Evidence map›Paper›PMID 37861971›Full record

ArticleBiomolecular NMR assignments2023

Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using

Fanni Sebák, Péter Ecsédi, László Nyitray, Andrea Bodor

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

Article in Biomolecular NMR assignments, 2023. 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
0.7field-weighted citation impact, top 22% 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, 3 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

4 authors at 1 institution in 1 country.

Fanni SebákAnalytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány 1/a, Budapest, 1117, Hungary.ORCID 0000-0001-9252-9961
Péter EcsédiDepartment of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, Budapest, 1117, Hungary.ORCID 0000-0002-4700-125X
László NyitrayDepartment of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/c, Budapest, 1117, Hungary.ORCID 0000-0003-4717-5994
Andrea BodorAnalytical and BioNMR Laboratory, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány 1/a, Budapest, 1117, Hungary. andrea.bodor@ttk.elte.hu.ORCID 0000-0002-7422-298X
Eötvös Loránd University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein p53 is mostly known for playing a key role in tumour suppression, and mutations in the p53 gene are amongst the most frequent genomic events accompanying oncogenic transformation. Continuous research is conducted to target disordered proteins/protein regions for cancer therapy, for which atomic level information is also necessary. The disordered N-terminal part of p53 contains the transactivation and the proline-rich domains-which besides being abundant in proline residues-contains repetitive Pro-Ala motifs. NMR assignment of such repetitive, proline-rich regions is challenging due to the lack of amide protons in the

Indexed as

NeoplasmsTumor Suppressor Protein p53HumansNuclear Magnetic Resonance, BiomolecularProlineProtonsProlineProtonsTumor Suppressor Protein p531Hα-detectionIntrinsically disordered proteinsp53Proline-rich domainReal-time homo- and heteronuclear decoupling acquisition

Identifiers

PMID37861971
PMCPMC10630184
OpenAlexW4387798270

What Socratic holds

Textmetadata
LicenceCC BY
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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 Socratic graph.