References of "Kettmann, Richard"
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See detailThe Yxxl Signaling Motifs Of The Bovine Leukemia-Virus Transmembrane Protein Are Required For In-Vivo Infection And Maintenance Of High Viral Loads
Willems, Luc ULg; Gatot, Js.; Mammerickx, M. et al

in Journal of Virology (1995), 69(7),

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See detailDéveloppement du tissu adipeux chez le porc
Claes, Victor; Chaput, Mariella; Nicolas, Nathalie et al

in Agricontact (1995), 279

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See detailIGF-I and IGFBPs in plasma of growing Landrace and Largewhite pigs
Messina, Maria; Prandi, Alberto; Kettmann, Richard ULg et al

in 14th International Pig Veterinary Society Congress (1995)

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See detailTaqI restriction fragment length polymorphism for pig growth hormone in pigs
Nicolas, Nathalie; Fumière, Olivier; Prandi, Alberto et al

in 14th International Pig Veterinary Society Congress (1995)

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See detailNucleotide sequence of the ovine P53 tumor-suppressor cDNA and its genomic organization.
Dequiedt, Franck ULg; Kettmann, Richard ULg; Burny, A. et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1995), 5(4),

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See detailNucleotide sequence of the bovine P53 tumor-suppressor cDNA.
Dequiedt, Franck ULg; Willems, Luc ULg; Burny, A. et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1995), 5(4),

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See detailStearoyl coenzyme A desaturase gene expression varies between adipose tissues and between Pietrain and Large White pig breeds
Nicolas, Nathalie; Claes, Victor; Chaput, Mariella et al

Poster (1995)

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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 detailInvolvement Of The Cyclic Amp-Responsive Element-Binding Protein In Bovine Leukemia-Virus Expression In-Vivo
Adam, E.; Kerkhofs, P.; Mammerickx, M. et al

in Journal of Virology (1994), 68(9),

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See detailAttenuation Of Bovine Leukemia-Virus By Deletion Of R3 And G4 Open Reading Frames
Willems, Luc ULg; Kerkhofs, P.; Dequiedt, Franck ULg et al

in Proceedings of the National Academy of Sciences of the United States of America (1994), 91(24),

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See detailExpression Of Interleukin-6 Receptors And Interleukin-6 Messenger-Rna By Bovine Leukemia Virus-Induced Tumor-Cells
Droogmans, L.; Cludts, I.; Cleuter, Y. et al

in Cytokine (1994), 6(6),

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See detailIsolation of the missing 5-end of the encoding region of the bovine leukemia virus cell receptor gene.
Ban, J.; Truong, A. T.; Horion, B. et al

in Archives of Virology (1994), 138(3-4),

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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 detailIn vivo infection of sheep by bovine leukemia virus mutants.
Willems, Luc ULg; Kettmann, Richard ULg; Dequiedt, Franck ULg et al

in Journal of virology (1993), 67(7),

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See detailBovine leukemia virus, an animal model for the study of intrastrain variability.
Willems, Luc ULg; Thienpont, E.; Kerkhofs, P. et al

in Journal of Virology (1993), 67(2),

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See detailFusogenic Segments Of Bovine Leukemia-Virus And Simian Immunodeficiency Virus Are Interchangeable And Mediate Fusion By Means Of Oblique Insertion In The Lipid Bilayer Of Their Target-Cells
Voneche, V.; Portetelle, Daniel ULg; Kettmann, Richard ULg et al

in Proceedings of the National Academy of Sciences of the United States of America (1992), 89(9),

Modified bovine leukemia virus (BLV) glycoproteins were expressed by using vaccinia virus recombinants, and their fusogenic capacities were examined by a syncytia-formation assay. This analysis indicates ... [more ▼]

Modified bovine leukemia virus (BLV) glycoproteins were expressed by using vaccinia virus recombinants, and their fusogenic capacities were examined by a syncytia-formation assay. This analysis indicates that (i) both BLV envelope glycoproteins gp51 and gp30 are necessary for cell fusion; (ii) insertion of the N-terminal segment of gp30 (fusion peptide) into the lipid bilayer in an oblique orientation, as predicted by computer conformational analysis, results in fusogenic capacities higher than insertion in a perpendicular or parallel orientation; and (iii) replacement of the BLV fusion peptide with its simian immunodeficiency virus counterpart does not modify the fusogenic capacity of the BLV glycoprotein. [less ▲]

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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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