Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Marie-Françoise O'Donohue"'
Autor:
Laura Plassart, Ramtin Shayan, Christian Montellese, Dana Rinaldi, Natacha Larburu, Carole Pichereaux, Carine Froment, Simon Lebaron, Marie-Françoise O'Donohue, Ulrike Kutay, Julien Marcoux, Pierre-Emmanuel Gleizes, Celia Plisson-Chastang
Publikováno v:
eLife, Vol 10 (2021)
Preventing premature interaction of pre-ribosomes with the translation apparatus is essential for translational accuracy. Hence, the final maturation step releasing functional 40S ribosomal subunits, namely processing of the 18S ribosomal RNA 3′ en
Externí odkaz:
https://doaj.org/article/8d570e25d8ea460faf54b11200b9693b
Autor:
Maname Benyelles, Harikleia Episkopou, Marie‐Françoise O'Donohue, Laëtitia Kermasson, Pierre Frange, Florian Poulain, Fatma Burcu Belen, Meltem Polat, Christine Bole‐Feysot, Francina Langa‐Vives, Pierre‐Emmanuel Gleizes, Jean‐Pierre deVillartay, Isabelle Callebaut, Anabelle Decottignies, Patrick Revy
Publikováno v:
EMBO Molecular Medicine, Vol 11, Iss 7, Pp n/a-n/a (2019)
Abstract PARN, poly(A)‐specific ribonuclease, regulates the turnover of mRNAs and the maturation and stabilization of the hTR RNA component of telomerase. Biallelic PARN mutations were associated with Høyeraal–Hreidarsson (HH) syndrome, a rare t
Externí odkaz:
https://doaj.org/article/6b17fc6a05d04cf4a3910e137cab5d9f
Autor:
Marcin W. Wlodarski, Lydie Da Costa, Marie-Françoise O’Donohue, Marc Gastou, Narjesse Karboul, Nathalie Montel-Lehry, Ina Hainmann, Dominika Danda, Amina Szvetnik, Victor Pastor, Nahuel Paolini, Franca M. di Summa, Hannah Tamary, Abed Abu Quider, Anna Aspesi, Riekelt H. Houtkooper, Thierry Leblanc, Charlotte M. Niemeyer, Pierre-Emmanuel Gleizes, Alyson W. MacInnes
Publikováno v:
Haematologica, Vol 103, Iss 6 (2018)
Diamond-Blackfan anemia (DBA) is a rare inherited bone marrow failure disorder linked predominantly to ribosomal protein gene mutations. Here the European DBA consortium reports novel mutations identified in the RPL15 gene in 6 unrelated individuals
Externí odkaz:
https://doaj.org/article/cf876bd41ad548e6828f1cff73feeeec
Autor:
Pavel Tchelidze, Aassif Benassarou, Hervé Kaplan, Marie-Françoise O'Donohue, Laurent Lucas, Christine Terryn, Levan Rusishvili, Giorgi Mosidze, Nathalie Lalun, Dominique Ploton
Publikováno v:
PLoS ONE, Vol 12, Iss 11, p e0187977 (2017)
The nucleolus produces the large polycistronic transcript (47S precursor) containing the 18S, 5.8S and 28S rRNA sequences and hosts most of the nuclear steps of pre-rRNA processing. Among numerous components it contains condensed chromatin and active
Externí odkaz:
https://doaj.org/article/cef43c67e5174e498ad8442b4c32837a
Publikováno v:
Biomolecules, Vol 8, Iss 4, p 123 (2018)
Ribosomal RNAs, the most abundant cellular RNA species, have evolved as the structural scaffold and the catalytic center of protein synthesis in every living organism. In eukaryotes, they are produced from a long primary transcript through an intrica
Externí odkaz:
https://doaj.org/article/4b217ec6fa6340f8a892d6f595b3ff7f
Autor:
Marie-Françoise O’Donohue, Lydie Da Costa, Marco Lezzerini, Sule Unal, Clément Joret, Marije Bartels, Eva Brilstra, Marijn Scheijde-Vermeulen, Ludivine Wacheul, Kim De Keersmaecker, Stijn Vereecke, Veerle Labarque, Manon Saby, Sophie D. Lefevre, Jessica Platon, Nathalie Montel-Lehry, Nathalie Laugero, Eric Lacazette, Koen van Gassen, Riekelt H. Houtkooper, Pelin Ozlem Simsek-Kiper, Thierry Leblanc, Nese Yarali, Arda Cetinkaya, Nurten A. Akarsu, Pierre-Emmanuel Gleizes, Denis L. J. Lafontaine, Alyson W. MacInnes
Publikováno v:
Blood, 139(21), 3111-3126. American Society of Hematology
O'Donohue, M-F, da Costa, L, Lezzerini, M, Unal, S, Joret, C, Bartels, M, Brilstra, E, Scheijde-Vermeulen, M, Wacheul, L, de Keersmaecker, K, Vereecke, S, Labarque, V, Saby, M, Lefevre, S D, Platon, J, Montel-Lehry, N, Laugero, N, Lacazette, E, van Gassen, K, Houtkooper, R H, Simsek-Kiper, P O, Leblanc, T, Yarali, N, Cetinkaya, A, Akarsu, N A, Gleizes, P-E, Lafontaine, D L J & MacInnes, A W 2022, ' HEATR3 variants impair nuclear import of uL18 (RPL5) and drive Diamond-Blackfan anemia ', Blood, vol. 139, no. 21, pp. 3111-3126 . https://doi.org/10.1182/blood.2021011846
O'Donohue, M-F, da Costa, L, Lezzerini, M, Unal, S, Joret, C, Bartels, M, Brilstra, E, Scheijde-Vermeulen, M, Wacheul, L, de Keersmaecker, K, Vereecke, S, Labarque, V, Saby, M, Lefevre, S D, Platon, J, Montel-Lehry, N, Laugero, N, Lacazette, E, van Gassen, K, Houtkooper, R H, Simsek-Kiper, P O, Leblanc, T, Yarali, N, Cetinkaya, A, Akarsu, N A, Gleizes, P-E, Lafontaine, D L J & MacInnes, A W 2022, ' HEATR3 variants impair nuclear import of uL18 (RPL5) and drive Diamond-Blackfan anemia ', Blood, vol. 139, no. 21, pp. 3111-3126 . https://doi.org/10.1182/blood.2021011846
The congenital bone marrow failure syndrome Diamond-Blackfan anemia (DBA) is typically associated with variants in ribosomal protein (RP) genes impairing erythroid cell development. Here we report multiple individuals with biallelic HEATR3 variants e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd4100cf484e864275fa42206f6a6809
https://research.vumc.nl/en/publications/7731263a-7b25-4244-b994-0a42cb7e6400
https://research.vumc.nl/en/publications/7731263a-7b25-4244-b994-0a42cb7e6400
Autor:
Simon Lebaron, Marie‐Françoise O'Donohue, Scott C. Smith, Kendra L. Engleman, Jane Juusola, Nicole P. Safina, Isabelle Thiffault, Carol J. Saunders, Pierre‐Emmanuel Gleizes
Publikováno v:
Human mutationREFERENCES. 43(3)
Diamond-Blackfan anemia is a rare genetic disease characterized by erythroblastopenia and a large spectrum of developmental anomalies. The vast majority of the cases genetically described are linked to heterozygous pathogenic variants in more than 20
Autor:
Dechamma Pandyanda Nanjappa, Anirban Chakraborty, Marie-Françoise O'Donohue, Arati Khanna-Gupta, Nishith Babu, Patrick Sips
Publikováno v:
Life Sciences
Life Sciences, Elsevier, 2021, 285, pp.119953. ⟨10.1016/j.lfs.2021.119953⟩
LIFE SCIENCES
Life Sciences, Elsevier, 2021, 285, pp.119953. ⟨10.1016/j.lfs.2021.119953⟩
LIFE SCIENCES
International audience; In eukaryotic cells, the balance between the synthesis and the degradation decides the steady-state levels of messenger RNAs (mRNA). The removal of adenosine residues from the poly(A) tail, called deadenylation, is the first a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92e9d0da9334ff8fedd566e4451915be
https://hal.archives-ouvertes.fr/hal-03363230/file/Nanjappa21LifeSci_PARN_ReviewAnir.pdf
https://hal.archives-ouvertes.fr/hal-03363230/file/Nanjappa21LifeSci_PARN_ReviewAnir.pdf
Author response: The final step of 40S ribosomal subunit maturation is controlled by a dual key lock
Autor:
Laura Plassart, Carole Pichereaux, Carine Froment, Marie-Françoise O'Donohue, Simon Lebaron, Christian Montellese, Pierre-Emmanuel Gleizes, Ulrike Kutay, Ramtin Shayan, Dana Rinaldi, Célia Plisson-Chastang, Natacha Larburu, Julien Marcoux
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7fcfec886f60f8d7a47c73d624d2a0be
https://doi.org/10.7554/elife.61254.sa2
https://doi.org/10.7554/elife.61254.sa2
Autor:
Pål Ø. Falnes, Sebastian A. Leidel, Marie-Françoise O'Donohue, Rita Pinto, Pierre-Emmanuel Gleizes, Magnus E. Jakobsson, Jȩdrzej M. Małecki, Anders Moen, Luca Gessa, Bernd Thiede, Erna Davydova, Jesper V. Olsen, Jie Wu, Yeji Kim
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2021, 49 (6), pp.3185-3203. ⟨10.1093/nar/gkab088⟩
Małecki, J M, Odonohue, M-F, Kim, Y, Jakobsson, M E, Gessa, L, Pinto, R, Wu, J, Davydova, E, Moen, A, Olsen, J V, Thiede, B, Gleizes, P-E, Leidel, S A & Falnes, P Ø 2021, ' Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function ', Nucleic Acids Research, vol. 49, no. 6, pp. 3185-3203 . https://doi.org/10.1093/nar/gkab088
Małecki, Jędrzej M; Odonohue, Marie-Francoise; Kim, Ye; Jakobsson, Magnus E; Gessa, Luca; Pinto, Rita; Wu, Jie; Davydova, Erna; Moen, Anders; Olsen, Jesper V; Thiede, Bernd; Gleizes, Pierre-Emmanuel; Leidel, Sebastian A.; Falnes, Pål Ø (2021). Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function. Nucleic acids research, 49(6), pp. 3185-3203. Oxford University Press 10.1093/nar/gkab088
Nucleic Acids Research, Oxford University Press, 2021, 49 (6), pp.3185-3203. ⟨10.1093/nar/gkab088⟩
Małecki, J M, Odonohue, M-F, Kim, Y, Jakobsson, M E, Gessa, L, Pinto, R, Wu, J, Davydova, E, Moen, A, Olsen, J V, Thiede, B, Gleizes, P-E, Leidel, S A & Falnes, P Ø 2021, ' Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function ', Nucleic Acids Research, vol. 49, no. 6, pp. 3185-3203 . https://doi.org/10.1093/nar/gkab088
Małecki, Jędrzej M; Odonohue, Marie-Francoise; Kim, Ye; Jakobsson, Magnus E; Gessa, Luca; Pinto, Rita; Wu, Jie; Davydova, Erna; Moen, Anders; Olsen, Jesper V; Thiede, Bernd; Gleizes, Pierre-Emmanuel; Leidel, Sebastian A.; Falnes, Pål Ø (2021). Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function. Nucleic acids research, 49(6), pp. 3185-3203. Oxford University Press 10.1093/nar/gkab088
Protein methylation occurs primarily on lysine and arginine, but also on some other residues, such as histidine. METTL18 is the last uncharacterized member of a group of human methyltransferases (MTases) that mainly exert lysine methylation, and here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99f382a1a17e37a996701f82e6a924fe
https://hal.archives-ouvertes.fr/hal-03363245
https://hal.archives-ouvertes.fr/hal-03363245