Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Marion Dosnon"'
Autor:
Louis-Marie Bloyet, Joanna Brunel, Marion Dosnon, Véronique Hamon, Jenny Erales, Antoine Gruet, Carine Lazert, Christophe Bignon, Philippe Roche, Sonia Longhi, Denis Gerlier
Publikováno v:
PLoS Pathogens, Vol 12, Iss 12, p e1006058 (2016)
Measles virus (MeV) and all Paramyxoviridae members rely on a complex polymerase machinery to ensure viral transcription and replication. Their polymerase associates the phosphoprotein (P) and the L protein that is endowed with all necessary enzymati
Externí odkaz:
https://doaj.org/article/a1aabcaba6c34ec1b458849c2a92a534
Autor:
Petter Storm, Thomas Kjaer Klausen, Maria Trulsson, James Ho C S, Marion Dosnon, Tomas Westergren, Yinxia Chao, Anna Rydström, Henry Yang, Stine Falsig Pedersen, Catharina Svanborg
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e58578 (2013)
Ion channels and ion fluxes control many aspects of tissue homeostasis. During oncogenic transformation, critical ion channel functions may be perturbed but conserved tumor specific ion fluxes remain to be defined. Here we used the tumoricidal protei
Externí odkaz:
https://doaj.org/article/69fb7928210a4b369b293ff6c9371286
Autor:
Edoardo Salladini, Yuko Fujioka, Marina Lotti, David Blocquel, Antoine Gruet, Noriyuki Kodera, Daisuke Noshiro, Nobuo N. Noda, Mineyuki Mizuguchi, Tetsuya Mori, Mamoru Sato, Marion Dosnon, Christophe Bignon, Takashi Oda, Sonia Longhi, Johnny Habchi, Sujit Kumar Dora, Toshio Ando
Publikováno v:
Nature Nanotechnology
Nature Nanotechnology, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩
Nature Nanotechnology, Nature Publishing Group, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩
Nature Nanotechnology, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩
Nature Nanotechnology, Nature Publishing Group, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩
International audience; High-speed AFM imaging enables a semiquantitative, realistic description of the dynamic structure of intrinsically disordered proteins.Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entire
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4f5c66b7933600b9a34f968937c68cd
http://hdl.handle.net/10281/295727
http://hdl.handle.net/10281/295727
Autor:
Jinyu Li, Albert Konijnenberg, Rita Grandori, Johny Habchi, Marion Dosnon, Paolo Carloni, Sonia Longhi, Giulia Rossetti, Frank Sobott
In recent years native mass spectrometry has been increasingly employed to study protein structure. As such a thorough understanding of the effect of the gas-phase on protein structure is becoming increasingly important. We show how a combination of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52068a2daaff16e3dee7f95966ac0a73
Autor:
Antoine Gruet, Carine Lazert, Christophe Bignon, Louis Marie Bloyet, Sonia Longhi, Joanna Brunel, Véronique Hamon, Marion Dosnon, Jenny Erales, Philippe Roche, Denis Gerlier
Publikováno v:
PLoS Pathogens
PLoS Pathogens, 2016, 12 (12), pp.e1006058. ⟨10.1371/journal.ppat.1006058⟩
PLoS Pathogens, Public Library of Science, 2016, 12 (12), pp.e1006058. ⟨10.1371/journal.ppat.1006058⟩
PLoS Pathogens, Vol 12, Iss 12, p e1006058 (2016)
PLoS Pathogens, 2016, 12 (12), pp.e1006058. ⟨10.1371/journal.ppat.1006058⟩
PLoS Pathogens, Public Library of Science, 2016, 12 (12), pp.e1006058. ⟨10.1371/journal.ppat.1006058⟩
PLoS Pathogens, Vol 12, Iss 12, p e1006058 (2016)
Measles virus (MeV) and all Paramyxoviridae members rely on a complex polymerase machinery to ensure viral transcription and replication. Their polymerase associates the phosphoprotein (P) and the L protein that is endowed with all necessary enzymati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89143c59dade05a6478f405c9278c38c
https://hal.science/hal-02474235/document
https://hal.science/hal-02474235/document
Autor:
Marion Dosnon, Stefano Gianni, Christophe Bignon, Joanna Brunel, Sonia Longhi, Denis Gerlier, Antoine Gruet, Daniela Bonetti, Rahul K. Das, Monika Fuxreiter, David Blocquel
Publikováno v:
FEBS Journal
FEBS Journal, 2016, 283 (4), pp.576-594. ⟨10.1111/febs.13631⟩
FEBS Journal, Wiley, 2016, 283 (4), pp.576-594. ⟨10.1111/febs.13631⟩
FEBS Journal, 2016, 283 (4), pp.576-594. ⟨10.1111/febs.13631⟩
FEBS Journal, Wiley, 2016, 283 (4), pp.576-594. ⟨10.1111/febs.13631⟩
Despite the partial disorder-to-order transition that intrinsically disordered proteins often undergo upon binding to their partners, a considerable amount of residual disorder may be retained in the bound form, resulting in a fuzzy complex. Fuzzy re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c425b1c929c59e3768b1ae36e226f2a
Autor:
Jenny, Erales, David, Blocquel, Johnny, Habchi, Matilde, Beltrandi, Antoine, Gruet, Marion, Dosnon, Christophe, Bignon, Sonia, Longhi
Publikováno v:
Advances in experimental medicine and biology. 870
In this review we summarize available data showing the abundance of structural disorder within the nucleoprotein (N) and phosphoprotein (P) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. We provide a detai
Autor:
Daniela Bonetti, Angela Morrone, Eva Di Silvio, Stefano Gianni, Marion Dosnon, Jenny Erales, Sonia Longhi
Publikováno v:
ACS Chemical Biology
ACS Chemical Biology, American Chemical Society, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
ACS Chemical Biology, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
ACS Chemical Biology, American Chemical Society, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
ACS Chemical Biology, 2015, 10 (3), pp.795-802. ⟨10.1021/cb5008579⟩
In the past decade, a wealth of experimental data has demonstrated that a large fraction of proteins, while functional, are intrinsically disordered at physiological conditions. Many intrinsically disordered proteins (IDPs) undergo a disorder-to-orde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47178be42b7aa51440ca777bb6a1bca0
https://hal.archives-ouvertes.fr/hal-01439003
https://hal.archives-ouvertes.fr/hal-01439003
Autor:
Jenny Erales, David Blocquel, Christophe Bignon, Sonia Longhi, Matilde Beltrandi, Antoine Gruet, Marion Dosnon, Johnny Habchi
Publikováno v:
INTRINSICALLY DISORDERED PROTEINS STUDIED BY NMR SPECTROSCOPY
Felli, IC and Pierattelli, R. INTRINSICALLY DISORDERED PROTEINS STUDIED BY NMR SPECTROSCOPY, 870, pp.351-381, 2015, Advances in Experimental Medicine and Biology, 978-3-319-20164-1; 978-3-319-20163-4. ⟨10.1007/978-3-319-20164-1_12⟩
Advances in Experimental Medicine and Biology ISBN: 9783319201634
Felli, IC and Pierattelli, R. INTRINSICALLY DISORDERED PROTEINS STUDIED BY NMR SPECTROSCOPY, 870, pp.351-381, 2015, Advances in Experimental Medicine and Biology, 978-3-319-20164-1; 978-3-319-20163-4. ⟨10.1007/978-3-319-20164-1_12⟩
Advances in Experimental Medicine and Biology ISBN: 9783319201634
In this review we summarize available data showing the abundance of structural disorder within the nucleoprotein (N) and phosphoprotein (P) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. We provide a detai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b37743ce4e65c80d5da901ef721daee8
https://hal.archives-ouvertes.fr/hal-01439008
https://hal.archives-ouvertes.fr/hal-01439008
Autor:
Joanna Brunel, Louis Marie Bloyet, Damien Chopy, Marion Dosnon, Sonia Longhi, Patricia Devaux, Denis Gerlier, Erica Urzua, Roberto Cattaneo
Publikováno v:
Journal of Virology
Journal of Virology, 2014, 88 (18), pp.10851-10863. ⟨10.1128/JVI.00664-14⟩
Journal of Virology, American Society for Microbiology, 2014, 88 (18), pp.10851-10863. ⟨10.1128/JVI.00664-14⟩
Journal of Virology, 2014, 88 (18), pp.10851-10863. ⟨10.1128/JVI.00664-14⟩
Journal of Virology, American Society for Microbiology, 2014, 88 (18), pp.10851-10863. ⟨10.1128/JVI.00664-14⟩
The genome of nonsegmented negative-strand RNA viruses is tightly embedded within a nucleocapsid made of a nucleoprotein (N) homopolymer. To ensure processive RNA synthesis, the viral polymerase L in complex with its cofactor phosphoprotein (P) binds
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca22c5ac827226807ef35d91a432f0fc
https://hal.science/hal-01911320
https://hal.science/hal-01911320