Evidence map›Paper›PMID 29203706›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018

Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective.

Adrienne L Edkins, John T Price, A Graham Pockley, Gregory L Blatch

Open access · bronzeAbstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 67 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  12. Genetic profiling ofBrazilian journal of veterinary medicine · 2022
    Article
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  19. Article
  20. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    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 3 institutions in 3 countries.

Adrienne L EdkinsBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South Africa.ORCID http://orcid.org/0000-0002-3615-6651
John T PriceCentre for Chronic Disease, College of Health and Biomedicine, Victoria University, St Albans, Victoria, Australia.ORCID http://orcid.org/0000-0002-8244-1023
A Graham PockleyJohn van Geest Cancer Research Centre, Nottingham Trent University, Clifton Campus, Clifton Lane, Nottingham, UK.ORCID http://orcid.org/0000-0001-9593-6431
Gregory L BlatchBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South Africa greg.blatch@nd.edu.au g.blatch@ru.ac.za.ORCID http://orcid.org/0000-0003-0778-8577
Rhodes University · ZANottingham Trent University · GBThe University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many heat shock proteins (HSPs) are essential to survival as a consequence of their role as molecular chaperones, and play a critical role in maintaining cellular proteostasis by integrating the fundamental processes of protein folding and degradation. HSPs are arguably among the most prominent classes of proteins that have been broadly linked to many human disorders, with changes in their expression profile and/or intracellular/extracellular location now being described as contributing to the pathogenesis of a number of different diseases. Although the concept was initially controversial, it is now widely accepted that HSPs have additional biological functions over and above their role in proteostasis (so-called 'protein moonlighting'). Most importantly, these new insights are enlightening our understanding of biological processes in health and disease, and revealing novel and exciting therapeutic opportunities. This theme issue draws on therapeutic insights from established research on HSPs in cancer and other non-communicable disorders, with an emphasis on how the intracellular function of HSPs contrasts with their extracellular properties and function, and interrogates their potential diagnostic and therapeutic value to the prevention, management and treatment of chronic diseases.This article is part of the theme issue 'Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective'.

Indexed as

Chronic DiseaseHeat-Shock ProteinsNeoplasmsWit and Humor as TopicHeat-Shock Proteinscancerchronic diseaseco-chaperonesextracellular and intracellular proteinsmolecular chaperonesprotein moonlighting

Identifiers

PMID29203706
PMCPMC5717521
OpenAlexW2772907481

What OpenQuestion holds

Textmetadata
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.