Evidence map›Paper›PMID 26443836›Full record

ArticlePathogens and disease2015

Different roles of the C-terminal end of Stx1A and Stx2A for AB5 complex integrity and retrograde transport of Stx in HeLa cells.

Linn Kymre, Roger Simm, Tore Skotland, Kirsten Sandvig

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

Article in Pathogens and disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

4 authors at 2 institutions in 1 country.

Linn KymreDepartment of Molecular Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, 0379 Oslo, Norway Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, 0379 Oslo, Norway.
Roger SimmDepartment of Molecular Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, 0379 Oslo, Norway Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, 0379 Oslo, Norway.
Tore SkotlandDepartment of Molecular Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, 0379 Oslo, Norway Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, 0379 Oslo, Norway.
Kirsten SandvigDepartment of Molecular Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, 0379 Oslo, Norway Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, 0379 Oslo, Norway Department of Biosciences, University of Oslo, 0316 Oslo, Norway ksandvig@ibv.uio.no.
Oslo University Hospital · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shiga toxin 1 (Stx1) and Shiga toxin 2 (Stx2) differ regarding receptor affinity, cellular toxicity and clinical outcome. To this date, it is not clarified in detail why the subtypes display these differences. Even though the crystal structures of Stx1 and Stx2 share overall similarities, significant differences were found in the C-terminal end of the A-subunits. The aim of this study was to investigate the role of the C-terminal end of the A-subunit in complex stability and retrograde transport by generating truncated mutants where 2, 4, 6 and 8 amino acids were removed from the C-terminal end of Stx1A and Stx2A. The results obtained show that removal of 6 or 8 amino acids from the Stx1A C-terminus abolishes the AB5 complex integrity, while removing up to 8 amino acids from Stx2A does not affect the complex in vivo (in the bacteria). We also present results showing different levels of A1-subunit in HeLa cells after exposure to Stx1, Stx2 and their truncated mutants.

Indexed as

Protein MultimerizationDNA Mutational AnalysisHeLa CellsHumansProtein SubunitsProtein TransportSequence DeletionShiga Toxin 1Shiga Toxin 2Protein SubunitsShiga Toxin 1Shiga Toxin 2A-subunitendocytosisretrograde transportShiga toxinStx1Stx2

Identifiers

PMID26443836
PMCPMC4626601
OpenAlexW2294899570

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.