Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src

Journal of Biological Chemistry

Volumn 281, Issue 16, 2006, Pages 11115-11125

  Ostareck Lederer, Antje ^a   Ostareck, Dirk H ^a   Rucknagel, Karl P ^b   Schierhorn, Angelika ^a   Moritz, Bodo ^a   Huttelmaier, Stefan ^a   Flach, Nadine ^a   Handoko, Lusy ^c   Wahle, Elmar ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

^c UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL CULTURE; CHEMICAL MODIFICATION; DEGRADATION; MASS SPECTROMETRY; RNA; SUBSTITUTION REACTIONS;

ARGININE; METHYLATION; PHOSPHORYLATION; RNA-BINDING ACTIVITY;

PROTEINS;

ANTIBODY; ARGININE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 1; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; TYROSINE KINASE C SRC; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; HELA CELL; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; MASS SPECTROMETRY; METHYLATION; PLASMID; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PURIFICATION; RNA BINDING;

AMINO ACID SEQUENCE; ARGININE; DNA METHYLATION; DOSE-RESPONSE RELATIONSHIP, DRUG; EMBRYO; ETHANOLAMINES; HELA CELLS; HETEROGENEOUS-NUCLEAR RIBONUCLEOPROTEIN K; HUMANS; MASS SPECTROMETRY; METHYLATION; MICROSCOPY, FLUORESCENCE; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PLASMIDS; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; PROTEIN INTERACTION MAPPING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; PROTEIN-ARGININE N-METHYLTRANSFERASE; PROTEIN-TYROSINE KINASES; RECOMBINANT PROTEINS; REPRESSOR PROTEINS; RNA; SEPHAROSE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STEM CELLS; TRANSCRIPTION, GENETIC; TRANSFECTION;

EID: 33744948703     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M513053200     Document Type: Article

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