Evidence map›Paper›PMID 28765280›Full record

ArticleThe Journal of biological chemistry2017

The exocyst subunit Sec3 is regulated by a protein quality control pathway.

Caroline Kampmeyer, Antonina Karakostova, Signe M Schenstrøm, Amanda B Abildgaard, Anne-Marie Lauridsen, Isabelle Jourdain, Rasmus Hartmann-Petersen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

6 citing papers in PubMed, 22 citations in OpenAlex.

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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 2 institutions in 2 countries.

Caroline KampmeyerFrom the Linderstrøm-Lang Center, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark and.
Antonina KarakostovaFrom the Linderstrøm-Lang Center, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark and.
Signe M SchenstrømFrom the Linderstrøm-Lang Center, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark and.
Amanda B AbildgaardFrom the Linderstrøm-Lang Center, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark and.
Anne-Marie LauridsenFrom the Linderstrøm-Lang Center, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark and.
Isabelle Jourdainthe College of Life and Environmental Sciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter EX4 4QD, United Kingdom i.jourdain@exeter.ac.uk.ORCID 0000-0002-5306-0723
Rasmus Hartmann-PetersenFrom the Linderstrøm-Lang Center, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark and rhpetersen@bio.ku.dk.ORCID 0000-0002-4155-7791
University of Copenhagen · DKUniversity of Exeter · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Exocytosis involves fusion of secretory vesicles with the plasma membrane, thereby delivering membrane proteins to the cell surface and releasing material into the extracellular space. The tethering of the secretory vesicles before membrane fusion is mediated by the exocyst, an essential phylogenetically conserved octameric protein complex. Exocyst biogenesis is regulated by several processes, but the mechanisms by which the exocyst is degraded are unknown. Here, to unravel the components of the exocyst degradation pathway, we screened for extragenic suppressors of a temperature-sensitive fission yeast strain mutated in the exocyst subunit Sec3 (

Indexed as

Models, BiologicalDeubiquitinating EnzymesEndocytosisEndopeptidasesEnzyme InhibitorsExocytosisGene DeletionHSP70 Heat-Shock ProteinsMicroscopy, Electron, TransmissionMutationProteasome Endopeptidase ComplexProtein StabilityProteolysisRecombinant Fusion ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsDeubiquitinating EnzymesEndopeptidasesEnzyme InhibitorsHSP70 Heat-Shock ProteinsProteasome Endopeptidase ComplexRecombinant Fusion Proteinsrpt2 protein, S pombeSchizosaccharomyces pombe ProteinsSec3 protein, S pombesks2 protein, S pombeUbiquitin-Protein LigasesVesicular Transport Proteinschaperoneexocytosisproteasomeprotein foldingubiquitin

Identifiers

PMID28765280
PMCPMC5602385
OpenAlexW2741381748

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.