R Shyama Prasad Rao1, Ning Zhang2,3, Dong Xu2,3,4, Ian Max Møller5. 1. Biostatistics and Bioinformatics Division, Yenepoya Research Center, Yenepoya University, Mangalore, Karnataka, India. 2. Informatics Institute, University of Missouri-Columbia, MO, USA. 3. C.S. Bond Life Sciences Center, University of Missouri-Columbia, MO, USA. 4. Department of Electrical Engineering and Computer Science, University of Missouri-Columbia,Columbia, MO, USA. 5. Department of Molecular Biology and Genetics, Aarhus University, Slagelse, Denmark.
Abstract
Motivation: Oxidative stress and protein damage have been associated with over 200 human ailments including cancer, stroke, neuro-degenerative diseases and aging. Protein carbonylation, a chemically diverse oxidative post-translational modification, is widely considered as the biomarker for oxidative stress and protein damage. Despite their importance and extensive studies, no database/resource on carbonylated proteins/sites exists. As such information is very useful to research in biology/medicine, we have manually curated a data-resource (CarbonylDB) of experimentally-confirmed carbonylated proteins/sites. Results: The CarbonylDB currently contains 1495 carbonylated proteins and 3781 sites from 21 species, with human, rat and yeast as the top three species. We have made further analyses of these carbonylated proteins/sites and presented their occurrence and occupancy patterns. Carbonylation site data on serum albumin, in particular, provides a fine model system to understand the dynamics of oxidative protein modifications/damage. Availability and implementation: The CarbonylDB is available as a web-resource and for download at http://digbio.missouri.edu/CarbonylDB/. Supplementary information: Supplementary data are available at Bioinformatics online.
Motivation: Oxidative stress and protein damage have been associated with over 200 human ailments including cancer, stroke, neuro-degenerative diseases and aging. Protein carbonylation, a chemically diverse oxidative post-translational modification, is widely considered as the biomarker for oxidative stress and protein damage. Despite their importance and extensive studies, no database/resource on carbonylated proteins/sites exists. As such information is very useful to research in biology/medicine, we have manually curated a data-resource (CarbonylDB) of experimentally-confirmed carbonylated proteins/sites. Results: The CarbonylDB currently contains 1495 carbonylated proteins and 3781 sites from 21 species, with human, rat and yeast as the top three species. We have made further analyses of these carbonylated proteins/sites and presented their occurrence and occupancy patterns. Carbonylation site data on serum albumin, in particular, provides a fine model system to understand the dynamics of oxidative protein modifications/damage. Availability and implementation: The CarbonylDB is available as a web-resource and for download at http://digbio.missouri.edu/CarbonylDB/. Supplementary information: Supplementary data are available at Bioinformatics online.
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