Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein

RNA

Volumn 7, Issue 11, 2001, Pages 1531-1542

  Brahms, Hero ^a   Meheus, Lydie ^b   De Brabandere, Veronique ^b   Fischer, Utz ^c   Lührmann, Reinhard ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b INNOGENETICS   (Belgium)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

mRNA decay; Posttranslational modification; Protein arginine methyltransferase (PRMT); Protein sequencing; sDMA; Spinal muscular atrophy (SMA); Spliceosome; UsnRNP

Indexed keywords

ARGININE; CYSTEINE DERIVATIVE; PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN LSM 4; PROTEIN SM; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; BIOGENESIS; CALCULATION; HUMAN; HUMAN CELL; METHYLATION; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN PURIFICATION; SIGNAL TRANSDUCTION; SPINAL MUSCULAR ATROPHY; SPLICEOSOME;

AMINO ACID SEQUENCE; ARGININE; AUTOANTIGENS; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN; CYTOPLASM; HELA CELLS; HUMANS; METHYLATION; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RIBONUCLEOPROTEINS, SMALL NUCLEAR; RNA-BINDING PROTEINS; SPLICEOSOMES;

EID: 0035171131     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S135583820101442X     Document Type: Article

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