References of "Wattiez, R"
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See detailSkin mucus of Cyprinus carpio inhibits cyprinid herpesvirus 3 binding to epidermal cells
RAJ, Victor; Fournier, Guillaume ULg; Rakus, Krzysztof ULg et al

in Veterinary Research (2011), 42(92),

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See detailIdentification and localization of the structural proteins of anguillid herpesvirus 1
Van Beurden, Steven ULg; Leroy, B; Wattiez, R et al

in Veterinary Research (2011), 42(1), 105

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See detailThe genome of cyprinid herpesvirus 3 encodes 40 proteins incorporated in mature virions
Michel, Benjamin ULg; Leroy, B.; Victor, Stalinraj ULg et al

in Journal of General Virology (The) (2010)

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See detailPhosphorylation Of Histone Deacetylase 7 By Protein Kinase D Mediates T Cell Receptor-Induced Nur77 Expression And Apoptosis
Dequiedt, Franck ULg; Van Lint, J.; Lecomte, E. et al

in Journal of Experimental Medicine (2005), 201(5),

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See detailIsolement et caractérisation de l'ostéocalcine équine
Carstanjen, Bianca; Wattiez, R.; Amory, Hélène ULg et al

in Annales de Médecine Vétérinaire (2002), 146

Equine bone gamma-carboxyglutamic acid containing protein - also called osteocalcin - has been isolated for the first time till homogeneity. After acid demineralisation and acid extraction, the ... [more ▼]

Equine bone gamma-carboxyglutamic acid containing protein - also called osteocalcin - has been isolated for the first time till homogeneity. After acid demineralisation and acid extraction, the purification procedure was based on reverse phase chromatography, gel filtration and ion exchange chromatography. The amino acid sequence of the primary structure has been determined to be YLDHWLGA(HYP) APYPDPL(GLA)PRR(GLA)VC (GLA)LNPDCDELADHIGF-AYRRFYGPV. The protein has a calculated molecular weight of 5,732 kDa and a calculated isoelectric point of 4,45. It contains 49 amino acids, from which 3 are gamma-carboxyglutamic acid residues at position 17, 21 and 24 and has a fully hydroxylated proline in position nine and cysteine in position 23 and 29. Equine osteocalcin shows a strong homology with bovine (98%), ovine (96%) and human (94%) osteocalcin [less ▲]

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See detailIsolation ad Characterization of osteocalcin in horses
Carstanjen, B; Wattiez, R; Amory, Hélène ULg et al

in Proceedings of the ECVS meeting 2002 (Resident Forum) (2002)

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See detailIsolation and Radioimmunoassay Formation of Equine Osteocalcin- Preliminary Results
Carstanjen, B; Sulon, J; Banga-Mboko, H et al

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2002), 6(1), 8-9

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See detailThe isolation and characterization of equine Osteocalcin
Carstanjen, B; Wattiez, R; Amory, Hélène ULg et al

in Proceedings of the 1st meeting of the International Bone and Mineral Society (IBMS) (2001)

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See detailIdentification of pregnancy-associated glycoprotein 1 (PAG-1) in zebu (Bos indicus) placenta
Melo de Sousa, Noelita ULg; Remy, Benoit; El Amiri, Bouchra et al

in Theriogenology (2001), 55(1), 327

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See detailIsolation of the pregnancy-associated glycoprotein 1 (PAG-1) from zebu (Bos indicus) placenta.
Melo de Sousa, Noelita ULg; Remy, B.; El Amiri, B. et al

in Proceedings of the 16th Scientific Meeting of the European Embryo Transfer Association. (2000)

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See detailEvidence For Specific And Non-Covalent Binding Of Lipids To Natural And Recombinant Mycobacterium Bovis Bcg Hsp60 Proteins, And To The Escherichia Coli Homologue Groel
De Bruyn, J.; Soetaert, K.; Buyssens, P. et al

in Microbiology-Sgm (2000), 146

Heat-shock proteins (Hsps) from various origins are known to share a conserved structure and are assumed to be key partners in the biogenesis of proteins. Fractionation of the mycobacterial Hsp60, a 65 ... [more ▼]

Heat-shock proteins (Hsps) from various origins are known to share a conserved structure and are assumed to be key partners in the biogenesis of proteins. Fractionation of the mycobacterial Hsp60, a 65 kDa protein also called Cpn60, from Mycobacterium bovis BCG zinc-deficient culture filtrate on phenyl-Sepharose followed by Western blotting revealed the existence of four Hsp60-1 and Hsp60-2 forms, based on their hydrophobicity behaviour. Hsp60-2 species were further purified by ion-exchange chromatography and partial amino acid sequences of cyanogen bromide (CNBr) peptides of purified Hsp60-2 species showed identity with the amino acid sequence deduced from the hsp60-2 gene, indicating that the various Hsp60-2 forms are encoded by the same gene. In addition, the mycobacterial Hsp60-2 was overexpressed in E. coli using the pRR3Hsp60-2 plasmid and analysed on phenyl-Sepharose. The elution pattern of the recombinant Hsp60-2, as well as that of Escherichia coli GroEL, was similar to that of the native Hsp60-2 from the culture filtrate of M. bovis BCG and entirely different from that of the mycobacterial antigen 85. Extraction of mycobacterial Hsp60-2 forms, recombinant BCG Hsp60-2 and E. coli GroEL with organic solvents releases various amounts of non-covalently bound lipids. The presence of lipids on Hsp60-2 was confirmed by labelling M. bovis BCG with radioactive palmitate. The radioactivity was specifically associated with Hsp60 in the aqueous phase and the 19 and 38 kDa lipoproteins in the Triton X-114 phase. Analysis of the lipids extracted from purified Hsp60-2, recombinant BCG Hsp60-2 and E. coli GroEL by TLC showed the same pattern for all the samples. Acid methanolysis of the lipids followed by GC analysis led to the identification of C(16:0), C(18:0) and C(18:1) as the major fatty acyl constituents, and of methylglycoside in these proteins. Altogether, these data demonstrate that lipids are non-covalently bound to Hsp60-2 and homologous proteins. [less ▲]

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See detailIdentification of antigens recognized in the developing mouse brain by the RC2 antibody, a marker of radial glia
Leprince, Pierre ULg; Chanas-Sacre, G.; Wattiez, R. et al

in International Journal of Developmental Neuroscience (1996), 14(Sup. 1), 84

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