References of "Brouta, F"
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See detailIn vivo m-RNA expression analysis of Microsporum canis secreted subtilisin-like serine proteases in feline dermatophytosis
Mignon, Bernard ULiege; Vermout, Sandy; Brouta, F. et al

in Advances in Veterinary Dermatology (2005)

Detailed reference viewed: 28 (8 ULiège)
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See detailEvaluation of immunogenicity and protective efficacy of a Microsporum canis metalloprotease subunit vaccine in guinea pigs
Vermout, S.; Brouta, F.; Descamps, F. et al

Conference (2004)

Detailed reference viewed: 11 (2 ULiège)
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See detailEvaluation of immunogenicity and protective efficacy of a Microsporum canis metalloprotease subunit vaccine in guinea pigs
Baldo, Aline ULiege; Vermout, S.; Brouta, F. et al

Conference (2004)

Detailed reference viewed: 14 (3 ULiège)
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See detailIn vivo expression analysis of Microsporum canis secreted subtilisin-like serine proteases in feline dermatophytosis
Mignon, Bernard ULiege; Descamps, F.; Brouta, F. et al

in Veterinary Dermatology (2004), 15(suppl 1), 17-18

Detailed reference viewed: 19 (5 ULiège)
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See detailIn vivo detection of three Microsporum canis subtilisin-like serine protease mRNAs in infected guinea-pigs
Descamps, F.; Brouta, F.; Vermout, S. et al

Conference (2003)

Detailed reference viewed: 10 (2 ULiège)
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See detailEvaluation of the specific immune response against a recombinant keratinase of Microsporum canis
Vermout, S.; Brouta, F.; Descamps, F. et al

Conference (2003)

Detailed reference viewed: 10 (2 ULiège)
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See detailIn vivo expression of a Microsporum canis 43.5 kDa metalloprotease in infected guinea pigs
Brouta, F.; Descamps, F.; Monod, M. et al

Poster (2002)

Detailed reference viewed: 16 (3 ULiège)
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See detailTranscription of the Microsporum canis 31.5 kDa keratinase gene in infected guinea-pigs
Descamps, F.; Brouta, F.; Vermout, S. et al

Poster (2002)

Detailed reference viewed: 15 (2 ULiège)
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See detailA retrospective epidemiological survey of canine and feline dermatophytosis in Belgium over the period 1996-2001
Mignon, Bernard ULiege; Hansen, P.; Le Bleis, K. et al

Poster (2002)

Detailed reference viewed: 5 (1 ULiège)
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See detailLe portage asymptomatique de Microsporum canis chez le chat
Mignon, Bernard ULiege; Brouta, F.; Descamps, F. et al

in Annales de Médecine Vétérinaire (2001), 145

Detailed reference viewed: 29 (1 ULiège)
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See detailPerspectives de vaccination anti-dermatophytique chez les carnivores domestiques
Descamps, F.; Brouta, F.; Losson, Bertrand ULiege et al

in Annales de Médecine Vétérinaire (2001), 145

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See detailDonnées récentes sur la pathogenèse de l'infection à Microsporum canis chez les carnivores domestiques
Brouta, F.; Descamps, F.; Losson, Bertrand ULiege et al

in Annales de Médecine Vétérinaire (2001), 145

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See detailPurification and characterization of a 43.5 kDa keratinolytic metalloprotease from Microsporum canis.
Brouta, F.; Descamps, F.; Fett, Thomas ULiege et al

in Medical Mycology (2001), 39(3), 269-275

A keratinolytic protease secreted by a feline clinical isolate of Microsporum canis cultivated in a broth containing feline keratin as the sole nitrogen source was purified from the culture filtrate by ... [more ▼]

A keratinolytic protease secreted by a feline clinical isolate of Microsporum canis cultivated in a broth containing feline keratin as the sole nitrogen source was purified from the culture filtrate by affinity chromatography on bacitracin-agarose and by hydrophobic chromatography on octyl-agarose. The enzyme had an apparent molecular mass of 43.5 kDa and the pI was 7.7. It had a significant activity against keratin azure, elastin-Congo red and denatured type I collagen (azocoll). Using the latter substrate, the optimum pH was around 8 and the apparent optimum temperature around 50 degrees C. The protease was strongly inhibited by 1,10-phenanthroline, phosphoramidon and EDTA. The first 13 N-terminal amino acid sequence showed a 61% homology with that of the extracellular metalloprotease of Aspergillus fumigatus and with the neutral protease I of A. oryzae, confirming that this 43.5 kDa keratinase is a metalloprotease. This keratinolytic metalloprotease could be a virulence-related factor involved in pathophysiological mechanisms of M. canis dermatophytosis. [less ▲]

Detailed reference viewed: 53 (12 ULiège)
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See detailPurification and characterization of a 43.5 kDa keratinolytic metalloprotease from the dermatophyte Microsporum canis
Brouta, F.; Descamps, F.; Fett, Thomas ULiege et al

Poster (2000)

Detailed reference viewed: 33 (7 ULiège)
See detailLe portage asymptomatique de Microsporum canis chez le chat
Mignon, Bernard ULiege; Brouta, F.; Descamps, F. et al

Conference (2000)

Detailed reference viewed: 16 (0 ULiège)
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See detailPurification and characterization of a 43.5 kDa keratinolytic protease from the dermatophyte Microsporum canis
Brouta, F.; Descamps, F.; Fett, Thomas ULiege et al

Poster (2000)

Detailed reference viewed: 15 (4 ULiège)
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See detailPurification and characterization of a 43.5 kDa keratinase from Microsporum canis
Brouta, F.; Descamps, F.; Fett, Thomas ULiege et al

Conference (2000)

Detailed reference viewed: 18 (4 ULiège)
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See detailManagement of Microsporum canis feline dermatophytosis: illustration with a clinical case in a persian cat
Descamps, F.; Brouta, F.; Meyrieux, C. et al

Conference (2000)

Detailed reference viewed: 25 (6 ULiège)