Evidence map›Paper›PMID 25063569›Full record

ArticleMethods (San Diego, Calif.)2014

Generation of nonhydrolyzable ubiquitin-histone mimics.

Lindsey Long, Melonnie Furgason, Tingting Yao

Open access · greenAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

41 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Photocatalytic Diselenide Contraction as a Tool for Site-Selective Isosteric Ubiquitylation.Journal of peptide science : an official publication of the European Peptide Society · 2025
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  17. Review
  18. Generation and Characterization of Site-Specifically Mono-Ubiquitylated p53.Chembiochem : a European journal of chemical biology · 2022
    Article
  19. 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

3 authors at 1 institution in 1 country.

Lindsey LongDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, United States.
Melonnie FurgasonDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, United States.
Tingting YaoDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, United States. Electronic address: Tingting.Yao@ColoState.edu.
Colorado State University · US

Funding

Regulation of a Deubiquitinating Enzyme in Proteolysis and Chromatin RemodelingR01GM098401 · NIGMS · COLORADO STATE UNIVERSITY · PI YAO, TINGTING · 2011 to 2021
$2.9M
NIGMS NIH HHS R01 GM098401NIGMS NIH HHS R01GM098401
6 · The paper itself

Abstract

Histone proteins undergo various types of post-translational modifications (PTMs) to regulate dynamic processes in the cell, including replication, transcription and DNA damage repair. One type of histone PTM is the attachment of a small protein, ubiquitin (Ub). In eukaryotic organisms, a single Ub is attached to specific lysine residues of histones H2A and H2B in a modification that, unlike many other forms of ubiquitination in the cell, does not signal degradation. Instead, both attachment and removal of Ub to these histones has been shown to affect gene transcription, pre-mRNA splicing, and DNA damage repair, but the mechanisms by which histone ubiquitination governs these processes are not well understood. In an effort to identify "readers" of Ub-histones, we developed a straightforward crosslinking strategy to generate nonhydrolyzable Ub-histone mimics. These mimics were assembled into Ub-histone-containing dimers or nucleosomes. We demonstrate that they can be used in pulldown assays to identify proteins that differentiate unmodified and ubiquitinated histones.

Indexed as

HistonesProtein EngineeringRecombinant ProteinsUbiquitinUbiquitinationHistonesRecombinant ProteinsUbiquitinEffector proteinsHistone modificationUbiquitin

Identifiers

PMID25063569
PMCPMC4268123
OpenAlexW2076783632

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.