Evidence map›Paper›PMID 31848225›Full record

ArticleThe Journal of biological chemistry2020

The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.

Christopher M Witham, Hasindu G Dassanayake, Aleshanee L Paxman, Kofi L P Stevens, Lamprini Baklous, Paris F White, Amy L Black, Robert F L Steuart, Colin J Stirling, Benjamin L Schulz and 1 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. 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
0.3field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Diverse Sphingolipid Species Harbor Different Effects on Ire1 Clustering.International journal of molecular sciences · 2022
    Article
  2. Article
  3. Article
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

11 authors at 3 institutions in 2 countries.

Christopher M WithamSchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia; Curtin Health Innovation Research Institute, Curtin University, Bentley, WA 6102, Australia.
Hasindu G DassanayakeSchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia.
Aleshanee L PaxmanSchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia.
Kofi L P StevensSchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia; Curtin Health Innovation Research Institute, Curtin University, Bentley, WA 6102, Australia.
Lamprini BaklousSchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia; Curtin Health Innovation Research Institute, Curtin University, Bentley, WA 6102, Australia.
Paris F WhiteSchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia.
Amy L BlackSchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia; Curtin Health Innovation Research Institute, Curtin University, Bentley, WA 6102, Australia.
Robert F L SteuartCurtin Health Innovation Research Institute, Curtin University, Bentley, WA 6102, Australia.
Colin J StirlingSchool of Biological Sciences, University of Manchester, Oxford Road, Manchester, M13 9PT, United Kingdom.
Benjamin L SchulzSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane St Lucia, QLD 4072, Australia.
Carl J MousleySchool of Pharmacy and Biomedical Sciences, Curtin University, Bentley, WA 6102, Australia; Curtin Health Innovation Research Institute, Curtin University, Bentley, WA 6102, Australia. Electronic address: Carl.Mousley@curtin.edu.au.
Curtin University · AUUniversity of Manchester · GBUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is the entry point to the secretory pathway and major site of protein biogenesis. Translocation of secretory and integral membrane proteins across or into the ER membrane occurs via the evolutionarily conserved Sec61 complex, a heterotrimeric channel that comprises the Sec61p/Sec61α, Sss1p/Sec61γ, and Sbh1p/Sec61β subunits. In addition to forming a protein-conducting channel, the Sec61 complex also functions to maintain the ER permeability barrier, preventing the mass free flow of essential ER-enriched molecules and ions. Loss in Sec61 integrity is detrimental and implicated in the progression of disease. The Sss1p/Sec61γ C terminus is juxtaposed to the key gating module of Sec61p/Sec61α, and we hypothesize it is important for gating the ER translocon. The ER stress response was found to be constitutively induced in two temperature-sensitive

Indexed as

Amino Acid SequenceEndoplasmic ReticulumEndoplasmic Reticulum StressMultiprotein ComplexesMutationPermeabilityProtein BiosynthesisProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsSEC61 protein, S cerevisiaeSEC Translocation ChannelsSSS1 protein, S cerevisiaeendoplasmic reticulum–associated protein degradation (ERAD)endoplasmic reticulum (ER)endoplasmic reticulum stress (ER stress)gatingSec61 complexSec61p/Sec61αSss1p/Sec61γtranslocationtranslocon gating

Identifiers

PMID31848225
PMCPMC7029116
OpenAlexW2996579785

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.