Evidence map›Paper›PMID 25863817›Full record

ArticleTopics in current chemistry2015

Chemical and biological tools for the preparation of modified histone proteins.

Cecil J Howard, Ruixuan R Yu, Miranda L Gardner, John C Shimko, Jennifer J Ottesen

Abstract read
In one paragraph

Article in Topics in current chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

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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 1 institution in 1 country.

Cecil J HowardDepartment of Chemistry and Biochemistry and The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH, 43210, USA.
Ruixuan R Yu
Miranda L Gardner
John C Shimko
Jennifer J Ottesen
The Ohio State University · US

Funding

Mechanisms of Chromatin Transcriptional RegulationR01GM083055 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2008 to 2016
$2.7M
NIGMS NIH HHS R01 GM083055
6 · The paper itself

Abstract

Eukaryotic chromatin is a complex and dynamic system in which the DNA double helix is organized and protected by interactions with histone proteins. This system is regulated through a large network of dynamic post-translational modifications (PTMs) which ensure proper gene transcription, DNA repair, and other processes involving DNA. Homogenous protein samples with precisely characterized modification sites are necessary to understand better the functions of modified histone proteins. Here, we discuss sets of chemical and biological tools developed for the preparation of modified histones, with a focus on the appropriate choice of tool for a given target. We start with genetic approaches for the creation of modified histones, including the incorporation of genetic mimics of histone modifications, chemical installation of modification analogs, and the use of the expanded genetic code to incorporate modified amino acids. We also cover the chemical ligation techniques which have been invaluable in the generation of complex modified histones indistinguishable from their natural counterparts. We end with a prospectus on future directions.

Indexed as

Chemistry Techniques, SyntheticChromatinEukaryotaGene Expression RegulationHistonesModels, MolecularProtein ConformationProtein EngineeringChromatinHistones

Identifiers

PMID25863817
PMCPMC4889135
OpenAlexW235893883

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.