Evidence map›Paper›PMID 27595789›Full record

ArticleScientific reports2016

High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes.

N Martinez, G Michoud, A Cario, J Ollivier, B Franzetti, M Jebbar, P Oger, J Peters

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
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  5. Review
  6. Unravelling the Adaptation Mechanisms to High Pressure in Proteins.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Experimental study of proteome halophilicity using nanoDSF: a proof of concept.Extremophiles : life under extreme conditions · 2021
    Article
  9. Article
  10. The Piezo-Hyperthermophilic ArchaeonFrontiers in microbiology · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. High Hydrostatic Pressure Induces a Lipid Phase Transition and Molecular Rearrangements in Low-Density Lipoprotein Nanoparticles.Particle & particle systems characterization : measurement and description of particle properties and behavior in powders and other disperse systems · 2018
    Article
  17. Article
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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

8 authors at 4 institutions in 1 country.

N MartinezInstitut Laue Langevin, F-38042 Grenoble Cedex 9, France.
G MichoudUniv. Brest, CNRS, Ifremer, LM2E, IUEM, 29280, Plouzané, France.
A CarioUniv Lyon, ENS Lyon, CNRS UMR 5276, F - 69364 Lyon cedex 07, France.
J OllivierInstitut Laue Langevin, F-38042 Grenoble Cedex 9, France.
B FranzettiUniv. Grenoble Alpes, IBS, F-38041 Grenoble Cedex 9, France.
M JebbarUniv. Brest, CNRS, Ifremer, LM2E, IUEM, 29280, Plouzané, France.
P OgerUniv Lyon, ENS Lyon, CNRS UMR 5276, F - 69364 Lyon cedex 07, France.
J PetersInstitut Laue Langevin, F-38042 Grenoble Cedex 9, France.
Institut Laue-Langevin · FRCentre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FRInstitut de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Water and protein dynamics on a nanometer scale were measured by quasi-elastic neutron scattering in the piezophile archaeon Thermococcus barophilus and the closely related pressure-sensitive Thermococcus kodakarensis, at 0.1 and 40 MPa. We show that cells of the pressure sensitive organism exhibit higher intrinsic stability. Both the hydration water dynamics and the fast protein and lipid dynamics are reduced under pressure. In contrast, the proteome of T. barophilus is more pressure sensitive than that of T. kodakarensis. The diffusion coefficient of hydration water is reduced, while the fast protein and lipid dynamics are slightly enhanced with increasing pressure. These findings show that the coupling between hydration water and cellular constituents might not be simply a master-slave relationship. We propose that the high flexibility of the T. barophilus proteome associated with reduced hydration water may be the keys to the molecular adaptation of the cells to high hydrostatic pressure.

Indexed as

Archaeal ProteinsPressureThermococcusWaterArchaeal ProteinsWater

Identifiers

PMID27595789
PMCPMC5011708
OpenAlexW2521211604

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.