Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Laura Tengo"'
Autor:
Luciano G. Dolce, Aubree A. Zimmer, Laura Tengo, Félix Weis, Mary Anne T. Rubio, Juan D. Alfonzo, Eva Kowalinski
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
The deamination of all adenosines in the wobble base position is essential to empower the individual tRNA to decode several codons. Here, the authors present the cryo-EM structure of the tRNA-bound ADAT2/3 deaminase, revealing how the geometry-specif
Externí odkaz:
https://doaj.org/article/99e518943ee04156af1a7ea3c09e57ba
Autor:
Jaka Kragelj, Thibault Orand, Elise Delaforge, Laura Tengo, Martin Blackledge, Andrés Palencia, Malene Ringkjøbing Jensen
Publikováno v:
Biomolecules, Vol 11, Iss 8, p 1204 (2021)
Intrinsically disordered proteins (IDPs) can engage in promiscuous interactions with their protein targets; however, it is not clear how this feature is encoded in the primary sequence of the IDPs and to what extent the surface properties and the sha
Externí odkaz:
https://doaj.org/article/3ab4ff216dac4200bd7a824cf22b4641
Autor:
Luciano G. Dolce, Aubree A. Zimmer, Laura Tengo, Félix Weis, Mary Anne T. Rubio, Juan D. Alfonzo, Eva Kowalinski
The essential deamination of adenosine A34 to inosine at the wobble base is the individual tRNA modification with the greatest effects on mRNA decoding, empowering a single tRNA to translate three different codons. To date, many aspects of how eukary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18c39ec92b2b9fe3c4fcc2973884ed36
https://doi.org/10.1101/2022.06.16.496122
https://doi.org/10.1101/2022.06.16.496122
Autor:
Mariette F. Ducatez, Laura Tengo, Justine Oliva, Caroline Mas, Myriam Miloudi, Amélie Donchet, Guy Schoehn, Alice Labaronne, Thibaut Crépin, Francine C. A. Gérard, Rob W. H. Ruigrok
Publikováno v:
Scientific Reports
Scientific Reports, 2019, 9, pp.600. ⟨10.1038/s41598-018-37306-y⟩
Scientific Reports, Nature Publishing Group, 2019, 9, pp.600. ⟨10.1038/s41598-018-37306-y⟩
'Scientific Reports ', vol: 9, pages: 600-1-600-14 (2019)
Scientific Reports, Nature Publishing Group, 2019, 9 (1), pp.600. ⟨10.1038/s41598-018-37306-y⟩
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Scientific Reports, 2019, 9, pp.600. ⟨10.1038/s41598-018-37306-y⟩
Scientific Reports, Nature Publishing Group, 2019, 9, pp.600. ⟨10.1038/s41598-018-37306-y⟩
'Scientific Reports ', vol: 9, pages: 600-1-600-14 (2019)
Scientific Reports, Nature Publishing Group, 2019, 9 (1), pp.600. ⟨10.1038/s41598-018-37306-y⟩
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
This paper focuses on the nucleoprotein (NP) of the newly identified member of the Orthomyxoviridae family, Influenza D virus. To date several X-ray structures of NP of Influenza A (A/NP) and B (B/NP) viruses and of infectious salmon anemia (ISA/NP)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37ccc7e661d59f9b732de77b35238155
https://hal.univ-grenoble-alpes.fr/hal-01997471
https://hal.univ-grenoble-alpes.fr/hal-01997471
Autor:
Amélie, Donchet, Justine, Oliva, Alice, Labaronne, Laura, Tengo, Myriam, Miloudi, Francine, C A Gerard, Caroline, Mas, Guy, Schoehn, Rob, W H Ruigrok, Mariette, Ducatez, Thibaut, Crépin
Publikováno v:
Scientific Reports
This paper focuses on the nucleoprotein (NP) of the newly identified member of the Orthomyxoviridae family, Influenza D virus. To date several X-ray structures of NP of Influenza A (A/NP) and B (B/NP) viruses and of infectious salmon anemia (ISA/NP)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::24d9498325568da2bb6ebaebe7fe2952
https://pubmed.ncbi.nlm.nih.gov/30679709
https://pubmed.ncbi.nlm.nih.gov/30679709
Autor:
Nicola Salvi, Laura Tengo, Martin Blackledge, Jaka Kragelj, Sigrid Milles, Malene Ringkjøbing Jensen, Elise Delaforge, Andrés Palencia, Guillaume Bouvignies
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2018, 140 (3), pp.1148-1158. ⟨10.1021/jacs.7b12407⟩
Journal of the American Chemical Society, 2018, 140 (3), pp.1148-1158. ⟨10.1021/jacs.7b12407⟩
Journal of the American Chemical Society, American Chemical Society, 2018, 140 (3), pp.1148-1158. ⟨10.1021/jacs.7b12407⟩
Journal of the American Chemical Society, 2018, 140 (3), pp.1148-1158. ⟨10.1021/jacs.7b12407⟩
International audience; Intrinsically disordered proteins (IDPs) display a large number of interaction modes including folding-upon-binding, binding without major structural transitions, or binding through highly dynamic, so-called fuzzy, complexes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a42f36d07d0651716689f833787c759d
https://hal.archives-ouvertes.fr/hal-01726157
https://hal.archives-ouvertes.fr/hal-01726157
Autor:
Alice Labaronne, Christopher Swale, Imre Berger, Laura Tengo, Thibaut Crépin, Rob W. H. Ruigrok, Alexandre Monod, Frederic Garzoni, Stephen Cusack, Jean-Marie Bourhis, Guy Schoehn
Publikováno v:
Scientific Reports
Scientific Reports, Nature Publishing Group, 2016, 6, pp.24727. ⟨10.1038/srep24727⟩
Swale, C, Monod, A, Tengo, L, Labaronne, A, Garzoni, F, Bourhis, J-M, Cusack, S, Schoehn, G, Berger, I, Ruigrok, R W H & Crépin, T 2016, ' Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5 ', Scientific Reports, vol. 6, 24727 . https://doi.org/10.1038/srep24727
'Scientific Reports ', vol: 6, pages: 24727-1-24727-14 (2016)
Scientific Reports, 2016, 6, pp.24727. ⟨10.1038/srep24727⟩
Scientific Reports, Nature Publishing Group, 2016, 6, pp.24727. ⟨10.1038/srep24727⟩
Swale, C, Monod, A, Tengo, L, Labaronne, A, Garzoni, F, Bourhis, J-M, Cusack, S, Schoehn, G, Berger, I, Ruigrok, R W H & Crépin, T 2016, ' Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5 ', Scientific Reports, vol. 6, 24727 . https://doi.org/10.1038/srep24727
'Scientific Reports ', vol: 6, pages: 24727-1-24727-14 (2016)
Scientific Reports, 2016, 6, pp.24727. ⟨10.1038/srep24727⟩
The genome of influenza A virus (IAV) comprises eight RNA segments (vRNA) which are transcribed and replicated by the heterotrimeric IAV RNA-dependent RNA-polymerase (RdRp). RdRp consists of three subunits (PA, PB1 and PB2) and binds both the highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2deeb85a14a28bd835a77f7c7547fd5
http://europepmc.org/articles/PMC4837377
http://europepmc.org/articles/PMC4837377