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Gidday, Department of Ophthalmology, Louisiana State University School of Medicine, 533 Bolivar St., CSRB Room 454, New Orleans, LA 70112; Phone: (504) 568-2360; email: [email protected] groups of proteins play integral roles in both the physiology and pathophysiology of the retina.

However, thorough proteomic analyses of retinas of experimental species are currently unavailable.

Using this high-throughput technique, we have further deciphered and updated the diverse proteome of the mouse retina, including the phosphoproteome, thereby providing the most comprehensive proteomic profile for this tissue known to date.

These findings, and the bioinformatic analyses we also provided, establish a platform for future studies, facilitating the elucidation of the relevance of these proteins to the molecular and cellular pathologies that underlie retinal function and disease.

The purpose of the present paper is providing the field with a comprehensive proteomic characterization of the retina of a commonly used laboratory mouse using a discovery-based mass spectrometry (MS) approach.

On SR-AOP, my group has made significant contribution to the scientific community in terms of advancing the understanding of the mechanisms of the heterogeneous SR-AOP with metal oxides (monometallic oxide and bimetallic oxides) and carbonaceous materials as catalysts to activate composites that exhibit multifunctional properties such as combined catalysis, adsorption-promoted catalysis, switchable catalysis, etc. A facile synthesis of monodispersed hierarchical layered double hydroxide on silica spheres for efficient removal of pharmaceuticals from water. “Cellular processing” and “metabolic processes” contributed the most to biologic activity, at 31% and 26%, respectively.Phosphopeptide enrichment yielded the identification of 610 additional unique proteins that were not originally identified.When coupled to liquid chromatography systems, in conjunction with fractionation and enrichment techniques, more information—and thus, deeper analysis—can be obtained from samples dedicated to MS-based proteomics; this not only yields more proteins, but in turn, also allows for a deeper analyses of the proteome at the bioinformatics level.Advances in the field of proteomics forthcoming from high-throughput, low-abundance molecular enrichment techniques appear to be growing rapidly in other fields, but much less so in ophthalmology.

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