Evidence map›Paper›PMID 30850047›Full record

ArticleMethods in enzymology2019

Semisynthesis of ubiquitinated histone H2B with a native or nonhydrolyzable linkage.

Michael Morgan, Muhammad Jbara, Ashraf Brik, Cynthia Wolberger

Abstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Multistate structures of the MLL1-WRAD complex bound to H2B-ubiquitinated nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
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 2 countries.

Michael MorganDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, United States.
Muhammad JbaraSchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, Israel.
Ashraf BrikSchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, Israel.
Cynthia WolbergerDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, United States. Electronic address: cwolberg@jhmi.edu.
Johns Hopkins Medicine · USTechnion – Israel Institute of Technology · IL

Funding

Mechanistic studies of chromatin modification in transcription regulationR35GM130393 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Cynthia Wolberger · 2019 to 2026
$7.3M
Structure and Function of the SAGA Deubiquitinating ModuleR01GM095822 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOLBERGER, CYNTHIA · 2011 to 2018
$2.7M
NIGMS NIH HHS R01 GM095822NIGMS NIH HHS R35 GM130393
6 · The paper itself

Abstract

Posttranslational modifications of histone proteins regulate all biological processes requiring access to DNA. Monoubiquitination of histone H2B is a mark of actively transcribed genes in all eukaryotes that also plays a role in DNA replication and repair. Solution and structural studies of the mechanism by which histone ubiquitination modulates these processes depend on the ability to generate homogeneous preparations of nucleosomes containing ubiquitin conjugated to a specific lysine residue. We describe here methods for generating milligram quantities of histone H2B with ubiquitin (Ub) conjugated to Lys 120 via either a nonhydrolyzable, dichloroacetone linkage or a cleavable isopeptide bond. H2B-Ub with an isopeptide linkage is generated by a combination of intein-fusion protein derivatization and native chemical ligation, yielding a fully native ubiquitinated lysine that can be cleaved by Ub isopeptidases. We also describe how to reconstitute nucleosomes containing ubiquitinated H2B.

Indexed as

Xenopus laevisAnimalsHistonesHydrolysisLysineModels, MolecularUbiquitinUbiquitinationXenopus ProteinsHistonesLysineUbiquitinXenopus ProteinsChromatinHistone modificationsInteinUbiquitin

Identifiers

PMID30850047
PMCPMC6917205
OpenAlexW2915788694

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.