Evidence map›Paper›PMID 40663321›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Resemblance-Ranking Peptide Library as a Representation of a Complex Proteome.

Dimitry Schmidt, Roman Popov, Sergey Biniaminov, Alexander Nesterov-Mueller

Abstract read
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Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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.

Dimitry SchmidtInstitute of Microstructure Technology, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany.
Roman PopovAxxelera, Karlsruhe, Germany.
Sergey BiniaminovHS Analysis, Karlsruhe, Germany.
Alexander Nesterov-MuellerInstitute of Microstructure Technology, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany. Alexander.Nesterov-Mueller@KIT.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide arrays facilitate the exploration of protein-protein interactions, allowing for analysis at the amino acid level. This study introduces a "deep screening" technique to represent entire proteomes with peptides, thereby revealing novel interactions that are not detectable with protein-only methods. We developed a method to construct a peptide library based on genomic peptide similarity, prioritizing peptides with the highest occurrence in the proteome. Using the monoclonal anti-CD20 antibody rituximab, we demonstrate the process of peptide library design, incubation, and photometric data acquisition. The method also includes hit validation through dissociation constant measurements and substitutional analysis to identify key amino acids for binding. This innovative approach enhances the identification of peptide interactions, offering significant potential for diagnostic and therapeutic developments.

Indexed as

Peptide LibraryPeptidesProteomeProteomicsHumansProtein Array AnalysisProtein BindingRituximabPeptide LibraryPeptidesProteomeRituximabAntibodiesEpitopesOff-targetingPeptide microarraysSpecific binders

Identifiers

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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.