Publications by authors named "Peiyi Meng"

Article Synopsis
  • Protein glycosylation is a key post-translational modification that impacts various cellular processes, but analyzing glycoproteins is challenging due to their low abundance and complex structures.
  • This study introduces a fast and efficient method for enriching glycopeptides using bioorthogonal ligation and trypsin cleavage, enabling the identification of over 900 O-GlcNAc sites from just a 500 μg sample.
  • The method allows for the simultaneous detection of multiple glycosylation sites and patterns, particularly during oxidative stress, thus providing a useful tool for studying the biological functions of glycosylation.
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Unlabelled: Asparagine-linked glycosylation protein 1 homolog (ALG1) participates in the initial stage of protein -glycosylation and -glycosylation has been implicated in the process of hepatocellular carcinoma (HCC) progression. However, whether ALG1 plays a role in human HCC remains unknown. In this study, the expression profile of ALG1 in tumorous and corresponding adjacent non-tumor tissues was analyzed.

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A newly synthesized proteome reflects perturbations sensitively and maintains homeostasis in cells. To investigate the low abundant newly synthesized proteins (NSPs) from a complex background proteome, an enrichment process with high selectivity and reliability is essential. Here, we have developed a strategy to realize comprehensive analysis of NSPs by integrating tandem orthogonal proteolysis (TOP) with cleavable bioorthogonal tagging (CBOT) called TOP-CBOT.

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Glycosylation inhibition has great potential in cancer treatment. However, the corresponding cellular response, protein expression and glycosylation changes remain unclear. As a cell-permeable small-molecule inhibitor with reduced cellular toxicity, N-linked glycosylation inhibitor-1 (NGI-1) has become a great approach to regulate glycosylation in mammalian cells.

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Protein synthesis and degradation responding to environmental cues is critical for understanding the mechanisms involved. Chemical proteomics introducing bioorthogonal tagging into proteins and isolation by biotin affinity purification is applicable for enrichment of newly synthesized proteins (NSPs). Current enrichment methods based on biotin-streptavidin interaction lack efficiency to release enriched NSPs under mild conditions.

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