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Showing 1–6 of 6 results
Advanced filters: Author: Claire Delahunty Clear advanced filters

  • Informatics has driven mass spectrometry–based protein analysis to create large-scale methods for proteomics. As software algorithms have developed, comparisons between algorithms are inevitable. We outline steps for fair and objective comparisons that will make true innovations apparent.

    • John R Yates III
    • Sung Kyu Robin Park
    • Paulo Costa Carvalho
    Comments & Opinion
    Nature Methods
    Volume: 9, P: 455-456

  • The analysis of site-specific glycosylation of HIV Envelope glycoprotein (Env) is challenging as it contains 25–30 glycosylation sites with multiple glycan forms at each site. Here the authors present a generally applicable mass spectrometry-based method for site-specific analysis of protein glycosylation that they apply to the analysis of the HIV-1 Env.

    • Liwei Cao
    • Jolene K. Diedrich
    • James C. Paulson
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13

  • HIV envelope (Env) is a potential vaccine antigen and its N-glycans are part of the epitope of broadly neutralizing antibodies. Here, the authors show that glycosylation of Env from infectious virus closely matches Env from recombinant membrane-bound trimers, while it differs significantly from recombinant soluble, cleaved Env trimers.

    • Liwei Cao
    • Matthias Pauthner
    • James C. Paulson
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-14

  • This protocol describes a semiquantitative glycoproteomics method using sequential treatment with endoglycosidases to create unique mass signatures to determine glycan occupancy and proportion of high-mannose and complex glycans at each glycosite.

    • Liwei Cao
    • Jolene K Diedrich
    • James C Paulson
    Protocols
    Nature Protocols
    Volume: 13, P: 1196-1212