Evidence map›Paper›PMID 27028523›Full record

ArticleProtein science : a publication of the Protein Society2016

The tangled bank of amino acids.

Richard A Goldstein, David D Pollock

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

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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

2 authors.

Richard A GoldsteinDivision of Infection and Immunity, University College London, London, WC1E 6BT, UK.
David D PollockDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, Colorado, 80045.

Funding

Modeling evolution of functional context in proteinsR01GM083127 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI POLLOCK, DAVID D · 2009 to 2019
$2.7M
Genome-wide mutation models to decipher functionR01GM097251 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI POLLOCK, DAVID D · 2012 to 2015
$1.2M
Medical Research Council MC_PC_13056Medical Research Council MC_U117573805NIGMS NIH HHS R01 GM083127NIGMS NIH HHS R01 GM097251
6 · The paper itself

Abstract

The use of amino acid substitution matrices to model protein evolution has yielded important insights into both the evolutionary process and the properties of specific protein families. In order to make these models tractable, standard substitution matrices represent the average results of the evolutionary process rather than the underlying molecular biophysics and population genetics, treating proteins as a set of independently evolving sites rather than as an integrated biomolecular entity. With advances in computing and the increasing availability of sequence data, we now have an opportunity to move beyond current substitution matrices to more interpretable mechanistic models with greater fidelity to the evolutionary process of mutation and selection and the holistic nature of the selective constraints. As part of this endeavour, we consider how epistatic interactions induce spatial and temporal rate heterogeneity, and demonstrate how these generally ignored factors can reconcile standard substitution rate matrices and the underlying biology, allowing us to better understand the meaning of these substitution rates. Using computational simulations of protein evolution, we can demonstrate the importance of both spatial and temporal heterogeneity in modelling protein evolution.

Indexed as

Amino Acid SubstitutionComputer SimulationDatabases, ProteinEvolution, MolecularModels, GeneticMutation RatePhylogenyProteinsSelection, GeneticProteinsepistasisepistatic interactionsevolutionary processevolutionary Stokes shiftmolecular evolutionphylogeneticsprotein evolutionsubstitution matricessubstitution rates

Identifiers

PMID27028523
PMCPMC4918418

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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.