Evidence map›Paper›PMID 39415059›Full record

ArticleNature biotechnology2025

Global profiling of protein complex dynamics with an experimental library of protein interaction markers.

Christian Dörig, Cathy Marulli, Thomas Peskett, Norbert Volkmar, Lorenzo Pantolini, Gabriel Studer, Camilla Paleari, Fabian Frommelt, Torsten Schwede, Natalie de Souza and 2 more

Abstract read
In one paragraph

Article in Nature biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  9. Analysis of Limited Proteolysis-Coupled Mass Spectrometry Data.Molecular & cellular proteomics : MCP · 2025
    Article
  10. 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

12 authors.

Christian Dörig *Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-4213-8855
Cathy Marulli *Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-2327-7016
Thomas PeskettInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-2008-688X
Norbert VolkmarInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Lorenzo PantoliniBiozentrum, University of Basel, Basel, Switzerland.
Gabriel StuderBiozentrum, University of Basel, Basel, Switzerland.
Camilla PaleariInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0009-0003-0488-0447
Fabian FrommeltInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-3666-8005
Torsten SchwedeBiozentrum, University of Basel, Basel, Switzerland.ORCID http://orcid.org/0000-0003-2715-335X
Natalie de SouzaInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Yves BarralInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-0989-3373
Paola PicottiInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland. picotti@imsb.biol.ethz.ch.ORCID http://orcid.org/0000-0002-4109-3552

Funding

EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 823839EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 866004Promedica Stiftung 1508/M
6 · The paper itself

Abstract

Methods to systematically monitor protein complex dynamics are needed. We introduce serial ultrafiltration combined with limited proteolysis-coupled mass spectrometry (FLiP-MS), a structural proteomics workflow that generates a library of peptide markers specific to changes in PPIs by probing differences in protease susceptibility between complex-bound and monomeric forms of proteins. The library includes markers mapping to protein-binding interfaces and markers reporting on structural changes that accompany PPI changes. Integrating the marker library with LiP-MS data allows for global profiling of protein-protein interactions (PPIs) from unfractionated lysates. We apply FLiP-MS to Saccharomyces cerevisiae and probe changes in protein complex dynamics after DNA replication stress, identifying links between Spt-Ada-Gcn5 acetyltransferase activity and the assembly state of several complexes. FLiP-MS enables protein complex dynamics to be probed on any perturbation, proteome-wide, at high throughput, with peptide-level structural resolution and informing on occupancy of binding interfaces, thus providing both global and molecular views of a system under study.

Indexed as

Protein Interaction MappingProteomicsSaccharomyces cerevisiae ProteinsMass SpectrometryPeptide LibraryProtein BindingSaccharomyces cerevisiaePeptide LibrarySaccharomyces cerevisiae Proteins

Identifiers

PMID39415059
PMCPMC12440823

What OpenQuestion 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 OpenQuestion graph.