Evidence map›Paper›PMID 37524235›Full record

ArticleMethods (San Diego, Calif.)2023

Advances in direct detection of lysine methylation and acetylation by nuclear magnetic resonance using

Olivia A Fraser, Kevin E W Namitz, Scott A Showalter

Open access · hybridAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 41% 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

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Article
  2. Acetylation-Dependent Compaction of the Histone H4 Tail Ensemble.The journal of physical chemistry. B · 2024
    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.

Olivia A FraserCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, United States.
Kevin E W NamitzDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802, United States.
Scott A ShowalterCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, United States; Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, United States. Electronic address: sas76@psu.edu.
Pennsylvania State University · US

Funding

Eukaryotic Gene Regulation (EGR) Predoctoral Training ProgramT32GM125592 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI REESE, JOSEPH C · 2018 to 2022
$920k
Acetyllysine Structure-Function Analysis by 13C Direct-Detect NMR SpectroscopyR21GM137129 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI SHOWALTER, SCOTT A · 2020 to 2021
$416k
NIGMS NIH HHS R21 GM137129NIGMS NIH HHS T32 GM125592
6 · The paper itself

Abstract

Post-translational modifications (PTMs) are reversible chemical modifications that can modulate protein structure and function. Methylation and acetylation are two such PTMs with integral and well-characterized biological roles, including modulation of chromatin structure; and unknown or poorly understood roles, exemplified by the influence of these PTMs on transcription factor structure and function. The need for biological insights into the function of these PTMs motivates the development of a nondestructive and label-free method that enables pursuit of molecular mechanisms. Here, we present a protocol for implementing nuclear magnetic resonance (NMR) methods that allow for unambiguous detection of methylation and acetylation events and demonstrate their utility by observing these marks on histone H3 tail as a model system. We leverage strategic isotopic enrichment of cofactor and peptide for visualization by [

Indexed as

LysineProtein Processing, Post-TranslationalAcetylationMagnetic Resonance SpectroscopyMethylationLysineAcetylationHistoneMethylationNuclear magnetic resonancePost-translational modification

Identifiers

PMID37524235
PMCPMC10528339
OpenAlexW4385383052

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.