PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

EMBO Reports

Volumn 3, Issue 3, 2002, Pages 268-273

  Lee, Jaeho ^a   Bedford, Mark T ^a  

^a UNIVERSITY OF TEXAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; HISTONE H3; HORMONE RECEPTOR; HYBRID PROTEIN; MEMBRANE PROTEIN; METHYLTRANSFERASE; PROTEIN P160; S ADENOSYLMETHIONINE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME MECHANISM; ENZYME SUBSTRATE; GENE MAPPING; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN METHYLATION; PROTEIN MOTIF; RNA BINDING; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION; TRANSLATION REGULATION;

AMINO ACID SEQUENCE; HELA CELLS; HUMANS; METHYLATION; MOLECULAR SEQUENCE DATA; POLY(A)-BINDING PROTEINS; PROTEIN-ARGININE N-METHYLTRANSFERASE; RNA-BINDING PROTEINS; SEQUENCE DELETION; SUBSTRATE SPECIFICITY;

EID: 0036205436     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kvf052     Document Type: Article

References (24)

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2. A protein of molecular weight 78 000 bound to the polyadenylate region of eukaryotic messenger RNAs
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13. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
14. TARPP, a novel protein that accompanies TCR gene rearrangement and thymocyte education
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23. Delivering messages from the 3′ end
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