Evidence map›Paper›PMID 26960207›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Chemical Synthesis of Phosphorylated Histone H2A at Tyr57 Reveals Insight into the Inhibition Mode of the SAGA Deubiquitinating Module.

Muhammad Jbara, Suman Kumar Maity, Michael Morgan, Cynthia Wolberger, Ashraf Brik

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.4field-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

27 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review on the o-Aminoaniline Moiety in Peptide and Protein Chemistry.Chembiochem : a European journal of chemical biology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
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  15. Article
  16. Review
  17. Review
  18. Article
  19. An explorative study towards the chemical synthesis of the immunoglobulin G1 Fc CH3 domain.Journal of peptide science : an official publication of the European Peptide Society · 2018
    Article
  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

5 authors at 3 institutions in 2 countries.

Muhammad JbaraSchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, 3200008, Israel.
Suman Kumar MaitySchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, 3200008, Israel.
Michael MorganDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD, 21205-2185, USA.
Cynthia WolbergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD, 21205-2185, USA. cwolberg@jhmi.edu.
Ashraf BrikSchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, 3200008, Israel. abrik@technion.ac.il.
Technion – Israel Institute of Technology · ILJohns Hopkins Medicine · USJohns Hopkins University · US

Funding

Structure and Function of the SAGA Deubiquitinating ModuleR01GM095822 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOLBERGER, CYNTHIA · 2011 to 2018
$2.7M
NIGMS NIH HHS GM-095822NIGMS NIH HHS R01 GM095822
6 · The paper itself

Abstract

Monoubiquitination of histone H2B plays a central role in transcription activation and is required for downstream histone-methylation events. Deubiquitination of H2B by the Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator complex is regulated by a recently discovered histone mark, phosphorylated H2AY57 (H2AY57p), which inhibits deubiquitination of H2B by the SAGA complex as well as restricting demethylation of H3 and increasing its acetylation. Evidence for the effect of H2AY57p, however, was indirect and was investigated in vivo by monitoring the effects of chemical inhibition of Tyr kinase CK2 or by mutating the phosphorylation site. We applied the total chemical synthesis of proteins to prepare H2AY57p efficiently and study the molecular details of this regulation. This analogue, together with semisynthetically prepared ubiquitinated H2B, enabled us to provide direct evidence for the cross-talk between those two marks and the inhibition of SAGA activity by H2AY57p.

Indexed as

AcetylationAmino Acid SequenceChromatography, High Pressure LiquidHistonesMass SpectrometryPhosphorylationTyrosineUbiquitinHistonesTyrosineUbiquitinchemical protein synthesisdeubiquitinationphosphorylationproteinstotal synthesis

Identifiers

PMID26960207
PMCPMC4944388
OpenAlexW2296541189

What OpenQuestion holds

Textmetadata
LicenceTDM
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.