Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Léna, Zig"'
Calcium wave dynamics in the embryonic mouse gut mesenchyme: impact on smooth muscle differentiation
Autor:
Nicolas R. Chevalier, Léna Zig, Anthony Gomis, Richard J. Amedzrovi Agbesi, Amira El Merhie, Laetitia Pontoizeau, Isabelle Le Parco, Nathalie Rouach, Isabelle Arnoux, Pascal de Santa Barbara, Sandrine Faure
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-11 (2024)
Abstract Intestinal smooth muscle differentiation is a complex physico-biological process involving several different pathways. Here, we investigate the properties of Ca2+ waves in the developing intestinal mesenchyme using GCamp6f expressing mouse e
Externí odkaz:
https://doaj.org/article/f6b69ba93654462389cbfa657e06dad8
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e54062 (2013)
RNase Y is a key endoribonuclease affecting global mRNA stability in Bacillus subtilis. Its characterization provided the first evidence that endonucleolytic cleavage plays a major role in the mRNA metabolism of this organism. RNase Y shares importan
Externí odkaz:
https://doaj.org/article/2942a30ec0664c13a27ec4a2443f3f6d
Autor:
Christian, Bressy, Dragomira, Majhen, Najat, Raddi, Wael, Jdey, Gaétan, Cornilleau, Léna, Zig, Josée, Guirouilh-Barbat, Bernard S, Lopez, Olivia, Bawa, Paule, Opolon, Elodie, Grellier, Karim, Benihoud
Publikováno v:
Oncotarget
The anti-tumor potential of oncolytic adenoviruses (CRAds) has been demonstrated in preclinical and clinical studies. While these agents failed to eradicate tumors when used as a monotherapy, they may be more effective if combined with conventional t
Autor:
Audrey Dorléans, Léna Zig, Inès Li de la Sierra-Gallay, Ciarán Condon, Laetitia Gilet, Harald Putzer, Jérémie Piton
Publikováno v:
Structure. 19(9):1252-1261
RNase J is a key member of the β-CASP family of metallo-β-lactamases involved in the maturation and turnover of RNAs in prokaryotes. The B. subtilis enzyme possesses both 5'-3' exoribonucleolytic and endonucleolytic activity, an unusual property fo
Publikováno v:
The EMBO Journal. 28:3523-3533
In contrast to Escherichia coli, initiation of mRNA decay in Gram-positive organisms is poorly understood. We studied the fate of the highly structured RNAs generated by premature transcription termination of S-adenosylmethionine (SAM)-dependent ribo
In Bacillus subtilis, the dual activity 5’ exo- and endoribonucleases J1 and J2 are important players in messenger RNA and stable RNA maturation and degradation. Recent work has improved our understanding of their structure, mechanism of action and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0326a007b3bdb2df625b90b1b3fcabcd
https://europepmc.org/articles/PMC3911265/
https://europepmc.org/articles/PMC3911265/
Publikováno v:
Plos One 1 (8), 1-12. (2013)
PLoS ONE
PLoS ONE, Public Library of Science, 2013, 8 (1), pp.1-12. ⟨10.1371/journal.pone.0054062⟩
www.plosone.org
PLoS ONE, Vol 8, Iss 1, p e54062 (2013)
PLoS ONE
PLoS ONE, Public Library of Science, 2013, 8 (1), pp.1-12. ⟨10.1371/journal.pone.0054062⟩
www.plosone.org
PLoS ONE, Vol 8, Iss 1, p e54062 (2013)
International audience; RNase Y is a key endoribonuclease affecting global mRNA stability in Bacillus subtilis. Its characterization provided the first evidence that endonucleolytic cleavage plays a major role in the mRNA metabolism of this organism.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f809087fbd03aa7dffa8d0d1b54a5a1d
https://hal.archives-ouvertes.fr/hal-00823296
https://hal.archives-ouvertes.fr/hal-00823296
Publikováno v:
Molecular microbiology. 70(1)
Ribonucleases J1 and J2 of Bacillus subtilis are evolutionarily conserved enzymes combining an endoribonucleolytic and a 5'-3' exoribonucleolytic activity in a single polypeptide. Their endoribonucleolytic cleavage specificity resembles that of RNase
Publikováno v:
Nature structuralmolecular biology. 15(2)
The maturation and stability of RNA transcripts is controlled by a combination of endo- and exoRNases. RNase J is unique, as it combines an RNase E–like endoribonucleolytic and a 5′-to-3′ exoribonucleolytic activity in a single polypeptide. The
Autor:
Sergine Even, Joëlle Vinh, Dominique Bréchemmier-Baey, Léna Zig, Olivier Pellegrini, Harald Putzer, Valérie Labas
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2005, 33 (7), pp.2141-2152. ⟨10.1093/nar/gki505⟩
Nucleic Acids Research, Oxford University Press, 2005, 33 (7), pp.2141-2152. ⟨10.1093/nar/gki505⟩
Many prokaryotic organisms lack an equivalent of RNase E, which plays a key role in mRNA degradation in Escherichia coli. In this paper, we report the purification and identification by mass spectrometry in Bacillus subtilis of two paralogous endorib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef9c5379be7dc06ae18d6fd6ce95cc38
https://hal.archives-ouvertes.fr/hal-01636919
https://hal.archives-ouvertes.fr/hal-01636919