A remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine

Journal of Biological Chemistry

Volumn 289, Issue 13, 2014, Pages 9320-9327

  Gui, Shanying ^a   Gathiaka, Symon ^b   Li, Jun ^c   Qu, Jun ^c   Acevedo, Orlando ^b   Hevel, Joan M ^a  

^a UTAH STATE UNIVERSITY   (United States)

^b AUBURN UNIVERSITY   (United States)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; METHYLATION; PROTEINS;

ACTIVE SITE RESIDUES; ASYMMETRIC DIMETHYLARGININE; HIGHER-ENERGY BARRIERS; POST-TRANSLATIONAL MODIFICATIONS; PRODUCT SPECIFICITY; PROTEIN ARGININE METHYLTRANSFERASE 1; QUANTUM-MECHANICAL CALCULATION; SYMMETRIC DIMETHYLARGININE;

ARGININE;

6 N,N' DIMETHYLARGININE; METHIONINE; N(G),N(G) DIMETHYLARGININE; PHENYLALANINE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 1; UNCLASSIFIED DRUG; ARGININE; DIMETHYLARGININE; PRMT1 PROTEIN, RAT;

AMINO ACID SUBSTITUTION; ARTICLE; COMPUTER SIMULATION; CONTROLLED STUDY; ENERGY; ENZYME ACTIVE SITE; ENZYME PURIFICATION; ENZYME REGULATION; ENZYME SPECIFICITY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROCESSING; QUANTUM MECHANICS; SYNTHESIS; ANALOGS AND DERIVATIVES; ANIMAL; BIOSYNTHESIS; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR DYNAMICS; MUTATION; RAT; THERMODYNAMICS;

ANIMALS; ARGININE; CATALYTIC DOMAIN; HUMANS; MOLECULAR DYNAMICS SIMULATION; MUTATION; PROTEIN-ARGININE N-METHYLTRANSFERASES; RATS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 84897399262     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.535278     Document Type: Article

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