Evidence map›Paper›PMID 33953265›Full record

ArticleScientific reports2021

FoldAffinity: binding affinities from nDSF experiments.

Stephan Niebling, Osvaldo Burastero, Jérôme Bürgi, Christian Günther, Lucas A Defelipe, Simon Sander, Ellen Gattkowski, Raghavendra Anjanappa, Matthias Wilmanns, Sebastian Springer and 2 more

Abstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

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  7. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
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  10. TrkA ofMicrobiology (Reading, England) · 2025
    Article
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  14. Review
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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

12 authors.

Stephan NieblingEuropean Molecular Biology Laboratory - Hamburg Outstation, Notkestr. 85, Hamburg, 22607, Germany. stephan.niebling@embl-hamburg.de.
Osvaldo BurasteroEuropean Molecular Biology Laboratory - Hamburg Outstation, Notkestr. 85, Hamburg, 22607, Germany.
Jérôme BürgiEuropean Molecular Biology Laboratory - Hamburg Outstation, Notkestr. 85, Hamburg, 22607, Germany.
Christian GüntherEuropean Molecular Biology Laboratory - Hamburg Outstation, Notkestr. 85, Hamburg, 22607, Germany.
Lucas A DefelipeEuropean Molecular Biology Laboratory - Hamburg Outstation, Notkestr. 85, Hamburg, 22607, Germany.
Simon SanderHamburg Advanced Research Centre for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Luruper Chaussee 149, 22761, Hamburg, Germany.
Ellen GattkowskiHamburg Advanced Research Centre for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Luruper Chaussee 149, 22761, Hamburg, Germany.
Raghavendra AnjanappaDepartment of Life Sciences and Chemistry, Jacobs University Bremen, 28759, Bremen, Germany.
Matthias WilmannsEuropean Molecular Biology Laboratory - Hamburg Outstation, Notkestr. 85, Hamburg, 22607, Germany.
Sebastian SpringerDepartment of Life Sciences and Chemistry, Jacobs University Bremen, 28759, Bremen, Germany.
Henning TidowHamburg Advanced Research Centre for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Luruper Chaussee 149, 22761, Hamburg, Germany.
María García-AlaiEuropean Molecular Biology Laboratory - Hamburg Outstation, Notkestr. 85, Hamburg, 22607, Germany. garcia@embl-hamburg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Differential scanning fluorimetry (DSF) using the inherent fluorescence of proteins (nDSF) is a popular technique to evaluate thermal protein stability in different conditions (e.g. buffer, pH). In many cases, ligand binding increases thermal stability of a protein and often this can be detected as a clear shift in nDSF experiments. Here, we evaluate binding affinity quantification based on thermal shifts. We present four protein systems with different binding affinity ligands, ranging from nM to high μM. Our study suggests that binding affinities determined by isothermal analysis are in better agreement with those from established biophysical techniques (ITC and MST) compared to apparent K

Identifiers

PMID33953265
PMCPMC8099913

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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.