Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Nathalie Teller"'
Autor:
Iulian I Oprea, Joana R Viola, Pedro M D Moreno, Oscar E Simonson, Sergey Rodin, Nathalie Teller, Karl Tryggvason, Karin E Lundin, Leonard Girnita, Carl Inge Edvard Smith
Publikováno v:
Molecular Therapy: Nucleic Acids, Vol 3, Iss C (2014)
Inducible systems for gene expression emerge as a new class of artificial vectors offering temporal and spatial exogenous control of gene expression. However, most inducible systems are less efficient in vivo and lack the target-organ specificity. In
Externí odkaz:
https://doaj.org/article/502466cfc7d34aeebe0b6b19531e8534
Autor:
Ana Amoroso, Julien Boudet, Stéphanie Berzigotti, Valérie Duval, Nathalie Teller, Dominique Mengin-Lecreulx, André Luxen, Jean-Pierre Simorre, Bernard Joris
Publikováno v:
PLoS Pathogens, Vol 8, Iss 3, p e1002571 (2012)
To resist to β-lactam antibiotics Eubacteria either constitutively synthesize a β-lactamase or a low affinity penicillin-binding protein target, or induce its synthesis in response to the presence of antibiotic outside the cell. In Bacillus licheni
Externí odkaz:
https://doaj.org/article/da1ae7cc0fa5464291959832d8779d50
Autor:
Nathalie Teller, Frédéric Mercier, Geoffroy Kaisin, André Luxen, Jessica Flagothier, Johan Wouters, David Thonon
Publikováno v:
Applied Radiation and Isotopes. 70:1549-1557
Oligonucleotides (ONs) and more particularly siRNAs are promising drugs but their pharmacokinetics and biodistribution are widely unknown. Positron Emission Tomography (PET) using fluorine-18 is a suitable technique to quantify these biological proce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fb622906dd2b2bff1e884bf8f5799a3
https://doi.org/10.1016/j.apradiso.2012.04.022
https://doi.org/10.1016/j.apradiso.2012.04.022
Autor:
Frédéric Mercier, Nathalie Teller, Bart Devreese, Michel Vandenbranden, Alain Jacquet, Andy Chevigné, Tetsuya Tanaka, Marie-Eve Dumez, André Matagne, Moreno Galleni, André Luxen, Isabel Vandenberghe, Jean-Marie Frère
Publikováno v:
Journal of Biological Chemistry. 283:30606-30617
The trypsin-like protease Der p 3, a major allergen of the house dust mite Dermatophagoides pteronyssinus, is synthesized as a zymogen, termed proDer p 3. No recombinant source of Der p 3 has been described yet, and the zymogen maturation mechanism r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db4bd6ba9287cdd3c61490452146ffec
https://doi.org/10.1074/jbc.m803041200
https://doi.org/10.1074/jbc.m803041200
Autor:
Sergey Rodin, Leonard Girnita, Nathalie Teller, Joana R Viola, Oscar E. Simonson, Karl Tryggvason, Pedro Moreno, Karin E. Lundin, Iulian I. Oprea, Carl Inge Edvard Smith
Publikováno v:
Molecular Therapy. Nucleic Acids
Molecular Therapy: Nucleic Acids, Vol 3, Iss C (2014)
Molecular Therapy: Nucleic Acids, Vol 3, Iss C (2014)
Inducible systems for gene expression emerge as a new class of artificial vectors offering temporal and spatial exogenous control of gene expression. However, most inducible systems are less efficient in vivo and lack the target-organ specificity. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdd42242f623353ca7a0cb29b18f40f4
General method for labeling siRNA by click chemistry with fluorine-18 for the purpose of PET imaging
Autor:
Nathalie Teller, André Luxen, Jessica Flagothier, Christian Lemaire, David Thonon, Jérôme Paris, Frédéric Mercier, Geoffroy Kaisin
Publikováno v:
Bioconjugate chemistry. 22(1)
The alkyne-azide Cu(I)-catalyzed Huisgen cycloaddition, a click-type reaction, was used to label a double-stranded oligonucleotide (siRNA) with fluorine-18. An alkyne solid support CPG for the preparation of monostranded oligonucleotides functionaliz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89bff83f9d5549cc95ef670a3db99128
https://pubmed.ncbi.nlm.nih.gov/21174402
https://pubmed.ncbi.nlm.nih.gov/21174402
Autor:
Frédéric Mercier, Anne Pennartz, Bernard Joris, Raphaël Herman, Nathalie Teller, Astrid Zervosen, Jean-Marie Frère, André Luxen
Publikováno v:
Bioorganicmedicinal chemistry. 18(21)
Various peptidoglycan fragments were synthesized from two anhydro-muramic acid derivatives protected with a Bn or a PMB group at the 4th position, in homogenate phase or on a solid support. In order to facilitate HPLC detection, a chromophoric group
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bee24cdfd2a9b41ce94f2d88e18e02cc
https://pubmed.ncbi.nlm.nih.gov/20889346
https://pubmed.ncbi.nlm.nih.gov/20889346
Autor:
Astrid Zervosen, Nathalie Teller, Colette Duez, Fabrice Bouillenne, Rémy Melkonian, Jean-Marie Frère, Emmanuel Banzubazé, André Luxen
Publikováno v:
FEMS microbiology letters. 300(1)
In Bacillus subtilis, the yoxA and dacC genes were proposed to form an operon. The yoxA gene was overexpressed in Escherichia coli and its product fused to a polyhistidine tag was purified. An aldose-1-epimerase or mutarotase activity was measured wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffe3440c044209238e9576b462c7d101
https://pubmed.ncbi.nlm.nih.gov/19758330
https://pubmed.ncbi.nlm.nih.gov/19758330
Autor:
Thomas Gerards, Steven R. Inglis, Christopher J. Schofield, Nathalie Teller, André Luxen, Astrid Zervosen, Esther C. Y. Woon, Delphine S Fischer
Publikováno v:
Journal of medicinal chemistry. 52(19)
Penicillin binding proteins (PBPs) catalyze steps in the biosynthesis of bacterial cell walls and are the targets for the beta-lactam antibiotics. Non-beta-lactam based antibiotics that target PBPs are of interest because bacteria have evolved resist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23f79345e64e0033bc4c3e4ba2a44b94
https://pubmed.ncbi.nlm.nih.gov/19731939
https://pubmed.ncbi.nlm.nih.gov/19731939
Autor:
Pauline, Macheboeuf, David, Lemaire, Nathalie, Teller, Alexandre Dos Santos, Martins, André, Luxen, Otto, Dideberg, Marc, Jamin, Andréa, Dessen
Publikováno v:
Journal of molecular biology. 376(2)
Class A penicillin-binding proteins (PBPs) catalyze the last two steps in the biosynthesis of peptidoglycan, a key component of the bacterial cell wall. Both reactions, glycosyl transfer (polymerization of glycan chains) and transpeptidation (cross-l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1d446887a26328031db3074adc1b0ec
https://pubmed.ncbi.nlm.nih.gov/18155726
https://pubmed.ncbi.nlm.nih.gov/18155726