Evidence map›Paper›PMID 32098369›Full record

ArticleBiomolecules2020

Investigation of a Direct Interaction between miR4749 and the Tumor Suppressor p53 by Fluorescence, FRET and Molecular Modeling.

Anna Rita Bizzarri, Salvatore Cannistraro

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Recent Advances in p53.Biomolecules · 2021
    Article
  5. Review
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

2 authors at 1 institution in 1 country.

Anna Rita BizzarriBiophysics and Nanoscience Centre, DEB, Università della Tuscia, 01100 Viterbo, Italy.ORCID 0000-0003-3298-6639
Salvatore CannistraroBiophysics and Nanoscience Centre, DEB, Università della Tuscia, 01100 Viterbo, Italy.ORCID 0000-0002-0228-7311
Università degli Studi della Tuscia · IT

Funding

Associazione Italiana per la Ricerca sul Cancro IG15866
6 · The paper itself

Abstract

The interactions between the DNA binding domain (DBD) of the tumor suppressor p53 and miR4749, characterized by a high sequence similarity with the DNA Response Element (RE) of p53, was investigated by fluorescence spectroscopy combined with computational modeling and docking. Fluorescence quenching experiments witnessed the formation of a specific complex between DBD and miR4749 with an affinity of about 10

Indexed as

DNAFluorescenceFluorescence Resonance Energy TransferHumansMicroRNAsMolecular Dynamics SimulationProtein BindingProtein DomainsSpectrometry, FluorescenceTumor Suppressor Protein p53DNAMicroRNAsTP53 protein, humanTumor Suppressor Protein p53computational dockingfluorescence quenchingFRETmiR4749oncomiRp53

Identifiers

PMID32098369
PMCPMC7072324
OpenAlexW3008121881

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.