Evidence map›Paper›PMID 28301766›Full record

ReviewAnnual review of biophysics2017

Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.

Julian Echave, Claus O Wilke

Abstract readReview
In one paragraph

Review in Annual review of biophysics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

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15 more citing papers are in PubMed but not listed here.

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.

Julian EchaveEscuela de Ciencia y Tecnología, Universidad Nacional de San Martín, 1650 San Martín, Buenos Aires, Argentina; email: julian.echave@unsam.edu.ar.
Claus O WilkeDepartment of Integrative Biology, The University of Texas at Austin, Texas 78712; email: wilke@austin.utexas.edu.

Funding

The biophysical basis of translational selectionR01GM088344 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BARRICK, JEFFREY EVAN, WILKE, CLAUS O · 2009 to 2023
$3.5M
Single-Cell VirologyR01AI120560 · NIAID · PENNSYLVANIA STATE UNIVERSITY, THE · PI CAMERON, CRAIG E., HUANG, TONY JUN · 2015 to 2017
$1.4M
NIAID NIH HHS R01 AI120560NIGMS NIH HHS R01 GM088344
6 · The paper itself

Abstract

For decades, rates of protein evolution have been interpreted in terms of the vague concept of functional importance. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger selection pressure. More recently, biophysical models of protein evolution, which combine evolutionary theory with protein biophysics, have completely revolutionized our view of the forces that shape sequence divergence. Slowly evolving proteins have been found to evolve slowly because of selection against toxic misfolding and misinteractions, linking their rate of evolution primarily to their abundance. Similarly, most slowly evolving sites in proteins are not directly involved in function, but mutating these sites has a large impact on protein structure and stability. In this article, we review the studies in the emerging field of biophysical protein evolution that have shaped our current understanding of sequence divergence patterns. We also propose future research directions to develop this nascent field.

Indexed as

Evolution, MolecularBiophysical PhenomenaBiophysicsGenetic FitnessHumansMutationProtein FoldingProteinsProtein StabilityThermodynamicsProteinsevolutionary ratefitness landscapeprotein foldingprotein misfoldingprotein–protein interaction

Identifiers

PMID28301766
PMCPMC5800964

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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.