G
Gilbert Richarme
Researcher at University of Paris
Publications - 65
Citations - 2839
Gilbert Richarme is an academic researcher from University of Paris. The author has contributed to research in topics: Chaperone (protein) & Protein folding. The author has an hindex of 28, co-authored 65 publications receiving 2629 citations. Previous affiliations of Gilbert Richarme include Paris Diderot University & Paris Descartes University.
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Chaperone Properties of Bacterial Elongation Factor EF-Tu
TL;DR: It is reported that the Escherichia coli EF-Tu interacts with unfolded and denatured proteins as do molecular chaperones that are involved in protein folding and protein renaturation after stress.
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Parkinsonism-associated Protein DJ-1/Park7 Is a Major Protein Deglycase That Repairs Methylglyoxal- and Glyoxal-glycated Cysteine, Arginine, and Lysine Residues
TL;DR: DJ-1 is the first protein deglycase that repairs proteins from glycation by glyoxals, which constitutes most glycation damage, and is established as a major anti-glycation and anti-aging protein.
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Thermoprotection by glycine betaine and choline
TL;DR: Glycine betaine and choline restore the viability of a dnaK deletion mutant at 42 degrees C, suggesting that glycine Betaine not only acts as a thermoprotectant in vitro, but also acts as an thermoprotsectant for Escherichia coli cells in vivo.
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The FtsJ/RrmJ Heat Shock Protein of Escherichia coli Is a 23 S Ribosomal RNA Methyltransferase *
TL;DR: FtsJ, the first encoded protein of the ftsJ-hflB heat shock operon, is identified as an Escherichia coli methyltransferase of the 23 S rRNA and is renamed RrmJ and its encoding gene,rrmJ, in view of its newly established function.
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Guanine glycation repair by DJ-1/Park7 and its bacterial homologs
Gilbert Richarme,Gilbert Richarme,Cailing Liu,Mouadh Mihoub,Jad Abdallah,Jad Abdallah,Thibaut Léger,Nicolas Joly,Jean-Claude Liebart,Ula V. Jurkunas,Marc Nadal,Philippe Bouloc,Julien Dairou,Aazdine Lamouri +13 more
TL;DR: The parkinsonism-associated protein DJ-1 and its prokaryotic homologs constitute a major nucleotide repair system that is named guanine glycation repair, and is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity.