Evidence map›Paper›PMID 15150418›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Global analysis of predicted proteomes: functional adaptation of physical properties.

Christopher G Knight, Rees Kassen, Holger Hebestreit, Paul B Rainey

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-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

38 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Physicochemical classification of organisms.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Virtual 2-D map of the fungal proteome.Scientific reports · 2021
    Article
  4. Protein pI and Intracellular Localization.Frontiers in molecular biosciences · 2021
    Review
  5. Article
  6. Article
  7. Misprediction of Structural Disorder in Halophiles.Molecules (Basel, Switzerland) · 2019
    Article
  8. Marginal protein stability drives subcellular proteome isoelectric point.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Local and global anatomy of antibody-protein antigen recognition.Journal of molecular recognition : JMR · 2018
    Article
  10. Bioinformation · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Function-valued traits in evolution.Journal of the Royal Society, Interface · 2013
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Christopher G KnightDepartment of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom. christopher.knight@plants.ox.ac.uk
Rees Kassen
Holger Hebestreit
Paul B Rainey
University of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The physical characteristics of proteins are fundamentally important in organismal function. We used the complete predicted proteomes of >100 organisms spanning the three domains of life to investigate the comparative biology and evolution of proteomes. Theoretical 2D gels were constructed with axes of protein mass and charge (pI) and converted to density estimates comparable across all types and sizes of proteome. We asked whether we could detect general patterns of proteome conservation and variation. The overall pattern of theoretical 2D gels was strongly conserved across all life forms. Nevertheless, coevolved replicons from the same organism (different chromosomes or plasmid and host chromosomes) encode proteomes more similar to each other than those from different organisms. Furthermore, there was disparity between the membrane and nonmembrane subproteomes within organisms (proteins of membrane proteomes are on the average more basic and heavier) and their variation across organisms, suggesting that membrane proteomes evolve most rapidly. Experimentally, a significant positive relationship independent of phylogeny was found between the predicted proteome and Biolog profile, a measure associated with the ecological niche. Finally, we show that, for the smallest and most alkaline proteomes, there is a negative relationship between proteome size and basicity. This relationship is not adequately explained by AT bias at the DNA sequence level. Together, these data provide evidence of functional adaptation in the properties of complete proteomes.

Indexed as

Evolution, MolecularAnimalsArchaeal ProteinsBacterial ProteinsElectrophoresis, Gel, Two-DimensionalFungal ProteinsMembrane ProteinsModels, TheoreticalProteomeStatistics as TopicArchaeal ProteinsBacterial ProteinsFungal ProteinsMembrane ProteinsProteome

Identifiers

PMID15150418
PMCPMC420404
OpenAlexW2140673944

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.