Evidence map›Paper›PMID 26831069›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Streamlined discovery of cross-linked chromatin complexes and associated histone modifications by mass spectrometry.

Barry M Zee, Artyom A Alekseyenko, Kyle A McElroy, Mitzi I Kuroda

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. An E2 ubiquitin-conjugating enzyme links diubiquitinated H2B to H3K27M oncohistone function.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Variant Polycomb complexes inScience advances · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. G3 (Bethesda, Md.) · 2017
    Article
  11. Article
  12. Article
  13. 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

4 authors.

Barry M ZeeDivision of Genetics, Brigham and Women's Hospital, Boston, MA 02115; Department of Genetics, Harvard Medical School, Boston, MA 02115;
Artyom A AlekseyenkoDivision of Genetics, Brigham and Women's Hospital, Boston, MA 02115; Department of Genetics, Harvard Medical School, Boston, MA 02115;
Kyle A McElroyDivision of Genetics, Brigham and Women's Hospital, Boston, MA 02115; Department of Genetics, Harvard Medical School, Boston, MA 02115; Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138.
Mitzi I KurodaDivision of Genetics, Brigham and Women's Hospital, Boston, MA 02115; Department of Genetics, Harvard Medical School, Boston, MA 02115; mkuroda@genetics.med.harvard.edu.

Funding

Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
Molecular Genetics of Dosage Compensation in DrosophilaR37GM045744 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI KURODA, MITZI I · 2004 to 2013
$3.7M
Comprehensive analysis of epigenetic regulators in their native chromatin contextR01GM101958 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI KURODA, MITZI I · 2012 to 2018
$2.4M
MOLECULAR GENETICS OF DOSAGE COMPENSATION IN DROSOPHILAR01GM045744 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI KURODA, MITZI I · 1991 to 2017
$2.3M
NIGMS NIH HHS GM101958NIGMS NIH HHS GM45744NIGMS NIH HHS R01 GM045744NIGMS NIH HHS R01 GM101958NIGMS NIH HHS R37 GM045744NIGMS NIH HHS T32 GM007598
6 · The paper itself

Abstract

Posttranslational modifications (PTMs) are key contributors to chromatin function. The ability to comprehensively link specific histone PTMs with specific chromatin factors would be an important advance in understanding the functions and genomic targeting mechanisms of those factors. We recently introduced a cross-linked affinity technique, BioTAP-XL, to identify chromatin-bound protein interactions that can be difficult to capture with native affinity techniques. However, BioTAP-XL was not strictly compatible with similarly comprehensive analyses of associated histone PTMs. Here we advance BioTAP-XL by demonstrating the ability to quantify histone PTMs linked to specific chromatin factors in parallel with the ability to identify nonhistone binding partners. Furthermore we demonstrate that the initially published quantity of starting material can be scaled down orders of magnitude without loss in proteomic sensitivity. We also integrate hydrophilic interaction chromatography to mitigate detergent carryover and improve liquid chromatography-mass spectrometric performance. In summary, we greatly extend the practicality of BioTAP-XL to enable comprehensive identification of protein complexes and their local chromatin environment.

Indexed as

AnimalsChromatinChromatography, LiquidDrosophilaHistonesHumansMass SpectrometryProteomicsChromatinHistonesaffinity pulldownBioTAP-XLchromatin complexeshistone modificationsliquid chromatography-mass spectrometry

Identifiers

PMID26831069
PMCPMC4763777

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.