarian Scientific Research Fund 124363
6 · The paper itself

Abstract

PDZ domains are abundant interaction hubs found in a number of different proteins and they exhibit characteristic differences in their structure and ligand specificity. Their internal dynamics have been proposed to contribute to their biological activity

Indexed as

Amino Acid SequenceAnimalsBinding SitesDisks Large Homolog 4 ProteinEntropyHumansIntracellular Signaling Peptides and ProteinsLigandsMembrane ProteinsModels, MolecularMolecular ConformationMolecular Dynamics SimulationPDZ DomainsProtein BindingDisks Large Homolog 4 ProteinIntracellular Signaling Peptides and ProteinsLigandsMembrane Proteinsallosteryinternal dynamicsPDZ domainrestrained molecular dynamics

Identifiers

PMID33172212
PMCPMC7672539

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.