An Investigation of Protein Arginine Methyltransferase 1 Substrate Recognition Through Ribonucleoprotein Modifications

Just as humans need to communicate with each other, our cells have a series of processes that allows them to communicate from one to another. Protein Arginine Methyltransferase I is an enzyme that helps mediate cellular communication by selectively binding to target proteins and performing chemistry that has broad-reaching downstream effects. However, the mechanisms that underly PRMT1 selectivity have yet to be elucidated. This study uses alterations to a series of known targets, called ribonucleoproteins, to identify some of the characteristics that govern recognition by the PRMT1 enzyme. I have made significant progress in the creation, expression, and purification of these targets that can be used to investigate binding to PRMT1.

Publication Details

Journal
Digital Commons - USU (Utah State University)
Published
2024-08-19
DOI
https://doi.org/10.26076/a094-dbd7
Primary Topic
Geology and Paleoclimatology Research
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

An Investigation of Protein Arginine Methyltransferase 1 Substrate Recognition Through Ribonucleoprotein Modifications

Digital Commons - USU (Utah State University)
Geology and Paleoclimatology Research
article

An Investigation of Protein Arginine Methyltransferase 1 Substrate Recognition Through Ribonucleoprotein Modifications

article en

Abstract

Just as humans need to communicate with each other, our cells have a series of processes that allows them to communicate from one to another. Protein Arginine Methyltransferase I is an enzyme that helps mediate cellular communication by selectively binding to target proteins and performing chemistry that has broad-reaching downstream effects. However, the mechanisms that underly PRMT1 selectivity have yet to be elucidated. This study uses alterations to a series of known targets, called ribonucleoproteins, to identify some of the characteristics that govern recognition by the PRMT1 enzyme. I have made significant progress in the creation, expression, and purification of these targets that can be used to investigate binding to PRMT1.

Digital Commons - USU (Utah State University)
Openalex Percentile: Top 57%
Geology and Paleoclimatology Research
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.