Evidence map›Paper›PMID 34923891›Full record

ReviewCritical reviews in biochemistry and molecular biology2022

Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis.

Robert T Sauer, Xue Fei, Tristan A Bell, Tania A Baker

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
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  8. Article
  9. 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
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Protein degradation by a component of the chaperonin-linked protease ClpP.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Review
  20. Article
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

4 authors at 1 institution in 1 country.

Robert T SauerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0002-1719-5399
Xue FeiDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Tristan A BellDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Tania A BakerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Massachusetts Institute of Technology · 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
REPRESSOR &ANTIREPRESSOR PROTEINS OF BACTERIOPHAGER01AI016892 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BAKER, TANIA A, SAUER, ROBERT T · 1985 to 2022
$13.0M
Sequence Determinants of Protein Structure and StabilityR37AI015706 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2002 to 2011
$4.7M
Sequence Determinants of Protein Structure and StabilityR01GM101988 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2012 to 2019
$3.5M
Macromolecular interactions controlling the ALA synthases, keystone enzymes that initiate heme biosynthesisR01DK115558 · NIDDK · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BAKER, TANIA A · 2017 to 2021
$2.1M
Structure and function of ClpXPR35GM141517 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2021 to 2024
$1.5M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI016892NIAID NIH HHS R37 AI015706NIDDK NIH HHS R01 DK115558NIGMS NIH HHS R01 GM101988NIGMS NIH HHS R35 GM141517NIGMS NIH HHS T32 GM007287
6 · The paper itself

Abstract

ClpXP is an archetypical AAA+ protease, consisting of ClpX and ClpP. ClpX is an ATP-dependent protein unfoldase and polypeptide translocase, whereas ClpP is a self-compartmentalized peptidase. ClpXP is currently the only AAA+ protease for which high-resolution structures exist, the molecular basis of recognition for a protein substrate is understood, extensive biochemical and genetic analysis have been performed, and single-molecule optical trapping has allowed direct visualization of the kinetics of substrate unfolding and translocation. In this review, we discuss our current understanding of ClpXP structure and function, evaluate competing sequential and probabilistic mechanisms of ATP hydrolysis, and highlight open questions for future exploration.

Indexed as

Adenosine TriphosphateEndopeptidase ClpATPases Associated with Diverse Cellular ActivitiesHydrolysisPeptide HydrolasesAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesEndopeptidase ClpPeptide HydrolasesAAA+ proteasesATP hydrolysisClpPClpXcryo-EMmolecular machineprotein degradation

Identifiers

PMID34923891
PMCPMC9871882
OpenAlexW4200084001

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.