Publications by authors named "Saudrais C"

Laparoscopic surgery brings substantial benefits to patients. However, it remains challenging for surgeons because of motion constraints and perception limitations. Notably, the perception of interactions with organs is largely compromised.

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We present an integrated proteomics platform designed for performing differential analyses. Since reproducible results are essential for comparative studies, we explain how we improved reproducibility at every step of our laboratory processes, e.g.

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Human blood plasma is a useful source of proteins associated with both health and disease. Analysis of human blood plasma is a challenge due to the large number of peptides and proteins present and the very wide range of concentrations. In order to identify as many proteins as possible for subsequent comparative studies, we developed an industrial-scale (2.

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Live trout spermatozoa initiate flagellar motility for a short period of time (30 s at 18 degrees C), during which their mean beat frequency (BF) decreases steadily from 60 to 20 Hz; motility then stops abruptly. When demembranated, the motility of axonemes lasts much longer, up to 20 min, with high beat frequency, provided that ATP (millimolar concentration) and cAMP (micromolar) are added. In the present paper, the motility of demembranated trout sperm was investigated in the absence of added ATP in various incubation conditions relative to other substrates.

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Binding of antigenic peptides to MHC class II (MHC-II) molecules occurs in the endocytic pathway. From previous studies in B lymphocytes, it is believed that most but not all of the newly synthesized MHC-II molecules are directly targeted from the trans-Golgi network to endosomal compartments. By using pulse-chase metabolic labeling followed by cell surface biotinylation, we show here that in contrast to an EBV-transformed B cell line and human monocytes, the majority of newly synthesized MHC-II molecules (at least 55 +/- 13%) are first routed to the plasma membrane of dendritic cells derived from human monocytes.

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The newly synthesized major histocompatibility complex (MHC) class II molecules, an alphabeta dimer associated with the Ii invariant chain, must be targeted to endosomal, lysosomal enzyme-rich compartments in order to bind and present immunogenic peptides. The precise route followed by this complex at the exit of the trans-Golgi network, the last sorting station of the biosynthetic pathway, is poorly understood. We show here that overexpression of alphabetaIi complexes in HeLa cells promotes the first step of clathrin-coat assembly in vitro, that is the ARF-dependent translocation of AP-1 Golgi-specific assembly proteins on membranes.

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