Evidence map›Paper›PMID 29985129›Full record

ArticleeLife2018

Engineering ER-stress dependent non-conventional mRNA splicing.

Weihan Li, Voytek Okreglak, Jirka Peschek, Philipp Kimmig, Meghan Zubradt, Jonathan S Weissman, Peter Walter

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Evolutionary Aspects of the Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. Translation Control ofInternational journal of molecular sciences · 2019
    Review
  10. Article
  11. Review
  12. Article
  13. Review
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

7 authors at 1 institution in 1 country.

Weihan LiDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.ORCID 0000-0003-4718-1884
Voytek OkreglakDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
Jirka PeschekDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.ORCID 0000-0001-8158-9301
Philipp KimmigDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
Meghan ZubradtHoward Hughes Medical Institute, San Francisco, United States.
Jonathan S WeissmanHoward Hughes Medical Institute, San Francisco, United States.ORCID 0000-0003-2445-670X
Peter WalterDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.ORCID 0000-0002-6849-708X
Howard Hughes Medical Institute · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins. The ER membrane-resident kinase/RNase Ire1 maintains ER protein homeostasis through two fundamentally distinct processes. First, Ire1 can initiate a transcriptional response through a non-conventional mRNA splicing reaction to increase the ER folding capacity. Second, Ire1 can decrease the ER folding burden through selective mRNA decay. In

Indexed as

Genetic EngineeringAmino Acid SequenceBase SequenceEndoplasmic Reticulum StressMembrane GlycoproteinsNucleic Acid ConformationProtein DomainsProtein MultimerizationProtein Serine-Threonine KinasesRibonucleasesRNA, MessengerRNA SplicingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsIRE1 protein, S cerevisiaeMembrane GlycoproteinsProtein Serine-Threonine KinasesRibonucleasesRNA, MessengerSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteinsbiochemistrycell biologychemical biologyevolutionary biologynon-conventional mRNA splicingRNA processingS. cerevisiaeS. pombeunfolded protein response

Identifiers

PMID29985129
PMCPMC6037481
OpenAlexW2878758614

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.