Evidence map›Paper›PMID 30478692›Full record

ArticleCell stress & chaperones2019

Function, evolution, and structure of J-domain proteins.

Harm H Kampinga, Claes Andreasson, Alessandro Barducci, Michael E Cheetham, Douglas Cyr, Cecilia Emanuelsson, Pierre Genevaux, Jason E Gestwicki, Pierre Goloubinoff, Jaime Huerta-Cepas and 20 more

Abstract readConference Proceedings
In one paragraph

Article 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 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
–field-weighted citation impact
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

99 citing papers in PubMed.

  1. Trial
  2. Chaperone-mediated remodelling of mutant huntingtin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026
    Review
  9. 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
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Unlocking Disease-Modifying Treatments for TDP-43-Mediated Neurodegeneration.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  20. Article

39 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

30 authors.

Harm H KampingaDepartment of Cell Biology, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands. h.h.kampinga@umcg.nl.
Claes AndreassonDepartment of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, SE-106 91, Stockholm, Sweden.
Alessandro BarducciInserm, U1054, CNRS, UMR 5048, Centre de Biochimie Structurale, Universite de Montpellier, Montpellier, France.
Michael E CheethamUCL Institute of Ophthalmology, London, UK.
Douglas CyrUniversity of North Carolina, Chapel Hill, NC, USA.
Cecilia EmanuelssonCenter for Molecular Protein Sciences, CMPS, Dept. Biochemistry and Structural Biology, Lund University, Lund, Sweden.
Pierre GenevauxLaboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), CNRS-Université de Toulouse, 118 route de Narbonne, 31062, Toulouse Cedex 9, France.
Jason E GestwickiInstitute for Neurodegenerative Diseases, University of California, San Francisco, CA, USA.
Pierre GoloubinoffDepartment of Plant Molecular Biology, University of Lausanne, Lausanne, Switzerland.
Jaime Huerta-CepasEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Janine KirsteinLeibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany.
Krzysztof LiberekIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307, Gdansk, Poland.
Matthias P MayerCenter for Molecular Biology of Heidelberg University (ZMBH), Heidelberg, Germany.
Kazuhiro NagataDepartment of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, 603-8555, Japan.
Nadinath B NillegodaCenter for Molecular Biology of Heidelberg University (ZMBH), Heidelberg, Germany.
Pablo PulidoPlant Molecular Biology, Faculty of Biology, Ludwig-Maximilians-University, Planegg-Martinsried, 82152, Munich, Germany.
Carlos RamosInstitute of Chemistry, University of Campinas UNICAMP, Campinas, SP, Brazil.
Paolo De Los RiosEPFL SB IPHYS LBS BSP 723 (Cubotron UNIL), Rte de la Sorge, CH-1015, Lausanne, Switzerland.
Sabine RospertInstitut fur Biochemie und Molekularbiologie, Universitat Freiburg, Freiburg, Germany.
Rina RosenzweigWeizmann Institute of Science, Rehovot, Israel.
Chandan SahiIndian Institute of Science Education and Research Bhopal, Bhauri Bhopal, Madhya Pradesh, 462 066, India.
Mikko TaipaleDonnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, Toronto, Canada.
Bratłomiej TomiczekIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307, Gdansk, Poland.
Ryo UshiodaDepartment of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, 603-8555, Japan.
Jason C YoungDepartment of Biochemistry, McGill University, Montreal, Canada.
Richard ZimmermannMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
Alicja ZyliczInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Maciej ZyliczInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Elizabeth A CraigDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.
Jaroslaw MarszalekIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307, Gdansk, Poland.

Funding

Roles for Hsp70 and Hsp40 in Membrane Protein TriageR01GM056981 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CYR, DOUGLAS M · 1998 to 2019
$6.1M
Medical Research Council MR/N004434/1Motor Neurone Disease Association CHEETHAM/OCT15/881-792NIGMS NIH HHS R01 GM056981
6 · The paper itself

Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Indexed as

Evolution, MolecularAnimalsDiseaseHSP70 Heat-Shock ProteinsHumansProtein AggregatesProtein DomainsProtein RefoldingHSP70 Heat-Shock ProteinsProtein Aggregates8-stranded β-sandwich domain (SBDβ)Heat shock protein 70 (Hsp70)J-domain proteins (JDPs)

Identifiers

PMID30478692
PMCPMC6363617

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.