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Journal articles on the topic 'Biochemistry of glycoproteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Quinn, Derek J., Neil V. McFerran, John Nelson, and W. Paul Duprex. "Live-cell visualization of transmembrane protein oligomerization and membrane fusion using two-fragment haptoEGFP methodology." Bioscience Reports 32, no. 3 (2012): 333–43. http://dx.doi.org/10.1042/bsr20110100.

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Protein interactions play key roles throughout all subcellular compartments. In the present paper, we report the visualization of protein interactions throughout living mammalian cells using two oligomerizing MV (measles virus) transmembrane glycoproteins, the H (haemagglutinin) and the F (fusion) glycoproteins, which mediate MV entry into permissive cells. BiFC (bimolecular fluorescence complementation) has been used to examine the dimerization of these viral glycoproteins. The H glycoprotein is a type II membrane-receptor-binding homodimeric glycoprotein and the F glycoprotein is a type I di

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2

Steven, A. C. "BIOCHEMISTRY: Viral Glycoproteins and an Evolutionary Conundrum." Science 313, no. 5784 (2006): 177–78. http://dx.doi.org/10.1126/science.1129761.

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3

Garner, Omai B., and Linda G. Baum. "Galectin–glycan lattices regulate cell-surface glycoprotein organization and signalling." Biochemical Society Transactions 36, no. 6 (2008): 1472–77. http://dx.doi.org/10.1042/bst0361472.

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The formation of multivalent complexes of soluble galectins with glycoprotein receptors on the plasma membrane helps to organize glycoprotein assemblies on the surface of the cell. In some cell types, this formation of galectin–glycan lattices or scaffolds is critical for organizing plasma membrane domains, such as lipid rafts, or for targeted delivery of glycoproteins to the apical or basolateral surface. Galectin–glycan lattice formation is also involved in regulating the signalling threshold of some cell-surface glycoproteins, including T-cell receptors and growth factor receptors. Finally,

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4

UEDA, Kazumitsu. "Biochemistry of Human P-Glycoproteins, the Multidrug Transporter." Journal of the agricultural chemical society of Japan 66, no. 11 (1992): 1617–24. http://dx.doi.org/10.1271/nogeikagaku1924.66.1617.

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5

Kukushkin, Nikolay V., Dominic S. Alonzi, Raymond A. Dwek, and Terry D. Butters. "Demonstration that endoplasmic reticulum-associated degradation of glycoproteins can occur downstream of processing by endomannosidase." Biochemical Journal 438, no. 1 (2011): 133–42. http://dx.doi.org/10.1042/bj20110186.

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During quality control in the ER (endoplasmic reticulum), nascent glycoproteins are deglucosylated by ER glucosidases I and II. In the post-ER compartments, glycoprotein endo-α-mannosidase provides an alternative route for deglucosylation. Previous evidence suggests that endomannosidase non-selectively deglucosylates glycoproteins that escape quality control in the ER, facilitating secretion of aberrantly folded as well as normal glycoproteins. In the present study, we employed FOS (free oligosaccharides) released from degrading glycoproteins as biomarkers of ERAD (ER-associated degradation),

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6

Bieńkowska-Szewczyk, K., and B. Szewczyk. "Expression of genes coding for animal virus glycoproteins in heterologous systems." Acta Biochimica Polonica 46, no. 2 (1999): 325–39. http://dx.doi.org/10.18388/abp.1999_4166.

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The outermost layers of animal viruses are usually composed of glycoproteins. They are responsible not only for the entrance of viruses into, and release from host cells but also for the initial interaction of a viral particle with immunological defense of the host. It is therefore not surprising that many laboratories devote a lot of effort to study viral glycoproteins at the molecular level. Very often such studies are possible only after the introduction of a glycoprotein gene into a heterologous system. Expression of glycoprotein genes is usually obtained in mammalian or insect cells. Expr

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7

Browning, Darren D., and Danton H. O'Day. "Concanavalin A and wheat germ agglutinin binding glycoproteins associated with cell fusion and zygote differentiation in Dictyostelium discoideum: effects of calcium ions and tunicamycin on glycoprotein profiles." Biochemistry and Cell Biology 69, no. 4 (1991): 282–90. http://dx.doi.org/10.1139/o91-043.

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To determine which glycoproteins may be critical to sexual development in Dictyostelium discoideum, cell samples from different developmental stages were separated by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and blotted to nitrocellulose. Concanavalin A (ConA) and wheat germ agglutinin (WGA) binding proteins were visualized on the blots using an immunochemical procedure employing peroxidase–antiperoxidase. ConA labelled at least 28 proteins, but only one band showed calcium-dependent changes in its expression. WGA bound at least 30 proteins and changes in several bands were

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8

Pan, Y. T., Hidetaka Hori, and Alan D. Elbein. "The effect of glycoprotein-processing inhibitors on the secretion of glycoproteins by Madin-Darby canine kidney cells." Biochemistry and Cell Biology 65, no. 4 (1987): 345–53. http://dx.doi.org/10.1139/o87-044.

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The effects of various glycoprotein-processing inhibitors on the biosynthesis and secretion of N-linked glycoproteins was examined in cultured Madin-Darby canine kidney (MDCK) cells. Since incorporation of [2-3H]mannose into lipid-linked saccharides and into glycoproteins was much greater in phosphate-buffered saline (PBS) than in serum-supplemented basal medium (BME), most experiments were done in PBS. Castanospermine, an inhibitor of glucosidase I, caused the formation of glycoproteins having mostly Glc3Man7–9(GlcNAc)2 structures; deoxymannojirimycin, an inhibitor of mannosidase I, gave most

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9

Michelson, AD, and MR Barnard. "Thrombin-induced changes in platelet membrane glycoproteins Ib, IX, and IIb-IIIa complex." Blood 70, no. 5 (1987): 1673–78. http://dx.doi.org/10.1182/blood.v70.5.1673.1673.

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Abstract Platelet membrane glycoprotein Ib (GPIb) and the GPIIb-IIIa complex have central roles in the interaction of platelets with the plasma coagulation system, damaged vessel walls, and other platelets. We investigated the effects of thrombin on these glycoproteins. Monoclonal antibodies were used to assess platelet surface glycoproteins by flow cytometry, total platelet glycoprotein content by immunoassay, and glycoproteins released from platelets, also by immunoassay. Five new observations were made with regard to thrombin-induced changes in platelet membrane glycoproteins: (a) The marke

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10

Michelson, AD, and MR Barnard. "Thrombin-induced changes in platelet membrane glycoproteins Ib, IX, and IIb-IIIa complex." Blood 70, no. 5 (1987): 1673–78. http://dx.doi.org/10.1182/blood.v70.5.1673.bloodjournal7051673.

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Platelet membrane glycoprotein Ib (GPIb) and the GPIIb-IIIa complex have central roles in the interaction of platelets with the plasma coagulation system, damaged vessel walls, and other platelets. We investigated the effects of thrombin on these glycoproteins. Monoclonal antibodies were used to assess platelet surface glycoproteins by flow cytometry, total platelet glycoprotein content by immunoassay, and glycoproteins released from platelets, also by immunoassay. Five new observations were made with regard to thrombin-induced changes in platelet membrane glycoproteins: (a) The marked decreas

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11

Dupuis, Gilles, and Marc Letellier. "Functional incorporation and preferred orientation of phytohemagglutinin receptor glycoproteins in phospholipid vesicles." Biochemistry and Cell Biology 65, no. 2 (1987): 120–29. http://dx.doi.org/10.1139/o87-017.

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Porcine lymphocyte Phaseolus vulgaris phytohemagglutinin (PHA) receptor glycoproteins purified by affinity chromatography have been reassembled into vesicles made of phosphatidylcholine and phosphatidylserine by detergent (dodecyltrimethylammonium bromide) dialysis. The receptor glycoproteins were incorporated into the lipid vesicles in a nonselective manner with a yield of 65–70%. Vesicles containing the glycoproteins were sealed as evidenced by their impermeability to calcium ions, using quin 2 trapped inside the vesicles. The vesicles were agglutinated by PHA, suggesting that the saccharidi

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12

Karthi, Sreedevi, K. C. Sumitha, Mandagini Geetha та Padinjaradath S. Appukuttan. "Amyloid β Binds to Albumin-Associated Lrp-Like Plasma O-Glycoproteins: Albumin Prevents Inhibition of Binding by LDL". Protein & Peptide Letters 26, № 11 (2019): 869–78. http://dx.doi.org/10.2174/0929866526666190722151027.

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<P>Background: Albumin was reported to engage nearly 95% of plasma Amyloid &#946; (A&#946;) and to reverse A&#946; fibril formation in brain. </P><P> Objective: Since O-glycosylated LRP family of receptors capture A&#946; in brain we compared Aβ binding to electrophoretically purified albumin and to O-glycoproteins AOP1 and AOP2 that adhere noncovalently to plasma albumin. </P><P> Methods: Strength of A&#946;-protein interaction was measured as fluorescence increase in Fluorescentlabeled A&#946; (F-A&#946;) resulting from conformational

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13

Alonzi, Dominic S., Kathryn A. Scott, Raymond A. Dwek, and Nicole Zitzmann. "Iminosugar antivirals: the therapeutic sweet spot." Biochemical Society Transactions 45, no. 2 (2017): 571–82. http://dx.doi.org/10.1042/bst20160182.

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Many viruses require the host endoplasmic reticulum protein-folding machinery in order to correctly fold one or more of their glycoproteins. Iminosugars with glucose stereochemistry target the glucosidases which are key for entry into the glycoprotein folding cycle. Viral glycoproteins are thus prevented from interacting with the protein-folding machinery leading to misfolding and an antiviral effect against a wide range of different viral families. As iminosugars target host enzymes, they should be refractory to mutations in the virus. Iminosugars therefore have great potential for developmen

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14

Jamieson, James C., Steven Wayne, Robert S. Belo, Jim A. Wright, and Maureen A. Spearman. "The importance of N-linked glycoproteins and dolichyl phosphate synthesis for fusion of L6 myoblasts." Biochemistry and Cell Biology 70, no. 6 (1992): 408–12. http://dx.doi.org/10.1139/o92-063.

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Myoblasts fuse to form multinucleated myotubes, one of the early steps in the formation of multinucleated muscle fiber. The fusion reaction is accompanied by biochemical differentiation resulting in the expression of a variety of enzyme activities and macromolecules, particularly creatine phosphokinase. The fusing myoblast is thus an excellent system for use in studies on the molecular basis of cellular recognition. This report focuses on the role played by glycoproteins in this process. It was found that alteration of cell-surface glycoproteins, using oligosaccharide-processing inhibitors tha

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15

Wassarman, Paul M. "Zona Pellucida Glycoproteins." Annual Review of Biochemistry 57, no. 1 (1988): 415–42. http://dx.doi.org/10.1146/annurev.bi.57.070188.002215.

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16

Shylaja, M., and HS Seshadri. "Glycoproteins: An overview." Biochemical Education 17, no. 4 (1989): 170–78. http://dx.doi.org/10.1016/0307-4412(89)90136-2.

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17

Graham, Sarah A., Aristotelis Antonopoulos, Paul G. Hitchen, et al. "Identification of Neutrophil Granule Glycoproteins as Lewisx-containing Ligands Cleared by the Scavenger Receptor C-type Lectin." Journal of Biological Chemistry 286, no. 27 (2011): 24336–49. http://dx.doi.org/10.1074/jbc.m111.244772.

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The scavenger receptor C-type lectin (SRCL) is a glycan-binding receptor that has the capacity to mediate endocytosis of glycoproteins carrying terminal Lewisx groups (Galβ1–4(Fucα1–3)GlcNAc). A screen for glycoprotein ligands for SRCL using affinity chromatography on immobilized SRCL followed by mass spectrometry-based proteomic analysis revealed that soluble glycoproteins from secondary granules of neutrophils, including lactoferrin and matrix metalloproteinases 8 and 9, are major ligands. Binding competition and surface plasmon resonance analysis showed affinities in the low micromolar rang

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18

Oswald, Douglas M., Mark B. Jones, and Brian A. Cobb. "Modulation of hepatocyte sialylation drives spontaneous fatty liver disease and inflammation." Glycobiology 30, no. 5 (2019): 346–59. http://dx.doi.org/10.1093/glycob/cwz096.

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Abstract Circulatory protein glycosylation is a biomarker of multiple disease and inflammatory states and has been applied in the clinic for liver dysfunction, heart disease and diabetes. With the notable exception of antibodies, the liver produces most of the circulatory glycoproteins, including the acute phase proteins released as a function of the inflammatory response. Among these proteins is β-galactoside α2,6-sialyltransferase (ST6Gal1), an enzyme required for α2,6-linked sialylation of glycoproteins. Here, we describe a hepatocyte-specific conditional knockout of ST6Gal1 (H-cKO) using a

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19

Peracaula, Rosa, Sílvia Barrabés, Ariadna Sarrats, Pauline M. Rudd, and Rafael de Llorens. "Altered Glycosylation in Tumours Focused to Cancer Diagnosis." Disease Markers 25, no. 4-5 (2008): 207–18. http://dx.doi.org/10.1155/2008/797629.

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The lack of specific and sensitive tumour markers for early detection of cancer is driving a search for new approaches that could identify biomarkers. Markers are needed to alert clinicians at the early stages of tumourogenesis, before the cancer has metastasized, when the therapeutic drugs are more effective. Most tumour markers currently used in clinics are serum glycoproteins, frequently highly glycosylated mucins. Typically, the disease marker is the protein and not the glycan moiety of the corresponding glycoprotein or mucin. The increasing knowledge of the role of glycans in cancer sugge

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20

Oliveira, Tiago, Morten Thaysen-Andersen, Nicolle H. Packer, and Daniel Kolarich. "The Hitchhiker's guide to glycoproteomics." Biochemical Society Transactions 49, no. 4 (2021): 1643–62. http://dx.doi.org/10.1042/bst20200879.

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Protein glycosylation is one of the most common post-translational modifications that are essential for cell function across all domains of life. Changes in glycosylation are considered a hallmark of many diseases, thus making glycoproteins important diagnostic and prognostic biomarker candidates and therapeutic targets. Glycoproteomics, the study of glycans and their carrier proteins in a system-wide context, is becoming a powerful tool in glycobiology that enables the functional analysis of protein glycosylation. This ‘Hitchhiker's guide to glycoproteomics’ is intended as a starting point fo

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21

Sharkey, C. Matthew, Cynthia L. North, Richard J. Kuhn, and David Avram Sanders. "Ross River Virus Glycoprotein-Pseudotyped Retroviruses and Stable Cell Lines for Their Production." Journal of Virology 75, no. 6 (2001): 2653–59. http://dx.doi.org/10.1128/jvi.75.6.2653-2659.2001.

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ABSTRACT Pseudotyped retroviruses have important applications as vectors for gene transfer and gene therapy and as tools for the study of viral glycoprotein function. Recombinant Moloney murine leukemia virus (Mo-MuLV)-based retrovirus particles efficiently incorporate the glycoproteins of the alphavirus Ross River virus (RRV) and utilize them for entry into cells. Stable cell lines that produce the RRV glycoprotein-pseudotyped retroviruses for prolonged periods of time have been constructed. The pseudotyped viruses have a broadened host range, can be concentrated to high titer, and mediate st

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22

Schwarz, P. M., and A. D. Elbein. "The effect of glycoprotein-processing inhibitors on fucosylation of glycoproteins." Journal of Biological Chemistry 260, no. 27 (1985): 14452–58. http://dx.doi.org/10.1016/s0021-9258(17)38590-3.

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23

Bowden, Thomas A., Max Crispin, E. Yvonne Jones, and David I. Stuart. "Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies." Biochemical Society Transactions 38, no. 5 (2010): 1349–55. http://dx.doi.org/10.1042/bst0381349.

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Members within the paramyxovirus subfamily Paramyxovirinae constitute a large number of highly virulent human and animal pathogens. The glycoproteins present on these viruses are responsible for mediating host cell attachment and fusion and are key targets for the design of antiviral entry inhibitors. In the present review, we discuss recent structural studies which have led to a better understanding of the various mechanisms by which different paramyxoviruses use their attachment glycoproteins to hijack specific protein and glycan cell-surface receptors to facilitate viral entry. It is observ

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24

Strous, Ger J., and Jan Dekker. "Mucin-Type Glycoproteins." Critical Reviews in Biochemistry and Molecular Biology 27, no. 1-2 (1992): 57–92. http://dx.doi.org/10.3109/10409239209082559.

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25

SCHMID, Karl, and Takashi OKUYAMA. "Microheterogeneity of Glycoproteins." Trends in Glycoscience and Glycotechnology 2, no. 5 (1990): 196–201. http://dx.doi.org/10.4052/tigg.2.196.

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26

Carlson, Don M. "Glycoproteins: carbohydrates to cloning." Glycobiology 1, no. 5 (1991): 463–67. http://dx.doi.org/10.1093/glycob/1.5.463.

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27

Winchester, Bryan. "Lysosomal metabolism of glycoproteins." Glycobiology 15, no. 6 (2005): 1R—15R. http://dx.doi.org/10.1093/glycob/cwi041.

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28

Hanwell, PA. "The Biology of Glycoproteins." Biochemical Education 13, no. 3 (1985): 148. http://dx.doi.org/10.1016/0307-4412(85)90221-3.

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29

Morimoto, Kanta, Noriko Suzuki, Isei Tanida, et al. "Blood group P1 antigen–bearing glycoproteins are functional but less efficient receptors of Shiga toxin than conventional glycolipid-based receptors." Journal of Biological Chemistry 295, no. 28 (2020): 9490–501. http://dx.doi.org/10.1074/jbc.ra120.013926.

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Shiga toxin (STx) is a virulence factor produced by enterohemorrhagic Escherichia coli. STx is taken up by mammalian host cells by binding to the glycosphingolipid (GSL) globotriaosylceramide (Gb3; Galα1-4Galβ1-4Glc-ceramide) and causes cell death after its retrograde membrane transport. However, the contribution of the hydrophobic portion of Gb3 (ceramide) to STx transport remains unclear. In pigeons, blood group P1 glycan antigens (Galα1-4Galβ1-4GlcNAc-) are expressed on glycoproteins that are synthesized by α1,4-galactosyltransferase 2 (pA4GalT2). To examine whether these glycoproteins can

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30

Ghosh-Choudhury, Nandini, Martin Butcher, Ed Reid, and Hara P. Ghosh. "Effect of tunicamycin and monensin on the transport to the cell surface and secretion of a viral membrane glycoprotein containing both N- and O-linked sugars." Biochemistry and Cell Biology 72, no. 1-2 (1994): 20–25. http://dx.doi.org/10.1139/o94-004.

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Most membrane glycoproteins contain either N-linked or O-linked oligosaccharides, which play important roles in correct folding, stability, and intracellular transport. Some glycoproteins, however, contain both the N- and O-linked sugars. To study the roles of the two types of glycosylation in intracellular transport we have used as a model the glycoprotein gC-1 of herpes simplex virus type 1 (HSV-1), which contains both N- and O-linked oligosaccharides. Cloned gene of gC-1 was expressed constitutively in mammalian cells to produce the gC-1 glycoprotein containing both types of glycosylation.

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31

Zhu, Zhongxin, Xuan Zhou, Yang Wang, et al. "Fluorescent staining of glycoproteins in sodium dodecyl sulfate polyacrylamide gels by 4H-[1]-benzopyrano[4,3-b]thiophene-2-carboxylic acid hydrazide." Analyst 139, no. 11 (2014): 2764–73. http://dx.doi.org/10.1039/c3an02309e.

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A sensitive, specific, economic and MS compatible staining method for gel-separated glycoproteins by using BH was described and demonstrated by 1-D and 2-D SDS-PAGE, deglycosylation, glycoprotein affinity enrichment and LC-MS/MS, respectively.

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32

Kosanović, Maja, and Miroslava Janković. "Evaluation of the Pattern of Human Serum Glycoproteins in Prostate Cancer." Journal of Medical Biochemistry 28, no. 3 (2009): 184–90. http://dx.doi.org/10.2478/v10011-009-0017-8.

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Evaluation of the Pattern of Human Serum Glycoproteins in Prostate CancerGlycoprotein profiling at the level of cells, tissues and biological fluids is aimed at discovering new cancer biomarkers and also at finding specific cancer-related structural alterations of known tumor markers. In this study we comparatively evaluated the glycoprotein patterns of human prostate cancer (PCa)- and normal human sera regarding sialylation and fucosylation as structural characteristics relevant for cancer progression. Glycoproteins were isolated using affinity chromatography on Sambucus nigra agglutinin- and

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33

Roth, GJ. "Developing relationships: arterial platelet adhesion, glycoprotein Ib, and leucine-rich glycoproteins." Blood 77, no. 1 (1991): 5–19. http://dx.doi.org/10.1182/blood.v77.1.5.5.

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34

Roth, GJ. "Developing relationships: arterial platelet adhesion, glycoprotein Ib, and leucine-rich glycoproteins." Blood 77, no. 1 (1991): 5–19. http://dx.doi.org/10.1182/blood.v77.1.5.bloodjournal7715.

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35

Gruol, Donald J., and Suzanne Bourgeois. "Expression of the mdr1 P-glycoprotein gene: a mechanism of escape from glucocorticoid-induced apoptosis." Biochemistry and Cell Biology 72, no. 11-12 (1994): 561–71. http://dx.doi.org/10.1139/o94-075.

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Glucocorticoid hormones cause apoptosis in the murine T-lymphoma cell line WEHI-7. Glucocorticoid receptors in these cells are cytoplasmic proteins that translocate to the nucleus upon binding hormone. Thus, regulation of cytoplasmic glucocorticoid concentrations controls the level of activated receptors and sensitivity to steroid-induced apoptosis. We found that expression of the mdr1 P-glycoprotein gene produces a reduced accumulation of dexamethasone in WEHI-7 cells. Concomitantly, there is a suppression of dexamethasone-induced changes in transcription and a decrease in steroid sensitivity

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36

Kelly, James T., Stacey Human, Joseph Alderman, et al. "BST2/Tetherin Overexpression Modulates Morbillivirus Glycoprotein Production to Inhibit Cell–Cell Fusion." Viruses 11, no. 8 (2019): 692. http://dx.doi.org/10.3390/v11080692.

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The measles virus (MeV), a member of the genus Morbillivirus, is an established pathogen of humans. A key feature of morbilliviruses is their ability to spread by virus–cell and cell–cell fusion. The latter process, which leads to syncytia formation in vitro and in vivo, is driven by the viral fusion (F) and haemagglutinin (H) glycoproteins. In this study, we demonstrate that MeV glycoproteins are sensitive to inhibition by bone marrow stromal antigen 2 (BST2/Tetherin/CD317) proteins. BST2 overexpression causes a large reduction in MeV syncytia expansion. Using quantitative cell–cell fusion as

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37

Wassarman, Paul M. "Zona Pellucida Glycoproteins." Journal of Biological Chemistry 283, no. 36 (2008): 24285–89. http://dx.doi.org/10.1074/jbc.r800027200.

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38

Miller, JL, JM Kupinski, and KO Hustad. "Characterization of a platelet membrane protein of low molecular weight associated with platelet activation following binding by monoclonal antibody AG-1." Blood 68, no. 3 (1986): 743–51. http://dx.doi.org/10.1182/blood.v68.3.743.743.

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Abstract With the exception of the major platelet glycoproteins IIb/IIIa and Ib, which function as receptors for fibrinogen and von Willebrand factor, little is presently known regarding the possible role of other platelet surface proteins in mediating platelet aggregation. We report the production of a murine monoclonal antibody (AG-1) recognizing human platelet membrane surface protein of relatively low molecular weight (mol wt) that may be involved in this process. AG-1 added to human platelet-rich plasma induces dense granule secretion and aggregation, with lag phase and maximal extent of

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39

Miller, JL, JM Kupinski, and KO Hustad. "Characterization of a platelet membrane protein of low molecular weight associated with platelet activation following binding by monoclonal antibody AG-1." Blood 68, no. 3 (1986): 743–51. http://dx.doi.org/10.1182/blood.v68.3.743.bloodjournal683743.

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With the exception of the major platelet glycoproteins IIb/IIIa and Ib, which function as receptors for fibrinogen and von Willebrand factor, little is presently known regarding the possible role of other platelet surface proteins in mediating platelet aggregation. We report the production of a murine monoclonal antibody (AG-1) recognizing human platelet membrane surface protein of relatively low molecular weight (mol wt) that may be involved in this process. AG-1 added to human platelet-rich plasma induces dense granule secretion and aggregation, with lag phase and maximal extent of aggregati

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40

Luchansky, Sarah J., Sulabha Argade, Bradley K. Hayes, and Carolyn R. Bertozzi. "Metabolic Functionalization of Recombinant Glycoproteins†." Biochemistry 43, no. 38 (2004): 12358–66. http://dx.doi.org/10.1021/bi049274f.

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41

Kawasaki, Nana, Satsuki Itoh, Akira Harazono, et al. "Mass Spectrometry of Glycoproteins." Trends in Glycoscience and Glycotechnology 17, no. 97 (2005): 193–203. http://dx.doi.org/10.4052/tigg.17.193.

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42

Sharon, Nathan. "The biology of glycoproteins." Trends in Biochemical Sciences 10, no. 9 (1985): 367–68. http://dx.doi.org/10.1016/0968-0004(85)90119-7.

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43

Fairbanks, Antony J. "Chemoenzymatic synthesis of glycoproteins." Current Opinion in Chemical Biology 53 (December 2019): 9–15. http://dx.doi.org/10.1016/j.cbpa.2019.05.015.

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44

Jeanloz, Roger W. "Proteoglycans and structural glycoproteins." Biochimie 70, no. 11 (1988): 1698. http://dx.doi.org/10.1016/0300-9084(88)90306-9.

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45

Moens, Sara, and J. Vanderleyden. "Glycoproteins in prokaryotes." Archives of Microbiology 168, no. 3 (1997): 169–75. http://dx.doi.org/10.1007/s002030050484.

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46

Horsewood, Peter, James W. Smith, and John G. Kelton. "Monoclonal Antibodies Against Platelet Glycoproteins." Transfusion Medicine Reviews 7, no. 3 (1993): 156–72. http://dx.doi.org/10.1016/s0887-7963(93)70135-2.

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47

Wang, Yu-Mei, Timothy R. Hare, Bokran Won, et al. "Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts." Clinica Chimica Acta 188, no. 3 (1990): 193–210. http://dx.doi.org/10.1016/0009-8981(90)90201-3.

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48

Szerlip, Harold M., and Malcolm Cox. "Aldosterone-induced glycoproteins: Further characterization." Journal of Steroid Biochemistry 32, no. 6 (1989): 815–22. http://dx.doi.org/10.1016/0022-4731(89)90457-3.

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Culp, David J., Bently Robinson, Melanie N. Cash, Indraneel Bhattacharyya, Carol Stewart, and Giancarlo Cuadra-Saenz. "Salivary Mucin 19 Glycoproteins." Journal of Biological Chemistry 290, no. 5 (2014): 2993–3008. http://dx.doi.org/10.1074/jbc.m114.597906.

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Kim, Young S., James Gum, and Inka Brockhausen. "Mucin glycoproteins in neoplasia." Glycoconjugate Journal 13, no. 5 (1996): 693–707. http://dx.doi.org/10.1007/bf00702333.

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