☰ Chemistry Tree

Richard Giegé

Affiliations:

CNRS, Strasbourg

Area:

structure/function relationships in tRNA

Website:

http://www.icbbe.org/2012/RichardGiege.aspx

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"Richard Giegé"

Mean distance: 7.91

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Parents

Jean-Pierre Ebel	grad student	1972	University Louis Pasteur in Strasbourg
Alexander Rich	post-doc	1973-1974	MIT

Children

Michaël Ryckelynck	grad student	2002-2005	Université Louis Pasteur
Joseph Puglisi	post-doc	1989-1991	Strasbourg

Collaborators

BETA: Related publications

Publications

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Giegé R, Eriani G. (2023) The tRNA identity landscape for aminoacylation and beyond. Nucleic Acids Research. 51: 1528-1570
Bonnet J, Giegé R, Ebel JP. (2019) Lack of specificity in the aminoacyl-tRNA synthetase-catalysed deacylation of aminoacyl-tRNA. Febs Letters. 27: 139-144
Giege R, Kern D, Ebel JP, et al. (2019) Incorrect heterologous aminoacylation of various yeast tRNAS catalysed by E. coli valyl-tRNA synthetase. Febs Letters. 15: 281-285
Stephen P, Ye S, Zhou M, et al. (2018) Structure of Escherichia coli arginyl-tRNA synthetase in complex with tRNA: pivotal role of the D-loop. Journal of Molecular Biology
Giegé R, Springer M. (2016) Aminoacyl-tRNA Synthetases in the Bacterial World. Ecosal Plus. 7
Stephen P, Lin SX, Giegé R. (2015) Interplay between Catalysts and Substrates for Activity of Class Ib Aminoacyl-tRNA Synthetases and Implications for Pharmacology. Current Topics in Medicinal Chemistry
Giegé R, Jühling F, Pütz J, et al. (2012) Structure of transfer RNAs: similarity and variability. Wiley Interdisciplinary Reviews. Rna. 3: 37-61
Bonnefond L, Florentz C, Giegé R, et al. (2008) Decreased aminoacylation in pathology-related mutants of mitochondrial tRNATyr is associated with structural perturbations in tRNA architecture. Rna (New York, N.Y.). 14: 641-8
Bonnefond L, Frugier M, Touzé E, et al. (2007) Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features. Structure (London, England : 1993). 15: 1505-16
Deniziak M, Sauter C, Becker HD, et al. (2007) Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation. Nucleic Acids Research. 35: 1421-31

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