Förster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization

Protein Science

Volumn 19, Issue 11, 2010, Pages 2141-2151

  Thomas, Dylan ^a   Lakowski, Ted M ^a   Pak, Magnolia L ^a   Kim, Jenny J ^a   Frankel, Adam ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Dimerization; F rster resonance energy transfer; Methylation potential; PRMT1; PRMT6

Indexed keywords

ARGININE; CERULEAN; CITRINE FLUORESCENT PROTEIN; METHYL GROUP; MONOMER; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE N METHYLTRANSFERASE 1; PROTEIN ARGININE N METHYLTRANSFERASE 6; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; DIMERIZATION; DISSOCIATION CONSTANT; ENZYME KINETICS; FORSTER RESONANCE ENERGY TRANSFER; MEASUREMENT; METHYLATION; PRIORITY JOURNAL;

DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; KINETICS; LUMINESCENT PROTEINS; MODELS, MOLECULAR; NUCLEAR PROTEINS; PROTEIN-ARGININE N-METHYLTRANSFERASES; RECOMBINANT FUSION PROTEINS; REPRESSOR PROTEINS; S-ADENOSYLHOMOCYSTEINE; S-ADENOSYLMETHIONINE;

EID: 78349299395     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.492     Document Type: Article

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