[HTML][HTML] Arginine metabolism in myeloid cells shapes innate and adaptive immunity
PC Rodriguez, AC Ochoa, AA Al-Khami - Frontiers in immunology, 2017 - frontiersin.org
Arginine metabolism has been a key catabolic and anabolic process throughout the
evolution of the immune response. Accruing evidence indicates that arginine-catabolizing …
evolution of the immune response. Accruing evidence indicates that arginine-catabolizing …
[HTML][HTML] Protein arginine methylation in mammals: who, what, and why
MT Bedford, SG Clarke - Molecular cell, 2009 - cell.com
The covalent marking of proteins by methyl group addition to arginine residues can promote
their recognition by binding partners or can modulate their biological activity. A small family …
their recognition by binding partners or can modulate their biological activity. A small family …
[HTML][HTML] Histone arginine methylation
A Di Lorenzo, MT Bedford - FEBS letters, 2011 - Elsevier
Arginine methylation is a common posttranslational modification (PTM). This type of PTM
occurs on both nuclear and cytoplasmic proteins, and is particularly abundant on shuttling …
occurs on both nuclear and cytoplasmic proteins, and is particularly abundant on shuttling …
[HTML][HTML] TDRD3 is an effector molecule for arginine-methylated histone marks
Specific sites of histone tail methylation are associated with transcriptional activity at gene
loci. These methyl marks are interpreted by effector molecules, which harbor protein …
loci. These methyl marks are interpreted by effector molecules, which harbor protein …
The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans
SS Wolf - Cellular and molecular life sciences, 2009 - Springer
Abstract Information about the family of protein arginine methyltransferases (PRMTs) has
been growing rapidly over the last few years and the emerging role of arginine methylation …
been growing rapidly over the last few years and the emerging role of arginine methylation …
A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation
Abstract Protein arginine methyltransferase 1 (PRMT1) is the major enzyme that generates
monomethylarginine and asymmetrical dimethylarginine. We report here a conditional null …
monomethylarginine and asymmetrical dimethylarginine. We report here a conditional null …
The role of protein arginine methyltransferases in inflammatory responses
Protein arginine methyltransferases (PRMTs) mediate the methylation of a number of protein
substrates of arginine residues and serve critical functions in many cellular responses …
substrates of arginine residues and serve critical functions in many cellular responses …
Human protein arginine methyltransferases in vivo–distinct properties of eight canonical members of the PRMT family
F Herrmann, P Pably, C Eckerich… - Journal of cell …, 2009 - journals.biologists.com
Methylation of arginine residues is a widespread post-translational modification of proteins
catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the …
catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the …
The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation
TB Nicholson, T Chen, S Richard - Pharmacological research, 2009 - Elsevier
Post-translational modifications are well-known effectors in DNA damage signaling and
epigenetic gene expression. Protein arginine methylation is a covalent modification that …
epigenetic gene expression. Protein arginine methylation is a covalent modification that …
PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential
WJ Shia, AJ Okumura, M Yan… - Blood, The Journal …, 2012 - ashpublications.org
Fusion protein AML1-ETO, resulting from t (8; 21) translocation, is highly related to leukemia
development. It has been reported that full-length AML1-ETO blocks AML1 function and …
development. It has been reported that full-length AML1-ETO blocks AML1 function and …