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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 (March 29, 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 disulfide-linked membrane glycoprotein which homotrimerizes. Together they co-operate to allow the enveloped virus to enter a cell by fusing the viral and cellular membranes. We generated a pair of chimaeric H glycoproteins linked to complementary fragments of EGFP (enhanced green fluorescent protein) – haptoEGFPs – which, on association, generate fluorescence. Homodimerization of H glycoproteins specifically drives this association, leading to the generation of a fluorescent signal in the ER (endoplasmic reticulum), the Golgi and at the plasma membrane. Similarly, the generation of a pair of corresponding F glycoprotein–haptoEGFP chimaeras also produced a comparable fluorescent signal. Co-expression of H and F glycoprotein chimaeras linked to complementary haptoEGFPs led to the formation of fluorescent fusion complexes at the cell surface which retained their biological activity as evidenced by cell-to-cell fusion.

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2

Steven, A. C. "BIOCHEMISTRY: Viral Glycoproteins and an Evolutionary Conundrum." Science 313, no. 5784 (July 14, 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 (November 19, 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, galectin–glycan lattices can determine receptor residency time by inhibiting endocytosis of glycoprotein receptors from the cell surface, thus modulating the magnitude or duration of signalling from the cell surface. This paper reviews recent evidence in vitro and in vivo for critical physiological and cellular functions that are regulated by galectin–glycoprotein interactions.

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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 (July 27, 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), allowing us to gain a global rather than single protein-centred view of ERAD. Glucosidase inhibition was used to discriminate between glucosidase- and endomannosidase-mediated ERAD pathways. Endomannosidase expression was manipulated in CHO (Chinese-hamster ovary)-K1 cells, naturally lacking a functional version of the enzyme, and HEK (human embryonic kidney)-293T cells. Endomannosidase was shown to decrease the levels of total FOS, suggesting decreased rates of ERAD. However, following pharmacological inhibition of ER glucosidases I and II, endomannosidase expression resulted in a partial switch between glucosylated FOS, released from ER-confined glycoproteins, to deglucosylated FOS, released from endomannosidase-processed glycoproteins transported from the Golgi/ERGIC (ER/Golgi intermediate compartment) to the ER. Using this approach, we have identified a previously unknown pathway of glycoprotein flow, undetectable by the commonly employed methods, in which secretory cargo is targeted back to the ER after being processed by endomannosidase.

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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 (June 30, 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. Expression in mammalian cells yields viral glycoproteins with glycan chains indistinguishable from the original counterparts in virion particles but the level of synthesis of glycoproteins is very low. Vaccinia virus is the most common vector for expression in mammalian cells. It is easy to grow, the introduction of foreign genes is relatively simple and, due to the size of the vaccinia genome, it can accept large pieces of foreign DNA. Glycosylation in insect cells is not as complex as in mammalian cells and usually glycoproteins produced in insect cells are of slightly lower molecular mass than those produced in mammalian cells. The most common vector for expression of glycoproteins in insect cells is a baculovirus, Autographa californica nuclear polyhedrosis virus (AcNPV). The great advantage of this system is a very high level of expression of foreign genes.

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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 (April 1, 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 observed that did not occur in calcium-deficient controls. Two WGA-binding glycoproteins which migrated at 200 and 166 kilodaltons (kDa), respectively, showed developmental changes associated with the time of cell fusion. One WGA-binding and one ConA-binding glycoprotein migrating at 130 and 126 kDa, respectively, appeared later during sexual development, in association with the phase of zygote differentiation. Several WGA- and ConA-binding glycoproteins decreased during sexual development, but were not affected by the absence of calcium ions. Tunicamycin (1 μg/mL) inhibited cell fusion when added to sexual cultures prior to the appearance of the 166-kDa glycoprotein gp166. The effects of this inhibitor on development support the importance of glycoproteins to cell fusion during sexual development in D. discoideum.Key words: Dictyostelium, cell fusion, glycoprotein, tunicamycin, concanavalin A, wheat germ agglutinin, calcium.

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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 (April 1, 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 mostly glycoproteins with Man9(GlcNAc)2 structures; swainsonine, an inhibitor of mannosidase II, caused the accumulation of hybrid types of oligosaccharides. Castanospermine and swainsonine, either in PBS or in BME medium, had no effect on the incorporation of [2-3H]mannose or [5,6-3H]leucine into the secreted glycoproteins and, in fact, there was some increase in mannose incorporation in their presence. These inhibitors also did not affect mannose incorporation into cellular glycoproteins nor did they affect the biosynthesis as measured by mannose incorporation into lipid-linked saccharides. On the other hand in PBS medium, deoxymannojirimycin, at 25 μg/mL, caused a 75% inhibition in mannose incorporation into secreted glycoproteins, but had no effect on the incorporation of [3H]leucine into the secreted glycoproteins. Since deoxymannojirimycin also strongly inhibited mannose incorporation into lipid-linked oligosaccharides in PBS, the decreased amount of radioactivity in the secreted and cellular glycoproteins may reflect the formation of glycoproteins with fewer than normal numbers of oligosaccharide chains, owing to the low levels of oligosaccharide donor. However, in BME medium, there was only slight inhibition of mannose incorporation into lipid-linked saccharides and into cellular and secreted glycoproteins.

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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 (November 1, 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 marked decrease in platelet surface binding of antibodies directed at GPIb was not confined to antibodies directed at the von Willebrand factor binding site. (b) There was a marked decrease in platelet surface binding of an antibody directed at GPIX, with maintenance of the 1:1 ratio of platelet surface binding of antibodies directed at GPIb and GPIX. (c) Changes in platelet surface binding of antibodies were not restricted to a distinct subpopulation of platelets. (d) There was no associated platelet release of glycocalicin (a proteolytic fragment of GPIb). (e) There was no associated platelet release of the GPIIb-IIIa complex. These thrombin-induced changes may be important in modulating the reactivity of platelets with the damaged vessel wall and with each other.

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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 (November 1, 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 decrease in platelet surface binding of antibodies directed at GPIb was not confined to antibodies directed at the von Willebrand factor binding site. (b) There was a marked decrease in platelet surface binding of an antibody directed at GPIX, with maintenance of the 1:1 ratio of platelet surface binding of antibodies directed at GPIb and GPIX. (c) Changes in platelet surface binding of antibodies were not restricted to a distinct subpopulation of platelets. (d) There was no associated platelet release of glycocalicin (a proteolytic fragment of GPIb). (e) There was no associated platelet release of the GPIIb-IIIa complex. These thrombin-induced changes may be important in modulating the reactivity of platelets with the damaged vessel wall and with each other.

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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 (February 1, 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 saccharidic moiety of the reconstituted glycoproteins was, at least in part, oriented towads the extravesicular medium. This observation was further supported by the fact that the vesicles bound 125I-labeled PHA in a specific and saturable manner. At maximum amount of lectin bound, a ratio of 1.01 ± 0.05 μg of PHA per microgram glycoprotein incorporated was measured. When the binding data were analyzed by Scatchard plot, a downward concave profile was observed, suggestive of a positive cooperativity at low concentrations of lectin. The orientation of the reconstituted lectin receptor glycoproteins was determined by proteolytic treatments of labeled glycoproteins. The combined action of trypsin and chymotrypsin released, in the 120 000 × g supernatant, approximately 80% of label when 125I-tagged PHA receptor glycoproteins were incorporated into the vesicles. When the oligosaccharidic moieties of the receptor glycoproteins were specifically labeled, the simultaneous action of the two enzymes released approximately 70% of tritium labeling present in the reconstituted system. Taken together, these results suggest that the reconstituted PHA receptors are preferentially oriented into the phospholipid vesicles. The reconstituted PHA receptor glycoproteins competed effectively with cellular receptors in the assay of PHA-induced porcine lymphocyte activation. A 50% inhibition of [3H]thymidine incorporation was observed when 1 μg of glycoproteins in vesicles was added to the cultured cells, whereas vesicles alone had no effect at this (equivalent) concentration.

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12

Karthi, Sreedevi, K. C. Sumitha, Mandagini Geetha, and 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, no. 11 (October 24, 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 β (Aβ) and to reverse Aβ fibril formation in brain. </P><P> Objective: Since O-glycosylated LRP family of receptors capture Aβ 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 Aβ-protein interaction was measured as fluorescence increase in Fluorescentlabeled Aβ (F-Aβ) resulting from conformational changes. Alternatively, differential segregation of free and protein-bound Aβ in Density Gradient Ultracentrifugation (DGUC) was also examined. </P><P> Results: Fluorescence enhancement in F-Aβ was significantly greater by AOP1 and AOP2 than by known Aβ reactants α -synuclein and β -cyclodextrin, but nil by albumin. In DGUC Aβ migrated with the O-glycoproteins but not with albumin. Free O-glycoproteins unlike their albumin-bound forms were blocked by LDL from capturing F-Aβ. Associated albumin did not affect Aβ binding of O-glycoproteins. De-O-glycosylation of AOP1/AOP2 enhanced their Aβ binding showing that peptide sequences at O-glycosylated regions were recognized by Aβ. Unlike albumin, AOP1 and AOP2 were immunologically cross-reactive with LRP. Albumin sample used earlier to report albumin-Aβ interaction contained two O-glycoproteins cross-reactive with human LRP and equal in size to human AOP1 or AOP2. </P><P> Conclusion: Unlike albumin, albumin-bound O-glycoproteins, immunologically cross-reactive with LRP, bind plasma Aβ. These O-glycoproteins are potential anti-amyloidogenic therapeutics if they inhibit Aβ aggregation as other Aβ reactants do. Circulating immune complexes of albuminbound O-glycoproteins with O-glycoprotein-specific natural antibodies can bind further to LRP-like membrane proteins and are possible O-glycoprotein transporters to tissues.</P>

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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 (April 13, 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 development as broad-spectrum antiviral therapeutics. We outline the mechanism giving rise to the antiviral activity of iminosugars, the current progress in the development of iminosugar antivirals and future prospects for this field.

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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 (June 1, 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 that interfered with the synthesis of the high-mannose type of N-linked oligosaccharide, resulted in the inhibition of both the fusion reaction and biochemical differentiation as determined by measurement of creatine phosphokinase. Ketoconazole, compactin, and lovastatin, which affect dolichol and cholesterol biosynthesis, were also potent fusion inhibitors. These observations, coupled with earlier studies on the characterization of fusion-defective myoblast cell lines defective in glycoprotein biosynthesis, point to the importance of surface glycoproteins in cellular recognition in L6 myoblasts.Key words: myoblast, dolichol, glycoprotein, fusion, ketoconazole, compactin, lovastatin.

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15

Wassarman, Paul M. "Zona Pellucida Glycoproteins." Annual Review of Biochemistry 57, no. 1 (June 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 (October 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, Stuart M. Haslam, Anne Dell, Kurt Drickamer, and Maureen E. Taylor. "Identification of Neutrophil Granule Glycoproteins as Lewisx-containing Ligands Cleared by the Scavenger Receptor C-type Lectin." Journal of Biological Chemistry 286, no. 27 (May 11, 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 range. Comparison of SRCL binding to neutrophil and milk lactoferrin indicates that the binding is dependent on cell-specific glycosylation in the neutrophils, as the milk form of the glycoprotein is a much poorer ligand. Binding to neutrophil glycoproteins is fucose-dependent, and mass spectrometry-based glycomic analysis of neutrophil and milk lactoferrin was used to establish a correlation between high affinity binding to SRCL and the presence of multiple clustered terminal Lewisx groups on a heterogeneous mixture of branched glycans, some with poly N-acetyllactosamine extensions. The ability of SRCL to mediate uptake of neutrophil lactoferrin was confirmed using fibroblasts transfected with SRCL. The common presence of Lewisx groups in granule protein glycans can thus target granule proteins for clearance by SRCL. PCR and immunohistochemical analysis confirm that SRCL is widely expressed on endothelial cells and thus represents a distributed system that could scavenge released neutrophil glycoproteins both locally at sites of inflammation or systemically when they are released in the circulation.

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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 (November 29, 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 albumin promoter-driven Cre-lox recombination. We confirm the loss of circulatory glycoprotein α2,6 sialylation and note no obvious dysfunction or pathology in young H-cKO mice, yet these mice show robust changes in plasma glycoprotein fucosylation, branching and the abundance of bisecting GlcNAc and marked changes in a number of metabolic pathways. As H-cKO mice aged, they spontaneously developed fatty liver disease characterized by the buildup of fat droplets in the liver, inflammatory cytokine production and a shift in liver leukocyte phenotype away from anti-inflammatory Kupffer cells and towards proinflammatory M1 macrophages. These findings connect hepatocyte and circulatory glycoprotein sialylation to the regulation of metabolism and inflammation, potentially identifying the glycome as a new target for liver-driven disease.

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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 suggests that further studies may assist both in determining their role in every step of tumour progression, and in the design of new therapeutic and diagnosic approaches. Detection of the altered glycans in serum tumour glycoproteins could be a way to achieve specificity in tumour detection. In this review, we focus on the glycan changes of two serum glycoproteins, prostate specific antigen - currently used as a tumour marker of prostate cancer - and human pancreatic ribonuclease in pancreatic adenocarcinoma. The detection of glycan changes, associated with subsets of glycoforms in serum glycoproteins that are specific to the tumour situation, could be the basis for developing more specific biomarkers.

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Oliveira, Tiago, Morten Thaysen-Andersen, Nicolle H. Packer, and Daniel Kolarich. "The Hitchhiker's guide to glycoproteomics." Biochemical Society Transactions 49, no. 4 (July 20, 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 for anyone who wants to explore the emerging world of glycoproteomics. The review moves from the techniques that have been developed for the characterisation of single glycoproteins to technologies that may be used for a successful complex glycoproteome characterisation. Examples of the variety of approaches, methodologies, and technologies currently used in the field are given. This review introduces the common strategies to capture glycoprotein-specific and system-wide glycoproteome data from tissues, body fluids, or cells, and a perspective on how integration into a multi-omics workflow enables a deep identification and characterisation of glycoproteins — a class of biomolecules essential in regulating cell function.

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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 (March 15, 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 stable transduction of genes into cells. The RRV glycoprotein-pseudotyped retroviruses and the cells that produce them have been employed to demonstrate that RRV glycoprotein-mediated viral entry occurs through endocytosis and that membrane fusion requires acidic pH. Alphavirus glycoprotein-pseudotyped retroviruses have significant advantages as reagents for the study of the biochemistry and prevention of alphavirus entry and as preferred vectors for stable gene transfer and gene therapy protocols.

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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 (November 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 (September 24, 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 observed that the paramyxovirus attachment glycoprotein consists of a conserved overall structure which includes an N-terminal six-bladed β-propeller domain which is responsible for cell receptor binding. Crystal structures of this domain from different biomedically important paramyxoviruses, including measles, Nipah, Hendra, Newcastle disease and parainfluenza viruses, alone and in complex with their functional cell-surface receptors, demonstrate three contrasting mechanisms of receptor engagement that paramyxoviruses have evolved to confer discreet protein- and glycan-receptor specificity. This structural information highlights the adaptability of the paramyxovirus attachment glycoprotein surface and the potential for the emergence of new and potentially harmful viruses in human hosts.

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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 (January 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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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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Winchester, Bryan. "Lysosomal metabolism of glycoproteins." Glycobiology 15, no. 6 (January 12, 2005): 1R—15R. http://dx.doi.org/10.1093/glycob/cwi041.

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

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29

Morimoto, Kanta, Noriko Suzuki, Isei Tanida, Soichiro Kakuta, Yoko Furuta, Yasuo Uchiyama, Kentaro Hanada, Yusuke Suzuki, and Toshiyuki Yamaji. "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 (May 14, 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 also function as STx receptors, here we constructed glycan-remodeled HeLa cell variants lacking Gb3 expression but instead expressing pA4GalT2-synthesized P1 glycan antigens on glycoproteins. We compared STx binding and sensitivity of these variants with those of the parental, Gb3-expressing HeLa cells. The glycan-remodeled cells bound STx1 via N-glycans of glycoproteins and were sensitive to STx1 even without Gb3 expression, indicating that P1-containing glycoproteins also function as STx receptors. However, these variants were significantly less sensitive to STx than the parent cells. Fluorescence microscopy and correlative light EM revealed that the STx1 B subunit accumulates to lower levels in the Golgi apparatus after glycoprotein-mediated than after Gb3-mediated uptake but instead accumulates in vacuole-like structures probably derived from early endosomes. Furthermore, coexpression of Galα1-4Gal on both glycoproteins and GSLs reduced the sensitivity of cells to STx1 compared with those expressing Galα1-4Gal only on GSLs, probably because of competition for STx binding or internalization. We conclude that lipid-based receptors are much more effective in STx retrograde transport and mediate greater STx cytotoxicity than protein-based receptors.

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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 (January 1, 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. Only a fraction of the gC-1 glycoprotein was secreted into the medium. Addition of tunicamycin blocked N-glycosylation and the gC-1 protein of reduced size containing only O-linked sugars was formed. This O-glycosylated gC-1 protein was transported to the cell surface and secreted into the medium, indicating that glycoprotein transport to and across the cell surface occurs in the absence of N-glycans. The data suggest either that O-glycans may contribute to this process or that transport can occur in the absence of both N- and O-glycans.Key words: intracellular transport, O-glycosylation, glycoprotein gC-1, herpes simplex virus type 1.

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31

Zhu, Zhongxin, Xuan Zhou, Yang Wang, Lisha Chi, Dandan Ruan, Yuanhu Xuan, Weitao Cong, and Litai Jin. "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 (July 1, 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 Lens culinaris agglutinin-columns and subsequently characterized by SDS-PAGE and on-chip normal phase-surface capture combined with surface-enhanced laser/desorption ionization time of flight mass spectrometry. Comparative analysis of the glycoproteins purified from healthy and PCa sera indicated differences and redundancy of the isolated molecules in terms of the microheterogeneity of counterpart glycans, the relative abundance and the presence/absence of particular molecular species. In PCa there was a general increase in sialylation and decrease in fucosylation of human serum glycans compared to normal sera. Taken together, the results obtained indicated that an affinity-approach based on the use of lectins of narrow specificity reduced the complexity of the examined samples and at this discovery-phase of our study pointed to specific glyco-changes that may be relevant for improving the monitoring of PCa progression.

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Roth, GJ. "Developing relationships: arterial platelet adhesion, glycoprotein Ib, and leucine-rich glycoproteins." Blood 77, no. 1 (January 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 (January 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 (November 1, 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. P-glycoproteins are known to cause an outward, ATP-dependent transport of a variety of unrelated hydrophobic drugs across the plasma membrane. Our results indicate that glucocorticoid transport by P-glycoproteins depends upon the presence of an hydroxyl group at position 11 of corticosteroids and is enhanced by hydroxyl groups at the positions 16, 17, and 21. The antiprogestin RU486, which contains a dimethyl aminophenyl substitution at the position 11, is not transported by the mdr 1 P-glycoprotein. We have found that RU486 is an inhibitor of P-glycoprotein function, indicating that steroid analogs could be useful chemosensitizers in patients undergoing chemotherapy.Key words: multidrug resistance, glucocorticoids, apoptosis, lymphomas, RU486.

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36

Kelly, James T., Stacey Human, Joseph Alderman, Fatoumatta Jobe, Leanne Logan, Thomas Rix, Daniel Gonçalves-Carneiro, et al. "BST2/Tetherin Overexpression Modulates Morbillivirus Glycoprotein Production to Inhibit Cell–Cell Fusion." Viruses 11, no. 8 (July 30, 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 assays, immunolabeling, and biochemistry we further demonstrate that ectopically expressed BST2 directly inhibits MeV cell–cell fusion. This restriction is mediated by the targeting of the MeV H glycoprotein, but not other MeV proteins. Using truncation mutants, we further establish that the C-terminal glycosyl-phosphatidylinositol (GPI) anchor of BST2 is required for the restriction of MeV replication in vitro and cell–cell fusion. By extending our study to the ruminant morbillivirus peste des petits ruminants virus (PPRV) and its natural host, sheep, we also confirm this is a broad and cross-species specific phenotype.

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37

Wassarman, Paul M. "Zona Pellucida Glycoproteins." Journal of Biological Chemistry 283, no. 36 (June 6, 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 (September 1, 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 aggregation dependent on antibody concentration. Aggregation induced by AG-1 is inhibited by AG-1 Fab fragments, indicating that the response is not Fc receptor-mediated. Although AG-1 continues to produce platelet shape change in the presence of EDTA, aggregation is fully inhibited and appears to be mediated by fibrinogen binding to glycoproteins IIb/IIIa. AG-1 is a potent stimulus of thromboxane formation, but full inhibition of thromboxane production by 30 mumol/L indomethacin does not significantly inhibit platelet aggregation induced by 25 micrograms/mL AG-1, indicating that aggregation induced by AG-1 may proceed by way of an endoperoxide-independent pathway. Quantitation of AG-1 Fab binding to platelets reveals approximately 65,000 binding sites per platelet. When intact platelets are radioiodinated, immunoprecipitation of NP-40 lysates by AG-1 reveals an intensely labeled protein with an apparent mol wt of approximately 21,000 daltons, and several additional bands in the mol wt range of 22,000 to 28,000 daltons, all sharing the AG-1 epitope. These bands appear to be distinct from glycoprotein IX or from the beta-chains of glycoprotein Ib or IIb. Finally, studies with platelets labeled by the periodate-[3H]borohydride procedure suggest the possibility of complex formation between subpopulations of glycoprotein Ib and the low-mol-wt glycoproteins recognized by AG-1.

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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 (September 1, 1986): 743–51. http://dx.doi.org/10.1182/blood.v68.3.743.bloodjournal683743.

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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 aggregation dependent on antibody concentration. Aggregation induced by AG-1 is inhibited by AG-1 Fab fragments, indicating that the response is not Fc receptor-mediated. Although AG-1 continues to produce platelet shape change in the presence of EDTA, aggregation is fully inhibited and appears to be mediated by fibrinogen binding to glycoproteins IIb/IIIa. AG-1 is a potent stimulus of thromboxane formation, but full inhibition of thromboxane production by 30 mumol/L indomethacin does not significantly inhibit platelet aggregation induced by 25 micrograms/mL AG-1, indicating that aggregation induced by AG-1 may proceed by way of an endoperoxide-independent pathway. Quantitation of AG-1 Fab binding to platelets reveals approximately 65,000 binding sites per platelet. When intact platelets are radioiodinated, immunoprecipitation of NP-40 lysates by AG-1 reveals an intensely labeled protein with an apparent mol wt of approximately 21,000 daltons, and several additional bands in the mol wt range of 22,000 to 28,000 daltons, all sharing the AG-1 epitope. These bands appear to be distinct from glycoprotein IX or from the beta-chains of glycoprotein Ib or IIb. Finally, studies with platelets labeled by the periodate-[3H]borohydride procedure suggest the possibility of complex formation between subpopulations of glycoprotein Ib and the low-mol-wt glycoproteins recognized by AG-1.

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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 (September 2004): 12358–66. http://dx.doi.org/10.1021/bi049274f.

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41

Kawasaki, Nana, Satsuki Itoh, Akira Harazono, Noritaka Hashii, Yukari Matsuishi, Takao Hayakawa, and Toru Kawanishi. "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 (September 1985): 367–68. http://dx.doi.org/10.1016/0968-0004(85)90119-7.

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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 (November 1988): 1698. http://dx.doi.org/10.1016/0300-9084(88)90306-9.

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Moens, Sara, and J. Vanderleyden. "Glycoproteins in prokaryotes." Archives of Microbiology 168, no. 3 (September 8, 1997): 169–75. http://dx.doi.org/10.1007/s002030050484.

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Horsewood, Peter, James W. Smith, and John G. Kelton. "Monoclonal Antibodies Against Platelet Glycoproteins." Transfusion Medicine Reviews 7, no. 3 (July 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, Christopher P. Stowell, Thomas F. Scanlin, Mary Catherine Glick, Karl Hård, J. Albert van Kuik, and Johannes F. G. Vliegenthart. "Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts." Clinica Chimica Acta 188, no. 3 (May 1990): 193–210. http://dx.doi.org/10.1016/0009-8981(90)90201-3.

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

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49

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 (December 15, 2014): 2993–3008. http://dx.doi.org/10.1074/jbc.m114.597906.

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50

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

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