Evidence map›Paper›PMID 31238511›Full record

ArticleInternational journal of molecular sciences2019

Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin.

Sara Signorelli, Salvatore Cannistraro, Anna Rita Bizzarri

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Macromolecular Interactions of Disordered Proteins.International journal of molecular sciences · 2020
    Article
  9. 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

3 authors at 1 institution in 1 country.

Sara SignorelliBiophysics & Nanoscience Centre, DEB, Università della Tuscia, 01100 Viterbo, Italy. signorellis@unitus.it.
Salvatore CannistraroBiophysics & Nanoscience Centre, DEB, Università della Tuscia, 01100 Viterbo, Italy. cannistr@unitus.it.ORCID 0000-0002-0228-7311
Anna Rita BizzarriBiophysics & Nanoscience Centre, DEB, Università della Tuscia, 01100 Viterbo, Italy. bizzarri@unitus.it.
Università degli Studi della Tuscia · IT

Funding

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

Abstract

Raman spectroscopy, which is a suitable tool to elucidate the structural properties of intrinsically disordered proteins, was applied to investigate the changes in both the structure and the conformational heterogeneity of the DNA-binding domain (DBD) belonging to the intrinsically disordered protein p53 upon its binding to Azurin, an electron-transfer anticancer protein from

Indexed as

Protein Interaction Domains and MotifsSpectrum Analysis, RamanAzurinBinding SitesDNAHumansModels, MolecularMolecular ConformationProtein BindingTumor Suppressor Protein p53AzurinDNATumor Suppressor Protein p53Amide I band deconvolutionblue copper protein Azurinintrinsically disordered proteinp53principal component analysisprotein–protein interactionRaman spectroscopy

Identifiers

PMID31238511
PMCPMC6627904
OpenAlexW2950312622

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.