Evidence map›Paper›PMID 22144639›Full record

ArticleMolecular biology and evolution2012

The evolution of multimeric protein assemblages.

Michael Lynch

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology and evolution, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 93 citations in OpenAlex.

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  6. Symmetry facilitated the evolution of heterospecificity and high-order stoichiometry in vertebrate hemoglobin.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  17. Simple mechanisms for the evolution of protein complexity.Protein science : a publication of the Protein Society · 2022
    Review
  18. Review
  19. Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022
    Review
  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

1 author at 1 institution in 1 country.

Michael LynchDepartment of Biology, Indiana University, IN, USA. milynch@indiana.edu
Indiana University – Purdue University Indianapolis · US

Funding

The Rate and Molecular Spectrum of Spontaneous MutationsR01GM036827 · NIGMS · UNIVERSITY OF OREGON · PI LYNCH, MICHAEL R · 1988 to 2016
$5.7M
NIGMS NIH HHS R01 GM036827
6 · The paper itself

Abstract

Although the mechanisms by which complex cellular features evolve constitute one of the great unsolved problems of evolutionary biology, it is clear that the emergence of new protein-protein interactions, often accompanied by the diversification of duplicate genes, is involved. Using information on the levels of protein multimerization in major phylogenetic groups as a guide to the patterns that must be explained and relying on results from population-genetic theory to define the relative plausibility of alternative evolutionary pathways, a framework for understanding the evolution of dimers is developed. The resultant theory demonstrates that the likelihoods of alternative pathways for the emergence of protein complexes depend strongly on the effective population size. Nonetheless, it is equally clear that further advancements in this area will require comparative studies on the fitness consequences of alternative monomeric and dimeric proteins.

Indexed as

Evolution, MolecularAnimalsBacteriaEukaryotaGenetic DriftGenomeMutationProtein MultimerizationProteinsProteins

Identifiers

PMID22144639
PMCPMC3339316
OpenAlexW2154660008

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.