This authentication occurs automatically, and it is not possible to sign out of an IP authenticated account.Ĭhoose this option to get remote access when outside your institution. Typically, access is provided across an institutional network to a range of IP addresses. If you are a member of an institution with an active account, you may be able to access content in one of the following ways: Get help with access Institutional accessĪccess to content on Oxford Academic is often provided through institutional subscriptions and purchases. With a 67% rise in entries corresponding to 119 genera of prokaryotes, the current update continues to be the exclusive database of experimentally validated comprehensive information about protein glycosylation in prokaryotes. Version 3.0 adds 45 N-glycoprotein entries found in publicly available MS datasets on PRIDE and reviewed by separate research groups, making the dataset more complete and reliable. Harnessing this legacy data for in-silico glycoprotein identification is a smart approach. Over the years, the influx of experimental proteomics data into public repositories like PRIDE has surged. The structure gallery is revamped, wherein the number and quality of the models are upgraded with the help of AlphaFold2. Accordingly, the third update comprises a new section on patents related to glycosylation methods, novel glycosyltransferases, and technologies developed therefrom. The growing research and technology interest in microbial glycoproteins and their enzymes is evident from the steady rise in academic publications and patents in this area. For the second release in 2019, the size and scope of the database were expanded twofold, and experimental data on cognate glycosyltransferases and their accessory proteins was additionally included. The first release of ProGlycProt featured experimentally validated information on glycoproteins only. ProGlycProt is a comprehensive database of experimentally validated information about protein glycosylation in prokaryotes, including the glycoproteins, glycosyltransferases, and their accessory enzymes.
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