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10.1021/ac4006556

http://scihub22266oqcxt.onion/10.1021/ac4006556
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C3692395!3692395!23662732
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suck abstract from ncbi


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pmid23662732      Anal+Chem 2013 ; 85 (12): 5666-75
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  • Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures #MMPMID23662732
  • Strum JS; Nwosu CC; Hua S; Kronewitter SR; Seipert RR; Bachelor RJ; An HJ; Lebrilla CB
  • Anal Chem 2013[Jun]; 85 (12): 5666-75 PMID23662732show ga
  • Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics. Effective methods require new approaches in sample preparation, detection, and data analysis. While the field has advanced in sample preparation and detection, automated data analysis remains an important goal. A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and compliments experimental techniques that are optimal for glycopeptides, including non-specific proteolysis and high mass resolution LC/MS/MS. SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of non-random glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA). The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
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