Evidence map›Paper›PMID 32587383›Full record

ArticleScientific reports2020

Enhanced protein adsorption upon bulk phase separation.

Madeleine R Fries, Daniel Stopper, Maximilian W A Skoda, Matthias Blum, Christoph Kertzscher, Alexander Hinderhofer, Fajun Zhang, Robert M J Jacobs, Roland Roth, Frank Schreiber

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

2 citing papers in PubMed, 17 citations in OpenAlex.

  1. Evidence for a semisolid phase state of aerosols and droplets relevant to the airborne and surface survival of pathogens.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. 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

10 authors at 3 institutions in 2 countries.

Madeleine R Fries *Institute for Applied Physics, Auf der Morgenstelle 10, University of Tübingen, 72076, Tübingen, Germany.
Daniel Stopper *Institute for Theoretical Physics, Auf der Morgenstelle 14, University of Tübingen, 72076, Tübingen, Germany.
Maximilian W A SkodaISIS Neutron and Muon Source, Science and Technology Facilities Council, Rutherford-Appleton Laboratory, Didcot, OX11 0QX, United Kingdom.
Matthias BlumInstitute for Applied Physics, Auf der Morgenstelle 10, University of Tübingen, 72076, Tübingen, Germany.
Christoph KertzscherInstitute for Applied Physics, Auf der Morgenstelle 10, University of Tübingen, 72076, Tübingen, Germany.
Alexander HinderhoferInstitute for Applied Physics, Auf der Morgenstelle 10, University of Tübingen, 72076, Tübingen, Germany.
Fajun ZhangInstitute for Applied Physics, Auf der Morgenstelle 10, University of Tübingen, 72076, Tübingen, Germany.
Robert M J JacobsSurface Analysis Facility, Chemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom.
Roland RothInstitute for Theoretical Physics, Auf der Morgenstelle 14, University of Tübingen, 72076, Tübingen, Germany. roland.roth@uni-tuebingen.de.
Frank SchreiberInstitute for Applied Physics, Auf der Morgenstelle 10, University of Tübingen, 72076, Tübingen, Germany. frank.schreiber@uni-tuebingen.de.
University of Tübingen · DEScience and Technology Facilities Council · GBUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In all areas related to protein adsorption, from medicine to biotechnology to heterogeneous nucleation, the question about its dominant forces and control arises. In this study, we used ellipsometry and quartz-crystal microbalance with dissipation (QCM-D), as well as density-functional theory (DFT) to obtain insight into the mechanism behind a wetting transition of a protein solution. We established that using multivalent ions in a net negatively charged globular protein solution (BSA) can either cause simple adsorption on a negatively charged interface, or a (diverging) wetting layer when approaching liquid-liquid phase separation (LLPS) by changing protein concentration (c

Identifiers

PMID32587383
PMCPMC7316800
OpenAlexW3037784470

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.