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N-linked is the most common type of glycosylation which plays a significant role in identifying various diseases such as type I diabetes and cancer and helps in drug development. Most of the proteins cannot perform their biological and psychological functionalities without undergoing such modification. Therefore, it is essential to identify such sites by computational techniques because of experimental limitations. This study aims to analyze and synthesize the progress to discover N-linked places using machine learning methods. It also explores the performance of currently available tools to predict such sites. Almost seventy research articles published in recognized journals of the N-linked glycosylation field have shortlisted after the rigorous filtering process. The findings of the studies have been reported based on multiple aspects: publication channel, feature set construction method, training algorithm, and performance evaluation. Moreover, a literature survey has developed a taxonomy of N-linked sequence identification. Our study focuses on the performance evaluation criteria, and the importance of N-linked glycosylation motivates us to discover resources that use computational methods instead of the experimental method due to its limitations.
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http://dx.doi.org/10.7717/peerj-cs.1069 | DOI Listing |
Mol Genet Metab
August 2025
Laboratory for Molecular Diagnosis, Department of Human Genetics, KU Leuven, Leuven, Belgium. Electronic address:
The polyisoprenoid lipid dolichol is critical for eukaryotic glycosylation. It is used as the membrane anchor for mono- or oligosaccharides transferred during N-glycosylation, O/C-mannosylation and glycosylphosphatidylinositol anchor biosynthesis. Disorders affecting the synthesis or utilization of dolichol cause defective glycosylation and are therefore classified as Congenital Disorders of Glycosylation (CDG).
View Article and Find Full Text PDFDevelopmental delay and seizures with or without movement abnormalities (OMIM 617836) caused by heterozygous pathogenic variants in the gene (DHDDS-CDG) is a rare genetic disease that belongs to the progressive encephalopathy spectrum. It results in developmental delay in affected children, accompanied by myoclonus, seizures, ataxia and tremor, which worsens over time. encodes a subunit of a DHDDS/NUS1 cis-prenyltransferase ( PTase), a branch point enzyme of the mevalonate pathway essential for N-linked glycosylation.
View Article and Find Full Text PDFVet Res
August 2025
Key Laboratory of Animal Diseases Diagnostic and Immunology, Ministry of Agriculture, MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, China.
Porcine epidemic diarrhea virus (PEDV), a highly virulent enteric coronavirus, induces severe watery diarrhea and mortality in suckling piglets. The spike (S) protein, a critical mediator of viral entry, undergoes extensive N-linked glycosylation. To elucidate the functional significance of these post-translational modifications, we employed a reverse genetics system to generate 19 recombinant PEDV strains with single-site mutations at predicted N-glycosylation sites.
View Article and Find Full Text PDFArch Iran Med
July 2025
Genetics Research Center, University of Social Welfare and Rehabilitation Sciences, Tehran, Iran.
Background: PMM2-CDG, also known as congenital disorder of glycosylation type 1a, is the most common N-linked glycosylation disorder, characterized by a wide range of neurological and multisystem manifestations. Understanding the genotype-phenotype correlations is essential for accurate diagnosis and patient management. This study aims to identify the genetic cause of PMM2-CDG in an Iranian family with multiple affected members, and to analyze the genetic and clinical spectrum of the disorder through a comprehensive literature review.
View Article and Find Full Text PDFJ Biol Chem
August 2025
Institute of Plant Biotechnology and Cell Biology, Department of Biotechnology and Food Sciences, BOKU University; Vienna, Austria. Electronic address:
N-glycosylation is essential for protein folding in the endoplasmic reticulum (ER). Glycan attachment facilitates the binding of newly synthesised polypeptides to calnexin and calreticulin, two ER-resident lectins that act as chaperones and promote folding. The regulatory mechanism underlying this process is dictated by the glycan composition, and this study has elucidated the function of mannose trimming in the release of misfolded glycoprotein from ER quality control and subsequent transfer to ER-associated degradation (ERAD) in plants.
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