Chance, destiny, and the inner workings of ClpXP.

Rick Russell, Andreas Matouschek

Abstract readComment

In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.Cell · 2015
Article

4 · The record

Corrections and comments

Comment on
Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine.2014

5 · Who and what money

Authors and funding

2 authors.

Rick RussellDepartment of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: rick_russell@cm.utexas.edu.

Andreas MatouschekDepartment of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: matouschek@austin.utexas.edu.

Funding

Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017

$3.7M

Physical and functional probing of DEAD-box proteins as general RNA chaperonesR01GM070456 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI RUSSELL, RICK · 2004 to 2017

$3.6M

NIGMS NIH HHS R01 GM070456NIGMS NIH HHS U54 GM105816

6 · The paper itself

Abstract

AAA+ proteases are responsible for protein degradation in all branches of life. Using single-molecule and ensemble assays, Cordova et al. investigate how the bacterial protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic model that recapitulates the interplay between stochastic and deterministic behaviors of ClpXP.

Indexed as

Endopeptidase ClpClpP protein, humanCLPX protein, humanEndopeptidase Clp

Identifiers

PMID25083864

DOI10.1016/j.cell.2014.07.009

PMCPMC4945115

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.