Evidence map›Paper›PMID 23442924›Full record

ArticleBiophysical journal2013

Highly abundant proteins favor more stable 3D structures in yeast.

Adrian W R Serohijos, S Y Ryan Lee, Eugene I Shakhnovich

Abstract readLetter
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Highly Abundant Proteins Are Highly Thermostable.Genome biology and evolution · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. How Do Cells Adapt? Stories Told in Landscapes.Annual review of chemical and biomolecular engineering · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Protein evolution speed depends on its stability and abundance and on chaperone concentrations.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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.

Adrian W R Serohijos
S Y Ryan Lee
Eugene I Shakhnovich

Funding

Study of Biological Evolution of Structure and Function in ProteinsR01GM068670 · NIGMS · HARVARD UNIVERSITY · PI SHAKHNOVICH, EUGENE I · 2004 to 2020
$7.0M
NIGMS NIH HHS R01 GM068670
6 · The paper itself

Abstract

To understand the variation of protein sequences in nature, we need to reckon with evolutionary constraints that are biophysical, cellular, and ecological. Here, we show that under the global selection against protein misfolding, there exists a scaling among protein folding stability, protein cellular abundance, and effective population size. The specific scaling implies that the several-orders-of-magnitude range of protein abundances in the cell should leave imprints on extant protein structures, a prediction that is supported by our structural analysis of the yeast proteome.

Indexed as

Protein ConformationProtein StabilityEvolution, MolecularModels, StatisticalProtein FoldingProteinsYeastsProteins

Identifiers

PMID23442924
PMCPMC3566449

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.