Evidence map›Paper›PMID 29203718›Full record

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

DNAJ Proteins in neurodegeneration: essential and protective factors.

Christina Zarouchlioti, David A Parfitt, Wenwen Li, Lauren M Gittings, Michael E Cheetham

Open access · greenAbstract readReview
In one paragraph

Review 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 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
4.5field-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

85 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
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  5. A J-domain protein enhances memory by promoting physiological amyloid formation inProceedings of the National Academy of Sciences of the United States of America · 2026
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  20. Heat shock proteins in hypothermia: a review.Frontiers in molecular biosciences · 2025
    Review

25 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 4 countries.

Christina ZarouchliotiUCL Institute of Ophthalmology, 11-43 Bath Street, London EC1 V 9EL, UK.
David A ParfittUCL Institute of Ophthalmology, 11-43 Bath Street, London EC1 V 9EL, UK.
Wenwen LiUCL Institute of Ophthalmology, 11-43 Bath Street, London EC1 V 9EL, UK.
Lauren M GittingsUCL Institute of Ophthalmology, 11-43 Bath Street, London EC1 V 9EL, UK.
Michael E CheethamUCL Institute of Ophthalmology, 11-43 Bath Street, London EC1 V 9EL, UK michael.cheetham@ucl.ac.uk.ORCID http://orcid.org/0000-0001-6429-654X
Google (United States) · US

Funding

Medical Research Council MR/N004434/1Motor Neurone Disease Association CHEETHAM/OCT15/881-792Wellcome Trust 205041/Z/16/Z
6 · The paper itself

Abstract

Maintenance of protein homeostasis is vitally important in post-mitotic cells, particularly neurons. Neurodegenerative diseases such as polyglutamine expansion disorders-like Huntington's disease or spinocerebellar ataxia (SCA), Alzheimer's disease, fronto-temporal dementia (FTD), amyotrophic lateral sclerosis (ALS) and Parkinson's disease-are often characterized by the presence of inclusions of aggregated protein. Neurons contain complex protein networks dedicated to protein quality control and maintaining protein homeostasis, or proteostasis. Molecular chaperones are a class of proteins with prominent roles in maintaining proteostasis, which act to bind and shield hydrophobic regions of nascent or misfolded proteins while allowing correct folding, conformational changes and enabling quality control. There are many different families of molecular chaperones with multiple functions in proteostasis. The DNAJ family of molecular chaperones is the largest chaperone family and is defined by the J-domain, which regulates the function of HSP70 chaperones. DNAJ proteins can also have multiple other protein domains such as ubiquitin-interacting motifs or clathrin-binding domains leading to diverse and specific roles in the cell, including targeting client proteins for degradation via the proteasome, chaperone-mediated autophagy and uncoating clathrin-coated vesicles. DNAJ proteins can also contain ER-signal peptides or mitochondrial leader sequences, targeting them to specific organelles in the cell. In this review, we discuss the multiple roles of DNAJ proteins and in particular focus on the role of DNAJ proteins in protecting against neurodegenerative diseases caused by misfolded proteins. We also discuss the role of DNAJ proteins as direct causes of inherited neurodegeneration via mutations in

Indexed as

AnimalsFetal ProteinsHSP40 Heat-Shock ProteinsHumansMiceMolecular ChaperonesNeurodegenerative DiseasesProtein FoldingRatsDNAJC14 protein, humanFetal ProteinsHSP40 Heat-Shock ProteinsMolecular ChaperonesDNAJmolecular chaperonesneurodegeneration

Identifiers

PMID29203718
PMCPMC5717533
OpenAlexW2774357023

What OpenQuestion holds

Textmetadata
LicenceTDM
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.