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Journal articles on the topic 'Glycans'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Barre, Annick, Els J. M. Van Damme, Bernard Klonjkowski, et al. "Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses." Cells 11, no. 3 (2022): 339. http://dx.doi.org/10.3390/cells11030339.

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Pathogenic enveloped viruses are covered with a glycan shield that provides a dual function: the glycan structures contribute to virus protection as well as host cell recognition. The three classical types of N-glycans, in particular complex glycans, high-mannose glycans, and hybrid glycans, together with some O-glycans, participate in the glycan shield of the Ebola virus, influenza virus, human cytomegalovirus, herpes virus, human immunodeficiency virus, Lassa virus, and MERS-CoV, SARS-CoV, and SARS-CoV-2, which are responsible for respiratory syndromes. The glycans are linked to glycoprotein

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2

Sun, Xiuping, Hieng Chiong Tie, Bing Chen, and Lei Lu. "Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking." Journal of Biological Chemistry 295, no. 43 (2020): 14750–62. http://dx.doi.org/10.1074/jbc.ra120.014476.

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Most proteins in the secretory pathway are glycosylated. However, the role of glycans in membrane trafficking is still unclear. Here, we discovered that transmembrane secretory cargos, such as interleukin 2 receptor α subunit or Tac, transferrin receptor, and cluster of differentiation 8a, unexpectedly displayed substantial Golgi localization when their O-glycosylation was compromised. By quantitatively measuring their Golgi residence times, we found that the observed Golgi localization of O-glycan–deficient cargos is due to their slow Golgi export. Using a superresolution microscopy method th

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3

Shirakawa, Asuka, Yoshiyuki Manabe, and Koichi Fukase. "Recent Advances in the Chemical Biology of N-Glycans." Molecules 26, no. 4 (2021): 1040. http://dx.doi.org/10.3390/molecules26041040.

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Asparagine-linked N-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of N-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis. This has allowed for progress in the elucidation of N-glycan functions at the molecular level. Interaction analyses with lectins by glycan arrays or nuclear magnetic resonance (NMR) using various N-glycans have revealed the molecular basis for the recognition of complex structures of N-glycans. Preparation of proteins modified with hom

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Cheng, Bo, Qi Tang, Che Zhang, and Xing Chen. "Glycan Labeling and Analysis in Cells and In Vivo." Annual Review of Analytical Chemistry 14, no. 1 (2021): 363–87. http://dx.doi.org/10.1146/annurev-anchem-091620-091314.

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As one of the major types of biomacromolecules in the cell, glycans play essential functional roles in various biological processes. Compared with proteins and nucleic acids, the analysis of glycans in situ has been more challenging. Herein we review recent advances in the development of methods and strategies for labeling, imaging, and profiling of glycans in cells and in vivo. Cellular glycans can be labeled by affinity-based probes, including lectin and antibody conjugates, direct chemical modification, metabolic glycan labeling, and chemoenzymatic labeling. These methods have been applied

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Bushkin, G. Guy, Daniel M. Ratner, Jike Cui, et al. "Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii." Eukaryotic Cell 9, no. 2 (2009): 228–41. http://dx.doi.org/10.1128/ec.00197-09.

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ABSTRACT We are interested in asparagine-linked glycans (N-glycans) of Plasmodium falciparum and Toxoplasma gondii, because their N-glycan structures have been controversial and because we hypothesize that there might be selection against N-glycans in nucleus-encoded proteins that must pass through the endoplasmic reticulum (ER) prior to threading into the apicoplast. In support of our hypothesis, we observed the following. First, in protists with apicoplasts, there is extensive secondary loss of Alg enzymes that make lipid-linked precursors to N-glycans. Theileria makes no N-glycans, and Plas

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Geissner, Andreas, Anika Reinhardt, Christoph Rademacher, et al. "Microbe-focused glycan array screening platform." Proceedings of the National Academy of Sciences 116, no. 6 (2019): 1958–67. http://dx.doi.org/10.1073/pnas.1800853116.

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Interactions between glycans and glycan binding proteins are essential for numerous processes in all kingdoms of life. Glycan microarrays are an excellent tool to examine protein–glycan interactions. Here, we present a microbe-focused glycan microarray platform based on oligosaccharides obtained by chemical synthesis. Glycans were generated by combining different carbohydrate synthesis approaches including automated glycan assembly, solution-phase synthesis, and chemoenzymatic methods. The current library of more than 300 glycans is as diverse as the mammalian glycan array from the Consortium

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7

Wu, Zhengliang L., Anthony D. Person, Yonglong Zou, et al. "Differential distribution of N- and O-Glycans and variable expression of sialyl-T antigen on HeLa cells—Revealed by direct fluorescent glycan imaging." Glycobiology 30, no. 7 (2020): 454–62. http://dx.doi.org/10.1093/glycob/cwz110.

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Abstract Cells are covered with glycans. The expression and distribution of specific glycans on the surface of a cell are important for various cellular functions. Imaging these glycans is essential to aid elucidation of their biological roles. Here, utilizing methods of direct fluorescent glycan imaging, in which fluorescent sialic acids are directly incorporated into substrate glycans via recombinant sialyltranferases, we report the differential distribution of N- and O-glycans and variable expression of sialyl-T antigen on HeLa cells. While the expression of N-glycans tends to be more perip

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8

Tsang, Kwong Y., Massimo Fantini, Anjum Zaki, et al. "Identification of the O-Glycan Epitope Targeted by the Anti-Human Carcinoma Monoclonal Antibody (mAb) NEO-201." Cancers 14, no. 20 (2022): 4999. http://dx.doi.org/10.3390/cancers14204999.

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Truncated O-glycans expressed in cancer cells support tumor progression, and they may serve as potential targets to improve the monitoring and treatment of cancers. Previously, we reported that NEO-201 binds to several tumors expressing tumor-associated CEACAM5 and CEACAM6 variants but does not bind to those expressed in healthy tissues. This specific binding may be associated with the presence of truncated O-glycans attached on the protein sequence of these variants. To evaluate the glycosylation pattern targeted by NEO-201 we performed an O-glycan array consisting of 94 O-glycans. O-glycan p

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Tharmalingam-Jaikaran, T., S. W. Walsh, P. A. McGettigan, et al. "N-glycan profiling of bovine follicular fluid at key dominant follicle developmental stages." REPRODUCTION 148, no. 6 (2014): 569–80. http://dx.doi.org/10.1530/rep-14-0035.

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Follicular fluid (FF), an important microenvironment for the development of oocytes, contains many proteins that are glycosylated withN-linked glycans. This study aimed i) to present an initial analysis of theN-linked glycan profile of bovine FF using hydrophilic interaction liquid chromatography, anion exchange chromatography, high performance liquid chromatography (HPLC)-based separations and subsequent liquid chromatography–mass spectrometry/mass spectrometry analysis; ii) to determine differences in theN-glycan profile between FF from dominant and subordinate follicles from dairy heifers a

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Feng, Hao, and Takumi Yamaguchi. "Effects of Different Adduct Ions, Ionization Temperatures, and Solvents on the Ion Mobility of Glycans." Molecules 30, no. 10 (2025): 2177. https://doi.org/10.3390/molecules30102177.

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The structural analysis of glycans remains a major challenge due to their high isomeric complexity and conformational flexibility arising from diverse glycosidic linkages and dynamic three-dimensional structures. Ion mobility–mass spectrometry (IM–MS) has been attracting attention as a way to develop the structural analysis of glycans. In this study, the effects of ionization conditions—including different types of adduct ions, ionization temperatures, and solvent environments—on the ion mobility behavior of glycans were systematically investigated. IM–MS measurements of ethylamine-tagged glyc

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Zhang, Ying, Yuyang Zhu, Yi Lasanajak, David F. Smith, and Xuezheng Song. "O-Benzylhydroxylamine (BHA) as a Cleavable Tag for Isolation and Purification of Reducing Glycans." SLAS TECHNOLOGY: Translating Life Sciences Innovation 25, no. 4 (2020): 388–96. http://dx.doi.org/10.1177/2472630319898150.

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Glycoscience has been recognized as an important area in biomedical research. Currently, a major obstacle for glycoscience study is the lack of diverse, biomedically relevant, and complex glycans in quantities sufficient for exploring their structural and functional aspects. Complementary to chemoenzymatic synthesis, natural glycans could serve as a great source of biomedically relevant glycans if they are available in sufficient quantities. We have recently developed oxidative release of natural glycans (ORNG) for large-scale release of N-glycans as free reducing glycans. While free reducing

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Han, Jing, Xi Huang, Huihui Liu, Jiyun Wang, Caiqiao Xiong, and Zongxiu Nie. "Laser cleavable probes for in situ multiplexed glycan detection by single cell mass spectrometry." Chemical Science 10, no. 47 (2019): 10958–62. http://dx.doi.org/10.1039/c9sc03912k.

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A single-cell MS approach for multiplexed glycan detection to investigate the relationship between drug resistance and glycans at a single-cell level and quantify multiple glycans, overcoming the limit of low ionization efficiency of glycans.

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Day, Christopher J., Katharina Röltgen, Gerd Pluschke, and Michael P. Jennings. "The cell surface protein MUL_3720 confers binding of the skin pathogen Mycobacterium ulcerans to sulfated glycans and keratin." PLOS Neglected Tropical Diseases 15, no. 2 (2021): e0009136. http://dx.doi.org/10.1371/journal.pntd.0009136.

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Mycobacterium ulceransis the causative agent of the chronic, necrotizing skin disease Buruli ulcer. Modes of transmission and molecular mechanisms involved in the establishment ofM.ulceransinfections are poorly understood. Interactions with host glycans are often crucial in bacterial pathogenesis and the 22 kDaM.ulceransprotein MUL_3720 has a putative role in host cell attachment. It has a predictedN-terminal lectin domain and aC-terminal peptidoglycan-binding domain and is highly expressed on the surface of the bacilli. Here we report the glycan-binding repertoire of whole, fixedM.ulceransbac

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Huxley, Kathryn E., and Lianne I. Willems. "Chemical reporters to study mammalian O-glycosylation." Biochemical Society Transactions 49, no. 2 (2021): 903–13. http://dx.doi.org/10.1042/bst20200839.

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Glycans play essential roles in a range of cellular processes and have been shown to contribute to various pathologies. The diversity and dynamic nature of glycan structures and the complexities of glycan biosynthetic pathways make it challenging to study the roles of specific glycans in normal cellular function and disease. Chemical reporters have emerged as powerful tools to characterise glycan structures and monitor dynamic changes in glycan levels in a native context. A variety of tags can be introduced onto specific monosaccharides via the chemical modification of endogenous glycan struct

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Hanzawa, Ken, Miki Tanaka-Okamoto, Hiroko Murakami, et al. "Increased levels of acidic free-N-glycans, including multi-antennary and fucosylated structures, in the urine of cancer patients." PLOS ONE 17, no. 4 (2022): e0266927. http://dx.doi.org/10.1371/journal.pone.0266927.

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We recently reported increased levels of urinary free-glycans in some cancer patients. Here, we focused on cancer related alterations in the levels of high molecular weight free-glycans. The rationale for this study was that branching, elongation, fucosylation and sialylation, which lead to increases in the molecular weight of glycans, are known to be up-regulated in cancer. Urine samples from patients with gastric cancer, pancreatic cancer, cholangiocarcinoma and colorectal cancer and normal controls were analyzed. The extracted free-glycans were fluorescently labeled with 2-aminopyridine and

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von Messling, Veronika, and Roberto Cattaneo. "N-Linked Glycans with Similar Location in the Fusion Protein Head Modulate Paramyxovirus Fusion." Journal of Virology 77, no. 19 (2003): 10202–12. http://dx.doi.org/10.1128/jvi.77.19.10202-10212.2003.

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ABSTRACT N-linked glycans not only orchestrate the folding and intracellular transport of viral glycoproteins but also modulate their function. We have characterized the three glycans attached to fusion (F) proteins of the morbilliviruses canine distemper virus and measles virus. The individual Morbillivirus glycans have similar functional properties: the glycan at position 68 is essential for protein transport, and those at positions 36 and 75 modulate fusion (numbering according to the Newcastle disease virus [NDV] F protein sequence). Based on the crystal structure of the NDV F protein, we

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Eckardt, Veit, Christian Weber, and Philipp von Hundelshausen. "Glycans and Glycan-Binding Proteins in Atherosclerosis." Thrombosis and Haemostasis 119, no. 08 (2019): 1265–73. http://dx.doi.org/10.1055/s-0039-1692720.

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AbstractComplex glycans are readily accessible on the endothelium and on cell and plasma components. They interact with glycan-binding proteins which translate their structure into function. Advanced analytical tools are available to investigate their structure and functional interactions. Modifications to glycan structures which alter their capacity to bind proteins are particularly relevant in atherosclerosis. We summarize the regulatory role of glycans and their binding partners in the development of the disease. Given their complexity, accessibility, and important functional role, glycans

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Tsuchiya, Shinichiro, Masaaki Matsubara, Kiyoko F. Aoki-Kinoshita, and Issaku Yamada. "SugarDrawer: A Web-Based Database Search Tool with Editing Glycan Structures." Molecules 26, no. 23 (2021): 7149. http://dx.doi.org/10.3390/molecules26237149.

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In life science fields, database integration is progressing and contributing to collaboration between different research fields, including the glycosciences. The integration of glycan databases has greatly progressed collaboration worldwide with the development of the international glycan structure repository, GlyTouCan. This trend has increased the need for a tool by which researchers in various fields can easily search glycan structures from integrated databases. We have developed a web-based glycan structure search tool, SugarDrawer, which supports the depiction of glycans including ambigui

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de Jong, Hanna, Marc M. S. M. Wösten, and Tom Wennekes. "Sweet impersonators: Molecular mimicry of host glycans by bacteria." Glycobiology 32, no. 1 (2021): 11–22. http://dx.doi.org/10.1093/glycob/cwab104.

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Abstract All bacteria display surface-exposed glycans that can play an important role in their interaction with the host and in select cases mimic the glycans found on host cells, an event called molecular or glycan mimicry. In this review, we highlight the key bacteria that display human glycan mimicry and provide an overview of the involved glycan structures. We also discuss the general trends and outstanding questions associated with human glycan mimicry by bacteria. Finally, we provide an overview of several techniques that have emerged from the discipline of chemical glycobiology, which c

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Nanno, Yoshihide, Asif Shajahan, Roberto N. Sonon, Parastoo Azadi, Bernhard J. Hering, and Christopher Burlak. "High-mannose type N-glycans with core fucosylation and complex-type N-glycans with terminal neuraminic acid residues are unique to porcine islets." PLOS ONE 15, no. 11 (2020): e0241249. http://dx.doi.org/10.1371/journal.pone.0241249.

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Objectives Islet transplantation is an emerging treatment option for type 1 diabetes but its application is limited by the shortage of human pancreas donors. Characterization of the N- and O-glycan surface antigens that vary between human and genetically engineered porcine islet donors could shed light on targets of antibody mediated rejection. Methods N- and O-glycans were isolated from human and adult porcine islets and analyzed using matrix-assisted laser-desorption time-of-flight mass spectrometry (MALDI-TOF-MS) and electrospray ionization mass spectrometry (ESI-MS/MS). Results A total of

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Homan, Kentaro, Hisatoshi Hanamatsu, Jun-ichi Furukawa, et al. "Alteration of the Total Cellular Glycome during Late Differentiation of Chondrocytes." International Journal of Molecular Sciences 20, no. 14 (2019): 3546. http://dx.doi.org/10.3390/ijms20143546.

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In normal articular cartilage, chondrocytes do not readily proliferate or terminally differentiate, and exhibit a low level of metabolism. Hypertrophy-like changes of chondrocytes have been proposed to play a role in the pathogenesis of osteoarthritis by inducing protease-mediated cartilage degradation and calcification; however, the molecular mechanisms underlying these changes are unclear. Glycans are located on the outermost cell surface. Dynamic cellular differentiation can be monitored and quantitatively characterized by profiling the glycan structures of total cellular glycoproteins. Thi

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Li, Haiying, Viral Patel, Shannon E. DiMartino, John W. Froehlich, and Richard S. Lee. "An in-depth Comparison of the Pediatric and Adult Urinary N-glycomes." Molecular & Cellular Proteomics 19, no. 11 (2020): 1767–76. http://dx.doi.org/10.1074/mcp.ra120.002225.

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We performed an in-depth characterization and comparison of the pediatric and adult urinary glycomes using a nanoLC-MS/MS based glycomics method, which included normal healthy pediatric (1–10 years, n = 21) and adult (21–50 years, n = 22) individuals. A total of 116 N-glycan compositions were identified, and 46 of them could be reproducibly quantified. We performed quantitative comparisons of the 46 glycan compositions between different age and sex groups. The results showed significant quantitative changes between the pediatric and adult cohorts. The pediatric urinary N-glycome was found to c

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CHITLARU, Theodor, Chanoch KRONMAN, Baruch VELAN, and Avigdor SHAFFERMAN. "Overloading and removal of N-glycosylation targets on human acetylcholinesterase: effects on glycan composition and circulatory residence time." Biochemical Journal 363, no. 3 (2002): 619–31. http://dx.doi.org/10.1042/bj3630619.

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Optimization of post-translational modifications was shown to affect the ability of recombinant human acetylcholinesterase (rHuAChE) produced in HEK-293 cells to be retained in the circulation for prolonged periods of time [Kronman, Velan, Marcus, Ordentlich, Reuveny and Shafferman (1995) Biochem. J. 311, 959–967; Chitlaru, Kronman, Zeevi, Kam, Harel, Ordentlich, Velan and Shafferman (1998) Biochem. J. 336, 647–658; Chitlaru, Kronman, Velan and Shafferman (2001) Biochem. J. 354, 613–625]. To evaluate the possible contribution of the number of appended N-glycans in determining the pharmacokinet

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Krüger, Lynn, Karina Biskup, Carola G. Schipke, et al. "The Cerebrospinal Fluid Free-Glycans Hex1 and HexNAc1Hex1Neu5Ac1 as Potential Biomarkers of Alzheimer’s Disease." Biomolecules 14, no. 5 (2024): 512. http://dx.doi.org/10.3390/biom14050512.

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Alzheimer’s disease (AD) is the most common neurodegenerative disorder, affecting a growing number of elderly people. In order to improve the early and differential diagnosis of AD, better biomarkers are needed. Glycosylation is a protein post-translational modification that is modulated in the course of many diseases, including neurodegeneration. Aiming to improve AD diagnosis and differential diagnosis through glycan analytics methods, we report the glycoprotein glycome of cerebrospinal fluid (CSF) isolated from a total study cohort of 262 subjects. The study cohort consisted of patients wit

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Kim, Jihye, Byoungju Lee, Junmyoung Lee, et al. "N-Glycan Modifications with Negative Charge in a Natural Polymer Mucin from Bovine Submaxillary Glands, and Their Structural Role." Polymers 13, no. 1 (2020): 103. http://dx.doi.org/10.3390/polym13010103.

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Bovine submaxillary mucin (BSM) is a natural polymer used in biomaterial applications for its viscoelasticity, lubricity, biocompatibility, and biodegradability. N-glycans are important for mucin stability and function, but their structures have not been fully characterized, unlike that of O-glycans. In this study, BSM N-glycans were investigated using liquid chromatography-tandem mass spectrometry. The microheterogeneous structures of 32 N-glycans were identified, and the quantities (%) of each N-glycan relative to total N-glycans (100%) were obtained. The terminal N-acetylgalactosamines in 1

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Belický, Štefan, Jaroslav Katrlík, and Ján Tkáč. "Glycan and lectin biosensors." Essays in Biochemistry 60, no. 1 (2016): 37–47. http://dx.doi.org/10.1042/ebc20150005.

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A short description about the importance of glycan biorecognition in physiological (blood cell type) and pathological processes (infections by human and avian influenza viruses) is provided in this review. Glycans are described as much better information storage media, compared to proteins or DNA, due to the extensive variability of glycan structures. Techniques able to detect an exact glycan structure are briefly discussed with the main focus on the application of lectins (glycan-recognising proteins) in the specific analysis of glycans still attached to proteins or cells/viruses. Optical, el

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Jacob, Rajesh Abraham, Thandeka Moyo, Michael Schomaker, Fatima Abrahams, Berta Grau Pujol, and Jeffrey R. Dorfman. "Anti-V3/Glycan and Anti-MPER Neutralizing Antibodies, but Not Anti-V2/Glycan Site Antibodies, Are Strongly Associated with Greater Anti-HIV-1 Neutralization Breadth and Potency." Journal of Virology 89, no. 10 (2015): 5264–75. http://dx.doi.org/10.1128/jvi.00129-15.

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ABSTRACTThe membrane-proximal external region (MPER), the V2/glycan site (initially defined by PG9 and PG16 antibodies), and the V3/glycans (initially defined by PGT121–128 antibodies) are targets of broadly neutralizing antibodies and potential targets for anti-HIV-1 antibody-based vaccines. Recent evidence shows that antibodies with moderate neutralization breadth are frequently attainable, with 50% of sera from chronically infected individuals neutralizing ≥50% of a large, diverse set of viruses. Nonetheless, there is little systematic information addressing which specificities are preferen

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Bachar-Wikstrom, Etty, Kristina A. Thomsson, Carina Sihlbom, et al. "Identification of Novel Glycans in the Mucus Layer of Shark and Skate Skin." International Journal of Molecular Sciences 24, no. 18 (2023): 14331. http://dx.doi.org/10.3390/ijms241814331.

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The mucus layer covering the skin of fish has several roles, including protection against pathogens and mechanical damage. While the mucus layers of various bony fish species have been investigated, the composition and glycan profiles of shark skin mucus remain relatively unexplored. In this pilot study, we aimed to explore the structure and composition of shark skin mucus through histological analysis and glycan profiling. Histological examination of skin samples from Atlantic spiny dogfish (Squalus acanthias) sharks and chain catsharks (Scyliorhinus retifer) revealed distinct mucin-producing

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García-García, A., S. Serna, Z. Yang, et al. "FUT8-Directed Core Fucosylation of N-glycans Is Regulated by the Glycan Structure and Protein Environment." ACS Catalysis 11, no. 15 (2021): 9052–65. https://doi.org/10.1021/acscatal.1c01698.

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FUT8 is an essential alpha-1,6-fucosyltransferase that fucosylates the innermost GlcNAc of N-glycans, a process called core fucosylation. In vitro, FUT8 exhibits substrate preference for the biantennary complex N-glycan oligosaccharide (G0), but the role of the underlying protein/peptide to which N-glycans are attached remains unclear. Here, we explored the FUT8 enzyme with a series of N-glycan oligosaccharides, N-glycopeptides, and an Asn-linked oligosaccharide. We found that the underlying peptide plays a role in fucosylation of paucimannose (low mannose) and high-mannose N-glycans but not f

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Przybyło, M., and A. Lityńska. "Characterization of the oligosaccharide component of arylsulfatase B from rat liver." Acta Biochimica Polonica 44, no. 2 (1997): 181–90. http://dx.doi.org/10.18388/abp.1997_4412.

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A glycan chain analysis of the total oligosaccharide pool derived from rat liver arylsulfatase B was carried out by. P4 Gel Permeation Chromatography and sequential exoglycosidase digestion. It was found that 71% of rat liver arylsulfatase B oligosaccharides were sialylated. The relative contribution of particular structures in the total glycan pool was as follows: sialylated biantennary complex type glycans with terminal galactose--65%, high-mannose type glycans--15%, biantennary complex type glycans with core fucose and terminal N-acetylglucosamine--5%, O-linked oligosaccharides--3.5%.

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Miura, Nobuaki, Hisatoshi Hanamatsu, Ikuko Yokota, et al. "Toolbox Accelerating Glycomics (TAG): Improving Large-Scale Serum Glycomics and Refinement to Identify SALSA-Modified and Rare Glycans." International Journal of Molecular Sciences 23, no. 21 (2022): 13097. http://dx.doi.org/10.3390/ijms232113097.

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Glycans are involved in many fundamental cellular processes such as growth, differentiation, and morphogenesis. However, their broad structural diversity makes analysis difficult. Glycomics via mass spectrometry has focused on the composition of glycans, but informatics analysis has not kept pace with the development of instrumentation and measurement techniques. We developed Toolbox Accelerating Glycomics (TAG), in which glycans can be added manually to the glycan list that can be freely designed with labels and sialic acid modifications, and fast processing is possible. In the present work,

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Wu, Zhengliang L., Mark Whittaker, James M. Ertelt, Anthony D. Person, and Vassili Kalabokis. "Detecting substrate glycans of fucosyltransferases with fluorophore-conjugated fucose and methods for glycan electrophoresis." Glycobiology 30, no. 12 (2020): 970–80. http://dx.doi.org/10.1093/glycob/cwaa030.

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Abstract Like sialylation, fucose usually locates at the nonreducing ends of various glycans on glycoproteins and constitutes important glycan epitopes. Detecting the substrate glycans of fucosyltransferases is important for understanding how these glycan epitopes are regulated in response to different growth conditions and external stimuli. Here we report the detection of these glycans on glycoproteins as well as in their free forms via enzymatic incorporation of fluorophore-conjugated fucose using FUT2, FUT6, FUT7, FUT8 and FUT9. Specifically, we describe the detection of the substrate glyca

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Le, Hoa Thi, Kyu H. Park, Woong Jung, Hyung Soon Park, and Tae Woo Kim. "Combination of Microwave-Assisted Girard Derivatization with Ionic Liquid Matrix for Sensitive MALDI-TOF MS Analysis of Human Serum N-Glycans." Journal of Analytical Methods in Chemistry 2018 (October 21, 2018): 1–7. http://dx.doi.org/10.1155/2018/7832987.

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We developed a new method for MALDI-TOF MS detection of N-glycans derived from human serum. The synergistic combination of microwave-assisted Girard T derivatization, solid-phase extraction desalting, and an ionic liquid matrix (2, 5-dihydroxybenzoic acid/aniline) (GT-SPE-DHB/An) allowed of more sensitive N-glycans detection than a conventional ionic liquid matrix in MALDI-TOF MS. The superior sensitivity of our method was confirmed by the number of assigned N-glycans in 900–2,000 m/z range. Using our GT-SPE-DHB/An method, we were successfully able to assign 31 glycans. However, with the estab

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Li, Yiran, Lele Wang, Lin Ding, and Huangxian Ju. "Cell-Surface Glycan Labeling and Sensing." Targets 2, no. 1 (2023): 1–31. http://dx.doi.org/10.3390/targets2010001.

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Cell-surface glycans are abundant and complex and play a critical role in maintaining protein stability, regulating cell behavior, and participating in cell communication. Obtaining structural information on glycans in situ is helpful to further understand the role of glycans in the physiological and pathological processes of cells and the regulatory mechanism. To achieve this, we can use recognition or labeling strategies to convert the presence of glycans on the cell surface into signals that can be detected. Currently, many different types of in situ sensing strategies for glycans have been

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Takashima, Shou, Masaki Kurogochi, Kenji Osumi та ін. "Novel endo-β-N-acetylglucosaminidases from Tannerella species hydrolyze multibranched complex-type N-glycans with different specificities". Glycobiology 30, № 11 (2020): 923–34. http://dx.doi.org/10.1093/glycob/cwaa037.

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Abstract Endo-β-N-acetylglucosaminidases are enzymes that hydrolyze the N,N′-diacetylchitobiose unit of N-glycans. Many endo-β-N-acetylglucosaminidases also exhibit transglycosylation activity, which corresponds to the reverse of the hydrolysis reaction. Because of these activities, some of these enzymes have recently been used as powerful tools for glycan remodeling of glycoproteins. Although many endo-β-N-acetylglucosaminidases have been identified and characterized to date, there are few enzymes that exhibit hydrolysis activity toward multibranched (tetra-antennary or more) complex-type N-g

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Fujita, Akihiro, Nobuyuki P. Aoki, Daisuke Shinmachi, et al. "The international glycan repository GlyTouCan version 3.0." Nucleic Acids Research 49, no. D1 (2020): D1529—D1533. http://dx.doi.org/10.1093/nar/gkaa947.

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Abstract Glycans serve important roles in signaling events and cell-cell communication, and they are recognized by lectins, viruses and bacteria, playing a variety of roles in many biological processes. However, there was no system to organize the plethora of glycan-related data in the literature. Thus GlyTouCan (https://glytoucan.org) was developed as the international glycan repository, allowing researchers to assign accession numbers to glycans. This also aided in the integration of glycan data across various databases. GlyTouCan assigns accession numbers to glycans which are defined as set

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Bolino, Matthew, Nadini Haththotuwe Gamage, Hatice Duman та ін. "Novel Endo-β-N-Acetylglucosaminidases Derived from Human Fecal Samples Selectively Release N-Glycans from Model Glycoproteins". Foods 14, № 8 (2025): 1288. https://doi.org/10.3390/foods14081288.

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Three novel endo-β-N-acetylglucosaminidases (AVUL01, BCAC01, and BFIN01) classified as members of the glucoside hydrolase (GH) family 18 were identified from human fecal samples and then cloned and characterized for their ability to hydrolyze two distinct classes of N-glycans. Endo-β-N-acetylglucosaminidases (ENGases) are known for the hydrolysis of chitin and the N,N′-diacetylchitobiose core of N-linked glycans, depending on the glycan architecture. N-glycans have shown bioactivity as substrates in the human gut microbiome for microbes that encode ENGases, thus demonstrating their ecological

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Zhou, Qingwen, Yixuan Xie, Matthew Lam, and Carlito B. Lebrilla. "N-Glycomic Analysis of the Cell Shows Specific Effects of Glycosyl Transferase Inhibitors." Cells 10, no. 9 (2021): 2318. http://dx.doi.org/10.3390/cells10092318.

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Glycomic profiling methods were used to determine the effect of metabolic inhibitors on glycan production. These inhibitors are commonly used to alter the cell surface glycosylation. However, structural analysis of the released glycans has been limited. In this research, the cell membranes were enriched and the glycans were released to obtain the N-glycans of the glycocalyx. Glycomic analysis using liquid chromatography–mass spectrometry (LC–MS) with a PGC chip column was used to profile the structures in the cell membrane. Glycans of untreated cells were compared to glycans of cells treated w

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Neelamegham, Sriram, Kiyoko Aoki-Kinoshita, Evan Bolton, et al. "Updates to the Symbol Nomenclature for Glycans guidelines." Glycobiology 29, no. 9 (2019): 620–24. http://dx.doi.org/10.1093/glycob/cwz045.

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Abstract The Symbol Nomenclature for Glycans (SNFG) is a community-curated standard for the depiction of monosaccharides and complex glycans using various colored-coded, geometric shapes, along with defined text additions. It is hosted by the National Center for Biotechnology Information (NCBI) at the NCBI-Glycans Page (www.ncbi.nlm.nih.gov/glycans/snfg.html). Several changes have been made to the SNFG page in the past year to update the rules for depicting glycans using the SNFG, to include more examples of use, particularly for non-mammalian organisms, and to provide guidelines for the depic

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Mickum, Megan L., Nina Salinger Prasanphanich, Xuezheng Song, et al. "Identification of Antigenic Glycans from Schistosoma mansoni by Using a Shotgun Egg Glycan Microarray." Infection and Immunity 84, no. 5 (2016): 1371–86. http://dx.doi.org/10.1128/iai.01349-15.

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Infection of mammals by the parasitic helminthSchistosoma mansoniinduces antibodies to glycan antigens in worms and eggs, but the differential nature of the immune response among infected mammals is poorly understood. To better define these responses, we used a shotgun glycomics approach in which N-glycans from schistosome egg glycoproteins were prepared, derivatized, separated, and used to generate an egg shotgun glycan microarray. This array was interrogated with sera from infected mice, rhesus monkeys, and humans and with glycan-binding proteins and antibodies to gather information about th

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Dimitroff, Charles J. "I-branched carbohydrates as emerging effectors of malignant progression." Proceedings of the National Academy of Sciences 116, no. 28 (2019): 13729–37. http://dx.doi.org/10.1073/pnas.1900268116.

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Cell surface carbohydrates, termed “glycans,” are ubiquitous posttranslational effectors that can tune cancer progression. Often aberrantly displayed or found at atypical levels on cancer cells, glycans can impact essentially all progressive steps, from malignant transformation to metastases formation. Glycans are structural entities that can directly bind promalignant glycan-binding proteins and help elicit optimal receptor–ligand activity of growth factor receptors, integrins, integrin ligands, lectins, and other type-1 transmembrane proteins. Because glycans play an integral role in a cance

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Feleke, Dereje G., Bryan M. Montalban, Solomon T. Gizaw, and Hiroshi Hinou. "Upregulation of Sulfated N-Glycans in Serum as Predictive Biomarkers for Early-Stage Breast Cancer." International Journal of Molecular Sciences 26, no. 11 (2025): 4968. https://doi.org/10.3390/ijms26114968.

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Breast cancer (BC) is a major global health concern, and early detection is key to improving patient outcomes. Aberrant glycosylation, particularly the sulfation of glycans, is implicated in cancer progression; however, analyzing these low-abundance glycans is challenging. This study aimed to profile serum sulfated N-glycans in Ethiopian patients with BC to identify novel biomarkers for the early detection of BC. Using a glycoblotting-based sulphoglycomics workflow, including high-throughput glycoblotting enrichment, weak anion exchange (WAX) separation, and MALDI-TOF MS, serum samples from 76

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Hatchett, Cody J., M. Kristen Hall, Abel R. Messer, and Ruth A. Schwalbe. "Lowered GnT-I Activity Decreases Complex-Type N-Glycan Amounts and Results in an Aberrant Primary Motor Neuron Structure in the Spinal Cord." Journal of Developmental Biology 12, no. 3 (2024): 21. http://dx.doi.org/10.3390/jdb12030021.

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The attachment of sugar to proteins and lipids is a basic modification needed for organismal survival, and perturbations in glycosylation cause severe developmental and neurological difficulties. Here, we investigated the neurological consequences of N-glycan populations in the spinal cord of Wt AB and mgat1b mutant zebrafish. Mutant fish have reduced N-acetylglucosaminyltransferase-I (GnT-I) activity as mgat1a remains intact. GnT-I converts oligomannose N-glycans to hybrid N-glycans, which is needed for complex N-glycan production. MALDI-TOF MS profiles identified N-glycans in the spinal cord

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Mu, Jinmin, Makoto Hirayama, Kinjiro Morimoto, and Kanji Hori. "A Complex-Type N-Glycan-Specific Lectin Isolated from Green Alga Halimeda borneensis Exhibits Potent Anti-Influenza Virus Activity." International Journal of Molecular Sciences 25, no. 8 (2024): 4345. http://dx.doi.org/10.3390/ijms25084345.

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Marine algal lectins specific for high-mannose N-glycans have attracted attention because they strongly inhibit the entry of enveloped viruses, including influenza viruses and SARS-CoV-2, into host cells by binding to high-mannose-type N-glycans on viral surfaces. Here, we report a novel anti-influenza virus lectin (named HBL40), specific for complex-type N-glycans, which was isolated from a marine green alga, Halimeda borneensis. The hemagglutination activity of HBL40 was inhibited with both complex-type N-glycan and O-glycan-linked glycoproteins but not with high-mannose-type N-glycan-linked

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Higai, Koji, Sayo Matsumoto, Megumi Kimura, et al. "NKG2D: Binding Properties for Glycan Ligands, and Mutagenesis Analysis." Open Biotechnology Journal 5, no. 1 (2011): 33–38. http://dx.doi.org/10.2174/1874070701105010033.

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Killer lectin-like receptor NKG2D, which is found on natural killer cells, recognizes MHC class 1-related ligands and also interacts with glycan ligands, heparin-conjugated bovine serum albumin (heparin-BSA) and sialyl Lewis X (sLeX) on multi-antennary N-glycans on transferrin secreted by HepG2 cells (HepTF). Using the glutathione-Stransferase- fused extracellular domain (AA 73-216) of NKG2D (rGST-NKG2D) and seven site-directed mutants, we explored in detail the binding of NKG2D to sulfate-containing glycan-BSA and HepTF. rGST-NKG2D binds to sulfatecontaining glycan-BSA with Kd values of 25 nM

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Koehler, Melanie, Martin Delguste, Christian Sieben, Laurent Gillet, and David Alsteens. "Initial Step of Virus Entry: Virion Binding to Cell-Surface Glycans." Annual Review of Virology 7, no. 1 (2020): 143–65. http://dx.doi.org/10.1146/annurev-virology-122019-070025.

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Virus infection is an intricate process that requires the concerted action of both viral and host cell components. Entry of viruses into cells is initiated by interactions between viral proteins and cell-surface receptors. Various cell-surface glycans function as initial, usually low-affinity attachment factors, providing a first anchor of the virus to the cell surface, and further facilitate high-affinity binding to virus-specific cell-surface receptors, while other glycans function as specific entry receptors themselves. It is now possible to rapidly identify specific glycan receptors using

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Giddens, John P., Joseph V. Lomino, David J. DiLillo, Jeffrey V. Ravetch, and Lai-Xi Wang. "Site-selective chemoenzymatic glycoengineering of Fab and Fc glycans of a therapeutic antibody." Proceedings of the National Academy of Sciences 115, no. 47 (2018): 12023–27. http://dx.doi.org/10.1073/pnas.1812833115.

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The N-glycans attached to the Fab and Fc domains play distinct roles in modulating the functions of antibodies. However, posttranslational site-selective modifications of glycans in antibodies and other multiply glycosylated proteins remain a challenging task. Here, we report a chemoenzymatic method that permits independent manipulation of the Fab and Fc N-glycans, using cetuximab as a model therapeutic monoclonal antibody. Taking advantage of the substrate specificity of three endoglycosidases (Endo-S, Endo-S2, and Endo-F3) and their glycosynthase mutants, together with an unexpected substrat

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VAN DIEPEN, ANGELA, NIELS S. J. VAN DER VELDEN, CORNELIS H. SMIT, MONIEK H. J. MEEVISSEN, and CORNELIS H. HOKKE. "Parasite glycans and antibody-mediated immune responses inSchistosomainfection." Parasitology 139, no. 9 (2012): 1219–30. http://dx.doi.org/10.1017/s0031182012000273.

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SUMMARYSchistosome infections in humans are characterized by the development of chronic disease and high re-infection rates after treatment due to the slow development of immunity. It appears that anti-schistosome antibodies are at least partially mediating protective mechanisms. Efforts to develop a vaccine based on immunization with surface-exposed or secreted larval or worm proteins are ongoing. Schistosomes also express a large number of glycans as part of their glycoprotein and glycolipid repertoire, and antibody responses to those glycans are mounted by the infected host. This observatio

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Tikhonov, Aleksei, Olga Smoldovskaya, Guzel Feyzkhanova, Nikolay Kushlinskii, and Alla Rubina. "Glycan-specific antibodies as potential cancer biomarkers: a focus on microarray applications." Clinical Chemistry and Laboratory Medicine (CCLM) 58, no. 10 (2020): 1611–22. http://dx.doi.org/10.1515/cclm-2019-1161.

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AbstractGlycosylation is one of the most common posttranslational modifications of proteins and lipids. In the case of tumors, cell transformation accompanied by aberrant glycosylation results in the expression of tumor-associated glycans that promote tumor invasion. As part of the innate immunity, anti-glycan antibodies recognize tumor-associated glycans, and these antibodies can be present in the bloodstream in the early stages of cancer. Recently, anti-glycan antibody profiles have been of interest in various cancer studies. Novel advantages in the field of analytical techniques have simpli

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Gristick, Harry B., Haoqing Wang, and Pamela J. Bjorkman. "X-ray and EM structures of a natively glycosylated HIV-1 envelope trimer." Acta Crystallographica Section D Structural Biology 73, no. 10 (2017): 822–28. http://dx.doi.org/10.1107/s2059798317013353.

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The structural and biochemical characterization of broadly neutralizing anti-HIV-1 antibodies (bNAbs) has been essential in guiding the design of potential vaccines to prevent infection by HIV-1. While these studies have revealed critical mechanisms by which bNAbs recognize and/or accommodate N-glycans on the trimeric envelope glycoprotein (Env), they have been limited to the visualization of high-mannose glycan forms only, since heterogeneity introduced from the presence of complex glycans makes it difficult to obtain high-resolution structures. 3.5 and 3.9 Å resolution crystal structures of

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