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Showing 1 to 20 of 32 for “"protein glycosylation"”.

  1. Protein glycosylation in the gram-negative gamma proteobacterium photorhabdus luminescens

    … that Photorhabdus luminescens produces glycoproteins and thus contains a protein glycosylation system. P. luminescens is a pathogen of insects and a symbiont of soil nematodes. Adhesion and invasion are very important in the life cycle of the organism and it is speculated that the bacteria …

    dcu Repository record for Protein glycosylation in the gram-negative gamma proteobacterium photorhabdus luminescens (opens in a new tab)

  2. Investigating asparagine-linked protein glycosylation in eukaryotic and prokaryotic systems

    N-linked protein glycosylation is characterized by the formation of a -glycosylamine linkage to an asparagine residue within the Asn-Xaa-Ser/Thr consensus sequence. This modification is found in organisms from eukaryotic, archaeal and bacterial domains and is implicated in numerous cellular …

    mit Repository record for Investigating asparagine-linked protein glycosylation in eukaryotic and prokaryotic systems (opens in a new tab)

  3. Protein glycosylation by NleB and the secretion of therapeutic nanobody fusions

    … glycosyltransferases. They glycosylate host protein substrates on arginine residues with N-acetyl glucosamine (GlcNAc) to inhibit the function of host proteins involved in the innate immune response. Originally, it was thought that the effectors are inactive within the bacterium and fold into …

    ksu Repository record for Protein glycosylation by NleB and the secretion of therapeutic nanobody fusions (opens in a new tab)

  4. NEW METHODS TO QUANTIFY METHIONINE OXIDATION AND PROTEIN GLYCOSYLATION AND A DE NOVO GLYCOPEPTIDE DECOY GENERATOR

    Protein post-translational modifications (PTMs) produce complex, heterogeneous species that can best be identified and analyzed using mass spectrometry (MS). The ever-growing number of protein bioetherapeutics need effective MS tools to characterize PTMs and ensure drug safety and efficacy. …

    ku Repository record for NEW METHODS TO QUANTIFY METHIONINE OXIDATION AND PROTEIN GLYCOSYLATION AND A DE NOVO GLYCOPEPTIDE DECOY GENERATOR (opens in a new tab)

  5. Biochemical characterization of Cj 1123 c, a putative acetyltransferase & Cj 1319, a putative C6 dehydratase from Campylobacter jejuni.

    Glycoproteins are important for the virulence of Campylobacter jejuni. The enzymes involved in protein glycosylation could provide new therapeutic targets. Two such proteins are Cjll23c, a putative acetyltransferase and Cj 1319, a putative GDP-mannose dehydratase encoded by the N- and O-linked …

    uwo Repository record for Biochemical characterization of Cj 1123 c, a putative acetyltransferase & Cj 1319, a putative C6 dehydratase from Campylobacter jejuni. (opens in a new tab)

  6. Elucidation of the pathways responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine in bacterial pathogens

    … microbes through its incorporation onto various protein virulence factors. In particular, diNAcBac is found at the reducing end of glycans in both asparagine (N-linked) and serine/threonine (0-linked) protein glycosylation pathways. The second and third chapters examine the O-linked protein

    mit Repository record for Elucidation of the pathways responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine in bacterial pathogens (opens in a new tab)

  7. Protein expression and glycosylation in CHO cells

    … depends on sufficient expression and correct glycosylation of the recombinant product. Low product titer and inconsistent protein glycosylation constitute two major problems frequently encountered in biopharmaceutical production. Using Chinese Hamster Ovary (CHO) cells expressing recombinant …

    mit Repository record for Protein expression and glycosylation in CHO cells (opens in a new tab)

  8. Characterization of Glycans Derived from Biological Samples Using LC-MS/MS

    Proteins are intricate compounds that play vital roles in biological activities. One of the most prevalent post-translational modifications (PTMs) is protein glycosylation, which enhances several biological functions, such as protein stability, localization, cellular communication, inflammation, …

    ttu Repository record for Characterization of Glycans Derived from Biological Samples Using LC-MS/MS (opens in a new tab)

  9. Unnatural glycopeptides with application on cancer research

    Protein glycosylation is the most frequent post-translational modification which mediates a variety of cellular processes. In addition, changes in protein glycosylation can modulate cellular phenotypes such as growth, development, and disease. Therefore, the main objective of the present PhD …

    dialnet Repository record for Unnatural glycopeptides with application on cancer research (opens in a new tab)

  10. Polyprenyl-dependent glycan assembly pathways in microbial pathogens

    … of the undecaprenyl-dependent O-linked protein glycosylation pathway in Neisseria gonorrhoeae. The N. gonorrhoeae pathway is shown to produce UDP-N,N'-diacetylbacillosamine, which is the UDP-sugar donor in the first membrane-associated step. Furthermore, it is demonstrated that …

    mit Repository record for Polyprenyl-dependent glycan assembly pathways in microbial pathogens (opens in a new tab)

  11. Structural underpinnings of membrane association and mechanism in the monotopic phosphoglycosyl transferase superfamily

    In prokaryotes, protein glycosylation can be a determinant of pathogenicity as it plays a role in host adherence, invasion, and colonization. Impairment of glycosylation in some organisms, for example N-linked glycosylation in Campylobacter jejuni, leads to decreased pathogenicity; thus, opening …

    bu Repository record for Structural underpinnings of membrane association and mechanism in the monotopic phosphoglycosyl transferase superfamily (opens in a new tab)

  12. IMPROVING GLYCOSYLATION EFFICIENCY IN ESCHERICHIA COLI BY MAMMALIAN-CELL-INSPIRED PROTEIN-PROTEIN INTERACTIONS

    Asparagine linked glycosylation (N-glycosylation) is one of the most common post-translational modifications found in proteins. The central enzyme in the N-glycosylation pathway responsible for the transfer of glycans onto asparagine residues is called the oligosaccharyltransferase (OST). In …

    cornell Repository record for IMPROVING GLYCOSYLATION EFFICIENCY IN ESCHERICHIA COLI BY MAMMALIAN-CELL-INSPIRED PROTEIN-PROTEIN INTERACTIONS (opens in a new tab)

  13. Development of novel conjugate vaccines against Salmonella

    … the pathogen, chemically coupled to a carrier protein. Several clinical trials have shown that glycoconjugates are promising vaccine candidates to prevent Salmonella infections. However, manufacturing of conjugate vaccines is a complex, multi-step process. An alternative approach to produce …

    zurich

  14. ENGINEERING WATER-SOLUBLE VARIANTS OF THE SINGLE-SUBUNIT OLIGOSACCHARYLTRANSFERASE

    … a key enzyme in the asparagine-linked (N-linked) protein glycosylation pathway. OSTs exist in all domains of life and are capable of transferring a preassembled glycan from lipid carrier to an acceptor peptide. Bacterial OSTs are an single-subunit enzyme that are amenable to recombinant expression …

    cornell Repository record for ENGINEERING WATER-SOLUBLE VARIANTS OF THE SINGLE-SUBUNIT OLIGOSACCHARYLTRANSFERASE (opens in a new tab)

  15. Functional analysis of glycosylation of Zika virus envelope and NS1 proteins

    … syndrome. ZIKV has two important glycoproteins, both the envelope (E) protein, and nonstructural protein 1 (NS1). The ZIKV envelope (E) protein is responsible for viral entry and represents a major determinant for viral pathogenesis. NS1 forms a homodimer necessary for viral replication …

    utmb Repository record for Functional analysis of glycosylation of Zika virus envelope and NS1 proteins (opens in a new tab)

  16. Functional analysis of glycosylation of Zika virus envelope and NS1 proteins

    … syndrome. ZIKV has two important glycoproteins, both the envelope (E) protein, and nonstructural protein 1 (NS1). The ZIKV envelope (E) protein is responsible for viral entry and represents a major determinant for viral pathogenesis. NS1 forms a homodimer necessary for viral replication …

    utmb Repository record for Functional analysis of glycosylation of Zika virus envelope and NS1 proteins (opens in a new tab)

  17. Studies towards the in vivo inhibition of oligosaccharyl transferase

    Protein glycosylation is an important process because of the great diversity of glycoproteins that can be produced by the introduction of different oligosaccharide sequences. Our group has made significant progress in the study of asparagine-linked glycosylation. This process is catalyzed by …

    mit Repository record for Studies towards the in vivo inhibition of oligosaccharyl transferase (opens in a new tab)

  18. Assembly and Display of Surface Proteins In Actinomyces Oris

    … oris</em> utilizes cell wall anchored proteins and glycoconjugates to initiate adherence to host surfaces, recruit additional bacterial species that could not bind otherwise, and maintain the structural integrity of the oral biofilm. In this thesis, I reveal mechanisms involved in the …

    uthsc Repository record for Assembly and Display of Surface Proteins In Actinomyces Oris (opens in a new tab)

  19. Structural Analysis of Carbohydrates by Mass Spectrometry

    <p>Protein glycosylation is a highly frequent post-translational modification. Glycosylation is actively involved in intermolecular and intercellular binding events that are important to a wide range of biological functions such as immunity and fertility. The unique functions of glycans are …

    purdue-thes Repository record for Structural Analysis of Carbohydrates by Mass Spectrometry (opens in a new tab)

  20. Complex N-Glycosylation in Anti-Tumor Immunity

    … potential anti-tumor target for two reasons: (i) protein glycosylation is known to play a role in tumor progression, and (ii) alternatively glycosylated proteins may function as tumor neoantigens. The glycosyltransferase Mgat5 catalyzes the formation of 1,6-N-acetylglucosamine branched glycans, …

    penn Repository record for Complex N-Glycosylation in Anti-Tumor Immunity (opens in a new tab)

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