Evidence map›Paper›PMID 32268488›Full record

ReviewInternational journal of molecular sciences2020

Translational Control of Secretory Proteins in Health and Disease.

Andrey L Karamyshev, Elena B Tikhonova, Zemfira N Karamysheva

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Human SRP Subunits Coordinate Protein Targeting and mRNA Quality Control.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Pathogenic signal peptide variants in the human genome.NAR genomics and bioinformatics · 2023
    Article
  12. Amyloid Precursor Protein and Alzheimer's Disease.International journal of molecular sciences · 2023
    Review
  13. Article
  14. Specialized Ribosomes in Health and Disease.International journal of molecular sciences · 2023
    Review
  15. Aberrant protein targeting activates quality control on the ribosome.Frontiers in cell and developmental biology · 2023
    Article
  16. Article
  17. Article
  18. Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022
    Review
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Andrey L KaramyshevDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Elena B TikhonovaDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Zemfira N KaramyshevaDepartment of Biological Sciences, Texas Tech University, Lubbock, TX 79409, USA.
Texas Tech University Health Sciences Center · USTexas Tech University · US

Funding

Regulation of Aberrant Protein ProductionR01GM135167 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI KARAMYSHEV, ANDREY L · 2019 to 2022
$1.3M
NIGMS NIH HHS R01 GM135167NIH HHS R01GM135167
6 · The paper itself

Abstract

Secretory proteins are synthesized in a form of precursors with additional sequences at their N-terminal ends called signal peptides. The signal peptides are recognized co-translationally by signal recognition particle (SRP). This interaction leads to targeting to the endoplasmic reticulum (ER) membrane and translocation of the nascent chains into the ER lumen. It was demonstrated recently that in addition to a targeting function, SRP has a novel role in protection of secretory protein mRNAs from degradation. It was also found that the quality of secretory proteins is controlled by the recently discovered Regulation of Aberrant Protein Production (RAPP) pathway. RAPP monitors interactions of polypeptide nascent chains during their synthesis on the ribosomes and specifically degrades their mRNAs if these interactions are abolished due to mutations in the nascent chains or defects in the targeting factor. It was demonstrated that pathological RAPP activation is one of the molecular mechanisms of human diseases associated with defects in the secretory proteins. In this review, we discuss recent progress in understanding of translational control of secretory protein biogenesis on the ribosome and pathological consequences of its dysregulation in human diseases.

Indexed as

Disease SusceptibilityGene Expression RegulationHomeostasisProtein BiosynthesisBiological TransportHumansMutationProtein Processing, Post-TranslationalRNA, MessengerRNA, Messengerdisease-causing mutationshuman diseasesprotein quality controlprotein synthesisprotein transportribosomeRNA degradationsignal recognition particle (SRP)signal sequencetranslation regulation

Identifiers

PMID32268488
PMCPMC7177344
OpenAlexW3014907486

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.