Evidence map›Paper›PMID 38747440›Full record

ArticleProtein science : a publication of the Protein Society2024

DSFworld: A flexible and precise tool to analyze differential scanning fluorimetry data.

Taiasean Wu, Zachary J Gale-Day, Jason E Gestwicki

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Structures of the sodium-coupled phosphate importer SLC34A2 reveal a distinct architecture and gating mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  5. Biophysical and enzymatic comparison ofbioRxiv : the preprint server for biology · 2026
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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

3 authors.

Taiasean WuDepartment of Pharmaceutical Chemistry, Chemistry & Chemical Biology Program and the Institute for Neurodegenerative Diseases, University of California San Francisco, San Francisco, California, USA.
Zachary J Gale-DayDepartment of Pharmaceutical Chemistry, Chemistry & Chemical Biology Program and the Institute for Neurodegenerative Diseases, University of California San Francisco, San Francisco, California, USA.
Jason E GestwickiDepartment of Pharmaceutical Chemistry, Chemistry & Chemical Biology Program and the Institute for Neurodegenerative Diseases, University of California San Francisco, San Francisco, California, USA.ORCID 0000-0002-6125-3154

Funding

Research Training in Chemistry and Chemical BiologyT32GM145460 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Jason E Gestwicki · 2022 to 2026
$3.1M
Differential Scanning Fluorimetry (DSF) Methods for Studying Protein StabilityR01GM141299 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GESTWICKI, JASON E · 2021 to 2024
$1.5M
Chemical Biology Approaches to Studying Collagen IV StabilityR21EY035366 · NEI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GESTWICKI, JASON E · 2023 to 2023
$436k
Defining the role of NC1 domain assembly in collagen biosynthesis and collagen associated disordersF31AR081704 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GALE-DAY, ZACHARY · 2023 to 2024
$82k
National Science Foundation 1000259744NEI NIH HHS R21 EY035366NIAMS NIH HHS F31 AR081704NIGMS NIH HHS R01 GM141299NIGMS NIH HHS T32 GM145460NIH HHS AR081704NIH HHS GM141299
6 · The paper itself

Abstract

Differential scanning fluorimetry (DSF) is a method to determine the apparent melting temperature (Tma) of a purified protein. In DSF, the raw unfolding curves from which Tma is calculated vary widely in shape and complexity. However, the tools available for calculating Tma are only compatible with the simplest of DSF curves, hindering many otherwise straightforward applications of the technology. To overcome this limitation, we designed new mathematical models for Tma calculation that accommodate common forms of variation in DSF curves, including the number of transitions, the presence of high initial signal, and temperature-dependent signal decay. When tested these models against DSFbase, an open-source database of 6235 raw, real-life DSF curves, these models outperformed the existing standard approaches of sigmoid fitting and maximum of the first derivative. To make these models accessible, we created an open-source software and website, DSFworld (https://gestwickilab.shinyapps.io/dsfworld/). In addition to these improved fitting capabilities, DSFworld also includes features that overcome the practical limitations of many analysis workflows, including automatic reformatting of raw data exported from common qPCR instruments, labeling of data based on experimental variables, and flexible interactive plotting. We hope that DSFworld will enable more streamlined and accurate calculation of Tma values for DSF experiments.

Indexed as

FluorometrySoftwareProteinsTransition TemperatureProteinsbiological softwarecurve fittingprotein stabilitythermal shift assaythermoflour

Identifiers

PMID38747440
PMCPMC11095082

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.