Evidence map›Paper›PMID 32027860›Full record

ArticleCell systems2020

A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS.

Moritz Heusel, Max Frank, Mario Köhler, Sabine Amon, Fabian Frommelt, George Rosenberger, Isabell Bludau, Simran Aulakh, Monika I Linder, Yansheng Liu and 4 more

Abstract read
In one paragraph

Article in Cell systems, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
–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

39 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  6. Methods for the Investigation of Protein-Ligands Interactions.Advances in experimental medicine and biology · 2026
    Review
  7. Article
  8. Article
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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

14 authors.

Moritz HeuselInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland; Division of Infection Medicine (BMC), Department of Clinical Sciences, Lund University, Lund, Sweden.
Max FrankInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Mario KöhlerInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Sabine AmonInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Fabian FrommeltInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
George RosenbergerInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Isabell BludauInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Simran AulakhInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Monika I LinderInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Yansheng LiuDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA.
Ben C CollinsSchool of Biological Sciences, Queen's University of Belfast, Belfast, UK.
Matthias GstaigerInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Ulrike KutayInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Ruedi AebersoldInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland; Faculty of Science, University of Zurich, Zurich, Switzerland. Electronic address: aebersold@imsb.biol.ethz.ch.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Living systems integrate biochemical reactions that determine the functional state of each cell. Reactions are primarily mediated by proteins. In proteomic studies, these have been treated as independent entities, disregarding their higher-level organization into complexes that affects their activity and/or function and is thus of great interest for biological research. Here, we describe the implementation of an integrated technique to quantify cell-state-specific changes in the physical arrangement of protein complexes concurrently for thousands of proteins and hundreds of complexes. Applying this technique to a comparison of human cells in interphase and mitosis, we provide a systematic overview of mitotic proteome reorganization. The results recall key hallmarks of mitotic complex remodeling and suggest a model of nuclear pore complex disassembly, which we validate by orthogonal methods. To support the interpretation of quantitative SEC-SWATH-MS datasets, we extend the software CCprofiler and provide an interactive exploration tool, SECexplorer-cc.

Indexed as

HumansMitosisProteomicsTandem Mass Spectrometrycell cyclemonitoring state of proteome organizationprotein complexessize exclusion chromatographySWATH-MS

Identifiers

PMID32027860
PMCPMC7042714

What OpenQuestion holds

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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.