Evidence map›Paper›PMID 40357643›Full record

ArticleNucleic acids research2025

BeStSel: analysis site for protein CD spectra-2025 update.

András Micsonai, Frank Wien, Nikoletta Murvai, Márton Péter Nyiri, Bori Balatoni, Young-Ho Lee, Tamás Molnár, Yuji Goto, Frédéric Jamme, József Kardos

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. 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
–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

20 citing papers in PubMed.

  1. Article
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  10. Peculiarities of the Interaction of the Bacteriolytic Protease Blp fromInternational journal of molecular sciences · 2026
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  15. bioRxiv : 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

10 authors.

András MicsonaiDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest H-1117, Hungary.ORCID 0000-0002-2539-4080
Frank WienSynchrotron SOLEIL, Gif-sur-Yvette 91192, France.ORCID 0000-0002-0752-8735
Nikoletta MurvaiDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest H-1117, Hungary.ORCID 0000-0001-7477-0911
Márton Péter NyiriDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest H-1117, Hungary.ORCID 0009-0006-6035-2931
Bori BalatoniDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest H-1117, Hungary.
Young-Ho LeeBiopharmaceutical Research Center, Korea Basic Science Institute (KBSI), Cheongju 28119, Republic of Korea.
Tamás MolnárDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest H-1117, Hungary.ORCID 0000-0002-6842-2715
Yuji GotoGraduate School of Engineering, Osaka University, Osaka 565-0871, Japan.ORCID 0000-0003-1221-1270
Frédéric JammeSynchrotron SOLEIL, Gif-sur-Yvette 91192, France.ORCID 0000-0002-7398-7868
József KardosDepartment of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest H-1117, Hungary.ORCID 0000-0002-2135-2932

Funding

Eötvös Loránd University Excellence Fund EKA 2022/045-P278-1Hungarian Academy of Sciences NAP2022-I-3/2022KBSI A412580KBSI A423310KBSI A439200KBSI C512120KBSI C523200KBSI C539200Ministry for Culture and InnovationNational Research, Development and Innovation Fund of Hungary K138937National Research Foundation of Korea RS-2021-NR057690National Research Foundation of Korea RS-2022-NR069719SOLEIL Synchrotron, France 20230777SOLEIL Synchrotron, France 20231948SOLEIL Synchrotron, France 20240797SOLEIL Synchrotron, France 20241998
6 · The paper itself

Abstract

Circular dichroism (CD) spectroscopy is a widely used technique to characterize the secondary structure composition of proteins. We have developed the Beta Structure Selection (BeStSel) method (PNAS, 112, E3095), which solves the main problem of protein CD spectroscopy-namely, the spectral variability of β-structures. The BeStSel web server utilizes this method to provide tools to the community for CD spectrum analysis. BeStSel uniquely provides information on eight secondary structure components, including parallel β-structure and antiparallel β-sheets with three different twist groups. It outperforms all available methods in accuracy and information content, and is also able to predict protein folds down to the topology/homology level of the CATH classification. The algorithm has been further developed, and the accuracy of the estimation of the secondary structure elements is improved by 0.7% as an average on the reference dataset. A new module of the web server calculates protein stability from the thermal denaturation profile followed by CD. Secondary structure calculations of uploaded PDB and mmcif files support the experimental verification of MD simulations and AlphaFold models by CD spectroscopy. Well-proven modules for disorder-order classification and extinction coefficient calculation continue to work. The BeStSel server is freely accessible at https://bestsel.elte.hu.

Indexed as

Circular DichroismProteinsSoftwareAlgorithmsInternetMolecular Dynamics SimulationProtein Conformation, beta-StrandProtein FoldingProtein StabilityProtein Structure, SecondaryProteins

Identifiers

PMID40357643
PMCPMC12230724

What OpenQuestion holds

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Registered trials

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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.