dbPTM: an information repository of protein post-translational modification
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چکیده
منابع مشابه
dbPTM: an information repository of protein post-translational modification
dbPTM is a database that compiles information on protein post-translational modifications (PTMs), such as the catalytic sites, solvent accessibility of amino acid residues, protein secondary and tertiary structures, protein domains and protein variations. The database includes all of the experimentally validated PTM sites from Swiss-Prot, PhosphoELM and O-GLYCBASE. Only a small fraction of Swis...
متن کاملdbPTM 2016: 10-year anniversary of a resource for post-translational modification of proteins
Owing to the importance of the post-translational modifications (PTMs) of proteins in regulating biological processes, the dbPTM (http://dbPTM.mbc.nctu.edu.tw/) was developed as a comprehensive database of experimentally verified PTMs from several databases with annotations of potential PTMs for all UniProtKB protein entries. For this 10th anniversary of dbPTM, the updated resource provides not...
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Post-translational modifications of proteins control many biological processes. This is also an important process in the pathogenesis of diabetes mellitus. Adiponectin is an insulin-sensitizing adipokine with antidiabetic, anti-atherogenic, anti-inflammatory and cardioprotective properties. The role of posttranslational modifications in regulating the biosynthesis of high molecular weight adipo...
متن کاملdbPTM 3.0: an informative resource for investigating substrate site specificity and functional association of protein post-translational modifications
Protein modification is an extremely important post-translational regulation that adjusts the physical and chemical properties, conformation, stability and activity of a protein; thus altering protein function. Due to the high throughput of mass spectrometry (MS)-based methods in identifying site-specific post-translational modifications (PTMs), dbPTM (http://dbPTM.mbc.nctu.edu.tw/) is updated ...
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Post-translational modifications (PTMs) have been recognized to impact protein function in two ways: (i) orthosterically, via direct recognition by protein domains or through interference with binding; and (ii) allosterically, via conformational changes induced at the functional sites. Because different chemical types of PTMs elicit different structural alterations, the effects of combinatorial...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2006
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/gkj083