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Keywords {🔍}

pubmed, article, google, scholar, cas, plant, cell, central, arabidopsis, protein, nglycosylation, glycosylation, analysis, proteins, deetiolation, biol, proteomics, supplementary, material, maize, plants, mol, shen, physiol, xlsx, nglycoproteome, wang, chem, sci, proteome, nat, seedling, lectin, affinity, development, quantitative, nlinked, kinase, rev, doitpc, research, leaves, concanavalin, chromatography, identification, roles, glycobiology, doipp, characterization, privacy,

Topics {✒️}

nano-lc–ms/ms-based itraq approach lc-maldi-ms/ms analysis quantitative n-glycoproteomic profile large-scale quantitative n-glycoproteome asn-x-ser/thr sequon noncanonical asn-x-cys sequences canonical asn-x-cys sequence bai-chen wang month download article/chapter dynamic n-glycoproteome analysis n-linked glycoproteome profiling n-glycan maturation mutants light-induced de-etiolation lectin affinity chromatography secreted plant n-glycoproteome significantly regulated n-glycopeptides s-locus receptor kinase n-glycosylation regulation patterns large-scale data sets mapping n-glycosylation sites extracytoplasmic leucine-rich repeats calcium/calmodulin-regulated member de-etiolated rice seedlings seedlings undergoing de-etiolation multiple n-glycans cooperate site-specific n-glycosylation prooncogenic factors mir-23b dark-grown arabidopsis thaliana chloroplast-localized carbonic anhydrase n-glycoproteome reveals maize n-glycoproteomic database n-linked glycopeptides van der ploeg n-glycan occupancy integrated view full article pdf n-linked glycosylation article bu applied glycoprotein research n-linked glycans glycosylation profiles n-glycosylation patterns de-etiolation obtained de-etiolation period van damme ej n-glycopeptide profiling zhen yan quantitative proteomics reveals abstract n-glycosylation n-glycan degradation

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         headline:Dynamic N-glycoproteome analysis of maize seedling leaves during de-etiolation using Concanavalin A lectin affinity chromatography and a nano-LC–MS/MS-based iTRAQ approach
         description: The identification of N -glycosylated proteins with information about changes in the level of N -glycosylation during de-etiolation provides a database that will aid further research on plant N -glycosylation and de-etiolation. N-glycosylation is one of the most prominent and abundant protein post-translational modifications in all eukaryotes and in plants it plays important roles in development, stress tolerance and immune responses. Because light-induced de-etiolation is one of the most dramatic developmental processes known in plants, seedlings undergoing de-etiolation are an excellent model for investigating dynamic proteomic profiles. Here, we present a comprehensive, quantitative N-glycoproteomic profile of maize seedlings undergoing 12 h of de-etiolation obtained using Concanavalin A (Con A) lectin affinity chromatography enrichment coupled with a nano-LC–MS/MS-based iTRAQ approach. In total, 1084 unique N-glycopeptides carrying 909 N-glycosylation sites and corresponding to 609 proteins were identified and quantified, including 186 N-glycosylation sites from 162 proteins that were significantly regulated over the course of the 12 h de-etiolation period. Based on hierarchical clustering analysis, the significantly regulated N-glycopeptides were divided into seven clusters that showed different N-glycosylation patterns during de-etiolation. We found no obvious difference in the enriched MapMan bincode categories for each cluster, and these clustered significantly regulated N-glycoproteins (SRNPs) are enriched in miscellaneous, protein, cell wall and signaling, indicating that although the N-glycosylation regulation patterns of these SRNPs might differ, they are involved in similar biological processes. Overall, this study represents the first large-scale quantitative N-glycoproteome of the model C4 plant, maize, which is one of the most important cereal and biofuel crops. Our results greatly expand the maize N-glycoproteomic database and also shed light on the potential roles of N-glycosylation modification during the greening of maize leaves.
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      headline:Dynamic N-glycoproteome analysis of maize seedling leaves during de-etiolation using Concanavalin A lectin affinity chromatography and a nano-LC–MS/MS-based iTRAQ approach
      description: The identification of N -glycosylated proteins with information about changes in the level of N -glycosylation during de-etiolation provides a database that will aid further research on plant N -glycosylation and de-etiolation. N-glycosylation is one of the most prominent and abundant protein post-translational modifications in all eukaryotes and in plants it plays important roles in development, stress tolerance and immune responses. Because light-induced de-etiolation is one of the most dramatic developmental processes known in plants, seedlings undergoing de-etiolation are an excellent model for investigating dynamic proteomic profiles. Here, we present a comprehensive, quantitative N-glycoproteomic profile of maize seedlings undergoing 12 h of de-etiolation obtained using Concanavalin A (Con A) lectin affinity chromatography enrichment coupled with a nano-LC–MS/MS-based iTRAQ approach. In total, 1084 unique N-glycopeptides carrying 909 N-glycosylation sites and corresponding to 609 proteins were identified and quantified, including 186 N-glycosylation sites from 162 proteins that were significantly regulated over the course of the 12 h de-etiolation period. Based on hierarchical clustering analysis, the significantly regulated N-glycopeptides were divided into seven clusters that showed different N-glycosylation patterns during de-etiolation. We found no obvious difference in the enriched MapMan bincode categories for each cluster, and these clustered significantly regulated N-glycoproteins (SRNPs) are enriched in miscellaneous, protein, cell wall and signaling, indicating that although the N-glycosylation regulation patterns of these SRNPs might differ, they are involved in similar biological processes. Overall, this study represents the first large-scale quantitative N-glycoproteome of the model C4 plant, maize, which is one of the most important cereal and biofuel crops. Our results greatly expand the maize N-glycoproteomic database and also shed light on the potential roles of N-glycosylation modification during the greening of maize leaves.
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         Plant Biochemistry
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