Evidence map›Paper›PMID 40025113›Full record

ArticleScientific reports2025

Lossless single-molecule counting to absolute quantify proteoforms.

Tobias Gross, Tobias Hundertmark, Villő Csiszár, András Attila Sulyok, Nina Gross, Maike Breiden, Niklas Kitschen, Uritza von Groll, Christoph Niemöller, Pablo Sánchez-Martín and 8 more

Abstract read
In one paragraph

Article in Scientific reports, 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

18 authors.

Tobias GrossLaboratory for MEMS Applications, Department of Microsystems Engineering, University of Freiburg, Georges-Köhler-Allee 103, Freiburg, 79110, Germany.
Tobias HundertmarkLaboratory for MEMS Applications, Department of Microsystems Engineering, University of Freiburg, Georges-Köhler-Allee 103, Freiburg, 79110, Germany.
Villő CsiszárDepartment of Probability Theory and Statistics, Institute of Mathematics, Eötvös Loránd University, Pázmány Péter sétány 1/C, Budapest, 1117, Hungary.
András Attila SulyokFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter Street 50/A, Budapest, Hungary.
Nina GrossActome GmbH, Georges-Köhler-Allee 302, Freiburg, 79110, Germany.
Maike BreidenQIAGEN, Qiagen Strasse 1, Hilden, 40724, Germany.
Niklas KitschenQIAGEN, Qiagen Strasse 1, Hilden, 40724, Germany.
Uritza von GrollQIAGEN, Qiagen Strasse 1, Hilden, 40724, Germany.
Christoph NiemöllerActome GmbH, Georges-Köhler-Allee 302, Freiburg, 79110, Germany.
Pablo Sánchez-MartínActome GmbH, Georges-Köhler-Allee 302, Freiburg, 79110, Germany.
Anne HeineNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstraße 55, Reutlingen, Germany.
Jens GöpfertNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstraße 55, Reutlingen, Germany.
Tamás SzórádiActome GmbH, Georges-Köhler-Allee 302, Freiburg, 79110, Germany.
Philipp LübbertActome GmbH, Georges-Köhler-Allee 302, Freiburg, 79110, Germany.
Peter KoltayLaboratory for MEMS Applications, Department of Microsystems Engineering, University of Freiburg, Georges-Köhler-Allee 103, Freiburg, 79110, Germany.
Peter PorschewskiQIAGEN, Qiagen Strasse 1, Hilden, 40724, Germany.
Roland ZengerleHahn-Schickard, Georges-Köhler-Allee 103, Freiburg, 79110, Germany.
Csaba JeneyActome GmbH, Georges-Köhler-Allee 302, Freiburg, 79110, Germany. csaba.jeney@actome.de.

Funding

Baden-Württemberg Stiftung MONOGRAM - MET-ID55Ministerium für Wirtschaft, Arbeit und Wohnungsbau Baden-Württemberg DINAMIK (Az: 7533-7-11-10-06)Ministerium für Wirtschaft, Arbeit und Wohnungsbau Baden-Württemberg PRIMO (Az: 3-4332.62-HSG/84)
6 · The paper itself

Abstract

A novel immunoassay, termed Protein Interaction Coupling (PICO), is introduced to deliver clear, reference-free quantification of proteoforms - precise quantification. PICO employs a compartmentalized, homogeneous single-molecule assay with lossless and sensitive signal generation, capable of detecting down to a few molecules per reaction. Additionally, it utilizes a background-free, digital enumeration principle, known as decouplexing. PICO is presented as mathematical theories, providing a theoretical understanding of its chemistry. Consequently, PICO demonstrates precise quantification, as exemplified with recombinant and non-recombinant ErbB2 and multi-tagged peptide rTRX targets, validating quantification against internal and external references in both analytical and cellular matrices. Furthermore, PICO enables combinatorial multiplexing (cplex), a readout between any two antibodies, demonstrated by an 8-plex antibody, 12-cplex PICO, measuring functional changes of the ErbB pathway upon mock and dactolisib treatment delivering quantitative cellular stoichiometry. PICO possesses significant potential for versatile, standardized, and accurate protein measurements, offering insights into physiological and perturbed cellular processes.

Indexed as

Single Molecule ImagingErb-b2 Receptor Tyrosine KinasesHumansImmunoassayERBB2 protein, humanErb-b2 Receptor Tyrosine Kinases

Identifiers

PMID40025113
PMCPMC11873291

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.