Evidence map›Paper›PMID 22192175›Full record

ArticleBMC structural biology2011

Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface.

Alessandro Siglioccolo, Alessandro Paiardini, Maria Piscitelli, Stefano Pascarella

Open access · hybridAbstract read
In one paragraph

Article in BMC structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

67 citing papers in PubMed, 167 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. HalophyticACS omega · 2025
    Article
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  12. Review
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  15. Article
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  17. Article
  18. Metabolic Potential of Halophilic Filamentous Fungi-Current Perspective.International journal of molecular sciences · 2022
    Review
  19. Article
  20. Article

7 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

4 authors at 1 institution in 1 country.

Alessandro SiglioccoloDipartimento di Scienze Biochimiche "A, Rossi Fanelli", Università di Roma La Sapienza, 00185 Roma, Italy.
Alessandro Paiardini
Maria Piscitelli
Stefano Pascarella
Sapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHalophiles are extremophilic microorganisms growing optimally at high salt concentrations. There are two strategies used by halophiles to maintain proper osmotic pressure in their cytoplasm: accumulation of molar concentrations of potassium and chloride with extensive adaptation of the intracellular macromolecules ("salt-in" strategy) or biosynthesis and/or accumulation of organic osmotic solutes ("osmolyte" strategy). Our work was aimed at contributing to the understanding of the shared molecular mechanisms of protein haloadaptation through a detailed and systematic comparison of a sample of several three-dimensional structures of halophilic and non-halophilic proteins. Structural differences observed between the "salt-in" and the mesophilic homologous proteins were contrasted to those observed between the "osmolyte" and mesophilic pairs.

resultsThe results suggest that haloadaptation strategy in the presence of molar salt concentration, but not of osmolytes, necessitates a weakening of the hydrophobic interactions, in particular at the level of conserved hydrophobic contacts. Weakening of these interactions counterbalances their strengthening by the presence of salts in solution and may help the structure preventing aggregation and/or loss of function in hypersaline environments.

conclusionsConsidering the significant increase of biotechnology applications of halophiles, the understanding of halophilicity can provide the theoretical basis for the engineering of proteins of great interest because stable at concentrations of salts that cause the denaturation or aggregation of the majority of macromolecules.

Indexed as

Computational BiologyConserved SequenceHydrophobic and Hydrophilic InteractionsAdaptation, PhysiologicalArchaeal ProteinsBacterial ProteinsDose-Response Relationship, DrugModels, MolecularProtein ConformationSaltsStatic ElectricitySurface PropertiesArchaeal ProteinsBacterial ProteinsSalts

Identifiers

PMID22192175
PMCPMC3293032
OpenAlexW2141272708

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.