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• W2100485404 abstract "Glycosides of hydroxyproline (Hyp) in the plant cell wall matrix were discovered by Lamport and co-workers in the 1960s. Since then, much has been learned about these Hyp-rich glycoproteins. The intent of this review was to compare and contrast some less common structural motifs, in nontraditional roles, to uncover themes. Arabinosylation of short-peptide plant hormones is essential for growth, cell differentiation and defense. In a very recent development, prolyl hydroxylase and arabinosyltransferase activity has been shown to have a direct impact on the growth of root hairs in Arabidopsis thaliana. Pollen allergens of mugwort and ragweed contain proline-rich domains that are hydroxylated and glycosylated and play a structural role. In the case of mugwort, this domain also presents a significant immunogenic epitope. Major crops, including tobacco and maize, have been used to express and produce recombinant proteins of mammalian origin. The risks of plant-imposed glycosylation are discussed. In unicellular eukaryotes, Skp1 (a subunit of the E3SCF ubiquitin ligase complex) harbors a key Hyp residue that is modified by a linear pentasaccharide. These modifications may be involved in sensing oxygen levels. A few studies have probed the impact of glycosylation on the structure of Hyp-containing peptides. These have necessarily looked at small, synthetic molecules, since natural peptides and proteins are often isolable in only minuscule amounts and/or are heterogeneous in nature. The characterization of native structural motifs, together with the determination of glycopeptide conformation and properties, holds the key to rationalizing nature's architectural design." @default.
• W2100485404 created "2016-06-24" @default.
• W2100485404 creator A5016593302 @default.
• W2100485404 creator A5025220460 @default.
• W2100485404 creator A5037751722 @default.
• W2100485404 date "2011-12-21" @default.
• W2100485404 modified "2023-10-16" @default.
• W2100485404 title "Glycosides of hydroxyproline: Some recent, unusual discoveries" @default.
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• W2100485404 doi "https://doi.org/10.1093/glycob/cwr188" @default.
• W2100485404 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3336868" @default.
• W2100485404 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22190471" @default.
• W2100485404 hasPublicationYear "2011" @default.
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