Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function.
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The Role of Protein Arginine Methyltransferases in Inflammatory ResponsesFunctional insights from structures of coactivator-associated arginine methyltransferase 1 domainsCrystal Structure of the Plant Epigenetic Protein Arginine Methyltransferase 10Effects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine productionProtein arginine methylation in mammals: who, what, and whyUnique Features of Human Protein Arginine Methyltransferase 9 (PRMT9) and Its Substrate RNA Splicing Factor SF3B2Identification and characterization of new molecular partners for the protein arginine methyltransferase 6 (PRMT6).Chemical biology of protein arginine modifications in epigenetic regulationThe HPV E6 oncoprotein targets histone methyltransferases for modulating specific gene transcription.Protein Arginine Methylation and Citrullination in Epigenetic RegulationNovel functions of protein arginine methyltransferase 1 in thyroid hormone receptor-mediated transcription and in the regulation of metamorphic rate in Xenopus laevis.Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulationAutomethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivityPRMT1 and PRMT8 regulate retinoic acid-dependent neuronal differentiation with implications to neuropathology.Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana.Novel inhibitors for PRMT1 discovered by high-throughput screening using activity-based fluorescence polarization.Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis.Alternative splicing of CNOT7 diversifies CCR4-NOT functions.Differential interaction of PRMT1 with RGG-boxes of the FET family proteins EWS and TAF15.A novel splicing isoform of protein arginine methyltransferase 1 (PRMT1) that lacks the dimerization arm and correlates with cellular malignancy.Intricate Effects of α-Amino and Lysine Modifications on Arginine Methylation of the N-Terminal Tail of Histone H4.
P2860
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P2860
Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Surface-scanning mutational an ...... ion, and coactivator function.
@ast
Surface-scanning mutational an ...... ion, and coactivator function.
@en
type
label
Surface-scanning mutational an ...... ion, and coactivator function.
@ast
Surface-scanning mutational an ...... ion, and coactivator function.
@en
prefLabel
Surface-scanning mutational an ...... ion, and coactivator function.
@ast
Surface-scanning mutational an ...... ion, and coactivator function.
@en
P2093
P2860
P356
P1476
Surface-scanning mutational an ...... ion, and coactivator function.
@en
P2093
Daniel Purcell
David Y Lee
Irina Ianculescu
Michael R Stallcup
Xiaodong Cheng
Xing Zhang
P2860
P304
P356
10.1210/ME.2006-0389
P577
2007-04-10T00:00:00Z