Evidence map›Paper›PMID 33177718›Full record

ArticleNature2020

HSP40 proteins use class-specific regulation to drive HSP70 functional diversity.

Ofrah Faust, Meital Abayev-Avraham, Anne S Wentink, Michael Maurer, Nadinath B Nillegoda, Nir London, Bernd Bukau, Rina Rosenzweig

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

117 citing papers in PubMed, 240 citations in OpenAlex.

  1. Review
  2. Human Hsp70 paralogs display selective J-domain interactions tuning proteostasis under stress.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. DNAJB6: A guardian against neurodegeneration.Neural regeneration research · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  13. Article
  14. Origin of class B J-domain proteins involved in amyloid transactions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. DnaJB1 chaperone inhibits tau aggregation by recognizing its N-terminus.bioRxiv : the preprint server for biology · 2025
    Article

57 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

8 authors at 2 institutions in 3 countries.

Ofrah Faust *Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Meital Abayev-Avraham *Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Anne S WentinkCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-4420-2427
Michael MaurerDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Nadinath B NillegodaCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Nir LondonDepartment of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.
Bernd BukauCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany. bukau@zmbh.uni-heidelberg.de.ORCID http://orcid.org/0000-0003-0521-7199
Rina RosenzweigDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel. rina.rosenzweig@weizmann.ac.il.ORCID http://orcid.org/0000-0002-4019-5135
German Cancer Research Center · DEWeizmann Institute of Science · IL

Funding

European Research Council
6 · The paper itself

Abstract

The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular chaperones, which perform numerous cellular functions that affect almost all aspects of the protein life cycle from synthesis to degradation

Indexed as

alpha-SynucleinAmyloidBinding SitesGlycineHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesMutationPhenylalanineProtein AggregatesProtein Aggregation, PathologicalProtein BindingProtein DomainsSequence DeletionSubstrate Specificityalpha-SynucleinAmyloidDNAJB1 protein, humanGlycineHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPhenylalanineProtein Aggregates

Identifiers

PMID33177718
OpenAlexW3106456053

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.