Evidence map›Paper›PMID 32108573›Full record

ArticleeLife2020

Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate.

Xue Fei, Tristan A Bell, Simon Jenni, Benjamin M Stinson, Tania A Baker, Stephen C Harrison, Robert T Sauer

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
18.7field-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

96 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Subunit specialization in AAA+ proteins and substrate unfolding during transcription complex remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Xue FeiDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Tristan A BellDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.ORCID 0000-0002-3668-8412
Simon JenniDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, United States.
Benjamin M StinsonDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Tania A BakerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.ORCID 0000-0002-0737-3411
Stephen C HarrisonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, United States.ORCID 0000-0001-7215-9393
Robert T SauerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.ORCID 0000-0002-1719-5399
Massachusetts Institute of Technology · USBoston University · USHoward Hughes Medical Institute · US

Funding

PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
Sequence Determinants of Protein Structure and StabilityR01GM101988 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2012 to 2019
$3.5M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM101988NIGMS NIH HHS T32 GM007287NIH HHS 5T32GM007287
6 · The paper itself

Abstract

ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the

Indexed as

Adenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesEndopeptidase ClpEscherichia coliEscherichia coli ProteinsProtein ConformationProteolysisSubstrate SpecificityAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesClpXP protease, E coliEndopeptidase ClpEscherichia coli ProteinsAAA+ proteaseE. colimolecular biophysicsprotein translocationprotein unfoldingstructural biology

Identifiers

PMID32108573
PMCPMC7112951
OpenAlexW3008938277

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.