H
Henri Grosjean
Researcher at University of Paris
Publications - 6
Citations - 1308
Henri Grosjean is an academic researcher from University of Paris. The author has contributed to research in topics: Transfer RNA & RNA. The author has an hindex of 6, co-authored 6 publications receiving 1188 citations. Previous affiliations of Henri Grosjean include Adam Mickiewicz University in Poznań & University of Mainz.
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Journal ArticleDOI
MODOMICS: a database of RNA modification pathways—2013 update
Magdalena A. Machnicka,Kaja Milanowska,Okan Osman Oglou,Elzbieta Purta,Malgorzata Kurkowska,Anna Olchowik,Witold Januszewski,Sebastian Kalinowski,Stanislaw Dunin-Horkawicz,Kristian M. Rother,Mark Helm,Janusz M. Bujnicki,Henri Grosjean +12 more
TL;DR: New features are included: a census of human and yeast snoRNAs involved in RNA-guided RNA modification, a new section covering the 5′-end capping process, and a catalogue of ‘building blocks’ for chemical synthesis of a large variety of modified nucleosides.
Journal ArticleDOI
MODOMICS: a database of RNA modification pathways. 2008 update
Anna Czerwoniec,Stanislaw Dunin-Horkawicz,Elzbieta Purta,Katarzyna Kamińska,Joanna M. Kasprzak,Janusz M. Bujnicki,Henri Grosjean,Kristian Rother +7 more
TL;DR: In addition to the previously available manually curated tRNA sequences from a few model organisms, MODOMICS has now included additional tRNAs and rRNAs, and all RNAs with 3D structures in the Nucleic Acid Database, in which modified nucleosides are present.
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Distribution and frequencies of post-transcriptional modifications in tRNAs
TL;DR: This work presents a new tool, tRNAmodviz web server, for easy comparative analysis and visualization of modification patterns in individual tRNAs, as well as in groups of selected tRNA sequences.
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Effect of a quaternary pentamine on RNA stabilization and enzymatic methylation.
TL;DR: In post-transcriptional in vitro methylation reactions, the formation of m2G/m2 2G by the methyltransferase Trm1p and of m1A by TrmIp were not affected or only slightly stimulated by polyamines.
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Crystal Structure and Mutational Study of a Unique SpoU Family Archaeal Methylase that Forms 2′-O-Methylcytidine at Position 56 of tRNA
TL;DR: The crystal structure of Pyrococcus horikoshii aTrm56 complexed with S-adenosyl-L-methionine at 2.48 A resolution is determined and it is shown that a Trm56 prefers the L-shaped tRNA to the lambda form as its substrate.