Evidence map›Paper›PMID 23651853›Full record

ArticleGenes & development2013

Protein segregase meddles in remodeling of mRNA-protein complexes.

Chyi-Ying A Chen, Ann-Bin Shyu

Open access · diamondAbstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in Genes & development, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Emerging mechanisms of mRNP remodeling regulation.Wiley interdisciplinary reviews. RNA
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Chyi-Ying A ChenDepartment of Biochemistry and Molecular Biology, The University of Texas Medical School at Houston, Houston, Texas 77030, USA.
Ann-Bin Shyu

Funding

Messenger RNA Turnover in Mammalian CellsR01GM046454 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SHYU, ANN-BIN · 1991 to 2016
$7.1M
NIGMS NIH HHS R01 GM046454
6 · The paper itself

Abstract

Remodeling of RNA-protein complexes (mRNPs) plays a critical role in mRNA biogenesis and metabolism. However, relatively little is known about the underlying mechanism and regulation of the mRNP remodeling. In this issue of Genes & Development, Zhou and colleagues (pp. 1046-1058) report that a protein remodeling machine, the p97-UBXD8 complex, disassembles mRNPs containing the AU-rich elements (AREs) bound by HuR proteins in a nondegradative, ubiquitin signaling-dependent manner, revealing a novel mechanism to regulate mRNA turnover.

Indexed as

RNA StabilityAdenosine TriphosphatasesAnimalsBlood ProteinsELAV ProteinsHumansMembrane ProteinsNuclear ProteinsRibonucleoproteinsRNA, MessengerAdenosine TriphosphatasesBlood ProteinsELAV ProteinsFAF2 protein, humanMembrane Proteinsmessenger ribonucleoproteinNuclear Proteinsp97 ATPaseRibonucleoproteinsRNA, MessengerHuRmRNA stabilityubiquitin

Identifiers

PMID23651853
PMCPMC3656327
OpenAlexW2149482796

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.