Evidence map›Paper›PMID 29991262›Full record

ArticleJournal of the American Chemical Society2018

Hydrazide Mimics for Protein Lysine Acylation To Assess Nucleosome Dynamics and Deubiquitinase Action.

Shridhar Bhat, Yousang Hwang, Matthew D Gibson, Michael T Morgan, Sean D Taverna, Yingming Zhao, Cynthia Wolberger, Michael G Poirier, Philip A Cole

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Advances in Proximity-Assisted Bioconjugation.Accounts of chemical research · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. DNAzymes for amine and peptide lysine acylation.Organic & biomolecular chemistry · 2021
    Article
  14. Review
  15. Review
  16. Article
  17. Methods and Applications of Expressed Protein Ligation.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  18. Article
  19. AKTivation mechanisms.Current opinion in structural biology · 2019
    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

9 authors at 4 institutions in 1 country.

Shridhar BhatDepartment of Pharmacology and Molecular Sciences , Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.
Yousang HwangDepartment of Pharmacology and Molecular Sciences , Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.
Matthew D GibsonDepartment of Physics , Ohio State University , Columbus , Ohio 43210 , United States.
Michael T MorganDepartment of Biophysics and Biophysical Chemistry , Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.
Sean D TavernaDepartment of Pharmacology and Molecular Sciences , Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.
Yingming ZhaoBen May Department for Cancer Research , The University of Chicago , Chicago , Illinois 60637 , United States.
Cynthia WolbergerDepartment of Biophysics and Biophysical Chemistry , Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.
Michael G PoirierDepartment of Physics , Ohio State University , Columbus , Ohio 43210 , United States.
Philip A ColeDepartment of Pharmacology and Molecular Sciences , Johns Hopkins University School of Medicine , Baltimore , Maryland 21205 , United States.ORCID 0000-0001-6873-7824
Johns Hopkins University · USThe Ohio State University · USBrigham and Women's Hospital · USUniversity of Chicago · US

Funding

Protein Acylation and Methylation Mechanisms_Administrative SupplementR37GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2013 to 2022
$4.1M
Mechanisms &Inhibition of Histone AcetyltransferasesR01GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2001 to 2012
$3.8M
Structure and Function of the SAGA Deubiquitinating ModuleR01GM095822 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOLBERGER, CYNTHIA · 2011 to 2018
$2.7M
Epigenetic profiling and enzymatic regulation of H3K23me3 during cellular differentiationR01GM118760 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI TAVERNA, SEAN D. · 2017 to 2020
$1.5M
Regulatory Mechanisms of Linker Histones and Their Post-Translational ModificationsR01GM121966 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM062437NIGMS NIH HHS R01 GM095822NIGMS NIH HHS R01 GM118760NIGMS NIH HHS R01 GM121966NIGMS NIH HHS R37 GM062437
6 · The paper itself

Abstract

A range of acyl-lysine (acyl-Lys) modifications on histones and other proteins have been mapped over the past decade but for most, their functional and structural significance remains poorly characterized. One limitation in the study of acyl-Lys containing proteins is the challenge of producing them or their mimics in site-specifically modified forms. We describe a cysteine alkylation-based method to install hydrazide mimics of acyl-Lys post-translational modifications (PTMs) on proteins. We have applied this method to install mimics of acetyl-Lys, 2-hydroxyisobutyryl-Lys, and ubiquityl-Lys that could be recognized selectively by relevant acyl-Lys modification antibodies. The acyl-Lys modified histone H3 proteins were reconstituted into nucleosomes to study nucleosome dynamics and stability as a function of modification type and site. We also installed a ubiquityl-Lys mimic in histone H2B and generated a diubiquitin analog, both of which could be cleaved by deubiquitinating enzymes. Nucleosomes containing the H2B ubiquityl-Lys mimic were used to study the SAGA deubiquitinating module's molecular recognition. These results suggest that acyl-Lys mimics offer a relatively simple and promising strategy to study the role of acyl-Lys modifications in the function, structure, and regulation of proteins and protein complexes.

Indexed as

AlkylationAnimalsAntibodiesBiomimeticsCysteineCysteine EndopeptidasesDeubiquitinating EnzymesEndopeptidasesEscherichia coliHistonesHumansHydrazinesNuclear ProteinsNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAntibodiesCysteineCysteine EndopeptidasesDeubiquitinating EnzymesEndopeptidasesHistonesHydrazinesNuclear ProteinsNucleosomesOTUB1 protein, humanSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin ThiolesteraseUBP10 protein, S cerevisiaeUBP8 protein, S cerevisiae

Identifiers

PMID29991262
PMCPMC6070418
OpenAlexW2834857163

What OpenQuestion holds

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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.