Evidence map›Paper›PMID 27071404›Full record

ReviewExtremophiles : life under extreme conditions2016

Potential applications of stress solutes from extremophiles in protein folding diseases and healthcare.

Carla D Jorge, Nuno Borges, Irina Bagyan, Andreas Bilstein, Helena Santos

Abstract readReview
PubMed Publisher
In one paragraph

Review in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Isolation and characterization of aApplied and environmental microbiology · 2024
    Article
  2. Review
  3. Article
  4. Article
  5. Exploring the Potential ofFrontiers in bioengineering and biotechnology · 2021
    Article
  6. The saltern-derived3 Biotech · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Observational
  12. Article
  13. Review
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

5 authors at 2 institutions in 2 countries.

Carla D JorgeInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República-EAN, 2780-157, Oeiras, Portugal. cjorge@itqb.unl.pt.
Nuno BorgesInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República-EAN, 2780-157, Oeiras, Portugal.
Irina BagyanBitop AG, Stockumer Straße 28, 58453, Witten, Germany.
Andreas BilsteinBitop AG, Stockumer Straße 28, 58453, Witten, Germany.
Helena SantosInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República-EAN, 2780-157, Oeiras, Portugal.
Universidade Nova de Lisboa · PTBitop (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein misfolding, aggregation and deposition in the brain, in the form of amyloid, are implicated in the etiology of several neurodegenerative disorders, such as Alzheimer's, Parkinson's and prion diseases. Drugs available on the market reduce the symptoms, but they are not a cure. Therefore, it is urgent to identify promising targets and develop effective drugs. Preservation of protein native conformation and/or inhibition of protein aggregation seem pertinent targets for drug development. Several studies have shown that organic solutes, produced by extremophilic microorganisms in response to osmotic and/or heat stress, prevent denaturation and aggregation of model proteins. Among these stress solutes, mannosylglycerate, mannosylglyceramide, di-myo-inositol phosphate, diglycerol phosphate and ectoine are effective in preventing amyloid formation by Alzheimer's Aβ peptide and/or α-synuclein in vitro. Moreover, mannosylglycerate is a potent inhibitor of Aβ and α-synuclein aggregation in living cells, and mannosylglyceramide and ectoine inhibit aggregation and reduce prion peptide-induced toxicity in human cells. This review focuses on the efficacy of stress solutes from hyper/thermophiles and ectoines to prevent amyloid formation in vitro and in vivo and their potential application in drug development against protein misfolding diseases. Current and envisaged applications of these extremolytes in neurodegenerative diseases and healthcare will also be addressed.

Indexed as

Stress, PhysiologicalAmino Acids, DiaminoAmyloidAnimalsArchaeaBacteriaGlyceric AcidsGlycerophosphatesHumansMannoseProteostasis DeficienciesAmino Acids, DiaminoAmyloiddiglycerol phosphateectoineGlyceric AcidsGlycerophosphatesMannosemannosylglycerateCompatible solutesEctoineExtremolytesMannosylglycerateNeurodegenerative diseasesProtein aggregation

Identifiers

PMID27071404
OpenAlexW2335846150

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.