Evidence map›Paper›PMID 34189470›Full record

ArticleSTAR protocols2021

Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics.

Yihang Jing, Zheng Liu, Xiang David Li

Abstract read
In one paragraph

Article in STAR protocols, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Yihang JingDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Zheng LiuDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Xiang David LiDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine succinylation is a recently discovered posttranslational modification that plays critical roles in metabolism, epigenetic signaling, and human diseases. To investigate the effects of site-specific histone lysine succinylation on nucleosome dynamics requires the generation of homogeneously modified histones, which is a significant challenge. Here, we report a protocol for the rapid site-specific installation of a succinyl lysine analog onto histone. We then use a Förster resonance energy transfer approach to characterize the impact on nucleosome dynamics. For complete details on the use and execution of this protocol, please refer to Jing et al. (2018).

Indexed as

Fluorescence Resonance Energy TransferHistonesHumansNucleosomesProtein Processing, Post-TranslationalSuccinic AcidHistonesNucleosomesSuccinic AcidBiophysicsChemistryMolecular BiologyMolecular/Chemical ProbesProtein BiochemistryProtein expression and purification

Identifiers

PMID34189470
PMCPMC8215284

What OpenQuestion holds

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Registered trials

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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.