A comprehensive resource for integrating and displaying protein post-translational modifications
نویسندگان
چکیده
منابع مشابه
Post-translational modifications of protein biopharmaceuticals.
The majority of therapeutic proteins display one or more post-translational modifications (PTMs). These modifications normally influence the biochemical and therapeutic properties of such proteins. Choosing an expression system capable of generating an appropriate product PTM profile remains one of the most crucial decisions a drug developer must make. This review considers the PTMs most often ...
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PhosphoSitePlus (http://www.phosphosite.org) is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins. It encompasses 1,30,000 non-redundant modification sites, primarily phosphorylation, ubiquitinylation and acetylation. The interface is designed for clarity and ease of navi...
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Gene duplication is common in all three domains of life, especially in eukaryotic genomes. The duplicates provide new material for the action of evolutionary forces such as selection or genetic drift. Here we describe a sophisticated procedure to extract duplicated genes (paralogs) from 26 available eukaryotic genomes, to pre-calculate several evolutionary indexes (evolutionary rate, synonymous...
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ProteomeScout (https://proteomescout.wustl.edu) is a resource for the study of proteins and their post-translational modifications (PTMs) consisting of a database of PTMs, a repository for experimental data, an analysis suite for PTM experiments, and a tool for visualizing the relationships between complex protein annotations. The PTM database is a compendium of public PTM data, coupled with us...
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The unique and remarkable physicochemical properties of protein surface topologies give rise to highly specific biomolecular interactions, which form the framework through which living systems are able to carry out their vast array of functions. Technological limitations undermine efforts to probe protein structures and interactions within unperturbed living systems on a large scale. Rapid chem...
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ژورنال
عنوان ژورنال: BMC Research Notes
سال: 2009
ISSN: 1756-0500
DOI: 10.1186/1756-0500-2-111