Alain Guimond

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Transforming growth factor-beta (TGF-beta) signaling requires the functional interaction of two distinct receptors, type I (RI) and type II (RII), at the cell surface. Exposure of cells to TGF-beta results in receptor internalization and down-regulation (Zwaagstra et al., 1999, Exp. Cell Res. 252, 352362); however, little is known about the subsequent fate(More)
XUBF is a Xenopus ribosomal transcription factor of the HMG-box family which contains five tandemly disposed homologies to the HMG1 & 2 DNA binding domains. XUBF has been isolated as a protein doublet and two cDNAs encoding the two molecular weight variants have been characterised. The major two forms of xUBF identified differ by the presence or absence of(More)
Binding surfaces of the type II transforming growth factor (TGF)-beta receptor extracellular domain (TbetaRII-ECD) are mapped by combining scanning-deletion mutagenesis results with knowledge-based modeling of the ectodomain structure. Of the 17 deletion mutants produced within the core binding domain of TbetaRII-ECD, only three retained binding to(More)
s: Session II 7 6 Norman, Sylvia [64] Analysis of TP53 mutations in human malignant gliomas Sylvia Norman1, Adrienne Scheck2 & Jeff Braman1 1Stratagene, La Jolla, California, USA 2Barrow Neurological Institute, Phoenix, Arizona, USA TP53 is involved in the regulation of the cell cycle, response to DNA damage and induction of apoptosis. Mutations in this(More)
Six charged amino acid residues located in the ectodomain of the full-length type I transforming growth factor (TGF)-beta receptor were individually mutated to alanine. Mutation of residues D47, D98, K102 and E104 resulted in functionally impaired receptors as demonstrated by a marked decrease in ligand-dependent signaling and ligand internalization(More)
Site-directed mutagenesis was used to map the ligand-binding surface of the type II transforming growth factor-beta receptor extracellular domain (TbetaRII-ECD). Two putative ligand-binding sites were probed, the first being a predicted hydrophobic patch, the second being the finger 1 surface loop. Nine residues were mutated in the context of full-length(More)
In order to clarify the role of TGF-beta in mammary development and tumorigenesis, we investigated the efficacy of full- or partial-length TbetaRII antisense RNA specifically to reduce TbetaRII levels in both in vitro and in vivo model systems. Here we show that the expression of TbetaRII antisense RNA in vitro reduced TbetaRII cell surface expression and(More)
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