Evidence map›Paper›PMID 20631681›Full record

ArticleMolecular systems biology2010

Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection.

Matthew I Peña, Milya Davlieva, Matthew R Bennett, John S Olson, Yousif Shamoo

Open access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2010. 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
3.0field-weighted citation impact, top 8% 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, 39 citations in OpenAlex.

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  19. Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.Proceedings of the National Academy of Sciences of the United States of America · 2012
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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

5 authors at 1 institution in 1 country.

Matthew I PeñaDepartment of Biochemistry and Cell Biology, Rice University, Houston, TX 77005, USA.
Milya Davlieva
Matthew R Bennett
John S Olson
Yousif Shamoo
Rice University · US

Funding

Function Properties of Hemoglobins and MyoglobinsR01GM035649 · NIGMS · RICE UNIVERSITY · PI OLSON, JOHN S. · 1985 to 2010
$3.3M
DESIGN OF HEME-PROTEIN BASED BLOOD SUBSTITUTESR01HL047020 · NHLBI · RICE UNIVERSITY · PI OLSON, JOHN S. · 1991 to 2010
$2.9M
NHLBI NIH HHS HL047020NHLBI NIH HHS R01 HL047020NIGMS NIH HHS GM35649NIGMS NIH HHS R01 GM035649
6 · The paper itself

Abstract

Systems biology can offer a great deal of insight into evolution by quantitatively linking complex properties such as protein structure, folding, and function to the fitness of an organism. Although the link between diseases such as Alzheimer's and misfolding is well appreciated, directly showing the importance of protein folding to success in evolution has been more difficult. We show here that predicting success during adaptation can depend critically on enzyme kinetic and folding models. We used a 'weak link' method to favor mutations to an essential, but maladapted, adenylate kinase gene within a microbial population that resulted in the identification of five mutants that arose nearly simultaneously and competed for success. Physicochemical characterization of these mutants showed that, although steady-state enzyme activity is important, success within the population is critically dependent on resistance to denaturation and aggregation. A fitness function based on in vitro measurements of enzyme activity, reversible and irreversible unfolding, and the physiological context reproduces in vivo evolutionary fates in the population linking organismal adaptation to its physical basis.

Indexed as

Protein FoldingAdenylate KinaseBacillus subtilisBacterial ProteinsCalorimetry, Differential ScanningCell ProliferationComputer SimulationEnzyme StabilityEvolution, MolecularGenetic FitnessGeobacillus stearothermophilusKineticsModels, MolecularMutationPopulation DynamicsSystems BiologyAdenylate KinaseBacterial Proteins

Identifiers

PMID20631681
PMCPMC2925523
OpenAlexW2161430329

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.