Evidence map›Paper›PMID 27692063›Full record

ArticleeLife2016

ATPase activity of the DEAD-box protein Dhh1 controls processing body formation.

Christopher Frederick Mugler, Maria Hondele, Stephanie Heinrich, Ruchika Sachdev, Pascal Vallotton, Adriana Y Koek, Leon Y Chan, Karsten Weis

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

92 citing papers in PubMed, 154 citations in OpenAlex.

  1. Article
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  13. Review
  14. Roles of P-body factors inbioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

32 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

8 authors at 2 institutions in 2 countries.

Christopher Frederick MuglerUniversity of California, Berkeley, Berkeley, United States.ORCID 0000-0001-8258-1192
Maria HondeleETH Zurich, Zurich, Switzerland.
Stephanie HeinrichETH Zurich, Zurich, Switzerland.ORCID 0000-0003-1607-4525
Ruchika SachdevETH Zurich, Zurich, Switzerland.
Pascal VallottonETH Zurich, Zurich, Switzerland.
Adriana Y KoekUniversity of California, Berkeley, Berkeley, United States.
Leon Y ChanUniversity of California, Berkeley, Berkeley, United States.
Karsten WeisETH Zurich, Zurich, Switzerland.ORCID 0000-0001-7224-925X
ETH Zurich · CHUniversity of California, Berkeley · US

Funding

Structure and function of the nuclear pore complexR01GM058065 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI HEALD, REBECCA W · 1998 to 2015
$4.6M
Mechanisms of gene-specific and genome-wide regulation of mRNA turnoverR01GM101257 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 2013 to 2016
$1.2M
Spinning Disk Confocal Microscope for the University of California, BerkeleyS10RR027696 · NCRR · UNIVERSITY OF CALIFORNIA BERKELEY · PI WEIS, KARSTEN · 2010 to 2010
$498k
NCRR NIH HHS S10 RR027696NIGMS NIH HHS R01 GM058065NIGMS NIH HHS R01 GM101257
6 · The paper itself

Abstract

Translational repression and mRNA degradation are critical mechanisms of posttranscriptional gene regulation that help cells respond to internal and external cues. In response to certain stress conditions, many mRNA decay factors are enriched in processing bodies (PBs), cellular structures involved in degradation and/or storage of mRNAs. Yet, how cells regulate assembly and disassembly of PBs remains poorly understood. Here, we show that in budding yeast, mutations in the DEAD-box ATPase Dhh1 that prevent ATP hydrolysis, or that affect the interaction between Dhh1 and Not1, the central scaffold of the CCR4-NOT complex and an activator of the Dhh1 ATPase, prevent PB disassembly

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsDEAD-box RNA HelicasesMacromolecular SubstancesMutant ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine TriphosphatasesCDC39 protein, S cerevisiaeCell Cycle ProteinsDEAD-box RNA HelicasesDHH1 protein, S cerevisiaeMacromolecular SubstancesMutant ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsTranscription Factorsbiochemistrycell biologyDEAD box ATPasesprocessing bodiesRNA turnoverS. cerevisiae

Identifiers

PMID27692063
PMCPMC5096884
OpenAlexW2527809167

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.