Evidence map›Paper›PMID 21490020›Full record

ReviewProceedings. Biological sciences2011

Binding constraints on the evolution of enzymes and signalling proteins: the important role of negative pleiotropy.

David A Liberles, Makayla D M Tisdell, Johan A Grahnen

Abstract readReview
In one paragraph

Review in Proceedings. Biological sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Highly Abundant Proteins Are Highly Thermostable.Genome biology and evolution · 2023
    Article
  5. Article
  6. Article
  7. Emerging Frontiers in the Study of Molecular Evolution.Journal of molecular evolution · 2020
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Selection on protein structure, interaction, and sequence.Protein science : a publication of the Protein Society · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Cellular crowding imposes global constraints on the chemistry and evolution of proteomes.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. The interface of protein structure, protein biophysics, and molecular evolution.Protein science : a publication of the Protein Society · 2012
    Review
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 1 institution in 1 country.

David A LiberlesDepartment of Molecular Biology, University of Wyoming, Laramie, WY 82071, USA. liberles@uwyo.edu
Makayla D M Tisdell
Johan A Grahnen
University of Wyoming · US

Funding

Wyoming IDeA Networks of Biomedical Research ExcellenceP20RR016474 · NCRR · UNIVERSITY OF WYOMING · PI LIBERLES, DAVID A. · 2001 to 2011
$28.2M
NCRR NIH HHS P20 RR016474
6 · The paper itself

Abstract

A number of biophysical and population-genetic processes influence amino acid substitution rates. It is commonly recognized that proteins must fold into a native structure with preference over an unfolded state, and must bind to functional interacting partners favourably to function properly. What is less clear is how important folding and binding specificity are to amino acid substitution rates. A hypothesis of the importance of binding specificity in constraining sequence and functional evolution is presented. Examples include an evolutionary simulation of a population of SH2 sequences evolved by threading through the structure and binding to a native ligand, as well as SH3 domain signalling in yeast and selection for specificity in enzymatic reactions. An example in vampire bats where negative pleiotropy appears to have been adaptive is presented. Finally, considerations of compartmentalization and macromolecular crowding on negative pleiotropy are discussed.

Indexed as

Evolution, MolecularGenetic PleiotropyProtein Bindingsrc Homology DomainsAmino Acid SubstitutionAnimalsBase SequenceChiropteraProtein FoldingSignal TransductionYeasts

Identifiers

PMID21490020
PMCPMC3107659
OpenAlexW2139920858

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.