Evidence map›Paper›PMID 17914231›Full record

ReviewJournal of biosciences2007

Protein mechanics: a route from structure to function.

Richard Lavery, Sophie Sacquin-Mora

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biosciences, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
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  8. Probing the toxic mechanism of bisphenol A with acid phosphatase at the molecular level.Environmental science and pollution research international · 2018
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  9. Review
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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 LaveryInstitut de Biologie et Chimie des Proteines, CNRS UMR 5086/Universite de Lyon, 7 passage du Vercors, Lyon 69367, France. Richard.Lavery@ibcp.fr
Sophie Sacquin-Mora

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to better understand the mechanical properties of proteins, we have developed simulation tools which enable these properties to be analysed on a residue-by-residue basis. Although these calculations are relatively expensive with all-atom protein models, good results can be obtained much faster using coarse-grained approaches. The results show that proteins are surprisingly heterogeneous from a mechanical point of view and that functionally important residues often exhibit unusual mechanical behaviour. This finding offers a novel means for detecting functional sites and also potentially provides a route for understanding the links between structure and function in more general terms.

Indexed as

Models, ChemicalModels, MolecularAnimalsBinding SitesComputational BiologyProtein BindingProteinsStructure-Activity RelationshipProteins

Identifiers

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.