Evidence map›Paper›PMID 35761047›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Preparation of Site-Specific Succinylated Histone Mimics to Investigate Its Impact on Nucleosome Dynamics.

Yihang Jing, Zheng Liu, Xiang David Li

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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
0.5field-weighted citation impact, top 40% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

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 at 1 institution in 1 country.

Yihang JingDepartment of Chemistry, The University of Hong Kong, Hong Kong, P. R. China.
Zheng LiuDepartment of Chemistry, The University of Hong Kong, Hong Kong, P. R. China.
Xiang David LiDepartment of Chemistry, The University of Hong Kong, Hong Kong, P. R. China. xiangli@hku.hk.
University of Hong Kong · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Posttranslational modifications (PTMs) of histones have been demonstrated to be the key regulating mechanism of nucleosome dynamics and chromatin structure. Lysine succinylation is a recently discovered PTM that plays critical roles in metabolism, epigenetic signaling, and is correlated with several diseases. One significant challenge in studying the effects of this modification on nucleosome dynamics is to obtain site-specifically modified histones. Here, we report the rapid site-specific incorporation of a succinylation mimic into histones, which facilitates the characterization of its impact on nucleosome dynamics with a Förster resonance energy transfer (FRET) approach.

Indexed as

HistonesNucleosomesFluorescence Resonance Energy TransferLysineProtein Processing, Post-TranslationalHistonesLysineNucleosomesChromatin structureHistone succinylationNucleosome dynamicsProtein chemistryProtein labeling

Identifiers

PMID35761047
OpenAlexW4285307507

What OpenQuestion holds

Textmetadata
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.