about
RNA recognition by double-stranded RNA binding domains: a matter of shape and sequenceCrystal structure of Thermus thermophilus tRNA m1A58 methyltransferase and biophysical characterization of its interaction with tRNAA unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesisAn extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast DicerSolution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNAA bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topologyThe m1A(58) modification in eubacterial tRNA: An overview of tRNA recognition and mechanism of catalysis by TrmIComparative analyses of the thermodynamic RNA binding signatures of different types of RNA recognition motifs.Dynamics of linker residues modulate the nucleic acid binding properties of the HIV-1 nucleocapsid protein zinc fingersStructural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditionsThe Interaction between tRNA(Lys) 3 and the primer activation signal deciphered by NMR spectroscopy.ADAR proteins: double-stranded RNA and Z-DNA binding domains.RNAi keeps Atf1-bound stress response genes in check at nuclear poresFunctions of double-stranded RNA-binding domains in nucleocytoplasmic transportAdvances in the structural understanding of Vif proteinsInitiation of HIV-1 reverse transcription and functional role of nucleocapsid-mediated tRNA/viral genome interactions.m1A Post-Transcriptional Modification in tRNAsTandem hnRNP A1 RNA recognition motifs act in concert to repress the splicing of survival motor neuron exon 7.Backbone resonance assignments of the m1A22 tRNA methyltransferase TrmK from Bacillus subtilisNew insights into the formation of HIV-1 reverse transcription initiation complexModulation of the HIV nucleocapsid dynamics finely tunes its RNA-binding properties during virion genesisStructural characterization of B. subtilis m1A22 tRNA methyltransferase TrmK: insights into tRNA recognitionMolecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2Bisubstrate analogues as structural tools to investigate m6A methyltransferase active sites.A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins1H, 15N chemical shift assignments of the imino groups of yeast tRNAPhe: influence of the post-transcriptional modificationsTime-resolved NMR monitoring of tRNA maturationTo be or not to be modified: Miscellaneous aspects influencing nucleotide modifications in tRNAsDesign of cross-linked RNA/protein complexes for structural studies
P50
Q27023888-AC3B277B-D55A-463D-9BBC-A864EC5CE7EEQ27649825-DA0EA83D-6EE1-44CB-BA77-12DA0597F867Q27651334-F13D5E6C-33F4-493A-9C0D-14AF2DEA93E2Q27671800-D175DB06-187F-4FD7-8EB6-E625F9796738Q27676498-C55E02AB-4EA8-4720-A2C0-004F28605345Q27683503-6269AE74-6391-4364-81C9-A43B3B7BE6D6Q27683612-829E173E-2356-45CF-9CFA-FB12DA75E984Q27701577-45AABB05-6261-4E46-B69B-7EDC60FD42A8Q33741058-9F9D828E-A38E-4D25-80BF-D94B620DB069Q33910275-F6AD5E18-94A1-43C9-A7AF-D0B561DC3BE8Q34100973-E441B758-D340-4E4F-B8BA-1E7C5FB0E082Q34769447-D73EA496-14E0-4E58-82E7-F2B67B23B16CQ35578834-64A8C92E-8143-4778-ADCE-43649474E941Q35882142-BBB91AF6-D459-44DB-9D79-C2E4DA26E5A2Q36191232-9127547C-2DC5-45CB-936B-C7C158D587D7Q37108363-74F7F5D9-2695-45F0-AAE0-34C60590205AQ38020621-B01790D4-2457-4408-A041-3061A4779410Q39147936-C5DCBF23-D31E-44A9-9ED4-72B8DC9D03BBQ40970778-F0E2BC15-CC00-49E4-BEDF-484125E3343BQ57526858-FBC303B7-6DE3-4352-95B6-8AB0AFF0C72EQ57526880-07C68EB9-8060-4912-8D55-B87773FDAC2CQ59357414-7915D214-AF3C-4617-AECD-544E8343E12EQ64096535-724DCA19-4FA3-4982-BCFB-F45C54C8AD96Q64226558-17094AE6-D32F-4760-9FA8-4A0B3AE3FFD1Q64999669-4CECE660-05A7-4635-9E33-23C78E1446F6Q83973860-5301D527-AC39-4E64-B413-9CF2FABA22AEQ90839148-7AE6EAC7-C47B-4EDE-B84E-D3A9DDDBAE06Q92265861-20E699FC-D4B1-44B7-8225-7F78D0CBB6E3Q92740707-3F986080-327C-4527-8F8D-D1DA790C7A10Q95431475-6BFD2ACF-6F15-4D9C-AC5E-332E350801EB
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Pierre Barraud
@ast
Pierre Barraud
@en
Pierre Barraud
@es
Pierre Barraud
@nl
Pierre Barraud
@sl
type
label
Pierre Barraud
@ast
Pierre Barraud
@en
Pierre Barraud
@es
Pierre Barraud
@nl
Pierre Barraud
@sl
prefLabel
Pierre Barraud
@ast
Pierre Barraud
@en
Pierre Barraud
@es
Pierre Barraud
@nl
Pierre Barraud
@sl
P106
P1153
36896891700
P31
P496
0000-0003-4460-8360