Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Manuela, Argentini"'
Autor:
Anne Durand, Asma Azzouzi, Marie-Line Bourbon, Anne-Soisig Steunou, Sylviane Liotenberg, Akinori Maeshima, Chantal Astier, Manuela Argentini, Shingo Saito, Soufian Ouchane
Publikováno v:
mBio, Vol 6, Iss 5 (2015)
ABSTRACT In the absence of a tight control of copper entrance into cells, bacteria have evolved different systems to control copper concentration within the cytoplasm and the periplasm. Central to these systems, the Cu+ ATPase CopA plays a major role
Externí odkaz:
https://doaj.org/article/1f05ba40726c494c91c6e6e6e675203a
Autor:
Nathalie, Dautin, Manuela, Argentini, Niloofar, Mohiman, Cécile, Labarre, David, Cornu, Laila, Sago, Mohamed, Chami, Christiane, Dietrich, Célia, de Sousa d'Auria, Christine, Houssin, Muriel, Masi, Christophe, Salmeron, Nicolas, Bayan
Publikováno v:
Microbiology (Reading, England). 166(8)
Bacterial lipoproteins are secreted proteins that are post-translationally lipidated. Following synthesis, preprolipoproteins are transported through the cytoplasmic membrane via the Sec or Tat translocon. As they exit the transport machinery, they a
Autor:
Christiane Dietrich, Laila Sago, David Cornu, Célia de Sousa d’Auria, Niloofar Mohiman, Muriel Masi, Mohamed Chami, Cécile Labarre, Christophe Salmeron, Manuela Argentini, Nicolas Bayan, Christine Houssin, Nathalie Dautin
Publikováno v:
Microbiology
Microbiology, Microbiology Society, 2020, 166 (8), ⟨10.1099/mic.0.000937⟩
Microbiology, 2020, 166 (8), ⟨10.1099/mic.0.000937⟩
Microbiology, Microbiology Society, 2020, 166 (8), ⟨10.1099/mic.0.000937⟩
Microbiology, 2020, 166 (8), ⟨10.1099/mic.0.000937⟩
Bacterial lipoproteins are secreted proteins that are post-translationally lipidated. Following synthesis, preprolipoproteins are transported through the cytoplasmic membrane via the Sec or Tat translocon. As they exit the transport machinery, they a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5c3c9eaf7d531c8d837f72b5ebf49b5
https://hal.archives-ouvertes.fr/hal-02768912/document
https://hal.archives-ouvertes.fr/hal-02768912/document
Autor:
Niloofar Mohiman, Manuela Argentini, Sarah M Batt, David Cornu, Muriel Masi, Lothar Eggeling, Gurdyal Besra, Nicolas Bayan
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e46225 (2012)
BACKGROUND: Due to their contribution to bacterial virulence, lipoproteins and members of the lipoprotein biogenesis pathway represent potent drug targets. Following translocation across the inner membrane, lipoprotein precursors are acylated by lipo
Externí odkaz:
https://doaj.org/article/1506c435413b441caf3c4a923ff39d4e
Autor:
Màté A Demény, Evi Soutoglou, Zita Nagy, Elisabeth Scheer, Agnes Jànoshàzi, Magalie Richardot, Manuela Argentini, Pascal Kessler, Laszlo Tora
Publikováno v:
PLoS ONE, Vol 2, Iss 3, p e316 (2007)
TFIID plays a role in nucleating RNA polymerase II preinitiation complex assembly on protein-coding genes. TFIID is a multisubunit complex comprised of the TATA box binding protein (TBP) and 14 TBP-associated factors (TAFs). Another class of multipro
Externí odkaz:
https://doaj.org/article/eafceda573f64921a4c463284e00d77e
Publikováno v:
Nucleic Acids Research
Stop codon readthrough may be promoted by the nucleotide environment or drugs. In such cases, ribosomes incorporate a natural suppressor tRNA at the stop codon, leading to the continuation of translation in the same reading frame until the next stop
Autor:
Manuela Argentini, Fawzi Khoder-Agha, David Cornu, Azaria Remion, Virginie Redeker, Marc Mirande
Publikováno v:
FEBS Open Bio
FEBS Open Bio, Wiley Open Access/Elsevier, 2016, 6 (7), pp.696-706. ⟨10.1002/2211-5463.12074⟩
FEBS Open Bio, Wiley Open Access/Elsevier, 2016, 6 (7), pp.696-706. 〈10.1002/2211-5463.12074〉
FEBS Open Bio, 2016, 6 (7), pp.696-706. ⟨10.1002/2211-5463.12074⟩
FEBS Open Bio, Wiley Open Access/Elsevier, 2016, 6 (7), pp.696-706. ⟨10.1002/2211-5463.12074⟩
FEBS Open Bio, Wiley Open Access/Elsevier, 2016, 6 (7), pp.696-706. 〈10.1002/2211-5463.12074〉
FEBS Open Bio, 2016, 6 (7), pp.696-706. ⟨10.1002/2211-5463.12074⟩
International audience; Human cytoplasmic lysyl-tRNA synthetase (LysRS) is associated within a multi-aminoacyl-tRNA synthetase complex (MSC). Within this complex, the p38 component is the scaffold protein that binds the catalytic domain of LysRS via
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::324da3a0db919098d3ab554f980812b7
https://hal.archives-ouvertes.fr/hal-01405679
https://hal.archives-ouvertes.fr/hal-01405679
Autor:
Stéphane Skouloubris, Hannu Myllykallio, Djemel Hamdane, Gaston Hui-Bon-Hoa, David Cornu, Manuela Argentini, Béatrice Golinelli-Pimpaneau
Publikováno v:
Journal of Biological Chemistry. 286:36268-36280
The flavoprotein TrmFO methylates specifically the C5 carbon of the highly conserved uridine 54 in tRNAs. Contrary to most methyltransferases, the 1-carbon unit transferred by TrmFO derives from 5,10-methylenetetrahydrofolate and not from S-adenosyl-
Publikováno v:
Protein Expression and Purification. 70:151-157
Bovine CD38, a type II glycoprotein, contains two potential N-glycosylation sites (Asn-201 and Asn-268) in its extracellular domain. This contrasts with the other mammalian members of the ADP-ribosyl cyclase family, such as human CD38 and BST-1/CD157
Autor:
Michel Vincent, Frédéric Boccard, Sophie Quevillon-Cheruel, Carlos Acosta Muniz, Jacques Gallay, David Cornu, Herman van Tilbeurgh, Bruno Lemaitre, Nicolas Leulliot, Manuela Argentini
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (6), pp.3552-62. ⟨10.1074/jbc.M808334200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (6), pp.3552-62. ⟨10.1074/jbc.M808334200⟩
International audience; Erwinia carotovora are phytopathogenic Gram-negative bacteria of agronomic interest as these bacteria are responsible for fruit soft rot and use insects as dissemination vectors. The Erwinia carotovora carotovora strain 15 (Ec