Evidence map›Paper›PMID 23042132›Full record

ArticleEukaryotic cell2012

Distribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation.

Simone Stork, Daniel Moog, Jude M Przyborski, Ilka Wilhelmi, Stefan Zauner, Uwe G Maier

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 71 citations in OpenAlex.

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  10. Genome assembly ofCommunications biology · 2019
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  12. Reduced vacuolar β-1,3-glucan synthesis affects carbohydrate metabolism as well as plastid homeostasis and structure inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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  17. The Potential for Microalgae as Bioreactors to Produce Pharmaceuticals.International journal of molecular sciences · 2016
    Review
  18. Article
  19. Article
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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

6 authors at 2 institutions in 1 country.

Simone StorkLaboratory for Cell Biology, Philipps-University Marburg, Marburg, Germany.
Daniel Moog
Jude M Przyborski
Ilka Wilhelmi
Stefan Zauner
Uwe G Maier
Philipps University of Marburg · DELoewe Center for Synthetic Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein import into complex plastids of red algal origin is a multistep process including translocons of different evolutionary origins. The symbiont-derived ERAD-like machinery (SELMA), shown to be of red algal origin, is proposed to be the transport system for preprotein import across the periplastidal membrane of heterokontophytes, haptophytes, cryptophytes, and apicomplexans. In contrast to the canonical endoplasmic reticulum-associated degradation (ERAD) system, SELMA translocation is suggested to be uncoupled from proteasomal degradation. We investigated the distribution of known and newly identified SELMA components in organisms with complex plastids of red algal origin by intensive data mining, thereby defining a set of core components present in all examined organisms. These include putative pore-forming components, a ubiquitylation machinery, as well as a Cdc48 complex. Furthermore, the set of known 20S proteasomal components in the periplastidal compartment (PPC) of diatoms was expanded. These newly identified putative SELMA components, as well as proteasomal subunits, were in vivo localized as PPC proteins in the diatom Phaeodactylum tricornutum. The presented data allow us to speculate about the specific features of SELMA translocation in contrast to the canonical ERAD system, especially the uncoupling of translocation from degradation.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceCell Cycle ProteinsDiatomsEndoplasmic Reticulum-Associated DegradationMolecular Sequence DataPlant ProteinsPlastidsProteasome Endopeptidase ComplexProtein Structure, TertiaryProtein TransportProteolysisRhodophytaUbiquitinValosin Containing ProteinAdenosine TriphosphatasesCell Cycle ProteinsPlant ProteinsProteasome Endopeptidase ComplexUbiquitinValosin Containing Protein

Identifiers

PMID23042132
PMCPMC3536273
OpenAlexW2149379180

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.