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Journal articles on the topic 'N-glycosylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Pasing, Yvonne, Albert Sickmann, and Urs Lewandrowski. "N-glycoproteomics: mass spectrometry-based glycosylation site annotation." Biological Chemistry 393, no. 4 (2012): 249–58. http://dx.doi.org/10.1515/hsz-2011-0245.

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Abstract Glycosylations are ubiquitous and, in many cases, essential protein modifications. Yet comprehensive and detailed analysis of glycosylations on a proteome-wide scale is a daunting and still unsolved challenge. However, a common workflow has emerged over the last decade for large-scale N-glycosylation site annotation by application of proteomic methodology. Thereby, the qualitative and quantitative assessment of hundreds or thousands of modification sites is enabled. This review presents a short overview about common enrichment techniques and glycosylation site detection for N-glycopep

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2

Dobrica, Mihaela-Olivia, Catalin Lazar, and Norica Branza-Nichita. "N-Glycosylation and N-Glycan Processing in HBV Biology and Pathogenesis." Cells 9, no. 6 (2020): 1404. http://dx.doi.org/10.3390/cells9061404.

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Hepatitis B Virus (HBV) glycobiology has been an area of intensive research in the last decades and continues to be an attractive topic due to the multiple roles that N-glycosylation in particular plays in the virus life-cycle and its interaction with the host that are still being discovered. The three HBV envelope glycoproteins, small (S), medium (M) and large (L) share a very peculiar N-glycosylation pattern, which distinctly regulates their folding, degradation, assembly, intracellular trafficking and antigenic properties. In addition, recent findings indicate important roles of N-linked ol

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3

Maia, Ivan G., and Adilson Leite. "N-glycosylation in sugarcane." Genetics and Molecular Biology 24, no. 1-4 (2001): 231–34. http://dx.doi.org/10.1590/s1415-47572001000100030.

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The N-linked glycosylation of secretory and membrane proteins is the most complex posttranslational modification known to occur in eukaryotic cells. It has been shown to play critical roles in modulating protein function. Although this important biological process has been extensively studied in mammals, much less is known about this biosynthetic pathway in plants. The enzymes involved in plant N-glycan biosynthesis and processing are still not well defined and the mechanism of their genetic regulation is almost completely unknown. In this paper we describe our first attempt to understand the

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Crunkhorn, Sarah. "Targeting tumour N-glycosylation." Nature Reviews Drug Discovery 21, no. 3 (2022): 180. http://dx.doi.org/10.1038/d41573-022-00028-y.

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5

Karav, Sercan, J. German, Camille Rouquié, Annabelle Le Parc, and Daniela Barile. "Studying Lactoferrin N-Glycosylation." International Journal of Molecular Sciences 18, no. 4 (2017): 870. http://dx.doi.org/10.3390/ijms18040870.

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6

Nino Guram, Karkashadze, Rusudan Zurab, Uridia, Nana Prokof, Tserodze, et al. "N-glycosylation of proteins." World Journal of Advanced Research and Reviews 26, no. 1 (2025): 3570–75. https://doi.org/10.30574/wjarr.2025.26.1.1348.

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Maillard reaction includes interaction of reducing sugar with any compound containing free amino group, which is resulted in formation of colored high-molecular compounds [1, 2]. Despite intensive research, a complete mechanism of Maillard reaction is still undefined. Primary product of reaction between sugars and amino acids, N-glycoside right after its formation experiences two types of transformations: 1. hydrolyzation into initial products and 2. rearrangement according to scheme offered by Amadori, which product is 1-amino-1-deoxy-2 ketose [3]. We have studied proteins N-glycosylation mec

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7

Balieu, Juliette, Jae-Wan Jung, Philippe Chan, George P. Lomonossoff, Patrice Lerouge, and Muriel Bardor. "Investigation of the N-Glycosylation of the SARS-CoV-2 S Protein Contained in VLPs Produced in Nicotiana benthamiana." Molecules 27, no. 16 (2022): 5119. http://dx.doi.org/10.3390/molecules27165119.

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The emergence of the SARS-CoV-2 coronavirus pandemic in China in late 2019 led to the fast development of efficient therapeutics. Of the major structural proteins encoded by the SARS-CoV-2 genome, the SPIKE (S) protein has attracted considerable research interest because of the central role it plays in virus entry into host cells. Therefore, to date, most immunization strategies aim at inducing neutralizing antibodies against the surface viral S protein. The SARS-CoV-2 S protein is heavily glycosylated with 22 predicted N-glycosylation consensus sites as well as numerous mucin-type O-glycosyla

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8

Pinna, Alessandro, and Christian Marcus Pedersen. "Chemoselectivity in Self-Promoted Glycosylation: N - vs. O -Glycosylation." European Journal of Organic Chemistry 2020, no. 25 (2020): 3914–17. http://dx.doi.org/10.1002/ejoc.202000526.

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9

Mammadova-Bach, Elmina, Jaak Jaeken, Thomas Gudermann, and Attila Braun. "Platelets and Defective N-Glycosylation." International Journal of Molecular Sciences 21, no. 16 (2020): 5630. http://dx.doi.org/10.3390/ijms21165630.

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N-glycans are covalently linked to an asparagine residue in a simple acceptor sequence of proteins, called a sequon. This modification is important for protein folding, enhancing thermodynamic stability, and decreasing abnormal protein aggregation within the endoplasmic reticulum (ER), for the lifetime and for the subcellular localization of proteins besides other functions. Hypoglycosylation is the hallmark of a group of rare genetic diseases called congenital disorders of glycosylation (CDG). These diseases are due to defects in glycan synthesis, processing, and attachment to proteins and li

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10

Ryu, Kyoung-Seok, Jie-Oh Lee, Taek Hun Kwon, et al. "The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin." Biochemical Journal 421, no. 1 (2009): 87–96. http://dx.doi.org/10.1042/bj20082170.

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Although N-glycosylation has been known to increase the stability of glycoproteins, it is difficult to assess the structural importance of glycans in the stabilization of glycoproteins. APA (Antheraea pernyi arylphorin) is an insect hexamerin that has two N-glycosylations at Asn196 and Asn344 respectively. The glycosylation of Asn344 is critical for the folding process; however, glycosylation of Asn196 is not. Interestingly, the N196-glycan (glycosylation of Asn196) remains in an immature form (Glc1Man9GlcNAc2). The mutation of Asn196 to glutamine does not change the ecdysone-binding activity

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11

Scheys, Freja, Els J. M. Van Damme, Jarne Pauwels, An Staes, Kris Gevaert, and Guy Smagghe. "N-glycosylation Site Analysis Reveals Sex-related Differences in Protein N-glycosylation in the Rice Brown Planthopper (Nilaparvata lugens)." Molecular & Cellular Proteomics 19, no. 3 (2020): 529–39. http://dx.doi.org/10.1074/mcp.ra119.001823.

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Glycosylation is a common modification of proteins and critical for a wide range of biological processes. Differences in protein glycosylation between sexes have already been observed in humans, nematodes and trematodes, and have recently also been reported in the rice pest insect Nilaparvata lugens. Although protein N-glycosylation in insects is nowadays of high interest because of its potential for exploitation in pest control strategies, the functionality of differential N-glycosylation between sexes is yet unknown. In this study, therefore, the occurrence and role of sex-related protein N-

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12

Altmann, Friedrich. "N-Glycosylation in Insects Revisited." Trends in Glycoscience and Glycotechnology 8, no. 40 (1996): 101–14. http://dx.doi.org/10.4052/tigg.8.101.

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13

Parodi, Armando J. "N-Glycosylation in trypanosomatid protozoa." Glycobiology 3, no. 3 (1993): 193–99. http://dx.doi.org/10.1093/glycob/3.3.193.

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14

Clerc, Florent, Karli R. Reiding, Bas C. Jansen, Guinevere S. M. Kammeijer, Albert Bondt, and Manfred Wuhrer. "Human plasma protein N-glycosylation." Glycoconjugate Journal 33, no. 3 (2015): 309–43. http://dx.doi.org/10.1007/s10719-015-9626-2.

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15

Pasala, Chiranjeevi, Sahil Sharma, Tanaya Roychowdhury, Elisabetta Moroni, Giorgio Colombo, and Gabriela Chiosis. "N-Glycosylation as a Modulator of Protein Conformation and Assembly in Disease." Biomolecules 14, no. 3 (2024): 282. http://dx.doi.org/10.3390/biom14030282.

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Glycosylation, a prevalent post-translational modification, plays a pivotal role in regulating intricate cellular processes by covalently attaching glycans to macromolecules. Dysregulated glycosylation is linked to a spectrum of diseases, encompassing cancer, neurodegenerative disorders, congenital disorders, infections, and inflammation. This review delves into the intricate interplay between glycosylation and protein conformation, with a specific focus on the profound impact of N-glycans on the selection of distinct protein conformations characterized by distinct interactomes—namely, protein

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16

Fisher, Adam C., Charles H. Haitjema, Cassandra Guarino, et al. "Production of Secretory and Extracellular N-Linked Glycoproteins inEscherichia coli." Applied and Environmental Microbiology 77, no. 3 (2010): 871–81. http://dx.doi.org/10.1128/aem.01901-10.

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ABSTRACTTheCampylobacter jejuni pglgene cluster encodes a complete N-linked protein glycosylation pathway that can be functionally transferred intoEscherichia coli. In this system, we analyzed the interplay between N-linked glycosylation, membrane translocation and folding of acceptor proteins in bacteria. We developed a recombinant N-glycan acceptor peptide tag that permits N-linked glycosylation of diverse recombinant proteins expressed in the periplasm of glycosylation-competentE. colicells. With this “glycosylation tag,” a clear difference was observed in the glycosylation patterns found o

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17

Bandini, Giulia, Andreia Albuquerque-Wendt, Jan Hegermann, John Samuelson, and Françoise H. Routier. "Protein O- and C-Glycosylation pathways in Toxoplasma gondii and Plasmodium falciparum." Parasitology 146, no. 14 (2019): 1755–66. http://dx.doi.org/10.1017/s0031182019000040.

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AbstractApicomplexan parasites are amongst the most prevalent and morbidity-causing pathogens worldwide. They are responsible for severe diseases in humans and livestock and are thus of great public health and economic importance. Until the sequencing of apicomplexan genomes at the beginning of this century, the occurrence of N- and O-glycoproteins in these parasites was much debated. The synthesis of rudimentary and divergent N-glycans due to lineage-specific gene loss is now well established and has been recently reviewed. Here, we will focus on recent studies that clarified classical O-glyc

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18

Kukuruzinska, M. A., and K. Lennon. "Protein N-Glycosylation: Molecular Genetics and Functional Significance." Critical Reviews in Oral Biology & Medicine 9, no. 4 (1998): 415–48. http://dx.doi.org/10.1177/10454411980090040301.

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Protein N-glycosylation is a metabolic process that has been highly conserved in evolution. In all eukaryotes, N-glycosylation is obligatory for viability. It functions by modifying appropriate asparagine residues of proteins with oligosaccharide structures, thus influencing their properties and bioactivities. N-glycoprotein biosynthesis involves a multitude of enzymes, glycosyltransferases, and glycosidases, encoded by distinct genes. The majority of these enzymes are transmembrane proteins that function in the endoplasmic reticulum and Golgi apparatus in an ordered and well-orchestrated mann

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19

Roy, Avishek, Steve Meregini, Zhenglan Chen, et al. "IgE production and stability regulated by Glycosylation in vivo." Journal of Immunology 210, no. 1_Supplement (2023): 151.19. http://dx.doi.org/10.4049/jimmunol.210.supp.151.19.

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Abstract Rationale: Essential functions of IgE have been attributed to specific glycosylations such as oligomannose (Fcer1a binding) and sialylation (pathogenicity). However, no study has examined how glycosylation affects IgE stability in vivo. Methods: Forward genetic screening for IgE specific phenotypes was performed using N-ethyl-N-nitrosourea (ENU) mutagenized mice. One low IgE phenotype, named benadryl, linked to a mutation in Mpi, which is essential for N-linked glycosylation. Benadrylwas validated by CRISPR knock-in . Immunological studies were performed to determine the causative mec

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20

ZHU, Jing, Itaru WATANABE, Amanda POHOLEK, et al. "Allowed N-glycosylation sites on the Kv1.2 potassium channel S1–S2 linker: implications for linker secondary structure and the glycosylation effect on channel function." Biochemical Journal 375, no. 3 (2003): 769–75. http://dx.doi.org/10.1042/bj20030517.

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N-glycosylation is a post-translational modification that plays a role in the trafficking and/or function of some membrane proteins. We have shown previously that N-glycosylation affected the function of some Kv1 voltage-gated potassium (K+) channels [Watanabe, Wang, Sutachan, Zhu, Recio-Pinto and Thornhill (2003) J. Physiol. (Cambridge, U.K.) 550, 51–66]. Kv1 channel S1–S2 linkers vary in length but their N-glycosylation sites are at similar relative positions from the S1 or S2 membrane domains. In the present study, by a scanning mutagenesis approach, we determined the allowed N-glycosylatio

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21

Sagt, C. M. J., B. Kleizen, R. Verwaal, et al. "Introduction of an N-Glycosylation Site Increases Secretion of Heterologous Proteins in Yeasts." Applied and Environmental Microbiology 66, no. 11 (2000): 4940–44. http://dx.doi.org/10.1128/aem.66.11.4940-4944.2000.

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ABSTRACT Saccharomyces cerevisiae is often used to produce heterologous proteins that are preferentially secreted to increase economic feasibility. We used N-glycosylation as a tool to enhance protein secretion. Secretion of cutinase, a lipase, and llama VHH antibody fragments by S. cerevisiae orPichia pastoris improved following the introduction of an N-glycosylation site. When we introduced an N-glycosylation consensus sequence in the N-terminal region of a hydrophobic cutinase, secretion increased fivefold. If an N-glycosylation site was introduced in the C-terminal region, however, secreti

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22

Chaban, Bonnie, Susan M. Logan, John F. Kelly, and Ken F. Jarrell. "AglC and AglK Are Involved in Biosynthesis and Attachment of Diacetylated Glucuronic Acid to the N-Glycan in Methanococcus voltae." Journal of Bacteriology 191, no. 1 (2008): 187–95. http://dx.doi.org/10.1128/jb.00885-08.

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ABSTRACT Recent advances in the field of prokaryotic N-glycosylation have established a foundation for the pathways and proteins involved in this important posttranslational protein modification process. To continue the study of the Methanococcus voltae N-glycosylation pathway, characteristics of known eukaryotic, bacterial, and archaeal proteins involved in the N-glycosylation process were examined and used to select candidate M. voltae genes for investigation as potential glycosyl transferase and flippase components. The targeted genes were knocked out via linear gene replacement, and the re

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23

Nie, Yongwei, and Dongjun Liu. "N-Glycosylation is required for FDNC5 stabilization and irisin secretion." Biochemical Journal 474, no. 18 (2017): 3167–77. http://dx.doi.org/10.1042/bcj20170241.

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Irisin, a myokine derived from the extracellular domain of FNDC5, has been shown to mediate thermogenesis of white adipose tissue. Biochemical data have shown that N-glycosylation of FNDC5 is unlikely to affect ligand or receptor activation of irisin. The N-glycosylation of FNDC5 remains poorly understood. In the present study, we analysed N-glycosylation sites of FNDC5 and found that two potential N-glycosylation sites (Asn36 and Asn81) could indeed be occupied by N-glycan. Furthermore we showed that the lack of N-glycosylation decreases the secretion of irisin, which is relevant to the insta

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24

Pugalenthi, Ganesan, Varadharaju Nithya, Kuo-Chen Chou, and Govindaraju Archunan. "Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence." Protein & Peptide Letters 27, no. 3 (2020): 178–86. http://dx.doi.org/10.2174/0929866526666191002111404.

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Background: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes. N-glycosylation predominantly occurs in N-X-[S/T] sequon where X is any amino acid other than proline. However, not all N-X-[S/T] sequons in proteins are glycosylated. Therefore, accurate prediction of N-glycosylation sites is essential to understand Nglycosylation mechanism. Objective: In this article, our motivation is to develop a computational method to predict Nglycosylation sites in eukaryotic protein sequences. Methods: In this article, we report a random forest method, Nglyc, to predic

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Zhang, Wenyao, Zhiping Yang, Xiaoliang Gao, and Qiong Wu. "Advances in the discovery of novel biomarkers for cancer: spotlight on protein N-glycosylation." Biomarkers in Medicine 14, no. 11 (2020): 1031–45. http://dx.doi.org/10.2217/bmm-2020-0185.

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Progress on glycosylation and tumor markers has not been extensively reported. Glycosylation plays an important part in post-translational modification. Previous research on glycosylation-modified biomarkers has lagged behind due to insufficient understanding of glycosylation-related regulations. However, some new methods and ideas illustrated in recent research may provide new inspirations in the field. This article aims to review current advances in revealing relationship between tumors and abnormal N-glycosylation and discuss leading-edge applications of N-glycosylation in developing novel

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Gong, Qiuming, Corey L. Anderson, Craig T. January, and Zhengfeng Zhou. "Role of glycosylation in cell surface expression and stability of HERG potassium channels." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 1 (2002): H77—H84. http://dx.doi.org/10.1152/ajpheart.00008.2002.

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The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart. We previously showed that HERG channel protein is modified by N-linked glycosylation. HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629). In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels. Our results show that N59

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Gebhard, L. Johanna, Zlata Vershinin, Tomás Alarcón-Schumacher, Jerry Eichler, and Susanne Erdmann. "Influence of N-Glycosylation on Virus–Host Interactions in Halorubrum lacusprofundi." Viruses 15, no. 7 (2023): 1469. http://dx.doi.org/10.3390/v15071469.

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N-glycosylation is a post-translational modification of proteins that occurs across all three domains of life. In Archaea, N-glycosylation is crucial for cell stability and motility, but importantly also has significant implications for virus–host interactions. While some archaeal viruses present glycosylated proteins or interact with glycosylated host proteins, the direct influence of N-glycosylation on archaeal virus–host interactions remains to be elucidated. In this study, we generated an N-glycosylation-deficient mutant of Halorubrum lacusprofundi, a halophilic archaeon commonly used to s

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Liu, Xue, Jiujiao Gao, Yan Sun, et al. "Mutation of N-linked glycosylation in EpCAM affected cell adhesion in breast cancer cells." Biological Chemistry 398, no. 10 (2017): 1119–26. http://dx.doi.org/10.1515/hsz-2016-0232.

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Abstract Epithelial cell adhesion molecule (EpCAM) expression is elevated in breast cancer tissue, and correlates with the cancer metastasis and cell adhesion. Although EpCAM glycosylation is supposed to be associated with its function, the contribution of N-glycosylation to its function remains unclear. Here we analyzed cell adhesion ability of EpCAM in breast cancer cells. The results showed that EpCAM expression was associated with cell adhesion and N-glycosylation mutation of EpCAM decreased adhesion capacity. N-glycosylation mutation of EpCAM was correlated with lower levels of integrin β

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Wiedmann, Felix, Daniel Schlund, Niels Voigt, et al. "N-glycosylation–dependent regulation of hK2P17.1 currents." Molecular Biology of the Cell 30, no. 12 (2019): 1425–36. http://dx.doi.org/10.1091/mbc.e18-10-0687.

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Two pore-domain potassium (K2P) channels mediate potassium background currents that stabilize the resting membrane potential and facilitate action potential repolarization. In the human heart, hK2P17.1 channels are predominantly expressed in the atria and Purkinje cells. Reduced atrial hK2P17.1 protein levels were described in patients with atrial fibrillation or heart failure. Genetic alterations in hK2P17.1 were associated with cardiac conduction disorders. Little is known about posttranslational modifications of hK2P17.1. Here, we characterized glycosylation of hK2P17.1 and investigated how

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Pakhrin, Subash C., Kiyoko F. Aoki-Kinoshita, Doina Caragea, and Dukka B. KC. "DeepNGlyPred: A Deep Neural Network-Based Approach for Human N-Linked Glycosylation Site Prediction." Molecules 26, no. 23 (2021): 7314. http://dx.doi.org/10.3390/molecules26237314.

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Protein N-linked glycosylation is a post-translational modification that plays an important role in a myriad of biological processes. Computational prediction approaches serve as complementary methods for the characterization of glycosylation sites. Most of the existing predictors for N-linked glycosylation utilize the information that the glycosylation site occurs at the N-X-[S/T] sequon, where X is any amino acid except proline. Not all N-X-[S/T] sequons are glycosylated, thus the N-X-[S/T] sequon is a necessary but not sufficient determinant for protein glycosylation. In that regard, comput

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Dell, Anne, Alaa Galadari, Federico Sastre, and Paul Hitchen. "Similarities and Differences in the Glycosylation Mechanisms in Prokaryotes and Eukaryotes." International Journal of Microbiology 2010 (2010): 1–14. http://dx.doi.org/10.1155/2010/148178.

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Recent years have witnessed a rapid growth in the number and diversity of prokaryotic proteins shown to carry N- and/or O-glycans, with protein glycosylation now considered as fundamental to the biology of these organisms as it is in eukaryotic systems. This article overviews the major glycosylation pathways that are known to exist in eukarya, bacteria and archaea. These are (i) oligosaccharyltransferase (OST)-mediated N-glycosylation which is abundant in eukarya and archaea, but is restricted to a limited range of bacteria; (ii) stepwise cytoplasmic N-glycosylation that has so far only been c

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32

Naito, Yuko. "Controlling N-Glycosylation in Therapeutic Antibodies." Trends in Glycoscience and Glycotechnology 22, no. 124 (2010): 89–91. http://dx.doi.org/10.4052/tigg.22.89.

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Shakin-Eshleman, Susan H. "Regulation of N-Linked Core-Glycosylation." Trends in Glycoscience and Glycotechnology 8, no. 40 (1996): 115–30. http://dx.doi.org/10.4052/tigg.8.115.

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Tanaka, M., A. Fukuhara, and I. Shimomura. "N-Linked Glycosylation of Mouse Adiponectin." Hormone and Metabolic Research 43, no. 08 (2011): 545–50. http://dx.doi.org/10.1055/s-0031-1280782.

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Nagashima, Yukihiro, Antje von Schaewen, and Hisashi Koiwa. "Function of N-glycosylation in plants." Plant Science 274 (September 2018): 70–79. http://dx.doi.org/10.1016/j.plantsci.2018.05.007.

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36

Österlund, Tommi, Heidi Korhonen, and Pasi Virta. "DNA-Templated N(Me)-Alkoxyamine Glycosylation." Organic Letters 20, no. 6 (2018): 1496–99. http://dx.doi.org/10.1021/acs.orglett.8b00113.

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37

Balog, Crina I. A., Kathrin Stavenhagen, Wesley L. J. Fung, et al. "N-glycosylation of Colorectal Cancer Tissues." Molecular & Cellular Proteomics 11, no. 9 (2012): 571–85. http://dx.doi.org/10.1074/mcp.m111.011601.

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38

Rayon, C., P. Lerouge, and L. Faye. "The protein N-glycosylation in plants." Journal of Experimental Botany 49, no. 326 (1998): 1463–72. http://dx.doi.org/10.1093/jxb/49.326.1463.

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39

He, Yi, Ronald J. Hinklin, Jiyoung Chang, and Laura L. Kiessling. "Stereoselective N-Glycosylation by Staudinger Ligation." Organic Letters 6, no. 24 (2004): 4479–82. http://dx.doi.org/10.1021/ol048271s.

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40

Parkinson, W., M. L. Dear, E. Rushton, and K. Broadie. "N-glycosylation requirements in neuromuscular synaptogenesis." Development 140, no. 24 (2013): 4970–81. http://dx.doi.org/10.1242/dev.099192.

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Gusakov, Alexander V., Alexey I. Antonov, and Boris B. Ustinov. "N-Glycosylation in Chrysosporium lucknowense enzymes." Carbohydrate Research 343, no. 1 (2008): 48–55. http://dx.doi.org/10.1016/j.carres.2007.10.014.

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Leroy, Jules G. "Congenital Disorders of N-Glycosylation Including Diseases Associated With O- as Well as N-Glycosylation Defects." Pediatric Research 60, no. 6 (2006): 643–56. http://dx.doi.org/10.1203/01.pdr.0000246802.57692.ea.

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43

van Beusekom, Bart, Natasja Wezel, Maarten L. Hekkelman, Anastassis Perrakis, Paul Emsley, and Robbie P. Joosten. "Building and rebuilding N-glycans in protein structure models." Acta Crystallographica Section D Structural Biology 75, no. 4 (2019): 416–25. http://dx.doi.org/10.1107/s2059798319003875.

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N-Glycosylation is one of the most common post-translational modifications and is implicated in, for example, protein folding and interaction with ligands and receptors. N-Glycosylation trees are complex structures of linked carbohydrate residues attached to asparagine residues. While carbohydrates are typically modeled in protein structures, they are often incomplete or have the wrong chemistry. Here, new tools are presented to automatically rebuild existing glycosylation trees, to extend them where possible, and to add new glycosylation trees if they are missing from the model. The method ha

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Gross, V., W. E. Hull, U. Berger, et al. "Inhibition of protein N-glycosylation by 2-deoxy-2-fluoro-d-galactose." Biochemical Journal 285, no. 3 (1992): 821–26. http://dx.doi.org/10.1042/bj2850821.

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The effects of 2-deoxy-2-fluoro-D-galactose (dGalF) on N- and O-glycosylation of proteins was studied in rat hepatocyte primary cultures and in human monocytes. In hepatocytes, dGalF at concentrations of 1 mM or higher completely inhibited N-glycosylation of alpha 1-antitrypsin and alpha 1-acid glycoprotein, whereas 4 mM-2-deoxy-D-galactose (dGal) only slightly impaired N-glycosylation. In monocytes, 1 mM- or 4 mM-dGalF blocked N-glycosylation of alpha 1-antitrypsin and of interleukin-6, while O-glycosylation of interleukin-6 remained unaffected. In monocytes, dGal had no effect on protein N-g

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Simard, Marc, Caroline Underhill, and Geoffrey L. Hammond. "Functional implications of corticosteroid-binding globulin N-glycosylation." Journal of Molecular Endocrinology 60, no. 2 (2018): 71–84. http://dx.doi.org/10.1530/jme-17-0234.

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Corticosteroid-binding globulin (CBG) is a plasma carrier of glucocorticoids. Human and rat CBGs have six N-glycosylation sites. Glycosylation of human CBG influences its steroid-binding activity, and there are N-glycosylation sites in the reactive center loops (RCLs) of human and rat CBGs. Proteolysis of the RCL of human CBG causes a structural change that disrupts steroid binding. We now show that mutations of conserved N-glycosylation sites at N238 in human CBG and N230 in rat CBG disrupt steroid binding. Inhibiting glycosylation by tunicamycin also markedly reduced human and rat CBG steroi

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Chen, Minzhen, Bin Yu, Lihua Xu, et al. "Phylogenetic Analysis of the S Gene of Porcine Epidemic Diarrhea Virus (PEDV) in Zhejiang Province, China (2019-2024)." Journal of Agricultural Science 17, no. 6 (2025): 18. https://doi.org/10.5539/jas.v17n6p18.

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To understand the genetic variation trend of the S gene of porcine epidemic diarrhea virus (PEDV) epidemic strains in various regions of Zhejiang Province, this study collected pig diarrhea samples from different pig farms in Zhejiang Province from 2019 to 2024. The positive samples were identified by fluorescence quantitative RT-PCR, and the S gene was cloned, sequenced, and sequenced for comparative analysis. The results showed that among the 49 epidemic strains obtained, 6 were from the GI group and 43 were from the GII group, including 26 from the GIIb subgroup, 12 from the GIIc subgroup,

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Águila, Sonia, Rosina Noto, Ginés Luengo-Gil, et al. "N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function." International Journal of Molecular Sciences 22, no. 2 (2021): 516. http://dx.doi.org/10.3390/ijms22020516.

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N-linked glycosylation is a crucial post-translational modification involved in protein folding, function, and clearance. N-linked glycosylation is also used therapeutically to enhance the half-lives of many proteins. Antithrombin, a serpin with four potential N-glycosylation sites, plays a pivotal role in hemostasis, wherein its deficiency significantly increases thrombotic risk. In this study, we used the introduction of N-glycosylation sites as a tool to explore what effect this glycosylation has on the protein folding, secretion, and function of this key anticoagulant. To accomplish this t

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Larsen, Joachim Steen, Richard Torbjörn Gustav Karlsson, Weihua Tian, et al. "Engineering mammalian cells to produce plant-specific N-glycosylation on proteins." Glycobiology 30, no. 8 (2020): 528–38. http://dx.doi.org/10.1093/glycob/cwaa009.

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Abstract Protein N-glycosylation is an essential and highly conserved posttranslational modification found in all eukaryotic cells. Yeast, plants and mammalian cells, however, produce N-glycans with distinct structural features. These species-specific features not only pose challenges in selecting host cells for production of recombinant therapeutics for human medical use but also provide opportunities to explore and utilize species-specific glycosylation in design of vaccines. Here, we used reverse cross-species engineering to stably introduce plant core α3fucose (α3Fuc) and β2xylose (β2Xyl)

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Mikolajczyk, Krzysztof, Radoslaw Kaczmarek, and Marcin Czerwinski. "How glycosylation affects glycosylation: the role of N-glycans in glycosyltransferase activity." Glycobiology 30, no. 12 (2020): 941–69. http://dx.doi.org/10.1093/glycob/cwaa041.

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Abstract N-glycosylation is one of the most important posttranslational modifications of proteins. It plays important roles in the biogenesis and functions of proteins by influencing their folding, intracellular localization, stability and solubility. N-glycans are synthesized by glycosyltransferases, a complex group of ubiquitous enzymes that occur in most kingdoms of life. A growing body of evidence shows that N-glycans may influence processing and functions of glycosyltransferases, including their secretion, stability and substrate/acceptor affinity. Changes in these properties may have a p

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Shrimal, Shiteshu, Natalia A. Cherepanova, Elisabet C. Mandon, Sergey V. Venev, and Reid Gilmore. "Asparagine-linked glycosylation is not directly coupled to protein translocation across the endoplasmic reticulum in Saccharomyces cerevisiae." Molecular Biology of the Cell 30, no. 21 (2019): 2626–38. http://dx.doi.org/10.1091/mbc.e19-06-0330.

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Mammalian cells express two oligosaccharyltransferase complexes, STT3A and STT3B, that have distinct roles in N-linked glycosylation. The STT3A complex interacts directly with the protein translocation channel to mediate glycosylation of proteins using an N-terminal–to–C-terminal scanning mechanism. N-linked glycosylation of proteins in budding yeast has been assumed to be a cotranslational reaction. We have compared glycosylation of several glycoproteins in yeast and mammalian cells. Prosaposin, a cysteine-rich protein that contains STT3A-dependent glycosylation sites, is poorly glycosylated

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