Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Paul Falmagne"'
Publikováno v:
Molecular & Cellular Proteomics. 5:2114-2123
The vomeronasal organ is a chemosensory organ present in most vertebrates and involved in chemical communication. In the last decade, the deciphering of the signal transduction process of this organ has progressed. However, less is known about the vo
Autor:
Tatiana Vallaeys, Sébastien Monchy, Isabelle Noël-Georis, Max Mergeay, Paul Falmagne, Ruddy Wattiez, Renaud Chauvaux
Publikováno v:
PROTEOMICS. 4:151-179
A proteome map of Ralstonia metallidurans strain CH34 was constructed using two-dimensional (2-D) gel electrophoresis in combination with automated Edman degradation and mass spectrometry (MS). R. metallidurans CH34 is the type-strain of a family of
Autor:
Isabelle Noël-Georis, Ruddy Wattiez, F Broeckaert, Christine Cruyt, Alfred Bernard, Paul Falmagne
Publikováno v:
PROTEOMICS. 3:658-665
Previous studies have shown that the pulmonary response to ozone (O(3)) varies greatly among strains of mice, but the factor(s) and the mechanism(s) that are responsible for this differential susceptibility have not yet been clearly identified. The p
Autor:
Jean Paul Langhendries, Cédric Hermans, Alfred Bernard, André Clippe, Ruddy Wattiez, Marjorie Robin, Valérie Libotte, Paul Falmagne
Publikováno v:
Pediatric Research. 50:487-494
The bronchiolar 16 kD Clara cell secretory protein (CC16) and the alveolar surfactant-associated protein A (SP-A) are secreted in the amniotic fluid (AF), where they reflect the growth and the maturity of the fetal lung. To evaluate the possible effe
Publikováno v:
Disease Markers, Vol 17, Iss 4, Pp 271-284 (2001)
Disease Markers
Disease Markers
Most lung disorders are known to be associated to considerable modifications of surfactant composition. Numerous of these abnormalities have been exploited in the past to diagnose lung diseases, allowing proper treatment and follow-up. Diagnosis was
Autor:
Ruddy Wattiez, Jean Marie Ruysschaert, Véronique Cabiaux, Claude Parsot, Philippe J. Sansonetti, Paul Falmagne, Carine De Geyter
Publikováno v:
European Journal of Biochemistry. 267:5769-5776
Entry of Shigella flexneri into epithelial cells and lysis of the phagosome involve the IpaB, IpaC, and IpaD proteins, which are secreted by type III secretion machinery. We report here the purification of IpaB and IpaD and the characterization of th
Autor:
Paul Falmagne, André Clippe, Bernard Knoops, Elee Duconseille, Alfred Bernard, K. Arsalane, Cédric Bogard, Ruddy Wattiez, Cédric Hermans
Publikováno v:
Journal of Biological Chemistry. 274:30451-30458
Using two-dimensional electrophoresis, we have recently identified in human bronchoalveolar lavage fluid a novel protein, termed B166, with a molecular mass of 17 kDa. Here, we report the cloning of human and rat cDNAs encoding B166, which has been r
Autor:
Gérard Toubeau, Jeanine-Anne Heuson-Stiennon, Paul Falmagne, Guy Laurent, Fabrice Journe, Régine Brohée, Denis Nonclercq
Publikováno v:
In Vitro Cellular & Developmental Biology - Animal. 35:339-345
This article describes HKT-1097, a new cell line established from renal tumors induced by the protracted administration of diethylstilbestrol (DES) to male Syrian golden hamsters. Cell culture was initiated from tumor samples obtained from two 14-mo.
Autor:
Paul Falmagne, Ruddy Wattiez, Cabiaux, Vander Borght P, Pierre Quertenmont, Christian Wolff, Jean Marie Ruysschaert
Publikováno v:
Biochemistry. 38:660-666
The interaction of the receptor-binding domain (R domain) of diphtheria toxin with a pure lipid membrane has been characterized by several approaches. Using a photoactivatable lipid, the R domain has been shown to deeply insert in the lipid membrane.
Autor:
Xiao-Ming Wang, Fabien Brossier, Paul Falmagne, Véronique Cabiaux, Jean Marie Ruysschaert, Ruddy Wattiez, Michèle Mock
Publikováno v:
European Journal of Biochemistry. 256:179-183
The protective antigen of Bacillus anthracis is a key protein that promotes the translocation of the enzymatic moieties of the two toxins of B. anthracis into the cell cytoplasm. The membrane topology of the active form of the protective antigen (PA6