Evidence map›Paper›PMID 30021884›Full record

ArticleMolecular & cellular proteomics : MCP2018

Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.

Domenico Fasci, Hugo van Ingen, Richard A Scheltema, Albert J R Heck

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
9.6field-weighted citation impact, top 1% of its field
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

67 citing papers in PubMed, 145 citations in OpenAlex.

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  12. Unlocking TRPM7 interactions: A database-driven quest.Computational and structural biotechnology journal · 2025
    Review
  13. A Photo-Caged Cross-Linker for Identifying Protein-Protein Interactions.Chembiochem : a European journal of chemical biology · 2024
    Article
  14. Article
  15. Article
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  20. Review

7 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 3 countries.

Domenico FasciFrom the ‡Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences.
Hugo van Ingen¶NMR Spectroscopy Research Group, Bijvoet Center for Biomolecular Research, University of Utrecht, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Richard A ScheltemaFrom the ‡Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences; R.A.Scheltema@uu.nl.ORCID 0000-0002-1668-0253
Albert J R HeckFrom the ‡Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences; A.J.R.Heck@uu.nl.ORCID 0000-0002-2405-4404
Utrecht University · NLUniversity of Applied Sciences Utrecht · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells organize their actions partly through tightly controlled protein-protein interactions-collectively termed the interactome. Here we use crosslinking mass spectrometry (XL-MS) to chart the protein-protein interactions in intact human nuclei. Overall, we identified ∼8,700 crosslinks, of which 2/3 represent links connecting distinct proteins. From these data, we gain insights on interactions involving histone proteins. We observed that core histones on the nucleosomes expose well-defined interaction hot spots. For several nucleosome-interacting proteins, such as USF3 and Ran GTPase, the data allowed us to build low-resolution models of their binding mode to the nucleosome. For HMGN2, the data guided the construction of a refined model of the interaction with the nucleosome, based on complementary NMR, XL-MS, and modeling. Excitingly, the analysis of crosslinks carrying posttranslational modifications allowed us to extract how specific modifications influence nucleosome interactions. Overall, our data depository will support future structural and functional analysis of cell nuclei, including the nucleoprotein assemblies they harbor.

Indexed as

Cell Line, TumorCell NucleusCross-Linking ReagentsHistonesHumansMass SpectrometryModels, MolecularNuclear ProteinsNucleosomesProtein BindingProtein Interaction MapsProtein Processing, Post-TranslationalReproducibility of ResultsCross-Linking ReagentsHistonesNuclear ProteinsNucleosomesChromatin function or biologyHistone interaction network – PTM interplayHistonesHistone variant specific interactionsMass SpectrometryNuclear interactomeProtein Cross-linkingProtein-Protein Interactions

Identifiers

PMID30021884
PMCPMC6166682
OpenAlexW2883227587

What OpenQuestion holds

Textmetadata
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.