Evidence map›Paper›PMID 24911415›Full record

ArticlePloS one2014

Most human proteins made in both nucleus and cytoplasm turn over within minutes.

Sabyasachi Baboo, Bhaskar Bhushan, Haibo Jiang, Chris R M Grovenor, Philippe Pierre, Benjamin G Davis, Peter R Cook

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Small ORFs as New Regulators of Pri-miRNAs and miRNAs Expression inInternational journal of molecular sciences · 2022
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. NanoSIMS imaging: an approach for visualizing and quantifying lipids in cells and tissues.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2017
    Review
  11. Review
  12. Article
  13. Multidimensional proteomics for cell biology.Nature reviews. Molecular cell biology · 2015
    Review
  14. Article
  15. 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

7 authors at 2 institutions in 2 countries.

Sabyasachi BabooSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Bhaskar BhushanChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, United Kingdom.
Haibo JiangDepartment of Materials, University of Oxford, Oxford, United Kingdom.
Chris R M GrovenorDepartment of Materials, University of Oxford, Oxford, United Kingdom.
Philippe PierreCentre d'Immunologie de Marseille-Luminy, Aix-Marseille Université, Marseille, France; Institut National de la Santé et de la Recherche Médicale, U1104, Marseille, France; Centre National de la Recherche Scientifique, Unités Mixtes de Recherche 7280, Marseille, France.
Benjamin G DavisChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, United Kingdom.
Peter R CookSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
University of Oxford · GBInserm · FR

Funding

Biotechnology and Biological Sciences Research Council BB/E004350/1Biotechnology and Biological Sciences Research Council EGA17763Wellcome Trust 091911
6 · The paper itself

Abstract

In bacteria, protein synthesis can be coupled to transcription, but in eukaryotes it is believed to occur solely in the cytoplasm. Using pulses as short as 5 s, we find that three analogues--L-azidohomoalanine, puromycin (detected after attaching fluors using 'click' chemistry or immuno-labeling), and amino acids tagged with 'heavy' 15N and 13C (detected using secondary ion mass spectrometry)--are incorporated into the nucleus and cytoplasm in a process sensitive to translational inhibitors. The nuclear incorporation represents a significant fraction of the total, and labels in both compartments have half-lives of less than a minute; results are consistent with most newly-made peptides being destroyed soon after they are made. As nascent RNA bearing a premature termination codon (detected by fluorescence in situ hybridization) is also eliminated by a mechanism sensitive to a translational inhibitor, the nuclear turnover of peptides is probably a by-product of proof-reading the RNA for stop codons (a process known as nonsense-mediated decay). We speculate that the apparently-wasteful turnover of this previously-hidden ('dark-matter') world of peptide is involved in regulating protein production.

Indexed as

Amino AcidsAnimalsCell LineCell NucleusCytoplasmHumansNonsense Mediated mRNA DecayPeptidesProtein BiosynthesisProteinsProtein TransportPuromycinRibosomesRNA, MessengerTime FactorsAmino AcidsPeptidesProteinsPuromycinRNA, Messenger

Identifiers

PMID24911415
PMCPMC4050049
OpenAlexW2154809063

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.