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1.
J Int Bioethique Ethique Sci ; 32(2): 99-117, 2021 06 18.
Article in French | MEDLINE | ID: mdl-34553859

ABSTRACT

Our aim is to study the Leopold-Potter relationship in order to draw lessons from it but also a judgement concerning the bioeconomy that the public authorities currently intend to set up (OECD, European Union…). It seems to us that articulating Leopold’s land ethic and Potter’s bioethics allows us to think of a bioeconomy embedded in a bioethics. Moreover, this bioeconomy can constitute an original benchmark against which to compare the bioeconomy that governments are implementing today. The bioeconomy as these authors present it therefore implicitly reveals the limits of the bioeconomy that we are seeking to apply today, and which we may fear will pose many problems in the context of the ecological crisis.


Subject(s)
Bioethics , Economic Development , Biotechnology , European Union , Humans
2.
ACS Chem Biol ; 2(12): 810-8, 2007 Dec 21.
Article in English | MEDLINE | ID: mdl-18154268

ABSTRACT

A 10,000 member peptide nucleic acid (PNA) encoded peptide library was prepared, treated with the Abelson tyrosine kinase (Abl), and decoded using a DNA microarray and a fluorescently labeled secondary antiphosphotyrosine antibody. A dual-color approach ensured internal referencing for each and every member of the library and the generation of robust data sets. Analysis identified 155 peptides (out of 10,000) that were strongly phosphorylated by Abl in full agreement with known Abl specificities. BLAST analysis identified known cellular Abl substrates such as c-Jun amino-terminal kinase as well as new potential target proteins such as the G-protein coupled receptor kinase 6 and diacylglycerol kinase gamma. To illustrate the generalization of this approach, two other tyrosine kinases, human epidermal growth factor 2 (Her2) and vascular endothelial growth factor receptor 2/kinase insert domain protein receptor (VEGFR2/KDR), were profiled allowing characterization of specific peptide sequences known to interact with these kinases; under these conditions Her2 was demonstrated to have a marked preference for D-proline perhaps offering a unique means of targeting and inhibiting this kinase.


Subject(s)
Peptide Library , Peptide Nucleic Acids/chemistry , Peptide Nucleic Acids/metabolism , Protein-Tyrosine Kinases/chemistry , Protein-Tyrosine Kinases/metabolism , Phosphorylation , Protein Kinase Inhibitors/chemistry , Protein Kinase Inhibitors/pharmacology , Protein-Tyrosine Kinases/antagonists & inhibitors , Protein-Tyrosine Kinases/genetics
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