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pro vyhledávání: '"Théobald-Dietrich A"'
Akademický článek
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Autor:
José R. Jaramillo Ponce, Anne Théobald‐Dietrich, Philippe Bénas, Caroline Paulus, Claude Sauter, Magali Frugier
Publikováno v:
Protein science : a publication of the Protein Society.
tRip is a tRNA import protein specific to Plasmodium, the causative agent of malaria. In addition to its membrane localization and tRNA trafficking properties, tRip has the capacity to associate with three aminoacyl-tRNA synthetases (aaRS), the gluta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80be480955bf00ebdc3d7a303ea432c4
https://pubmed.ncbi.nlm.nih.gov/36606712
https://pubmed.ncbi.nlm.nih.gov/36606712
Autor:
Marta Cela, Philippe Wolff, Magali Frugier, Joëlle Rudinger-Thirion, Renaud Geslain, Anne Théobald-Dietrich
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2021, ⟨10.1093/nar/gkab769⟩
Nucleic Acids Research, Oxford University Press, 2021, ⟨10.1093/nar/gkab769⟩
Malaria is a life-threatening and devastating parasitic disease. Our previous work showed that parasite development requires the import of exogenous transfer RNAs (tRNAs), which represents a novel and unique form of host–pathogen interaction, as we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfe510627c23251ea662f8170fd5dcc5
https://doi.org/10.1093/nar/gkab769
https://doi.org/10.1093/nar/gkab769
Autor:
Jaramillo Ponce, José R., Théobald‐Dietrich, Anne, Bénas, Philippe, Paulus, Caroline, Sauter, Claude, Frugier, Magali
Publikováno v:
Protein Science: A Publication of the Protein Society; Feb2023, Vol. 32 Issue 2, p1-18, 18p
Autor:
Frugier, Magali, Bour, Tania, Ayach, Maya, Santos, Manuel A.S., Rudinger-Thirion, Joëlle, Théobald-Dietrich, Anne, Pizzi, Elizabetta
Publikováno v:
In FEBS Letters 2010 584(2):448-454
Akademický článek
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Autor:
Anne, Théobald-Dietrich, Raphaël, de Wijn, Kévin, Rollet, Alexandra, Bluhm, Joëlle, Rudinger-Thirion, Caroline, Paulus, Bernard, Lorber, Aurélien, Thureau, Magali, Frugier, Claude, Sauter
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2113
Over the past two decades small-angle X-ray scattering (SAXS) has become a popular method to characterize solutions of biomolecules including ribonucleic acid (RNA). In an integrative structural approach, SAXS is complementary to crystallography, NMR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6c7d1946e412ee6db104bd62cee505a6
https://pubmed.ncbi.nlm.nih.gov/32006316
https://pubmed.ncbi.nlm.nih.gov/32006316
Autor:
Joëlle Rudinger-Thirion, Alexandra Bluhm, Aurélien Thureau, Claude Sauter, Anne Théobald-Dietrich, Raphaël de Wijn, Magali Frugier, Caroline Paulus, K. Rollet, Bernard Lorber
Publikováno v:
Methods in Molecular Biology ISBN: 9781071602775
Methods Mol Biol
Methods Mol Biol, pp.189-215, 2020, ⟨10.1007/978-1-0716-0278-2_14⟩
Methods Mol Biol
Methods Mol Biol, pp.189-215, 2020, ⟨10.1007/978-1-0716-0278-2_14⟩
Over the past two decades small-angle X-ray scattering (SAXS) has become a popular method to characterize solutions of biomolecules including ribonucleic acid (RNA). In an integrative structural approach, SAXS is complementary to crystallography, NMR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e913da3e6912910b12cb259e918f412
https://doi.org/10.1007/978-1-0716-0278-2_14
https://doi.org/10.1007/978-1-0716-0278-2_14
Publikováno v:
FEBS Letters
FEBS Letters, Wiley, 2016, 590 (23), pp.4180-4191. ⟨10.1002/1873-3468.12441⟩
FEBS Letters, Wiley, 2016, 590 (23), pp.4180-4191. ⟨10.1002/1873-3468.12441⟩
In this Review, we examine the so-called 'OB-fold′, a tRNA-binding domain homologous to the bacterial tRNA-binding protein Trbp111. We highlight the ability of OB-fold homologs to bind tRNAs and summarize their distribution in evolution. Nature has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3d95223ab610c6d91e917cc03722080
https://doi.org/10.1002/1873-3468.12441
https://doi.org/10.1002/1873-3468.12441
Publikováno v:
In Journal of Crystal Growth 2001 232(1):399-408