Journal of Biological Chemistry
Volume 297, Issue 5, November 2021, 101336
Research ArticleNaturally occurring cancer-associated mutations disrupt oligomerization and activity of protein arginine methyltransferase 1 (PRMT1)
Under a Creative Commons license
open access
Keywords
arginine methylation
enzyme mutation
molecular dynamics
oligomerization
posttranslational modification (PTM)
structure–function
signaling
dimerization
protein arginine methyltransferase
PRMT1
Abbreviations
AdoMet
S-adenosyl-L-methionine
ADMA
asymmetric dimethylarginine
aMD
accelerated molecular dynamics
AUC
analytical ultracentrifugation
COSMIC
Catalogue of Somatic Mutations in Cancer
hPRMT1
H. sapiens PRMT1
MD
molecular dynamics
MMA
monomethylarginine
NAC
near attack conformation
PRMT
protein arginine methyltransferase
QM
quantum mechanics
rPRMT1
R. norvegicus PRMT1
SDMA
symmetric dimethylarginine
SV
sedimentation velocity
Cited by (0)
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These authors contributed equally to this work.
© 2021 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.