Evidence map›Paper›PMID 31734893›Full record

ReviewCell stress & chaperones2019

Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes.

Dorota Scieglinska, Zdzisław Krawczyk, Damian Robert Sojka, Agnieszka Gogler-Pigłowska

Open access · hybridAbstract readReview
In one paragraph

Review in Cell stress & chaperones, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
6.2field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
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  15. Halotolerant bacterial endophyteFrontiers in plant science · 2024
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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.

Dorota ScieglinskaCenter for Translational Research and Molecular Biology of Cancer, Maria Skłodowska-Curie Institute-Oncology Center Gliwice Branch, ul. Wybrzeże Armii Krajowej 15, 44-101, Gliwice, Poland. dorota.scieglinska@io.gliwice.pl.ORCID https://orcid.org/0000-0003-3489-8464
Zdzisław KrawczykCenter for Translational Research and Molecular Biology of Cancer, Maria Skłodowska-Curie Institute-Oncology Center Gliwice Branch, ul. Wybrzeże Armii Krajowej 15, 44-101, Gliwice, Poland.
Damian Robert SojkaCenter for Translational Research and Molecular Biology of Cancer, Maria Skłodowska-Curie Institute-Oncology Center Gliwice Branch, ul. Wybrzeże Armii Krajowej 15, 44-101, Gliwice, Poland.
Agnieszka Gogler-PigłowskaCenter for Translational Research and Molecular Biology of Cancer, Maria Skłodowska-Curie Institute-Oncology Center Gliwice Branch, ul. Wybrzeże Armii Krajowej 15, 44-101, Gliwice, Poland.
The Maria Sklodowska-Curie National Research Institute of Oncology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes.

Indexed as

AnimalsCell LineEpidermisHeat-Shock ProteinsHumansKeratinocytesMiceRatsHeat-Shock ProteinsCytoprotectionEpidermal homeostasisEpidermisHeat shock proteinsKeratinocyte differentiationKeratinocytes

Identifiers

PMID31734893
PMCPMC6882751
OpenAlexW2989451198

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.