Evidence map›Paper›PMID 33140490›Full record

ArticleProtein science : a publication of the Protein Society2021

In-depth interrogation of protein thermal unfolding data with MoltenProt.

Vadim Kotov, Georg Mlynek, Oliver Vesper, Marina Pletzer, Jiri Wald, Celso M Teixeira-Duarte, Herve Celia, Maria Garcia-Alai, Stephan Nussberger, Susan K Buchanan and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

46 citing papers in PubMed, 74 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

14 authors at 6 institutions in 5 countries.

Vadim KotovCentre for Structural Systems Biology (CSSB), Hamburg, Germany.
Georg MlynekDepartment of Structural and Computational Biology, Max Perutz Labs Vienna, University of Vienna, Vienna, Austria.
Oliver VesperCentre for Structural Systems Biology (CSSB), Hamburg, Germany.
Marina PletzerDepartment of Structural and Computational Biology, Max Perutz Labs Vienna, University of Vienna, Vienna, Austria.
Jiri WaldCentre for Structural Systems Biology (CSSB), Hamburg, Germany.
Celso M Teixeira-DuarteInstituto de Investigação e Inovação em Saúde (i3S) and Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal.
Herve CeliaLaboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Maria Garcia-AlaiCentre for Structural Systems Biology (CSSB), Hamburg, Germany.
Stephan NussbergerDepartment of Biophysics, Institute of Biomaterials and Biomolecular Systems, University of Stuttgart, Stuttgart, Germany.
Susan K BuchananLaboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
João H Morais-CabralInstituto de Investigação e Inovação em Saúde (i3S) and Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal.
Christian LoewCentre for Structural Systems Biology (CSSB), Hamburg, Germany.
Kristina Djinovic-CarugoDepartment of Structural and Computational Biology, Max Perutz Labs Vienna, University of Vienna, Vienna, Austria.
Thomas C MarlovitsCentre for Structural Systems Biology (CSSB), Hamburg, Germany.ORCID 0000-0001-8106-4038
Universität Hamburg · DEUniversity of Vienna · ATEuropean Molecular Biology Laboratory · DEi3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto · PTNational Institutes of Health · USUniversity of Stuttgart · DE

Funding

Structural characterization of outer membrane proteins from Yersinia pestisZIADK011011 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.1M
Austrian Science Fund FWF I1593Austrian Science Fund FWF I525Austrian Science Fund FWF P19060Austrian Science Fund FWF P22276Austrian Science Fund FWF W1221NIDDK NIH HHSWellcome TrustWellcome Trust 201543/Z/16
6 · The paper itself

Abstract

Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consumption or compatibility with sample buffer components. Here we describe how miniaturized measurement of intrinsic tryptophan fluorescence (NanoDSF assay) in combination with a simplified description of protein unfolding can be used to interrogate the stability of a protein sample. We demonstrate that improved protein stability measures, such as apparent Gibbs free energy of unfolding, rather than melting temperature T

Indexed as

Protein FoldingProtein UnfoldingSoftwareCrystallography, X-RayHot TemperatureMembrane ProteinsMultiprotein ComplexesMembrane ProteinsMultiprotein Complexesbuffer optimizationhigh-throughput screeningmelting temperatureMoltenProtNanoDSFprotein unfoldingthermostability

Identifiers

PMID33140490
PMCPMC7737771
OpenAlexW3097522440

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.