Evidence map›Paper›PMID 19879880›Full record

ArticleJournal of molecular biology2010

Evolution of protein binding modes in homooligomers.

Judith E Dayhoff, Benjamin A Shoemaker, Stephen H Bryant, Anna R Panchenko

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Molecular basis for protein-protein interactions.Beilstein journal of organic chemistry · 2021
    Review
  8. Article
  9. Evolution of protein interfaces in multimers and fibrils.The Journal of chemical physics · 2019
    Article
  10. Article
  11. Article
  12. Homo- and Heterodimerization of Proteins in Cell Signaling: Inhibition and Drug Design.Advances in protein chemistry and structural biology · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Dimerization of lipocalin allergens.Scientific reports · 2015
    Article
  20. Evolutionary meandering of intermolecular interactions along the drift barrier.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

4 authors.

Judith E DayhoffDepartment of Biochemistry and Molecular and Cellular Biology, Georgetown University, Washington, DC, USA.
Benjamin A Shoemaker
Stephen H Bryant
Anna R Panchenko

Funding

Structural Biology Information ResourcesZIALM000046 · NLM · NATIONAL LIBRARY OF MEDICINE · PI BRYANT, STEPHEN H · 2009 to 2017
$45.4M
Chemical Biology Information ResourcesZIALM100604 · NLM · NATIONAL LIBRARY OF MEDICINE · PI BRYANT, STEPHEN H · 2009 to 2017
$39.6M
Intramural NIH HHS Z99 LM999999
6 · The paper itself

Abstract

The evolution of protein interactions cannot be deciphered without a detailed analysis of interaction interfaces and binding modes. We performed a large-scale study of protein homooligomers in terms of their symmetry, interface sizes, and conservation of binding modes. We also focused specifically on the evolution of protein binding modes from nine families of homooligomers and mapped 60 different binding modes and oligomerization states onto the phylogenetic trees of these families. We observed a significant tendency for the same binding modes to be clustered together and conserved within clades on phylogenetic trees; this trend is especially pronounced for close homologs with 70% sequence identity or higher. Some binding modes are conserved among very distant homologs, pointing to their ancient evolutionary origin, while others are very specific for a certain phylogenetic group. Moreover, we found that the most ancient binding modes have a tendency to involve symmetrical (isologous) homodimer binding arrangements with larger interfaces, while recently evolved binding modes more often exhibit asymmetrical arrangements and smaller interfaces.

Indexed as

Evolution, MolecularProtein BindingProtein MultimerizationAnimalsConserved SequenceEsterasesGalectinsHumansLipaseModels, MolecularPhylogenyProtein Interaction Domains and MotifsProteinsProtein Serine-Threonine KinasesProtein Structure, QuaternaryEsterasesGalectinsLipaseProteinsProtein Serine-Threonine Kinases

Identifiers

PMID19879880
PMCPMC2813322

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Registered trials

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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.