Evidence map›Paper›PMID 23319141›Full record

ArticleMolecular & cellular proteomics : MCP2013

The proteomic investigation of chromatin functional domains reveals novel synergisms among distinct heterochromatin components.

Monica Soldi, Tiziana Bonaldi

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

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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

2 authors.

Monica SoldiDepartment of Experimental Oncology, European Institute of Oncology (IEO), Via Adamello 16, Milan, Italy.
Tiziana Bonaldi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromatin is a highly dynamic, well-structured nucleoprotein complex of DNA and proteins that controls virtually all DNA transactions. Chromatin dynamicity is regulated at specific loci by the presence of various associated proteins, histones, post-translational modifications, histone variants, and DNA methylation. Until now the characterization of the proteomic component of chromatin domains has been held back by the challenge of enriching distinguishable, homogeneous regions for subsequent mass spectrometry analysis. Here we describe a modified protocol for chromatin immunoprecipitation combined with quantitative proteomics based on stable isotope labeling by amino acids in cell culture to identify known and novel histone modifications, variants, and complexes that specifically associate with silent and active chromatin domains. Our chromatin proteomics strategy revealed unique functional interactions among various chromatin modifiers, suggesting new regulatory pathways, such as a heterochromatin-specific modulation of DNA damage response involving H2A.X and WICH, both enriched in silent domains. Chromatin proteomics expands the arsenal of tools for deciphering how all the distinct protein components act together to enforce a given region-specific chromatin status.

Indexed as

Adenosine TriphosphatasesAnimalsBlotting, WesternBromodomain Containing ProteinsChromatinChromatin ImmunoprecipitationDNA DamageHeLa CellsHeterochromatinHistonesHumansIsotope LabelingLysineMethylationMiceNIH 3T3 CellsAdenosine TriphosphatasesBAZ1B protein, humanBromodomain Containing ProteinsChromatinH2AX protein, humanHeterochromatinHistonesISWI proteinLysineProteomeTranscription FactorsTyrosine

Identifiers

PMID23319141
PMCPMC3591667

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.