Evidence map›Paper›PMID 41321999›Full record

ArticleComputational and structural biotechnology journal2025

An integrative structural biology approach to identify the binding mode of a nanobody towards the pea ascorbate peroxidase.

Claudia D'Ercole, Marco Orlando, Kristina Eleršič Filipič, Ario de Marco

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Computational and structural biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Claudia D'ErcoleLab of Environmental and Life Sciences, University of Nova Gorica, Vipavska cesta 13, Nova Gorica 5000, Slovenia.
Marco OrlandoDepartment of Biotechnology and Biosciences, University of Milano Bicocca, Piazza della Scienza 2, Milano 20126, Italy.
Kristina Eleršič FilipičNational Institute of Chemistry, Hajdrihova 19, Ljubljana SI-1000, Slovenia.
Ario de MarcoLab of Environmental and Life Sciences, University of Nova Gorica, Vipavska cesta 13, Nova Gorica 5000, Slovenia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The optimization of diagnostic devices such as biosensors often requires understanding the molecular details of the interaction between capture and target biomolecules. This can be experimentally obtained by cryo-electron microscopy, the preferred method for the analysis of large protein complexes, while NMR and x-ray crystallography are effective for determining the structure of complexes formed by relatively small molecules. Nevertheless, all these approaches are demanding in terms of time and resources and, therefore, we explored the possibility to reduce the experimental load by compensating with

Indexed as

Ascorbate peroxidaseHydrogen-deuterium exchange coupled to mass spectrometryIntegrative structural biologyNanobodiesProtein cross-linking

Identifiers

PMID41321999
PMCPMC12664111

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.