Relevant bibliographies by topics / Glycoproteins

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Glycoproteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 29 July 2024

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Journal articles on the topic "Glycoproteins"

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Garbutt, Michael, Ryan Liebscher, Victoria Wahl-Jensen, Steven Jones, Peggy Möller, Ralf Wagner, Viktor Volchkov, Hans-Dieter Klenk, Heinz Feldmann, and Ute Ströher. "Properties of Replication-Competent Vesicular Stomatitis Virus Vectors Expressing Glycoproteins of Filoviruses and Arenaviruses." Journal of Virology 78, no. 10 (May 15, 2004): 5458–65. http://dx.doi.org/10.1128/jvi.78.10.5458-5465.2004.

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ABSTRACT Replication-competent recombinant vesicular stomatitis viruses (rVSVs) expressing the type I transmembrane glycoproteins and selected soluble glycoproteins of several viral hemorrhagic fever agents (Marburg virus, Ebola virus, and Lassa virus) were generated and characterized. All recombinant viruses exhibited rhabdovirus morphology and replicated cytolytically in tissue culture. Unlike the rVSVs with an additional transcription unit expressing the soluble glycoproteins, the viruses carrying the foreign transmembrane glycoproteins in replacement of the VSV glycoprotein were slightly attenuated in growth. Biosynthesis and processing of the foreign glycoproteins were authentic, and the cell tropism was defined by the transmembrane glycoprotein. None of the rVSVs displayed pathogenic potential in animals. The rVSV expressing the Zaire Ebola virus transmembrane glycoprotein mediated protection in mice against a lethal Zaire Ebola virus challenge. Our data suggest that the recombinant VSV can be used to study the role of the viral glycoproteins in virus replication, immune response, and pathogenesis.
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Jorgenson, Rebecca L., Volker M. Vogt, and Marc C. Johnson. "Foreign Glycoproteins Can Be Actively Recruited to Virus Assembly Sites during Pseudotyping." Journal of Virology 83, no. 9 (February 18, 2009): 4060–67. http://dx.doi.org/10.1128/jvi.02425-08.

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ABSTRACT Retroviruses like human immunodeficiency virus type 1 (HIV-1), as well as many other enveloped viruses, can efficiently produce infectious virus in the absence of their own surface glycoprotein if a suitable glycoprotein from a foreign virus is expressed in the same cell. This process of complementation, known as pseudotyping, often can occur even when the glycoprotein is from an unrelated virus. Although pseudotyping is widely used for engineering chimeric viruses, it has remained unknown whether a virus can actively recruit foreign glycoproteins to budding sites or, alternatively, if a virus obtains the glycoproteins through a passive mechanism. We have studied the specificity of glycoprotein recruitment by immunogold labeling viral glycoproteins and imaging their distribution on the host plasma membrane using scanning electron microscopy. Expressed alone, all tested viral glycoproteins were relatively randomly distributed on the plasma membrane. However, in the presence of budding HIV-1 or Rous sarcoma virus (RSV) particles, some glycoproteins, such as those encoded by murine leukemia virus and vesicular stomatitis virus, were dramatically redistributed to viral budding sites. In contrast, the RSV Env glycoprotein was robustly recruited only to the homologous RSV budding sites. These data demonstrate that viral glycoproteins are not in preformed membrane patches prior to viral assembly but rather that glycoproteins are actively recruited to certain viral assembly sites.
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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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Lay Mendoza, Maria Fernanda, Marissa Danielle Acciani, Courtney Nina Levit, Christopher Santa Maria, and Melinda Ann Brindley. "Monitoring Viral Entry in Real-Time Using a Luciferase Recombinant Vesicular Stomatitis Virus Producing SARS-CoV-2, EBOV, LASV, CHIKV, and VSV Glycoproteins." Viruses 12, no. 12 (December 17, 2020): 1457. http://dx.doi.org/10.3390/v12121457.

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Viral entry is the first stage in the virus replication cycle and, for enveloped viruses, is mediated by virally encoded glycoproteins. Viral glycoproteins have different receptor affinities and triggering mechanisms. We employed vesicular stomatitis virus (VSV), a BSL-2 enveloped virus that can incorporate non-native glycoproteins, to examine the entry efficiencies of diverse viral glycoproteins. To compare the glycoprotein-mediated entry efficiencies of VSV glycoprotein (G), Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S), Ebola (EBOV) glycoprotein (GP), Lassa (LASV) GP, and Chikungunya (CHIKV) envelope (E) protein, we produced recombinant VSV (rVSV) viruses that produce the five glycoproteins. The rVSV virions encoded a nano luciferase (NLucP) reporter gene fused to a destabilization domain (PEST), which we used in combination with the live-cell substrate EndurazineTM to monitor viral entry kinetics in real time. Our data indicate that rVSV particles with glycoproteins that require more post-internalization priming typically demonstrate delayed entry in comparison to VSV G. In addition to determining the time required for each virus to complete entry, we also used our system to evaluate viral cell surface receptor preferences, monitor fusion, and elucidate endocytosis mechanisms. This system can be rapidly employed to examine diverse viral glycoproteins and their entry requirements.
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Joshua, G. W. P., L. J. S. Harrison, and M. M. H. Sewell. "Developmental changes in proteins and glycoproteins revealed by direct radio-iodination of viable Taenia saginata larvae." Parasitology 99, no. 2 (October 1989): 265–74. http://dx.doi.org/10.1017/s0031182000058728.

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SummaryDirect surface I radio-isotope labelling techniques and SDS—PAGE analysis were used to compare the proteins and lentil—lectin adherent glycoproteins of the bovine stage of viable Taenia saginata larvae at three points in their development, the invasive oncospheres, immature (4-week-old) and mature (12 to 16-week-old) cysticerci. Some proteins and glycoproteins were present on all three of the ages of the parasite examined but there were also distinct age-specific proteins and glycoproteins detected on oncospheres and 4-week-old cysticerci and a marked difference between the protein/glycoprotein profiles of the parasite was apparent at these earlier stages of development and the mature cysticerci. The latter were characterized by the presence of high, 160–200 kDa molecular weight, lysine rich, glycoproteins, whereas small 16 and 18 kDa glycoproteins and a reduction-sensitive 23 kDa glycoprotein were first detected on 4-week-old immature cysticerci. Antigenic characterization of the isotope-labelled proteins and glycoproteins by immunoprecipitation against a panel of clinically defined bovine sera combined with SDS–PAGE analysis indicated that relatively few proteins were precipitated by sera from T. saginata-infected cattle as compared to the glycoproteins. However, both protein and glycoprotein antigens of possible protective and/or diagnostic significance were identified from oncospheres and cysticerci.
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Zhang, Libo, Yanhong Li, Riyao Li, Xiaohong Yang, Zimin Zheng, Jingxin Fu, Hai Yu, and Xi Chen. "Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed in E. coli." Molecules 28, no. 6 (March 18, 2023): 2753. http://dx.doi.org/10.3390/molecules28062753.

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Protein N-glycosylation is a common post-translational modification that plays significant roles on the structure, property, and function of glycoproteins. Due to N-glycan heterogeneity of naturally occurring glycoproteins, the functions of specific N-glycans on a particular glycoprotein are not always clear. Glycoprotein in vitro N-glycan engineering using purified recombinant enzymes is an attractive strategy to produce glycoproteins with homogeneous N-glycoforms to elucidate the specific functions of N-glycans and develop better glycoprotein therapeutics. Toward this goal, we have successfully expressed in E. coli glycoside hydrolases and glycosyltransferases from bacterial and human origins and developed a robust enzymatic platform for in vitro processing glycoprotein N-glycans from high-mannose-type to α2–6- or α2–3-disialylated biantennary complex type. The recombinant enzymes are highly efficient in step-wise or one-pot reactions. The platform can find broad applications in N-glycan engineering of therapeutic glycoproteins.
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Si, Zhihai, Mark Cayabyab, and Joseph Sodroski. "Envelope Glycoprotein Determinants of Neutralization Resistance in a Simian-Human Immunodeficiency Virus (SHIV-HXBc2P 3.2) Derived by Passage in Monkeys." Journal of Virology 75, no. 9 (May 1, 2001): 4208–18. http://dx.doi.org/10.1128/jvi.75.9.4208-4218.2001.

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ABSTRACT The simian-human immunodeficiency virus SHIV-HXBc2 contains the envelope glycoproteins of a laboratory-adapted, neutralization-sensitive human immunodeficiency virus type 1 variant, HXBc2. Serial in vivo passage of the nonpathogenic SHIV-HXBc2 generated SHIV KU-1, which causes rapid CD4+ T-cell depletion and an AIDS-like illness in monkeys. A molecularly cloned pathogenic SHIV, SHIV-HXBc2P 3.2, was derived from the SHIV KU-1 isolate and differs from the parental SHIV-HXBc2 by only 12 envelope glycoprotein amino acid residues. Relative to SHIV-HXBc2, SHIV-HXBc2P 3.2 was resistant to neutralization by all of the antibodies tested with the exception of the 2G12 antibody. The sequence changes responsible for neutralization resistance were located in variable regions of the gp120 exterior envelope glycoprotein and in the gp41 transmembrane envelope glycoprotein. The 2G12 antibody, which neutralized SHIV-HXBc2 and SHIV-HXBc2P 3.2 equally, bound the HXBc2 and HXBc2P 3.2 envelope glycoproteins on the cell surface comparably. The ability of the other tested antibodies to achieve saturation was less for the HXBc2P 3.2 envelope glycoproteins than for the HXBc2 envelope glycoproteins, even though the affinity of the antibodies for the two envelope glycoproteins was similar. Thus, a highly neutralization-sensitive SHIV, by modifying both gp120 and gp41 glycoproteins, apparently achieves a neutralization-resistant state by decreasing the saturability of its envelope glycoproteins by antibodies.
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Calvete, J. J., J. L. McGregor, G. Rivas, and J. González-Rodríguez. "Identification of a Glycoprotein III a Dimer in Polyacrylamide Gel Separations of Human Platelet Membranes." Thrombosis and Haemostasis 58, no. 02 (1987): 694–97. http://dx.doi.org/10.1055/s-0038-1645957.

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SummaryMembrane glycoproteins IIb and IIIa play a major role in human blood platelet aggregation. The absence or the severe reduction of these two membrane glycoproteins, as observed in platelets of Glanzmann’s thrombasthenic patients, is related to a lack of platelet aggregation. Separation of Glanzmann’s thrombasthenic platelet samples by two-dimensional polyacrylamide O’Farrell gels show the absence of a high and several low molecular mass glycoproteins, in addition to the loss of glycoproteins IIb and IIIa (McGregor J. L. et al. Eur. J. Biochem. 1981; 116: 379-388). The aim of this study was to identify the nature of the high molecular mass component, absent in thrombasthenic platelets. A high molecular mass glycoprotein (200 kDa), present in two-dimensional SDS-polyacrylamide O-Farrell gel separations, was recognized by a monoclonal antibody (MP37) directed against glycoprotein IIIa. Moreover, the tryptic peptide map of this high molecular mass glycoprotein was nearly identical to that of glycoprotein IIIa. These results indicate that this high molecular mass glycoprotein present in SDS-polyacrylamide gels is a dimer of glycoprotein IIIa. This work raises the possibility that the high molecular mass glycoprotein, absent in two-dimensional O’Farrell gel separations of thrombasthenic platelets, is a dimer of glycoprotein IIIa.
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LaBonte, Jason A., Navid Madani, and Joseph Sodroski. "Cytolysis by CCR5-Using Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Is Dependent on Membrane Fusion and Can Be Inhibited by High Levels of CD4 Expression." Journal of Virology 77, no. 12 (June 15, 2003): 6645–59. http://dx.doi.org/10.1128/jvi.77.12.6645-6659.2003.

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ABSTRACT T-tropic (X4) and dualtropic (R5X4) human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins kill primary and immortalized CD4+ CXCR4+ T cells by mechanisms involving membrane fusion. However, because much of HIV-1 infection in vivo is mediated by M-tropic (R5) viruses whose envelope glycoproteins use CCR5 as a coreceptor, we tested a panel of R5 and R5X4 envelope glycoproteins for their ability to lyse CCR5+ target cells. As is the case for CXCR4+ target cells, HIV-1 envelope glycoproteins expressed by single-round HIV-1 vectors killed transduced CD4+ CCR5+ cells in a membrane fusion-dependent manner. Furthermore, a CD4-independent R5 HIV-1 envelope glycoprotein was able to kill CD4-negative target cells expressing CCR5, demonstrating that CD4 is not intrinsically required for the induction of death. Interestingly, high levels of CD4 expression protected cells from lysis and syncytium formation mediated by the HIV-1 envelope glycoproteins. Immunoprecipitation experiments showed that high levels of CD4 coexpression inhibited proteolytic processing of the HIV-1 envelope glycoprotein precursor gp160. This inhibition could be overcome by decreasing the CD4 binding ability of gp120. Studies were also undertaken to investigate the ability of virion-bound HIV-1 envelope glycoproteins to kill primary CD4+ T cells. However, neither X4 nor R5X4 envelope glycoproteins on noninfectious virions caused death in primary CD4+ T cells. These results demonstrate that the interaction of CCR5 with R5 HIV-1 envelope glycoproteins capable of inducing membrane fusion leads to cell lysis; overexpression of CD4 can inhibit cell killing by limiting envelope glycoprotein processing.
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Shammala, Farid Abu. "Mass spectrometry-based analysis of glycoproteins and its clinical applications in cancer biomarker discovery." Brazilian Journal of Biological Sciences 4, no. 7 (2017): 203–15. http://dx.doi.org/10.21472/bjbs.040720.

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Most proteins are glycosylated, glycosylation is one of the most important posttranslational modifications of proteins and plays essential roles in various biological processes. Aberration in the glycan moieties of glycoproteins is associated with many diseases. It is especially critical to develop the rapid and sensitive methods for analysis of aberrant glycoproteins associated with diseases. With recent advances in proteomics, analytical and computational technologies, glycoproteomics, the global analysis of glycoproteins, is rapidly emerging as a subfield of proteomics with high biological and clinical relevance. Glycoproteomics integrates glycoprotein enrichment and proteomics technologies to support the systematic identification and quantification of glycoproteins in a complex sample. It is especially critical to develop the rapid and sensitive methods for analysis of aberrant glycoproteins associated with diseases. Mass spectrometry (MS) has become a powerful tool for mapping glycoprotein glycosylation and detailed glycan structural determination. Especially, tandem mass spectrometry can provide highly informative fragments for structural identification of glycoproteins. This review provides an overview of the development of MS technologies and their applications in identification of abnormal glycoproteins and glycans in human serum to screen cancer biomarkers in recent years.
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Dissertations / Theses on the topic "Glycoproteins"

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Jefferies, W. A. "Lymphocyte surface glycoproteins." Thesis, University of Oxford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355757.

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Clark, R. A. C. "Characterisation of neural glycoproteins." Thesis, University of Cambridge, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.363826.

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Premdjee, B. "Semi-synthesis of glycoproteins." Thesis, University College London (University of London), 2014. http://discovery.ucl.ac.uk/1434897/.

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Glycosylation is a prevalent form of post translational modification, believed to occur on over 50% of human proteins. Homogeneous forms of glycoproteins are essential for developing an understanding of how activity is mediated at a structural level. As biological origins of glycoproteins give rise to complex mixtures of glycoforms, homogeneous glycoprotein production has become an important goal. As chemical protein synthesis is often limited to sequences of 30-50 residues, access to large native glycoproteins is currently restricted to fragment based approaches. Protein semi-synthesis enables the preparation of larger proteins which can be difficult to obtain through chemical synthesis alone. Consequently, a general semi-synthetic strategy towards N-glycoproteins has been proposed and demonstrated on Interferon-β-1 (IFNβ), a 166 residue glycoprotein. A three fragment strategy was designed, relying on the chemical synthesis of a short glycopeptide segment and recombinant expression of the two flanking domains. Homogeneity was established through the chemical synthesis of a glycopeptide containing a natively linked N-acetylglucosamine (GlcNAc), also enabling the selective transfer of complex oligosaccharides. After cloning and expression, the recombinant fragments were functionalised to allow assembly of the protein using Native Chemical Ligation. These desired protein modifications were achieved through the application of highly chemoselective reactions. These reactions were also applied towards the generation of N-glycopeptides compatible with the ligation strategy. Further to this, existing methods enabling the direct synthesis of functionalised N-glycopeptides were also explored. After glycopeptide synthesis, endoglycosidase A enabled the transfer of oligosaccharides to the N-acetylglucosamine motif. This has allowed the preparation of the desired IFNβ glycopeptide as well as a glycosylated variant of glucagon like peptide-1. To expand the utility of endoglycosidase methodology, a novel sugar nucleotide was synthesised to facilitate the incorporation of a sialyl galactose mimic onto N-glycans. The resulting oligosaccharides may serve as novel substrates for endoglycosidases in the preparation of N-glycoprotein mimics.
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Crispin, Matthew D. M. "Manipulation and crystallisation of glycoproteins." Thesis, University of Oxford, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.426374.

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Priyanka, Pragya. "Chemoenzymatic synthesis of phosphorylated glycoproteins." Thesis, University of Canterbury. Chemistry, 2015. http://hdl.handle.net/10092/10578.

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Phosphorylation of the glycan portion of glycoproteins is an important posttranslational modification. In particular, the presence of mannose-6-phosphate (M6P) residues on high mannose glycans of lysosomal enzymes is important for the transfer of these enzymes to the lysosomes. The synthesis of different types of N-glycan structures containing M6P residues have been reported by various groups. This thesis work concerns the chemoenzymatic synthesis of phosphorylated glycoproteins, wherein M6P containing N-glycans were synthesised chemically and then enzymatically coupled to give homogeneous glycoproteins. Endo-β-N-acetylglucosaminidases (ENGases), have been employed by various research groups for the synthesis of variety of homogeneous glycopeptides and proteins by using oxazolines as activated donors. This thesis reports the synthesis of bis-phosphorylated tetrasaccharide and hexasaccharide oxazoline donors, and the use of ENGases to catalyse their transfer to peptides and proteins.
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Duffy, Iain. "Analysis of measles virus glycoproteins." Thesis, Queen's University Belfast, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324842.

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Kaye, Jane Frances. "Studies of human cytomegalovirus glycoproteins." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.259731.

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BECKMANN, M. PATRICIA. "SYNTHESIS AND OLIGOSACCHARIDE PROCESSING OF NORMAL AND ALTERED IMMUNOGLOBULIN M DURING B-CELL DIFFERENTIATION (GLYCOPROTEIN, GLYCOPEPTIDE, MUTANT, CARBOHYDRATE, ASPARAGINE-LINKED)." Diss., The University of Arizona, 1985. http://hdl.handle.net/10150/187906.

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Glycoproteins play a key role in cellular growth and differentiation. In order to study glycoprotein biosynthesis and processing, we have chosen the murine Immunoglobulin M (IgM) system as a model. Our system utilizes hybridoma, lymphoma and plasmacytoma cell lines which synthesize intracellular, membrane-bound and secreted IgM. Each type of IgM is synthesized during a specific phase of B-cell differentiation. We have examined the kinetics of IgM synthesis and processing in cells at each developmental stage. The rate of synthesis of membrane-bound and soluble IgM are different. Characteristic rates for membrane versus soluble IgM may be dependent on the extent of oligosaccharide processing. The membrane-bound IgM contains more high-mannose oligosaccharide than does the secreted product. In addition, we have begun to determine how protein structural requirements can affect final glycosylation patterns on the glycoprotein. Two cell lines were studied which secreted smaller than normal IgM heavy chains in tissue culture. One cell line studied (208) contains one glycosylation site, while another (562) retains three sites on the molecule synthesized in tissue culture. Studies performed on these cell lines in tissue culture indicate greater processing of the oligosaccharides on these mutant IgM molecules when compared to the parental cell line (PC700). Studies on the 208 IgM molecules synthesized in the mouse and purified from ascites fluid confirm these results. Upon injection into the mouse, the 562 cell line reverts to produce protein and carbohydrate structures characteristic of the parental cell line. Studies on the 562 protein purified from ascites fluid illustrate the need for more precisely defined cell lines and genetic engineering for the study of altered protein structures.
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Chan, Chun-yu. "Mass spectrometric analysis of selected glycoproteins." Thesis, Click to view the E-thesis via HKUTO, 2005. http://sunzi.lib.hku.hk/hkuto/record/B3147942X.

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Perry, J. Jefferson P. "Structural studies of cell surface glycoproteins." Thesis, University of Cambridge, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.368608.

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Books on the topic "Glycoproteins"

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Bradfute, Steven B., ed. Recombinant Glycoproteins. New York, NY: Springer US, 2024. http://dx.doi.org/10.1007/978-1-0716-3666-4.

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1920-, Montreuil Jean, Vliegenthart J. F. G, and Schachter H, eds. Glycoproteins II. Amsterdam: Elsevier, 1997.

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Wittmann, Valentin, ed. Glycopeptides and Glycoproteins. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/978-3-540-36761-1.

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George, James N., Alan T. Nurden, and David R. Phillips, eds. Platelet Membrane Glycoproteins. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4880-1.

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1920-, Montreuil Jean, Vliegenthart J. F. G, and Schachter H, eds. Glycoproteins and disease. Amsterdam: Elsevier, 1996.

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N, George James, Nurden Alan T, and Phillips David R. 1942-, eds. Platelet membrane glycoproteins. New York: Plenum Press, 1985.

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A, Keel Brooks, and Grotjan H. Edward, eds. Microheterogeneity of glycoprotein hormones. Boca Raton, Fla: CRC Press, 1989.

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Delobel, Arnaud, ed. Mass Spectrometry of Glycoproteins. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1241-5.

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Kohler, Jennifer J., and Steven M. Patrie, eds. Mass Spectrometry of Glycoproteins. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-146-2.

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Tan, Zhongping, and Lai-Xi Wang, eds. Chemical Biology of Glycoproteins. Cambridge: Royal Society of Chemistry, 2017. http://dx.doi.org/10.1039/9781782623823.

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Book chapters on the topic "Glycoproteins"

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Hounsell, Elizabeth. "Glycoproteins." In Encyclopedia of Biophysics, 1–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-642-35943-9_72-1.

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Hounsell, Elizabeth. "Glycoproteins." In Encyclopedia of Biophysics, 918–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_72.

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Bährle-Rapp, Marina. "Glycoproteins." In Springer Lexikon Kosmetik und Körperpflege, 231. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_4434.

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Wittmann, Valentin. "Glycoproteins: Properties." In Glycoscience, 1771–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-30429-6_44.

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Messner, P., and C. Schäffer. "Prokaryotic Glycoproteins." In Fortschritte der Chemie organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products, 51–124. Vienna: Springer Vienna, 2003. http://dx.doi.org/10.1007/978-3-7091-6051-0_2.

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Zaucke, Frank. "Cartilage Glycoproteins." In Cartilage, 55–81. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-29568-8_3.

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Lüscher, Ernst F. "Plasma Membrane Receptors and Platelet Response." In Platelet Membrane Glycoproteins, 3–9. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4880-1_1.

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Coller, Barry S. "Platelet—von Willebrand Factor Interactions." In Platelet Membrane Glycoproteins, 215–44. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4880-1_10.

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Nachman, Ralph L., Lawrence L. K. Leung, and Margaret J. Polley. "Molecular Mechanisms of Platelet Adhesion and Platelet Aggregation." In Platelet Membrane Glycoproteins, 245–57. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4880-1_11.

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Gartner, T. Kent. "Lectin—Carbohydrate Binding as a Model for Platelet Contact Interactions." In Platelet Membrane Glycoproteins, 259–70. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4880-1_12.

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Conference papers on the topic "Glycoproteins"

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Gorski, J., L. Van Hove, F. Vanlangendonck, M. A. Boogaerts, R. L. Verwilghen, and J. Vermylen. "PLATELET MEMBRANE GLYCOPROTEINS ABNORMALITIES IN PATIENTS WITH ACUTE LEUKEMIAS AND MALIGNANT LYMPHOMAS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643201.

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Membrane glycoproteins are implicated in platelet functions.In myeloproliferative disorders some of the platelet functions are known to be perturbated and an abnormal glycoproteins pattern was demonstrated ear-lier.In this study flow cytometry analysis of human platelet membrane glycoproteins IIa and IIIa in patients with acute leukemias and malignant lymphomas has been performed using monoclonal antibodies against these glycoproteins.A reduction in number of glycoproteins receptors on platelet membrane was demonstrated in patients with acute leukemias and malignant lymphomas in comparison with platelets of healthy donors.In patients with leukemias the positive correlation of percentage of platelets recovered in various density receptor regions to bleeding time and negative correlation to platelet number for both glycoproteins have been found.The study demonstrated that flow cytometry can be a useful method of analysis of platelet membrane glycoproteins, and that the patients with acute leukemias and malignant lymphomas have the number of glycoproteins reduced.
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Kunz, Horst. "Synthetic glycopeptides and glycoproteins." In Future Aspect in Peptide Chemistry - Ringberg Conference. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199901067.

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Wilkinson, J. M., N. Hack, L. I. Thorsen, and J. A. Thomas. "MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644493.

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Platelet membrane preparations can be fractionated into two major subpopulations by free flow electrophoresis and these have been shown to correspond to the plasma membrane and the endoplasmic reticulum of the platelet. The plasma membrane fraction can be shown, by two-dimensional electrophoresis, to contain the major surface glycoproteins together with considerable amounts of actin and actin-associated proteins such as the 250 kDa actin-binding protein (filamin), P235 (talin), myosin, α-actinin and tropomyosin (Hack, N. … Crawford, N., Biochem. J. 222, 235 (1984). These cytoskeletal proteins are associated with the cytoplasmic face of the plasma membrane and probably interact with transmembrane glycoproteins. We have raised monoclonal antibodies to the purified plasma membrane preparation in order to investigate the nature of these glycoprotein-cytoskeletal interactions. In two fusion experiments, out of 804 tested, 104 hybrids secreted antibody to the membrane preparation and of these 24 were selected for further study. Initial assays were by ELISA using either the membrane preparation or whole fixed platelets as the target antigen. The specificity of the antibodies was investigated further by immunoblotting of SDS gels of total platelet proteins prepared under reducing and nonreducing conditions, by immunofluorescence, by immunohisto-chemistry and by crossed immunoelectrophoresis. The majority of the antibodies recognise major surface glycoproteins; of these, four bind to glycoprotein Ib under all conditions examined while another seven recognise the glycoprotein IIb/IIIa complex as detected by crossed immunoelectrophoresis. Three antibodies recognise the actin binding protein and these cross-react with the smooth muscle protein filamin in a number of different species. Further characterisation of these antibodies in both structural and functional terms will be presented.We are grateful to the Smith and Nephew Foundation for financial support for these studies
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Bienz, D., T. Wager, and K. J. Clemetson. "ISOLATION AND CHARACTERIZATION OF HUMAN PLATELET MEMBRANE GLYCOPROTEINS Ia AND IIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643910.

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Glycoproteins (GP) Ia and IIa are relatively minor components of the platelet surface with similar molecular properties. Nieuwenhuis et al. (Nature 319, 470-72, 1985) described a patient whose platelets show no response to collagen. The correlating lack of GPIa in the platelets of this patient suggests this glycoprotein being the receptor for collagen. Santoro (Cell, 46, 913-20, 1986) described a 160 kDa glycoprotein that binds to collagen in the presence of MG2 + and is possibly identical with GPIa. The role of GPIIa is still unknown but a similar molecule has also been found on endothelial cells. It has been suggested that GPIa and GPIIa are complexed with a further membrane component GPIc. The two glycoproteins show only slight difference in molecular weight, isoelectric point and in their affinity for various lectins. As a result they coisolate using most separation techniques.GPIa is usually associated with the cytoskeleton while GPIIa is mostly found in the soluble phase. GPIa is dissociated from the cytoskeleton by addition of 2% SDS (final conc.) and sonication. Performing Triton X-114 phase partition, GPIIa is found in the detergent phase. After the detergents of the GPIa and GPIIa enriched protein solutions are exchanged with the non-ionic octanoyl-N-methyl glucamide, the glycoproteins are further purified by affinity chromatography on wheat germ agglutinin-Sepharose followed by Lens culinaris lectin-Sepharose both of which bind GPIa and GPIIa. A major contaminant during the purification is GPIb. Final purification of GPIa and GPIIa was obtained by preparative SDS-PAGE using electroelution into a membrane trap. Latest results show an enrichment of GPIa and a lack of GPIb in pseudopodes, isolated by the method of Rotman et al. (Proc. Natl. Acad. Sci. USA, 4357-61, 1982).
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Sears, Pamela, Krista Witte, and Chi-Huey Wong. "Synthesis of glycopeptides and glycoproteins." In Future Aspect in Peptide Chemistry - Ringberg Conference. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199901211.

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Jabbal-Gill, I., G. I. Johnston, and S. Heptinstall. "EXTRACELLULAR CALCIUM AND PLATELET GLYCOPROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643507.

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Platelet membrane glycoproteins lib and Ilia form Ca++-dependent heterodimer complexes that contain binding sites for fibrinogen and therefore are relevant to the ability of platelets to aggregate together. In this study we investigated the effects of extracellular Ca++ on the stability and expression of IIb-IIIa complexes using a IIb-IIIa complex-specific monoclonal antibody M148. Its specificity was examined using crossed immunoelectrophoresis: the antibody reacted only with intact IIb-IIIa complexes and not with either glycoprotein alone.SDS-polyacrylamide gel electrophoresis of immunoprecipitates of soluble glycoproteins that interacted with Ml48 showed that lib and Ilia were present as complexes in Ca++-depleted media at 25°C, pH7.4. However, Ca++-depletion at 37°C, pH7.4 or 37°C, pH8.7 or 25°C, pH8.7 caused dissociation of the complexThe effect of extracellular Ca++ on the expression of IIb-Illa complexes on the surface of intact platelets was studied by a technique which is based upon indirect binding of M148 using a fluorescent- labelled second antibody (FITC-RAM) and measuring the fluorescence per platelet using the FACS IV cytofluorometer. Intact platelets were incubated in Ca++-depleted media at 25°C, pH7.4 or 37°C, pH7.4 either (i) prior to or (ii) after adding M148. At 25°C increased M148-binding was observed, compared to the value prior to Ca++-depletion. This increased binding could be reversed by adding Ca++ back to the preparation. Under condition (i) at 37°C a marked decrease in M148 binding was observed, which could not be reversed by restoring Ca++, while under condition (ii) at 37°C the results were the same as at 25°C.Our studies demonstrate that (a) Ca++-depletion at 37°C and/or alkaline pH causes dissociation of the Ilb-IIIa complex (b) Ca++ depletion at 25°C possibly alters distribution of the complexes thereby increasing their availability to the antibody and (c) M148 prevents the dissociation of complexes in Ca++-depleted media at 37°C, possibly by holding lib and Ilia together
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Schlosser, Gitta, Adrienn Molnár, Dávid Papp, Gabriella Gellén, Dávid Virág, Krisztina Ludányi, Borbála Dalmadi Kiss, et al. "Omics Mass Spectrometry Analysis of Canine Plasma." In Socratic lectures 10. University of Lubljana Press, 2024. http://dx.doi.org/10.55295/psl.2024.i11.

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Abstract: Blood derived products, such as autologous plasma, have high clinical importance and are applied in numerous therapeutic fields. The preparation of autologous plasma from the patient's own blood is easy to perform by centrifugation, however, the prep-aration procedure can significantly affect the blood cells, platelets and vesicles in the sample. Therefore, it is of utmost importance to understand the impact of sample pro-cessing on the chemical composition of plasma preparations as well as on their biolog-ical activity. Here, we present a mass spectrometry-based plasma profiling method in which three compound groups: lipids, proteins and glycoproteins are analysed in a single workflow. Analysis of the chemical composition of plasma samples prepared by different centrifugation protocols revealed differences in the lipid and glycoprotein profiles, demonstrating the importance of standardized protocols for the preparation of plasma products. Keywords: Plasma; Lipids; Proteins; Glycoproteins; Mass Spectrometry, Ion Mobility
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Grossi, L., K. V. Honn, B. F. Sloane, J. Thomopson, D. Ohannesian, A. Kendall, and M. Newcombe. "ROLE OF PLATELET GLYCOPROTEINS lb AND llb/llla IN TUMOR CELL INDUCED PLATELET AGGREGATION AND TUMOR CELL ADHESION TO EXTRACELLULAR MATRIX. I. Grossi." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644670.

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Platelet glycoproteins are known to play a role in platelet platelet interactions, platelet activation, and platelet adhesion to extracellular matrix (ECM). Monoclonal antibody to human platelet glycoprotein lb (mAblb) and polyclonal antibodies to the llb/llla complex (pAbllb/llla) were used to evaluate the involvement of these glycoproteins in tumor cellinduced platelet aggregation (TCIPA and tumor cell adhesion to the ECM. We have demonstrated that human cervical carcinoma (MS5I7), human colon carcinoma (Clone A), and rat Walker 256 carcinosarcoma (W256) cells induce aggregation of homologous platelets via thrombin generation. MAblb and pAbllb/llla were shown to inhibit TCIPA by MS517, Clone A, and W256 in a dose dependent manner. MAblb was also shown to inhibit platelet thromboxane B2 production in response to tumor cells in a dose dependent manner. Neither mAblb nor pAbllb/llla had any effect on ADP stimulated platelet aggregation. Concentrations of mAblb and pAbllb/llla which produced half maximal inhibition alone were combined resulting in complete inhibition of TCIPA. Preincubation of MS5I7 and W256 with mAblb also resulted in inhibition of TCIPA, while preincubation of Clone A with mAblb did not, suggesting the presence of this glycoprotein on the cell membranes of MS5I7 and W256, but not on Clone A. Immunofluorescence studies confirmed the presence of this glycoprotein on the cell plasma membrane of the MS5I7 and W256, but not on Clone A. Preincubation of MS5I7 and W256 with both mAblb and pAbllb/llla alone or in combination, also resulted in decreased (12S)-12 -hydroxy -5, 8,10, 14 -eicosatetraenoic acid (12-HETE) production, while platelets preincubated with these antibodies had no effect on the concentration of 12-HETE produced. Isolation of platelet membranes and released platelet contentswere tested separately and in combination on platelet adhesion to ECM. Platelet release factors were ineffective, while isolated platelet membrane ghosts enhanced adhesion. Disruption of the platelet cytoskeleton andinhibition of the formation of the llb/llla complex decreased platelet enhanced tumor cell adhesion. These findings suggest a role for these platelet glycoproteins in TCIPA, platelet enhanced tumor cell adhesion to ECM and subsequent tumor metastasis.
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McGregor, J. L., L. McGregor, M. Hans, A. Sayegh, M. C. Trzeeiak, and M. Dechavanne. "PLATELETS OF A PATIENT LACKING GLYCOPROTEINS lib AND Ilia AGGREGATE TO HIGH CONCENTRATIONS OF THROMBIN OR COLLAGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643863.

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The aim of this study was to investigate the platelets of a patient having bleeding episodes that began in infancy. The patient’s platelets in citrated-PRP did not aggregate when stimulated with ADP (5 and 10 uM), collagen (2.5 ug/ml), or sodium arachidonate (1 uM). However, washed patient platelets, in the presence of 2mM calcium, aggregated and secreted when stimulated with high concentrations of thrombin (0.36, 0.72 and lU/ml) or collagen (2, 4, 10 ug/ml). Monoclonal antibodies (Mab) LYP18 (directed against the IIb-IIIa glycoprotein complex) and LYP8 (anti-thrombospondin) inhibited thrombin and collagen induced aggregation of control but not the patient platelets. Patient thrombin -stimulated platelets did not bind 125I-labelled fibrinogen (40 to 320 ug/ml). Moreover, stimulating the washed patient's platelets with ADP (10-100 uM), in the presence of fibrinogen (2mg/ml), did not result in aggregation. Binding studies using Mab 125I-LYP2 (directed against the IIb-IIIa glycoprotein complex) showed the absence of the complex on the patient's platelets. The absence of the IIb-IIIa complex on the patient's platelets was also observed using crossed immunoelectro -phoresis and Mab 125I-LYP2 or 125I-LYP18. Individual glycoproteins (lib or Ilia) were not detected on silver stained two-dimensional (non-reduced/reduced) SDS-PAGE. Moreover, Western blots of |he patients platelets used in combination with anti-PLA or anti-LEK polyclonal antibodies failed to detect the presence of these two glycoproteins. These results indicate that this patient has Glanzmann's thrombasthenia or a variant of this disease. Moreover, this study shows that platelets lacking the IIb-IIIa glycoprotein complex can aggregate in responseto collagen or thrombin in the presence of physiological concentrations of calcium.
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Tritean, Naomi, Ștefan-Ovidiu Dima, Anisoara Cimpean, Diana Constantinescu-Aruxandei, and Florin Oancea. "Optimized Extraction of Glycoproteins from Ganoderma lucidum." In Priochem 2021. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/chemproc2022007053.

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Reports on the topic "Glycoproteins"

1

Varner, J. (Hydroxyproline-rich glycoproteins of the plant cell wall). Office of Scientific and Technical Information (OSTI), January 1990. http://dx.doi.org/10.2172/6855639.

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Dveksler, Gabriela S. Role of Pregnancy Specific Glycoproteins in Breast Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, September 1998. http://dx.doi.org/10.21236/ada361663.

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Varner, J. E. [Hydroxyproline: Rich glycoproteins of the plant and cell wall]. Office of Scientific and Technical Information (OSTI), January 1993. http://dx.doi.org/10.2172/6806611.

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Wong, Ho-Lun. Targeting Extracellular Matrix Glycoproteins in Metastases for Tumor-Initiating Cell Therapy. Fort Belvoir, VA: Defense Technical Information Center, February 2015. http://dx.doi.org/10.21236/ada618341.

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Varner, J. E. [Hydroxyproline: Rich glycoproteins of the plant and cell wall]. Annual technical progress report, 1993. Office of Scientific and Technical Information (OSTI), June 1993. http://dx.doi.org/10.2172/10156257.

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Barnard, M. R., H. MacGregor, A. D. Michelson, and C. R. Valeri. Effects of Liquid Storage and Cryopreservation on Platelet Surface Glycoproteins, Light Scatter, and Procoagulant Activity. Fort Belvoir, VA: Defense Technical Information Center, May 1996. http://dx.doi.org/10.21236/ada360295.

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Fusco, Deborah L. The Role of the Hendra Virus and Nipah Virus Attachment Glycoproteins in Receptor Binding and Antibody Neutralization. Fort Belvoir, VA: Defense Technical Information Center, January 2014. http://dx.doi.org/10.21236/ad1012829.

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Pavlin, Julie A. Characterization of the Fusion and Attachment Glycoproteins of Human Metapneumovirus and Human Serosurvey to Determine Reinfection Rates. Fort Belvoir, VA: Defense Technical Information Center, May 2007. http://dx.doi.org/10.21236/ad1014038.

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Lu, Jinhua. The Role of the MHV Receptor and Related Glycoproteins in Murine Hepatitis Virus Infection of Murine Cell Lines. Fort Belvoir, VA: Defense Technical Information Center, March 1995. http://dx.doi.org/10.21236/ad1011449.

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Yamamoto, Fumichiro. Phage Display Breast Carcinoma cDNA Libraries: Isolation of Clones Which Specifically Bind to Membrane Glycoproteins, Mucins, and Endothelial Cell Surface. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada398247.

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