Evidence map›Paper›PMID 24243009›Full record

ArticleCell2013

ClpX shifts into high gear to unfold stable proteins.

Michael R Maurizi, George Stan

Abstract readComment
PubMed Publisher
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–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

3 citing papers in PubMed.

  1. Article
  2. Effects of a Mutation in theFrontiers in molecular biosciences · 2016
    Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Michael R MauriziLaboratory of Cell Biology, National Cancer Institute, Bethesda, MD 20892, USA. Electronic address: mmaurizi@helix.nih.gov.
George Stan

Funding

Biochemistry of Energy-Dependent (Intracellular) Protein DegradationZIABC005597 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MAURIZI, MICHAEL · 2009 to 2017
$7.1M
Intramural NIH HHS
6 · The paper itself

Abstract

Protein degradation by the ClpXP protease requires collaboration among the six AAA+ domains of ClpX. Using single-molecule optical tweezers, Sen et al. show that ClpX uses a coordinated succession of power strokes to translocate polypeptides in ATP-tunable bursts before reloading with nucleotide. This strategy allows ClpX to kinetically capture transiently unfolded intermediates.

Indexed as

Endopeptidase ClpEscherichia coliEscherichia coli ProteinsClpXP protease, E coliEndopeptidase ClpEscherichia coli Proteins

Identifiers

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.