Evidence map›Paper›PMID 34625496›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Selective promiscuity in the binding of

Eugenia M Clerico, Alexandra K Pozhidaeva, Rachel M Jansen, Can Özden, Joseph M Tilitsky, Lila M Gierasch

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. HSP70-binding motifs function as protein quality control degrons.Cellular and molecular life sciences : CMLS · 2023
    Article
  15. Review
  16. Conformational dynamics of the Hsp70 chaperone throughout key steps of its ATPase cycle.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Article
  19. Review
  20. Review
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

6 authors at 1 institution in 1 country.

Eugenia M ClericoDepartment of Biochemistry & Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003.ORCID 0000-0002-4433-8842
Alexandra K PozhidaevaDepartment of Biochemistry & Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003.ORCID 0000-0001-8602-1790
Rachel M JansenDepartment of Biochemistry & Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003.ORCID 0000-0003-4666-9976
Can ÖzdenDepartment of Biochemistry & Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003.ORCID 0000-0002-5673-878X
Joseph M TilitskyDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003.ORCID 0000-0001-8555-398X
Lila M GieraschDepartment of Biochemistry & Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003; gierasch@biochem.umass.edu.ORCID 0000-0002-5706-115X
University of Massachusetts Amherst · US

Funding

Protein folding in the cell: Challenges and coping mechanisms Administrative Supplement for Equipment PurchaseR35GM118161 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2016 to 2025
$5.5M
NIGMS NIH HHS R35 GM118161
6 · The paper itself

Abstract

Heat shock protein 70 (Hsp70) chaperones bind many different sequences and discriminate between incompletely folded and folded clients. Most research into the origins of this "selective promiscuity" has relied on short peptides as substrates to dissect the binding, but much less is known about how Hsp70s bind full-length client proteins. Here, we connect detailed structural analyses of complexes between the

Indexed as

Alkaline PhosphataseBinding SitesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsModels, MolecularMolecular ChaperonesProtein BindingProtein DomainsProtein FoldingAlkaline PhosphatasednaK protein, E coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonescrystallographyDnaKHsp70 molecular chaperoneNMRsubstrate binding

Identifiers

PMID34625496
PMCPMC8521663
OpenAlexW3201946800

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.