Evidence map›Paper›PMID 12147708›Full record

ReviewMolecular pathology : MP2002

Chaperonins in disease: mechanisms, models, and treatments.

J C Ranford, B Henderson

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular pathology : MP, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

27 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Antibodies to Heat Shock Proteins 90α and 90β in Psoriasis.Archivum immunologiae et therapiae experimentalis · 2020
    Article
  6. Article
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  8. Expression of Heat Shock Protein 27 in Benign Prostatic Hyperplasia with Chronic Inflammation.Medical science monitor : international medical journal of experimental and clinical research · 2015
    Article
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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

2 authors at 2 institutions in 1 country.

J C RanfordCellular Microbiology Research Group, Eastman Dental Institute, University College London, 256 Gray's Inn Road, London WC1X 8LD, UK.
B Henderson
Eastman Dental Hospital · GBUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chaperonins are oligomeric proteins that assist in the folding of nascent or denatured proteins. Bacterial chaperonins are strongly immunogenic and can cause tissue pathology. They have been implicated in infection, autoimmune disease, and idiopathic or multifactorial diseases, such as arthritis and atherosclerosis. Chaperonin 60 proteins are also involved in prion diseases. In the past few years, much progress has been made in unravelling the involvement of various bacterial and mammalian chaperonin 60 (Cpn 60 or hsp 60) proteins in such diseases, and in proposing mechanisms for their biological actions, although we are still some way from a full understanding of chaperonin action that might lead to immunotherapeutic approaches. This review focuses on the current knowledge of the roles of Cpn 60 in the pathology of infectious and immune diseases, and discusses models for the actions of this molecule. Some potential therapeutic strategies will also be reviewed.

Indexed as

Autoimmune DiseasesBone ResorptionChaperonin 60HumansImmunotherapyModels, ImmunologicalPrion DiseasesChaperonin 60

Identifiers

PMID12147708
PMCPMC1187180
OpenAlexW2107140071

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.