Evidence map›Paper›PMID 21975514›Full record

ReviewChemical Society reviews2012

Thermophilic proteins: insight and perspective from in silico experiments.

Fabio Sterpone, Simone Melchionna

Abstract readReview
In one paragraph

Review in Chemical Society reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. AnFrontiers in chemistry · 2026
    Article
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  4. Frontiers in plant science · 2023
    Article
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  17. Critical structural fluctuations of proteins upon thermal unfolding challenge the Lindemann criterion.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Role of Proteome Physical Chemistry in Cell Behavior.The journal of physical chemistry. B · 2016
    Review
  19. Article
  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

2 authors.

Fabio SterponeLaboratoire de Biochimie Théorique, CNRS, UPR9080, Univ Paris Diderot, Sorbonne Paris Cité, 13 rue Pierre et Marie Curie, 75005, Paris, France. fabio.sterpone@ibpc.fr
Simone Melchionna

Funding

European Research Council 258748
6 · The paper itself

Abstract

Proteins from thermophilic and hyperthermophilic organisms are stable and function at high temperatures (50-100 °C). The importance of understanding the microscopic mechanisms underlying this thermal resistance is twofold: it is key for acquiring general clues on how proteins maintain their fold stable and for targeting those medical and industrial applications that aim at designing enzymes that can work under harsh conditions. In this tutorial review we first provide the general background of protein thermostability by specifically focusing on the structural and thermodynamic peculiarities; next, we discuss how computational studies based on Molecular Dynamics simulations can broaden and refine our knowledge on such special class of proteins.

Indexed as

Catalytic DomainMolecular Dynamics SimulationProteinsProtein StabilityQuantum TheoryTemperatureThermodynamicsProteins

Identifiers

PMID21975514
PMCPMC3775309

What OpenQuestion holds

Textmetadata
LicenceTDM
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.