Evidence map›Paper›PMID 34443661›Full record

ArticleMolecules (Basel, Switzerland)2021

Photoregulation of PRMT-1 Using a Photolabile Non-Canonical Amino Acid.

Elizabeth A King, Emily M Peairs, Diya M Uthappa, Jordan K Villa, Cameron M Goff, Naya K Burrow, Rebecca T Deitch, Anna K Martin, Douglas D Young

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 56% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
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

9 authors at 1 institution in 1 country.

Elizabeth A KingDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.
Emily M PeairsDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.ORCID 0000-0001-6809-0565
Diya M UthappaDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.ORCID 0000-0003-2233-2295
Jordan K VillaDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.
Cameron M GoffDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.ORCID 0000-0002-4162-4659
Naya K BurrowDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.
Rebecca T DeitchDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.
Anna K MartinDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.ORCID 0000-0003-3011-6410
Douglas D YoungDepartment of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA.ORCID 0000-0003-4433-4101
William & Mary · US

Funding

Bioconjugations Employing Unnatural Amino AcidsR15GM113203 · NIGMS · COLLEGE OF WILLIAM AND MARY · PI YOUNG, DOUGLAS · 2016 to 2025
$1.0M
NIGMS NIH HHS R15 GM113203NIH HHS R15GM113203
6 · The paper itself

Abstract

Protein methyltransferases are vital to the epigenetic modification of gene expression. Thus, obtaining a better understanding of and control over the regulation of these crucial proteins has significant implications for the study and treatment of numerous diseases. One ideal mechanism of protein regulation is the specific installation of a photolabile-protecting group through the use of photocaged non-canonical amino acids. Consequently, PRMT1 was caged at a key tyrosine residue with a nitrobenzyl-protected Schultz amino acid to modulate protein function. Subsequent irradiation with UV light removes the caging group and restores normal methyltransferase activity, facilitating the spatial and temporal control of PRMT1 activity. Ultimately, this caged PRMT1 affords the ability to better understand the protein's mechanism of action and potentially regulate the epigenetic impacts of this vital protein.

Indexed as

Amino AcidsAmino Acid SequenceEpigenesis, GeneticGene ExpressionHumansMethylationProtein-Arginine N-MethyltransferasesProtein MethyltransferasesRepressor ProteinsTranscription FactorsTyrosineUltraviolet RaysAmino AcidsPRMT1 protein, humanProtein-Arginine N-MethyltransferasesProtein MethyltransferasesRepressor ProteinsTranscription FactorsTyrosinenon-canonical amino acidphotoactivationprotein methylation

Identifiers

PMID34443661
PMCPMC8398576
OpenAlexW3194898562

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.