Evidence map›Paper›PMID 22355525›Full record

ArticleScientific reports2011

Halophilic enzyme activation induced by salts.

Gabriel Ortega, Ana Laín, Xavier Tadeo, Blanca López-Méndez, David Castaño, Oscar Millet

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Xylan Degradation in the Halotolerant BacteriumJournal of agricultural and food chemistry · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Halophiles and their enzymes: negativity put to good use.Current opinion in microbiology · 2015
    Review
  18. Article
  19. Review
  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

6 authors at 1 institution in 1 country.

Gabriel OrtegaStructural Biology Unit, CIC bioGUNE , Bizkaia Technology Park, Building 800, 48160 Derio, Spain.
Ana Laín
Xavier Tadeo
Blanca López-Méndez
David Castaño
Oscar Millet
CIC bioGUNE · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Halophilic archea (halobacteriae) thrive in hypersaline environments, avoiding osmotic shock by increasing the ion concentration of their cytoplasm by up to 3-6 M. To remain folded and active, their constitutive proteins have evolved towards a biased amino acid composition. High salt concentration affects catalytic activity in an enzyme-dependent way and a unified molecular mechanism remains elusive. Here, we have investigated a DNA ligase from Haloferax volcanii (Hv LigN) to show that K(+) triggers catalytic activity by preferentially stabilising a specific conformation in the reaction coordinate. Sodium ions, in turn, do not populate such isoform and the enzyme remains inactive in the presence of this co-solute. Our results show that the halophilic amino acid signature enhances the enzyme's thermodynamic stability, with an indirect effect on its catalytic activity. This model has been successfully applied to reengineer Hv LigN into an enzyme that is catalytically active in the presence of NaCl.

Indexed as

CatalysisDNA LigasesEnzyme ActivationEuryarchaeotaPotassiumSaltsSodiumDNA LigasesPotassiumSaltsSodium

Identifiers

PMID22355525
PMCPMC3216494
OpenAlexW1986022901

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.