References of "Callebaut, I"
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See detailBovine Leukemia Virus Su Protein Interacts With Zinc, And Mutations Within Two Interacting Regions Differentially Affect Viral Fusion And Infectivity In Vivo
Gatot, Js.; Callebaut, I.; Van Lint, C. et al

in Journal of Virology (2002), 76(16),

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See detailConservative Mutations In The Immunosuppressive Region Of The Bovine Leukemia Virus Transmembrane Protein Affect Fusion But Not Infectivity In Vivo
Gatot, Js.; Callebaut, I.; Mornon, Jp. et al

in Journal of Biological Chemistry (1998), 273(21),

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See detailCommon Prevalence Of Alanine And Glycine In Mobile Reactive Center Loops Of Serpins And Viral Fusion Peptides - Do Prions Possess A Fusion Peptide
Callebaut, I.; Tasso, A.; Brasseur, Robert ULg et al

in Journal of Computer-Aided Molecular Design (1994), 8(2),

Serpin reactive centre loops and fusion peptides released by proteolytic cleavage are particularly mobile. Their amino acid compositions reveal a common and unusual abundance of alanine, accompanied by ... [more ▼]

Serpin reactive centre loops and fusion peptides released by proteolytic cleavage are particularly mobile. Their amino acid compositions reveal a common and unusual abundance of alanine, accompanied by high levels of glycine. These two small residues, which are not simultaneously abundant in stable helices (standard or transmembrane), probably play an important role in mobility. Threonine and valine (also relatively small amino acids) are also abundant in these two kinds of peptides. Moreover, the known 3D structures of an uncleaved serpin reactive centre and a fusion peptide are strikingly similar. Such sequences possess many small residues and are found in several signal peptides and in PrP, a protein associated with spongiform encephalopathies and resembling virus envelope proteins. These properties may be related to the infection mechanisms of these diseases. [less ▲]

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See detailRedox Mechanism For The Chaperone Activity Of Heat-Shock Proteins Hsp-60, Hsp-70 And Hsp-90 As Suggested By Hydrophobic Cluster-Analysis - Hypothesis
Callebaut, I.; Catelli, Mg.; Portetelle, Daniel ULg et al

in Comptes Rendus de l'Académie des Sciences. Série III, Sciences de la Vie (1994), 317(8),

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See detailCloning And Characterization Of Mn, A Human Tumor-Associated Protein With A Domain Homologous To Carbonic-Anhydrase And A Putative Helix-Loop-Helix Dna-Binding Segment
Pastorek, J.; Pastorekova, S.; Callebaut, I. et al

in Oncogene (1994), 9(10),

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See detailBovine Leukaemia Virus: biology and mode of transformation
Burny, A.; Willems, Luc ULg; Callebaut, I. et al

in Viruses and Cancer, Cambridge University Press (1994)

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See detailFunctional Sites Of The Bovine Leukemia-Virus Envelope Glycoproteins Using Structural And Immunological Data
Callebaut, I.; Mornon, Jp.; Burny, A. et al

in Archives Internationales de Physiologie de Biochimie et de Biophysique (1994), 102(2),

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See detailIdentification Of Functional-Sites On Bovine Leukemia-Virus Envelope Glycoproteins Using Structural And Immunological Data
Callebaut, I.; Portetelle, Daniel ULg; Burny, A. et al

in European Journal of Biochemistry (1994), 222(2),

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See detailStructural Similarities Between Chaperone Molecules Of The Hsp60 And Hsp70 Families Deduced From Hydrophobic Cluster-Analysis
Callebaut, I.; Catelli, Mg.; Portetelle, Daniel ULg et al

in Febs Letters (1994), 342(3),

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See detailBovine Leukemia Virus
Kettmann, Richard ULg; Burny, A.; Callebaut, I. et al

in The Retroviridae (1994)

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See detailEnhancement of bovine leukemia virus-induced syncytia formation by di- and tripeptides.
Voneche, V.; Callebaut, I.; Lambrecht, B. et al

in Virology (1993), 192(1),

Short hydrophobic peptides were previously shown to inhibit infectivity of para- and orthomyxoviruses. We tested the ability of a series of di- and tripeptides to interfere with cell fusion induced by ... [more ▼]

Short hydrophobic peptides were previously shown to inhibit infectivity of para- and orthomyxoviruses. We tested the ability of a series of di- and tripeptides to interfere with cell fusion induced by bovine leukemia virus (BLV). Peptides containing a hydrophobic contribution and/or a positive net charge strongly enhanced syncytia formation induced by BLV on CC81 indicator cells. The size of the multinucleated cells was strongly increased (up to 10-fold) in the presence of the enhancer peptides whereas no effect was observed on the indicator cells in the absence of BLV. The peptides thus amplified the fusion process initiated by BLV envelope glycoproteins. The effect was dose-dependent at concentrations ranging from 20 to 640 microM and did not result from an increased expression of BLV proteins. The peptides did not compete with anti-gp51 monoclonal antibodies for the recognition of eight well-defined epitopes of gp51. We consequently hypothesize that the enhancer peptides interact with the membrane of BLV-producing cells and/or indicator cells and propose a model based on molecular modeling. [less ▲]

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See detailVaccination against animal retroviruses.
Portetelle, Daniel ULg; Callebaut, I.; Bex, F. et al

Book (1993)

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See detailPresence Of Growth Hormone-Binding Proteins In Cattle Plasma And Milk
Devolder, A.; Renaville, Robert ULg; Sneyers, M. et al

in Journal of Endocrinology (1993), 138(1),

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See detailMapping Of B-Neutralizing And T-Helper Cell Epitopes On The Bovine Leukemia-Virus External Glycoprotein Gp51
Callebaut, I.; Voneche, V.; Mager, A. et al

in Journal of Virology (1993), 67(9),

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See detailThe 19-27 Amino-Acid Segment Of Gp51 Adopts An Amphiphilic Structure And Plays A Key Role In The Fusion Events Induced By Bovine Leukemia-Virus
Voneche, V.; Callebaut, I.; Kettmann, Richard ULg et al

in Journal of Biological Chemistry (1992), 267(21),

Previous results indicate that the external glycoprotein gp51 of bovine leukemia virus plays an important role in the process of cell fusion induced by bovine leukemia virus (Bruck, C., Mathot, S ... [more ▼]

Previous results indicate that the external glycoprotein gp51 of bovine leukemia virus plays an important role in the process of cell fusion induced by bovine leukemia virus (Bruck, C., Mathot, S., Portetelle, D., Berte, C., Franssen, J. D., Herion, P., and Burny, A. (1982) Virology 122, 342-352; Voneche, V., Portetelle., D., Kettmann, R., Willems, L., Limbach, K., Paoletti, E., Ruysschaert, J. M., Burny, A., and Brasseur, R. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 3810-3814) and suggest that a region encompassing residues 23 and 25 of gp51 is involved in this process (Portetelle, D., Couez, D., Bruck, C., Kettmann, R., Mammerickx, M., Van der Maaten, M., Brasseur, R., and Burny, A. (1989) Virology 169, 27-33; Mamoun, R., Morisson, M., Rebeyrotte, N., Busetta, B., Couez, D., Kettmann, R., Hospital, M., and Guillemain, B. (1990) J. Virol. 64, 4180-4188). X-ray diffraction studies performed on envelope glycoproteins of influenza virus indicate that the NH2-terminal part of the external glycoprotein lies very close to the fusion peptide. The same overall structure seems to exist in human immunodeficiency virus as suggested by site-directed mutagenesis followed by syncytia induction assays. Our theoretical studies indicate that a segment expanding between residues 19 and 27 of gp51 probably adopts an amphipathic beta-strand structure. We hypothesize that the amphipathic 19-27 structure of gp51 plays an important role in the process of membrane fusion by interacting with the fusion peptide or with another region of gp30. Mutational analysis disrupting the amphipathy of the 19-27 region strongly altered the fusogenic capacity of the gp51-gp30 complex. [less ▲]

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See detailUse Of Synthetic Peptides To Map Sequential Epitopes Recognized By Monoclonal-Antibodies On The Bovine Leukemia-Virus External Glycoprotein
Callebaut, I.; Burny, A.; Krchnak, V. et al

in Virology (1991), 185(1),

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