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FEBS Letters|November 17, 2009
Processivity of translation in the eukaryote cell: role of aminoacyl-tRNA synthetasesMarc MirandeBiochemistry|August 16, 2006
Identity elements for specific aminoacylation of a tRNA by mammalian lysyl-tRNA synthetase bearing a nonspecific tRNA-interacting factorMathilde Francin, Marc MirandeThe Journal of Biological Chemistry|November 6, 2002
Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetaseMathilde Francin, Marc MirandeBiochemistry|December 14, 2005
Determinants in tRNA for activation of arginyl-tRNA synthetase: evidence that tRNA flexibility is required for the induced-fit mechanismLudovic Guigou, Marc MirandeInternational Journal of Molecular Sciences|March 26, 2015
Aminoacyl-tRNA synthetase complexes in evolutionSvitlana Havrylenko, Marc MirandeMolecular and Cellular Biochemistry|November 30, 2006
Arc1p is required for cytoplasmic confinement of synthetases and tRNAMarie-Pierre Golinelli-Cohen, Marc MirandeBiochemistry|April 14, 2004
The tRNA-interacting factor p43 associates with mammalian arginyl-tRNA synthetase but does not modify its tRNA aminoacylation propertiesLudovic Guigou, Vyacheslav Shalak, Marc MirandeBiochemistry|September 25, 2009
Translation initiation from two in-frame AUGs generates mitochondrial and cytoplasmic forms of the p43 component of the multisynthetase complexVyacheslav Shalak, Monika Kaminska, Marc MirandeThe Journal of Biological Chemistry|November 14, 2001
The N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domainMathilde Francin, Monika Kaminska, Pierre Kerjan, et al.Pageof 4