Evidence map›Paper›PMID 41653152›Full record

ArticleJournal of proteome research2026

Above-Filter Digestion Proteomics Reveals Drug Targets and Localizes Ligand Binding Site.

Bohdana Sokolova, Hassan Gharibi, Maryam Jafari, Hezheng Lyu, Silvia Lovera, Massimiliano Gaetani, Amir Ata Saei, Roman A Zubarev

Abstract read
In one paragraph

Article in Journal of proteome research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
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

8 authors.

Bohdana SokolovaDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden.ORCID 0000-0003-3751-7129
Hassan GharibiDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden.ORCID 0000-0002-3072-4929
Maryam JafariDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden.
Hezheng LyuDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden.
Silvia LoveraUCB Pharma, Chemin du Foriest 1, 1420 Braine-l'Alleud, Belgium.
Massimiliano GaetaniDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden.ORCID 0000-0001-5610-0797
Amir Ata SaeiDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden.
Roman A ZubarevDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden.ORCID 0000-0001-9839-2089

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identifying how drugs interact with proteins is fundamental to understanding their therapeutic effects and side effects. While numerous chemical proteomics methods exist for determining protein targets of drugs, each exhibits "blind spots," necessitating complementary approaches. We introduce Above-Filter Digestion Proteomics (AFDIP), which monitors trypsin digestion rates that decrease at ligand-binding sites, while potentially increasing elsewhere. Molecular dynamics simulations showed that these changes relate to backbone flexibility. Using AFDIP, we identified targets of various drugs and metabolites, allowing two-dimensional analysis with the drug concentration as the second dimension. The method identifies binding sites within ≤10 Å of crystallography-determined locations with improved resolution (≤5 Å) for larger proteins. Compared with existing proteolysis approaches, AFDIP offers simpler sample preparation, deeper proteome analysis, and broader sequence coverage. AFDIP addresses the blind spots of current techniques and provides structural insights, enhancing the chemical proteomics toolkit.

Indexed as

ProteinsProteomicsBinding SitesHumansLigandsMolecular Dynamics SimulationProtein BindingProteolysisTrypsinLigandsProteinsTrypsinbinding site localizationchemical proteomicsdigestion proteomicsdrug–target identificationlimited proteolysismass spectrometryprotein-drug interactionsproteolysisstructural proteomicstrypsin digestion kinetics

Identifiers

PMID41653152
PMCPMC12973292

What Socratic 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 Socratic graph.