Recovery of polarimetric Stokes images by spatial mixture models.

A Bayesian approach for joint restoration and segmentation of polarization encoded images is presented with emphasis on both physical admissibility and smoothness of the solution. Two distinct models for the sought polarized radiances are used: (i) the polarized light at each site of the image is described by its Stokes vector, which directly follows a mixture of truncated Gaussians, explicitly assigning zero probability to inadmissible configurations and (ii) polarization at each site is represented by the coherency matrix, which is parameterized by a set of variables assumed to be generated by a spatially varying mixture of Gaussians. Application on real and synthetic images using the proposed methods assesses the pertinence of the approach.

Extending mass spectrometry contribution to therapeutic monoclonal antibody lead optimization: characterization of immune complexes using noncovalent ESI-MS.

Monoclonal antibodies (mAbs) have taken on an increasing importance for the treatment of various diseases including cancers, immunological disorders, and other pathologies. These large biomolecules display specific structural features, which affect their efficiency and need, therefore, to be extensively characterized using sensitive and orthogonal analytical techniques. Among them, mass spectrometry (MS) has become the method of choice to study mAb amino acid sequences as well as their post-translational modifications.

Characterization of human and bovine phosphatidylethanolamine-binding protein (PEBP/RKIP) interactions with morphine and morphine-glucuronides determined by noncovalent mass spectrometry.

Background: The phosphatidylethanolamine-binding protein (PEBP/RKIP), initially found to bind phosphatidylethanolamine (PE), has been shown to be associated with morphine derivatives. Our recent study on bovine primary chromaffin cells showed that inside secretory granules, PEBP is noncovalently associated to endogenous morphine-6-glucuronide (M6G), a highly analgesic morphine metabolite. During stress, M6G-PEBP complexes may be released into circulation to target peripheral opioid receptors.