Publications by authors named "Laurette Tavel"

Multiple myeloma (MM) is a malignancy of plasma cells characterized by multifocal osteolytic bone lesions. Macroscopic and genetic heterogeneity has been documented within MM lesions. Understanding the bases of such heterogeneity may unveil relevant features of MM pathobiology.

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Despite the considerable progress in understanding the molecular bases of acute myeloid leukemia (AML), new tools to link disease biology to the unpredictable patient clinical course are still needed. Herein, high-throughput metabolomics, combined with the other "-omics" disciplines, holds promise in identifying disease-specific and clinically relevant features.In this study, we took advantage of nuclear magnetic resonance (NMR) to trace AML-associated metabolic trajectory employing two complementary strategies.

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Article Synopsis
  • The study focuses on human Phosphatidylethanolamine binding protein 1 (hPEBP1), which has roles in various cellular processes and is linked to diseases like Alzheimer's and cancer metastasis.
  • Researchers utilized NMR and mass spectrometry to identify the binding site of hPEBP1 for four ligands (GTP, FMN, and a Raf-1 peptide) under conditions that mimic the human body.
  • The findings indicate that all ligands bind to a conserved pocket in hPEBP1, with binding affinities affected by changes in pH, salt concentration, and temperature, and suggest that nearby residues may be crucial for interaction with Raf-1 rather than those directly in the pocket.
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Interactions between beta-lactoglobulin (BLG) in its monomeric form and a wide range of aroma compounds were investigated by Fourier transform infrared (FT-IR) and 2D nuclear magnetic resonance (NMR) spectroscopies. A screening of the ligands was carried out by FT-IR through the amide I region changes of BLG upon binding. The location of two binding sites was determined by 2D NMR from the study of 10 selected ligands with different structures.

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