A proteomic analysis of arginine-methylated protein complexes.
about
Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implicationsArginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA bindingRibosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginineFriend of Prmt1, a novel chromatin target of protein arginine methyltransferasesAccurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometryThe histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteinsProtein arginine methylation during lytic adenovirus infectionAnalysis of a noncanonical poly(A) site reveals a tripartite mechanism for vertebrate poly(A) site recognitionMethylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expressionArginine methylation of the human immunodeficiency virus type 1 Tat protein by PRMT6 negatively affects Tat Interactions with both cyclin T1 and the Tat transactivation regionPRMT6 diminishes HIV-1 Rev binding to and export of viral RNASPOC: a widely distributed domain associated with cancer, apoptosis and transcriptionIdentification of a SmD3 epitope with a single symmetrical dimethylation of an arginine residue as a specific target of a subpopulation of anti-Sm antibodies.The Role of Oxygen Sensors, Hydroxylases, and HIF in Cardiac Function and DiseaseCurrent chemical biology approaches to interrogate protein methyltransferasesStructural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteinsA selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL modelsDidehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane FormationProteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signalingSMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control terminationIdentifying and quantifying in vivo methylation sites by heavy methyl SILACProtein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylationThe roles of post-translational modifications in the context of protein interaction networksProtein arginine methylation in mammals: who, what, and whyMethylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity.Thrombospondin-1 is a transcriptional repression target of PRMT6.Protein post-translational modifications: In silico prediction tools and molecular modeling.Approaches to measuring the activities of protein arginine N-methyltransferasesArginine methylation of vasa protein is conserved across phylaArginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control.iMethyl-PseAAC: identification of protein methylation sites via a pseudo amino acid composition approachActivation of nuclear receptor coactivator PGC-1alpha by arginine methylationTopology of splicing and snRNP biogenesis in dinoflagellate nuclei.Arginine methylation in subunits of mammalian pre-mRNA cleavage factor I.Complications in the assignment of 14 and 28 Da mass shift detected by mass spectrometry as in vivo methylation from endogenous proteins.Emerging technologies to map the protein methylome.
P2860
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P2860
A proteomic analysis of arginine-methylated protein complexes.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
A proteomic analysis of arginine-methylated protein complexes.
@en
A proteomic analysis of arginine-methylated protein complexes.
@nl
type
label
A proteomic analysis of arginine-methylated protein complexes.
@en
A proteomic analysis of arginine-methylated protein complexes.
@nl
prefLabel
A proteomic analysis of arginine-methylated protein complexes.
@en
A proteomic analysis of arginine-methylated protein complexes.
@nl
P2093
P2860
P1476
A proteomic analysis of arginine-methylated protein complexes.
@en
P2093
François-Michel Boisvert
Marie-Chloé Boulanger
Stéphane Richard
P2860
P304
P356
10.1074/MCP.M300088-MCP200
P50
P577
2003-10-07T00:00:00Z