Search Results - "Prat, Laure"
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A synthetic tRNA for EF-Tu mediated selenocysteine incorporation in vivo and in vitro
Published in FEBS letters (04-08-2015)“…•A chimera of tRNASer and tRNASec, tRNAUTuX, binds EF-Tu to insert Sec at UAG codons.•tRNAUTuX was used for complete, high fidelity Sec insertion.•We show in…”
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Rewiring Translation for Elongation Factor Tu-Dependent Selenocysteine Incorporation
Published in Angewandte Chemie International Edition (28-01-2013)“…Enjoying UTu in concert: A synthetic tRNA (tRNAUTu) was used as a substrate for three E. coli proteins: seryl‐tRNA synthetase (SerRS) forming Ser‐tRNAUTu,…”
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Physiological Adaptation of Desulfitobacterium hafniense Strain TCE1 to Tetrachloroethene Respiration
Published in Applied and Environmental Microbiology (01-06-2011)“…Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit…”
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Carbon source-dependent expansion of the genetic code in bacteria
Published in Proceedings of the National Academy of Sciences - PNAS (18-12-2012)“…Despite the fact that the genetic code is known to vary between organisms in rare cases, it is believed that in the lifetime of a single cell the code is…”
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Transfer RNA Misidentification Scrambles Sense Codon Recoding
Published in Chembiochem : a European journal of chemical biology (11-10-2013)“…Sense codon recoding is the basis for genetic code expansion with more than two different noncanonical amino acids. It requires an unused (or rarely used)…”
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Reducing the genetic code induces massive rearrangement of the proteome
Published in Proceedings of the National Academy of Sciences - PNAS (02-12-2014)“…Expanding the genetic code is an important aim of synthetic biology, but some organisms developed naturally expanded genetic codes long ago over the course of…”
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An unusual tandem‐domain rhodanese harbouring two active sites identified in Desulfitobacterium hafniense
Published in The FEBS journal (01-08-2012)“…The rhodanese protein domain is common throughout all kingdoms of life and is characterized by an active site cysteine residue that is able to bind sulfane…”
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An unusual tandem-domain rhodanese harbouring two active sites identified in Desulfitobacteriumhafniense
Published in The FEBS journal (01-08-2012)“…The rhodanese protein domain is common throughout all kingdoms of life and is characterized by an active site cysteine residue that is able to bind sulfane…”
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Near‐cognate suppression of amber, opal and quadruplet codons competes with aminoacyl‐tRNA Pyl for genetic code expansion
Published in FEBS letters (02-11-2012)“…Over 300 amino acids are found in proteins in nature, yet typically only 20 are genetically encoded. Reassigning stop codons and use of quadruplet codons…”
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Proteomic analysis of Marinobacter hydrocarbonoclasticus SP17 biofilm formation at the alkane-water interface reveals novel proteins and cellular processes involved in hexadecane assimilation
Published in Research in microbiology (01-12-2009)“…Many hydrocarbon-degrading bacteria form biofilms at the hydrocarbon-water interface to overcome the weak accessibility of these poorly water-soluble…”
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Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion
Published in FEBS letters (02-11-2012)“…► Nonsense suppression by natural amino acids hinders genetic code expansion. ► Higher levels of near-cognate suppression found in opal versus amber codons. ►…”
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Rewiring Translation for Elongation Factor Tu-Dependent Selenocysteine Incorporation
Published in Angewandte Chemie (28-01-2013)“…Eine synthetische tRNA (tRNAUTu) wurde als Substrat für drei E.‐coli‐Proteine verwendet: Seryl‐tRNA‐Synthetase, die Ser‐tRNAUTu bildet,…”
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Rücktitelbild: Rewiring Translation for Elongation Factor Tu-Dependent Selenocysteine Incorporation (Angew. Chem. 5/2013)
Published in Angewandte Chemie (28-01-2013)Get full text
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Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation
Published in Angewandte Chemie (28-01-2013)Get full text
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