Recherche - Archive ouverte HAL

Notice
16
Document
4

anglais
20

		Expression and purification of FtsW and RodA from Streptococcus pneumoniae, two membrane proteins involved in cell division and cell growth, respectively Marjolaine Noirclerc-Savoye , Cécile Morlot , Philippe Gerard , Thierry Vernet , André Zapun Protein Expression and Purification, 2003, 30 (1), pp.18-25. ⟨10.1016/S1046-5928(03)000⟩ Article dans une revue hal-01601007v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox Jules Philippe , Benoit Gallet , Cécile Morlot , Dalia Denapaite , Regine Hakenbeck , et al. Antimicrobial Agents and Chemotherapy, 2015, 59, pp.609-621. ⟨10.1128/AAC.04283-14⟩ Article dans une revue hal-01093880v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Resistance to β-Lactams in Neisseria ssp Due to Chromosomally Encoded Penicillin-Binding Proteins André Zapun , Cécile Morlot , Muhamed-Kheir Taha Antibiotics, 2016, 5 (4), ⟨10.3390/antibiotics5040035⟩ Article dans une revue hal-01426909v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae. Marjolaine Noirclerc-Savoye , Audrey Le Gouellec , Cécile Morlot , Otto Dideberg , Thierry Vernet , et al. Molecular Microbiology, 2004, pp.413-24 Article dans une revue hal-01464086v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Substitutions in PBP2b from β-Lactam-resistant Streptococcus pneumoniae Have Different Effects on Enzymatic Activity and Drug Reactivity. Philippe Calvez , Eefjan Breukink , David I Roper , Mélanie Dib , Carlos Contreras-Martel , et al. Journal of Biological Chemistry, 2017, 292 (7), pp.2854-2865. ⟨10.1074/jbc.M116.764696⟩ Article dans une revue hal-01497668v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		In vitro reconstitution of peptidoglycan assembly from the Gram-positive pathogen Streptococcus pneumoniae. André Zapun , Jules Philippe , Katherine A Abrahams , Luca Signor , David I Roper , et al. ACS Chemical Biology, 2013, 8 (12), pp.2688-96 Article dans une revue hal-01322359v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Inhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline. Astrid Zervosen , André Zapun , Jean-Marie Frère Antimicrobial Agents and Chemotherapy, 2013, 57 (1), pp.661-3 Article dans une revue hal-01322362v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Reconstitution of membrane protein complexes involved in pneumococcal septal cell wall assembly. Marjolaine Noirclerc-Savoye , Violaine Lantez , Luca Signor , Jules Philippe , Thierry Vernet , et al. PLoS ONE, 2013, 8 (9), pp.e75522 Article dans une revue hal-01322355v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Lipid Phases and Cell Geometry During the Cell Cycle of Streptococcus pneumoniae Philippe Calvez , Juliette Jouhet , Véronique Vie , Claire Durmort , André Zapun Frontiers in Microbiology, 2019, 10, pp.351. ⟨10.3389/fmicb.2019.00351⟩ Article dans une revue hal-02086215v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod. Soizic Masson , Thomas Kern , Audrey Le Gouellec , Cécile Giustini , Jean-Pierre Simorre , et al. Journal of Biological Chemistry, 2009, pp.27687-700 Article dans une revue hal-01464089v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Roles of pneumococcal DivIB in cell division. Audrey Le Gouellec , Laure Roux , Daniela Fadda , Orietta Massidda , Thierry Vernet , et al. Journal of Bacteriology, 2008, pp.4501-11 Article dans une revue hal-01464088v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance. Laurent Chesnel , Raphaël Carapito , Jacques Croizé , Otto Dideberg , Thierry Vernet , et al. Antimicrobial Agents and Chemotherapy, 2005, 49 (7), pp.2895-902. ⟨10.1128/AAC.49.7.2895-2902.2005⟩ Article dans une revue hal-00194104v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Pneumococcal beta-lactam resistance due to a conformational change in penicillin-binding protein 2x. Raphaël Carapito , Laurent Chesnel , Thierry Vernet , André Zapun Journal of Biological Chemistry, 2006, 281 (3), pp.1771-7. ⟨10.1074/jbc.M511506200⟩ Article dans une revue hal-00194094v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Common alterations in PBP1a from resistant streptococcus pneumoniae decrease its reactivity towards beta -lactams: Structural insights. Viviana Job , Raphaël Carapito , Thierry Vernet , Andréa Dessen , André Zapun Journal of Biological Chemistry, 2007, epub ahead of print. ⟨10.1074/jbc.M706181200⟩ Article dans une revue hal-00195479v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		The elongation of ovococci Jules Philippe , Thierry Vernet , André Zapun Microbial Drug Resistance, 2014, 20 (3), pp.215-221. ⟨10.1089/mdr.2014.0032⟩ Article dans une revue hal-01093390v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Membrane topology of the Streptococcus pneumoniae FtsW division protein Philippe Gerard , Thierry Vernet , André Zapun Journal of Bacteriology, 2002, 184 (7), pp.1925-1931 Article dans une revue hal-01601049v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae Cécile Morlot , Daniel Straume , Katharina Peters , Olav A Hegnar , Nolwenn Simon , et al. Nature Communications, 2018, 9, pp.3180. ⟨10.1038/s41467-018-05602-w⟩ Article dans une revue hal-01861372v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		One-Pot Two-Step Metabolic Labeling of Teichoic Acids and Direct Labeling of Peptidoglycan Reveals Tight Coordination of Both Polymers Inserted into Pneumococcus Cell Wall Julie Bonnet , Yung-Sing Wong , Thierry Vernet , Anne-Marie Di Guilmi , André Zapun , et al. ACS Chemical Biology, 2018, 13 (8), pp.2010-2015. ⟨10.1021/acschembio.8b00559⟩ Article dans une revue hal-01861375v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Penicillin-binding proteins and beta-lactam resistance André Zapun , Pauline Macheboeuf , Thierry Vernet Mayers D., Sobel J., Ouelette M., Lerner S. Antimicrobial Drug Resistance : Principles for the Clinic and Bench, 1 (13), Humana Press, p. 145-170, 2014 Chapitre d'ouvrage hal-01158934v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More
		Automated high-throughput process for site-directed mutagenesis, production, purification, and kinetic characterization of enzymes. Raphaël Carapito , Benoit Gallet , André Zapun , Thierry Vernet Analytical Biochemistry, 2006, 355 (1), pp.110-6. ⟨10.1016/j.ab.2006.04.047⟩ Article dans une revue istex hal-00194103v1	Envoyer sur ORCID Exporter BibTeX XML-TEI Dublin Core DC Terms EndNote DataCite Export avancé Partager Gmail Facebook X LinkedIn More

Filtrer vos résultats

Expression and purification of FtsW and RodA from Streptococcus pneumoniae, two membrane proteins involved in cell division and cell growth, respectively

Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox

Resistance to β-Lactams in Neisseria ssp Due to Chromosomally Encoded Penicillin-Binding Proteins

In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae.

Substitutions in PBP2b from β-Lactam-resistant Streptococcus pneumoniae Have Different Effects on Enzymatic Activity and Drug Reactivity.

In vitro reconstitution of peptidoglycan assembly from the Gram-positive pathogen Streptococcus pneumoniae.

Inhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline.

Reconstitution of membrane protein complexes involved in pneumococcal septal cell wall assembly.

Lipid Phases and Cell Geometry During the Cell Cycle of Streptococcus pneumoniae

Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod.

Roles of pneumococcal DivIB in cell division.

Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance.

Pneumococcal beta-lactam resistance due to a conformational change in penicillin-binding protein 2x.

Common alterations in PBP1a from resistant streptococcus pneumoniae decrease its reactivity towards beta -lactams: Structural insights.

The elongation of ovococci

Membrane topology of the Streptococcus pneumoniae FtsW division protein

Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae

One-Pot Two-Step Metabolic Labeling of Teichoic Acids and Direct Labeling of Peptidoglycan Reveals Tight Coordination of Both Polymers Inserted into Pneumococcus Cell Wall

Penicillin-binding proteins and beta-lactam resistance

Automated high-throughput process for site-directed mutagenesis, production, purification, and kinetic characterization of enzymes.