Evidence map›Paper›PMID 35011655›Full record

ArticleCells2021

The Role of p53 Protein in the Realization of the Exogenous Heat Shock Protein 70 Anti-Apoptotic Effect during Axotomy.

Svetlana V Demyanenko, Maria A Pitinova, Valentina A Dzreyan, Yuliya N Kalyuzhnaya, Moez A Eid, Andrey Y Abramov, Michael B Evgen'ev, David G Garbuz

Open access · goldAbstract read
In one paragraph

Article in Cells, 2021. 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
0.2field-weighted citation impact, top 46% 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, 4 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 3 institutions in 2 countries.

Svetlana V DemyanenkoLaboratory of Molecular Neurobiology, Academy of Biology and Biotechnology, Southern Federal University, 344090 Rostov-on-Don, Russia.ORCID 0000-0002-4245-0427
Maria A PitinovaLaboratory of Molecular Neurobiology, Academy of Biology and Biotechnology, Southern Federal University, 344090 Rostov-on-Don, Russia.
Valentina A DzreyanLaboratory of Molecular Neurobiology, Academy of Biology and Biotechnology, Southern Federal University, 344090 Rostov-on-Don, Russia.ORCID 0000-0003-3249-5020
Yuliya N KalyuzhnayaLaboratory of Molecular Neurobiology, Academy of Biology and Biotechnology, Southern Federal University, 344090 Rostov-on-Don, Russia.
Moez A EidLaboratory of Molecular Neurobiology, Academy of Biology and Biotechnology, Southern Federal University, 344090 Rostov-on-Don, Russia.
Andrey Y AbramovDepartment of Clinical and Movement Neurosciences, UCL Queen Square Institute of Neurology, Queen Square, London WC1N 3BG, UK.ORCID 0000-0002-7646-7235
Michael B Evgen'evEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
David G GarbuzEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
Southern Federal University · RUEngelhardt Institute of Molecular Biology · RUNational Hospital for Neurology and Neurosurgery · GB

Funding

Ministry of Education and Science of Russian Federation 13.2251.21.0080
6 · The paper itself

Abstract

The search for effective neuroprotective agents for the treatment of neurotrauma has always been of great interest to researchers around the world. Extracellular heat shock protein 70 (eHsp70) is considered a promising agent to study, as it has been demonstrated to exert a significant neuroprotective activity against various neurodegenerative diseases. We showed that eHsp70 can penetrate neurons and glial cells when added to the incubation medium, and can accumulate in the nuclei of neurons and satellite glial cells after axotomy. eHsp70 reduces apoptosis and necrosis of the glial cells, but not the neurons. At the same time, co-localization of eHsp70 with p53 protein, one of the key regulators of apoptosis, was noted. eHsp70 reduces the level of the p53 protein apoptosis promoter both in glial cells and in the nuclei and cytoplasm of neurons, which indicates its neuroprotective effect. The ability of eHsp70 to reverse the proapoptotic effect of the p53 activator WR1065 may indicate its ability to regulate p53 activity or its proteosome-dependent degradation.

Indexed as

ApoptosisAxotomyAnimalsAstacoideaDown-RegulationE2F1 Transcription FactorHSP70 Heat-Shock ProteinsHumansMechanoreceptorsMercaptoethylaminesNecrosisNeurogliaNeuronsProto-Oncogene Proteins c-mycRecombinant ProteinsTumor Suppressor Protein p53E2F1 Transcription FactorHSP70 Heat-Shock ProteinsMercaptoethylaminesN-(2-mercaptoethyl)-1,3-diaminopropaneProto-Oncogene Proteins c-mycRecombinant ProteinsTumor Suppressor Protein p53axotomyexogenous Hsp70neurotraumap53

Identifiers

PMID35011655
PMCPMC8750896
OpenAlexW4200149967

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.