ArticleBiophysical journal2001
Database analysis of O-glycosylation sites in proteins.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 137 citations in OpenAlex.
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- Cylindracin, a Cys-rich protein expressed in the fruiting body of Cyclocybe cylindracea, inhibits growth of filamentous fungi but not yeasts or bacteria.FEBS open bio · 2024Article
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- Reg-1α, a New Substrate of Calpain-2 Depending on Its Glycosylation Status.International journal of molecular sciences · 2022Article
- Antiviral strategies should focus on stimulating the biosynthesis of heparan sulfates, not their inhibition.Life sciences · 2021Review
- Impact of Expressing Cells on Glycosylation and Glycan of the SARS-CoV-2 Spike Glycoprotein.ACS omega · 2021Article
- Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2.Glycobiology · 2020Article
- Parallel Determination of Polypeptide and Oligosaccharide Connectivities by Energy-Resolved Collison-Induced Dissociation of Protonated O-Glycopeptides Derived from Nonspecific Proteolysis.Journal of the American Society for Mass Spectrometry · 2020Article
- UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase from the snail Biomphalaria glabrata - structural reflections.Glycoconjugate journal · 2020Article
- Family-based exome sequencing combined with linkage analyses identifies rare susceptibility variants of MUC4 for gastric cancer.PloS one · 2020Article
- Sequence-Specific Mucins for Glycocalyx Engineering.ACS synthetic biology · 2019Article
- Ridge regression estimated linear probability model predictions of O-glycosylation in proteins with structural and sequence data.BMC molecular and cell biology · 2019Article
- Toward Spider Glue: Long Read Scaffolding for Extreme Length and Repetitious Silk Family Genes AgSp1 and AgSp2 with Insights into Functional Adaptation.G3 (Bethesda, Md.) · 2019Article
- Article
- Structural and In Vitro Functional Comparability Analysis of Altebrel™, a Proposed Etanercept Biosimilar: Focus on Primary Sequence and Glycosylation.Pharmaceuticals (Basel, Switzerland) · 2019Article
- From Desert to Medicine: A Review of Camel Genomics and Therapeutic Products.Frontiers in genetics · 2019Review
- Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).Molecular systems biology · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Statistical analysis was carried out to study the sequential aspects of amino acids around the O-glycosylated Ser/Thr. 992 sequences containing O-glycosylated Ser/Thr were selected from the O-GLYCBASE database of O-glycosylated proteins. The frequency of occurrence of amino acid residues around the glycosylated Ser/Thr revealed that there is an increased number of proline residues around the O-glycosylation sites in comparison with the nonglycosylated serine and threonine residues. The deviation parameter calculated as a measure of preferential and nonpreferential occurrence of amino acid residues around the glycosylation site shows that Pro has the maximum preference around the O-glycosylation site. Pro at +3 and/or -1 positions strongly favors glycosylation irrespective of single and multiple glycosylation sites. In addition, serine and threonine are preferred around the multiple glycosylation sites due to the effect of clusters of closely spaced glycosylated Ser/Thr. The preference of amino acids around the sites of mucin-type glycosylation is found likely to be similar to that of the O-glycosylation sites when taken together, but the acidic amino acids are more preferred around Ser/Thr in mucin-type glycosylation when compared totally. Aromatic amino acids hinder O-glycosylation in contrast to N-glycosylation. Cysteine and amino acids with bulky side chains inhibit O-glycosylation. The preference of certain potential sequence motifs of glycosylation has been discussed.
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