Evidence map›Paper›PMID 21736903›Full record

ReviewBiochimica et biophysica acta2012

ClpXP, an ATP-powered unfolding and protein-degradation machine.

Tania A Baker, Robert T Sauer

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 283 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
283citing papers in PubMed, 1 pooled it
–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

283 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
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  12. Review
  13. Article
  14. ClpP2 modulates ClpXP assembly to promote multiple pathogenic phenotypes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  15. Review
  16. Article
  17. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  18. Article
  19. Review
  20. Article

223 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

2 authors.

Tania A BakerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Robert T Sauer

Funding

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
VIRAL PROTEINS: STRUCTURE AND ASSEMBLY PATHWAYSR01AI015706 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 1985 to 2001
$693k
Howard Hughes Medical InstituteNIAID NIH HHS AI-15706NIAID NIH HHS AI-16892NIAID NIH HHS R01 AI015706NIAID NIH HHS R01 AI016892NIAID NIH HHS R37 AI015706NIGMS NIH HHS GM-499224NIGMS NIH HHS R01 GM101988
6 · The paper itself

Abstract

ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform mechanical work during targeted protein degradation within cells. ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP). Asymmetric ClpX hexamers bind unstructured peptide tags in protein substrates, unfold stable tertiary structure in the substrate, and then translocate the unfolded polypeptide chain into an internal proteolytic compartment in ClpP. Here, we review our present understanding of ClpXP structure and function, as revealed by two decades of biochemical and biophysical studies.

Indexed as

Protein UnfoldingProteolysisAdenosine TriphosphateAmino Acid MotifsCatalytic DomainEndopeptidase ClpEscherichia coli ProteinsHumansHydrolysisProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryAdenosine TriphosphateClpXP protease, E coliEndopeptidase ClpEscherichia coli Proteins

Identifiers

PMID21736903
PMCPMC3209554

What OpenQuestion holds

Textmetadata
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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.