Evidence map›Paper›PMID 21836164›Full record

ArticleMolecular & cellular proteomics : MCP2011

Chromatin affinity purification and quantitative mass spectrometry defining the interactome of histone modification patterns.

Miroslav Nikolov, Alexandra Stützer, Kerstin Mosch, Andrius Krasauskas, Szabolcs Soeroes, Holger Stark, Henning Urlaub, Wolfgang Fischle

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Chemical biology approaches to study histone interactors.Biochemical Society transactions · 2021
    Review
  8. Article
  9. Quantitative Mass Spectrometry-Based Proteomics: An Overview.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Understanding the interplay between CpG island-associated gene promoters and H3K4 methylation.Biochimica et biophysica acta. Gene regulatory mechanisms · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Cryo-electron microscopy of chromatin biology.Acta crystallographica. Section D, Structural biology · 2017
    Review
  20. 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

8 authors at 1 institution in 1 country.

Miroslav NikolovBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Alexandra Stützer
Kerstin Mosch
Andrius Krasauskas
Szabolcs Soeroes
Holger Stark
Henning Urlaub
Wolfgang Fischle
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA and histone modifications direct the functional state of chromatin and thereby the readout of the genome. Candidate approaches and histone peptide affinity purification experiments have identified several proteins that bind to chromatin marks. However, the complement of factors that is recruited by individual and combinations of DNA and histone modifications has not yet been defined. Here, we present a strategy based on recombinant, uniformly modified chromatin templates used in affinity purification experiments in conjunction with SILAC-based quantitative mass spectrometry for this purpose. On the prototypic H3K4me3 and H3K9me3 histone modification marks we compare our method with a histone N-terminal peptide affinity purification approach. Our analysis shows that only some factors associate with both, chromatin and peptide matrices but that a surprisingly large number of proteins differ in their association with these templates. Global analysis of the proteins identified implies specific domains mediating recruitment to the chromatin marks. Our proof-of-principle studies show that chromatin templates with defined modification patterns can be used to decipher how the histone code is read and translated.

Indexed as

Protein Processing, Post-TranslationalAnimalsCell LineChromatinChromatography, AffinityHistonesHumansImmobilized ProteinsIsotope LabelingMethylationMicePeptide FragmentsProtein BindingProtein Interaction MappingProteolysisProteomeChromatinHistonesImmobilized ProteinsPeptide FragmentsProteomeRecombinant Proteins

Identifiers

PMID21836164
PMCPMC3226395
OpenAlexW2146345525

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.