Evidence map›Paper›PMID 28445752›Full record

ArticleBiophysical journal2017

Refolding of SDS-Unfolded Proteins by Nonionic Surfactants.

Jørn Døvling Kaspersen, Anne Søndergaard, Daniel Jhaf Madsen, Daniel E Otzen, Jan Skov Pedersen

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 57 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Jørn Døvling KaspersenInterdisciplinary Nanoscience Centre (iNANO), Aarhus University, Aarhus, Denmark.
Anne SøndergaardDepartment of Chemistry, Aarhus University, Aarhus, Denmark.
Daniel Jhaf MadsenInterdisciplinary Nanoscience Centre (iNANO), Aarhus University, Aarhus, Denmark.
Daniel E OtzenInterdisciplinary Nanoscience Centre (iNANO), Aarhus University, Aarhus, Denmark. Electronic address: dao@inano.au.dk.
Jan Skov PedersenInterdisciplinary Nanoscience Centre (iNANO), Aarhus University, Aarhus, Denmark; Department of Chemistry, Aarhus University, Aarhus, Denmark. Electronic address: jsp@chem.au.dk.
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The strong and usually denaturing interaction between anionic surfactants (AS) and proteins/enzymes has both benefits and drawbacks: for example, it is put to good use in electrophoretic mass determinations but limits enzyme efficiency in detergent formulations. Therefore, studies of the interactions between proteins and AS as well as nonionic surfactants (NIS) are of both basic and applied relevance. The AS sodium dodecyl sulfate (SDS) denatures and unfolds globular proteins under most conditions. In contrast, NIS such as octaethylene glycol monododecyl ether (C

Indexed as

AnimalsCattleChickensCircular DichroismEgg ProteinsEthylene GlycolsGlucosidesLactalbuminLactoglobulinsMicellesMilk ProteinsMuramidaseProtein RefoldingProtein UnfoldingScattering, Small AngleSerum Albumindodecyl maltosideEgg ProteinsEthylene GlycolsGlucosidesLactalbuminLactoglobulinsMicellesMilk ProteinsMuramidaseoctaethylene glycol monotetradecyl etherSerum AlbuminSodium Dodecyl SulfateSurface-Active Agents

Identifiers

PMID28445752
PMCPMC5406375
OpenAlexW2607724955

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.