Evidence map›Paper›PMID 41191219›Full record

ArticleBiomolecular NMR assignments2025

Eszter Nagy-Kanta, Anna Sánta, Zsófia E Kálmán, Jessica Amy Li, Perttu Permi, Zoltán Gáspári, Bálint Péterfia

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecular NMR assignments, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Eszter Nagy-KantaFaculty of Information Technology and Bionincs, Pázmány Péter Catholic University, Budapest, Hungary. peterfia.balint.ferenc@itk.ppke.hu.ORCID http://orcid.org/0009-0003-1322-2008
Anna SántaFaculty of Information Technology and Bionincs, Pázmány Péter Catholic University, Budapest, Hungary.ORCID http://orcid.org/0009-0004-0593-888X
Zsófia E KálmánFaculty of Information Technology and Bionincs, Pázmány Péter Catholic University, Budapest, Hungary.ORCID http://orcid.org/0000-0003-4634-0433
Jessica Amy LiFaculty of Information Technology and Bionincs, Pázmány Péter Catholic University, Budapest, Hungary.
Perttu PermiDepartment of Biological and Environmental Science, University of Jyväskylä, Jyväskylä, Finland.ORCID http://orcid.org/0000-0002-6281-1138
Zoltán GáspáriFaculty of Information Technology and Bionincs, Pázmány Péter Catholic University, Budapest, Hungary.ORCID http://orcid.org/0000-0002-8692-740X
Bálint PéterfiaFaculty of Information Technology and Bionincs, Pázmány Péter Catholic University, Budapest, Hungary.ORCID http://orcid.org/0000-0001-9090-9979

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Guanylate kinase-associated protein, GKAP, is a largely disordered scaffold protein with multiple interaction partners, playing a role in the organization of the postsynaptic protein network. Its C-terminus contains a binding motif for the PDZ domain of Shank proteins, another class of postsynaptic scaffolds. Based on predictions, this motif is preceded by a ~ 40-residue disordered segment with no known additional binding sites or established functional role. Here we report the expression, purification, and

Indexed as

Intrinsically Disordered ProteinsNerve Tissue ProteinsNuclear Magnetic Resonance, BiomolecularAmino Acid SequenceNitrogen IsotopesIntrinsically Disordered ProteinsNerve Tissue ProteinsNitrogen-15Nitrogen IsotopesGKAPHelical propensityIntrinsically disordered proteinPDZ domainPostsynaptic densityShank1

Identifiers

PMID41191219
PMCPMC12589307

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.