Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Jean-Claude Talbot"'
Autor:
Cedric Hurth, Chantal Tassius, Françoise Argoul, Abdelhamid Maali, Cendrine Moskalenko, Jean-Claude Talbot, Philippe Minard, Jean-Pierre Aimé
Publikováno v:
Biosensors and Bioelectronics. 22:2449-2455
This work reports the first evidence that recombinant yeast phosphoglycerate kinase (PGK) is still significantly active when immobilized on glass and muscovite mica. Using previous work to improve the sensitivity of the existing setup, Tapping Mode a
Publikováno v:
Journal of Peptide Science. 11:153-160
Two coumarin-labelled lysines were conveniently prepared as a fluorescence resonance energy transfer (FRET) pair for peptide cleavage detection. 7-Methoxy and 7-diethylamino coumarin-3-carboxylic acids were synthesized according to a modification of
Autor:
Marcel Jozefowicz, Emmanuelle de Raucourt, Sandrine Mauray, Jeanne Dachary-Prigent, Jean-Claude Talbot, Anne-Marie Fischer
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1387:184-194
Heparin exerts its anticoagulant activity by catalysing the inhibition of coagulation proteases by antithrombin (AT). Its main target is thrombin but it also catalyses the inhibition of the other serine-proteases of the coagulation cascade, such as f
Publikováno v:
Colloids and Surfaces B: Biointerfaces. 10:405-412
In order to elucidate the influence on the lipidic environment on the recognition process of its membrane associated receptor, the interactions of the vasoconstrictor peptide endothelin 1 with various phospholipids have been investigated using differ
Autor:
Abdelhamid Maali, Ange Polidori, Bernard Pucci, Jean-Claude Talbot, Bénédicte Salin, Alain Dautant, Marie-France Giraud, Touria Cohen-Bouhacina, Jean Velours, Daniel Brèthes
Publikováno v:
Journal of Bioenergetics and Biomembranes
Journal of Bioenergetics and Biomembranes, Springer Verlag, 2009, 41 (4), pp.349-360. ⟨10.1007/s10863-009-9235-5⟩
Journal of Bioenergetics and Biomembranes, Springer Verlag, 2009, 41 (4), pp.349-360. ⟨10.1007/s10863-009-9235-5⟩
Loss of stability and integrity of large membrane protein complexes as well as their aggregation in a non-lipidic environment are the major bottlenecks to their structural studies. We have tested C(12)H(25)-S-poly-Tris-(hydroxymethyl)acrylamidomethan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d5ac72af899fc3ccf07d70b50855a3d
http://hdl.handle.net/20.500.12278/100406
http://hdl.handle.net/20.500.12278/100406
Autor:
Eric Thiaudière, Odile Siffert, Jean-Claude Talbot, Jean Dufourcq, Joseph E. Alouf, Jacques Bolard
Publikováno v:
European Journal of Biochemistry. 195:203-213
Staphylococcal delta-toxin, a synthetic analogue and a fragment were studied in order to determine their structure in solution and bound in lipids. In solution, a self-association process is observed. Analytical ultracentrifuge and quasi-elastic ligh
Publikováno v:
Journal of peptide science : an official publication of the European Peptide Society. 11(3)
Two coumarin-labelled lysines were conveniently prepared as a fluorescence resonance energy transfer (FRET) pair for peptide cleavage detection. 7-Methoxy and 7-diethylamino coumarin-3-carboxylic acids were synthesized according to a modification of
Autor:
Jean Dufourcq, Odile Siffert, Jean-Claude Talbot, Eric Thiaudière, Michel Vincent, Jacques Gallay
Publikováno v:
European biophysics journal : EBJ. 30(2)
The environment of both the hydrophilic and hydrophobic sides of alpha-helical delta-toxin are probed by tryptophanyl (Trp) fluorescence, when self-association occurs in solution and on binding to membranes. The fluorescence parameters of staphylococ
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 494:19-32
Kinetic studies of pyridoxal 5′-phosphate binding to glutamate dehydrogenase (EC 1.4.1.3) has provided evidence for two specific binding sites, chemically identified as Lys 126 and Lys 333. Use of protecting ligands permitted the selective modifica
Publikováno v:
European Biophysics Journal. 15
Melittin is known to self-associate as tetramers in solutions of high ionic strength. Here, an N-bromosuccinimide oxidized-Trp19 melittin is prepared. This derivative can act as an acceptor of the fluorescence of native melittin and is used in order