Evidence map›Paper›PMID 35008565›Full record

ReviewInternational journal of molecular sciences2021

The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum.

Andrea Tirincsi, Mark Sicking, Drazena Hadzibeganovic, Sarah Haßdenteufel, Sven Lang

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. YeastbioRxiv : the preprint server for biology · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Loss of the endoplasmic reticulum protein Tmem208 affects cell polarity, development, and viability.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. COVID-19 Biogenesis and Intracellular Transport.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Mechanisms of ER Protein Import.International journal of molecular sciences · 2022
    Article
  15. Review
  16. 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

5 authors at 2 institutions in 2 countries.

Andrea TirincsiDepartment of Medical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Mark SickingDepartment of Medical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Drazena HadzibeganovicDepartment of Medical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.
Sarah HaßdenteufelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Sven LangDepartment of Medical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany.ORCID 0000-0003-1326-1851
Saarland University · DEWeizmann Institute of Science · IL

Funding

Deutsche Forschungsgemeinschaft IRTG 1830Deutsche Forschungsgemeinschaft SFB 894Saarland University Medical Center HOMFORexcellent programWeizmann Institute of Science FGS Excellence postdoc fellowship
6 · The paper itself

Abstract

Looking at the variety of the thousands of different polypeptides that have been focused on in the research on the endoplasmic reticulum from the last five decades taught us one humble lesson: no one size fits all. Cells use an impressive array of components to enable the safe transport of protein cargo from the cytosolic ribosomes to the endoplasmic reticulum. Safety during the transit is warranted by the interplay of cytosolic chaperones, membrane receptors, and protein translocases that together form functional networks and serve as protein targeting and translocation routes. While two targeting routes to the endoplasmic reticulum, SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins), prefer targeting determinants at the N- and C-terminus of the cargo polypeptide, respectively, the recently discovered SND (SRP-independent) route seems to preferentially cater for cargos with non-generic targeting signals that are less hydrophobic or more distant from the termini. With an emphasis on targeting routes and protein translocases, we will discuss those functional networks that drive efficient protein topogenesis and shed light on their redundant and dynamic nature in health and disease.

Indexed as

AnimalsCytosolEndoplasmic ReticulumHumansProteinsProtein Sorting SignalsProtein TransportSignal Recognition ParticleProteinsProtein Sorting SignalsSignal Recognition ParticleEMCendoplasmic reticulumGEThydrophobicitypositive-inside ruleprotein targetingprotein transportSec61 complexsignal peptideSNDSRPtransmembrane helix

Identifiers

PMID35008565
PMCPMC8745461
OpenAlexW4200471314

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.