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Structure (London, England : 1993)|December 17, 2009
E pluribus tres: the 2009 nobel prize in chemistryCharles W CarterThe Journal of Biological Chemistry|September 12, 2014
Urzymology: experimental access to a key transition in the appearance of enzymesCharles W CarterStructure (London, England : 1993)|October 17, 2007
A conformational transition state accompanies tryptophan activation by B. stearothermophilus tryptophanyl-tRNA synthetaseMaryna Kapustina, Violetta Weinreb, Li Li, et al.Structural Dynamics (Melville, N.Y.)|February 14, 2017
Combining multi-mutant and modular thermodynamic cycles to measure energetic coupling networks in enzyme catalysisCharles W Carter, Srinivas Niranj Chandrasekaran, Violetta Weinreb, et al.ACS Chemical Biology|March 24, 2016
An Ancestral Tryptophanyl-tRNA Synthetase Precursor Achieves High Catalytic Rate Enhancement without Ordered Ground-State Tertiary StructuresPaul J Sapienza, Li Li, Tishan Williams, et al.Structure (London, England : 1993)|July 17, 2009
Mg2+-assisted catalysis by B. stearothermophilus TrpRS is promoted by allosteric effectsVioletta Weinreb, Li Li, Cassandra L Campbell, et al.RNA Biology|November 24, 2015
tRNA acceptor-stem and anticodon bases embed separate features of amino acid chemistryCharles W Carter, Richard WolfendenJournal of Molecular Biology|September 5, 2006
Computational studies of tryptophanyl-tRNA synthetase: activation of ATP by induced-fitMaryna Kapustina, Charles W CarterProceedings of the National Academy of Sciences of the United States of America|June 3, 2015
tRNA acceptor stem and anticodon bases form independent codes related to protein foldingCharles W Carter, Richard WolfendenJournal of the American Chemical Society|January 5, 2008
Mg2+-free Bacillus stearothermophilus tryptophanyl-tRNA synthetase retains a major fraction of the overall rate enhancement for tryptophan activationVioletta Weinreb, Charles W CarterPageof 2,815