Evidence map›Paper›PMID 26839000›Full record

ArticleMolecular & cellular proteomics : MCP2016

Proteome Dynamics: Tissue Variation in the Kinetics of Proteostasis in Intact Animals.

Dean E Hammond, Amy J Claydon, Deborah M Simpson, Dominic Edward, Paula Stockley, Jane L Hurst, Robert J Beynon

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Muscle Proteome Dynamics.Advances in experimental medicine and biology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Revealing mechanisms of mating plug function under sexual selection.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Cross-species Comparison of Proteome Turnover Kinetics.Molecular & cellular proteomics : MCP · 2018
    Article
  15. Article
  16. Article
  17. Review
  18. Protein turnover measurement using selected reaction monitoring-mass spectrometry (SRM-MS).Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Article
  19. 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 1 institution in 1 country.

Dean E HammondFrom the ‡Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK;
Amy J ClaydonFrom the ‡Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK;
Deborah M SimpsonFrom the ‡Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK;
Dominic Edward§Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
Paula Stockley§Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
Jane L Hurst§Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, CH64 7TE, UK.
Robert J BeynonFrom the ‡Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Crown Street, L697ZB, UK; r.beynon@liverpool.ac.uk.ORCID http://orcid.org/0000-0003-0857-495X
University of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C007433/1
6 · The paper itself

Abstract

Understanding the role of protein turnover in the maintenance of proteostasis requires accurate measurements of the rates of replacement of proteins in complex systems, such as intact animals. Moreover, any investigation of allometric scaling of protein turnover is likely to include species for which fully annotated proteomes are not available. We have used dietary administration of stable isotope labeled lysine to assess protein turnover rates for proteins from four tissues in the bank vole,Myodes glareolus The annotated genome for this species is not available, so protein identification was attained through cross-species matching to the mouse. For proteins for which confident identifications were derived, the pattern of lysine incorporation over 40 days was used to define the rate of synthesis of individual proteins in the four tissues. The data were heavily filtered to retain a very high quality dataset of turnover rates for 1088 proteins. Comparative analysis of the four tissues revealed different median rates of degradation (kidney: 0.099 days(-1); liver 0.136 days(-1); heart, 0.054 days(-1), and skeletal muscle, 0.035 days(-1)). These data were compared with protein degradation rates from other studies on intact animals or from cells in culture and indicate that both cell type and analytical methodology may contribute to variance in turnover data between different studies. These differences were not only due to tissue-specific proteins but were reflected in gene products common to all tissues. All data are available via ProteomeXchange with identifier PXD002054.

Indexed as

AnimalsArvicolinaeIsotope LabelingKidneyKineticsLiverLysineMiceMuscle, SkeletalMyocardiumOrgan SpecificityProteolysisProteomeProteomicsTissue DistributionLysineProteome

Identifiers

PMID26839000
PMCPMC4824850
OpenAlexW2269976016

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.