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  1. Article ; Online: Glyco-Engineering Cell Surfaces by Exo-Enzymatic Installation of GlcNAz and LacNAz Motifs.

    De León González, Fabiola V / Boddington, Marie E / Kofsky, Joshua M / Prindl, Martha I / Capicciotti, Chantelle J

    ACS chemical biology

    2024  Volume 19, Issue 3, Page(s) 629–640

    Abstract: Exo-enzymatic glyco-engineering of cell-surface glycoconjugates enables the selective display of well-defined glyco-motifs bearing bioorthogonal functional groups, which can be used to study glycans and their interactions with glycan-binding proteins. In ...

    Abstract Exo-enzymatic glyco-engineering of cell-surface glycoconjugates enables the selective display of well-defined glyco-motifs bearing bioorthogonal functional groups, which can be used to study glycans and their interactions with glycan-binding proteins. In recent years, strategies to edit cellular glycans by installing monosaccharides and their derivatives using glycosyltransferase enzymes have rapidly expanded. However, analogous methods to introduce chemical reporter-functionalized type 2 LacNAc motifs have not been reported. Herein, we report the chemo-enzymatic synthesis of unnatural UDP-GlcNAc and UDP-GalNAc nucleotide-sugars bearing azide, alkyne, and diazirine functionalities on the C2-acetamido group using the mutant uridylyltransferase AGX1
    MeSH term(s) Humans ; Polysaccharides/metabolism ; Glycoconjugates ; Cell Membrane/metabolism ; Transferases ; Uridine Diphosphate
    Chemical Substances Polysaccharides ; Glycoconjugates ; Transferases (EC 2.-) ; Uridine Diphosphate (58-98-0)
    Language English
    Publishing date 2024-02-23
    Publishing country United States
    Document type Journal Article
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.3c00542
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Glycosyltransferases as versatile tools to study the biology of glycans.

    Kofsky, Joshua M / Babulic, Jonathan L / Boddington, Marie E / De León González, Fabiola V / Capicciotti, Chantelle J

    Glycobiology

    2023  Volume 33, Issue 11, Page(s) 888–910

    Abstract: All cells are decorated with complex carbohydrate structures called glycans that serve as ligands for glycan-binding proteins (GBPs) to mediate a wide range of biological processes. Understanding the specific functions of glycans is key to advancing an ... ...

    Abstract All cells are decorated with complex carbohydrate structures called glycans that serve as ligands for glycan-binding proteins (GBPs) to mediate a wide range of biological processes. Understanding the specific functions of glycans is key to advancing an understanding of human health and disease. However, the lack of convenient and accessible tools to study glycan-based interactions has been a defining challenge in glycobiology. Thus, the development of chemical and biochemical strategies to address these limitations has been a rapidly growing area of research. In this review, we describe the use of glycosyltransferases (GTs) as versatile tools to facilitate a greater understanding of the biological roles of glycans. We highlight key examples of how GTs have streamlined the preparation of well-defined complex glycan structures through chemoenzymatic synthesis, with an emphasis on synthetic strategies allowing for site- and branch-specific display of glyco-epitopes. We also describe how GTs have facilitated expansion of glyco-engineering strategies, on both glycoproteins and cell surfaces. Coupled with advancements in bioorthogonal chemistry, GTs have enabled selective glyco-epitope editing of glycoproteins and cells, selective glycan subclass labeling, and the introduction of novel biomolecule functionalities onto cells, including defined oligosaccharides, antibodies, and other proteins. Collectively, these approaches have contributed great insight into the fundamental biological roles of glycans and are enabling their application in drug development and cellular therapies, leaving the field poised for rapid expansion.
    MeSH term(s) Humans ; Glycosyltransferases/metabolism ; Glycosylation ; Polysaccharides/chemistry ; Glycoproteins/metabolism ; Glycomics
    Chemical Substances Glycosyltransferases (EC 2.4.-) ; Polysaccharides ; Glycoproteins
    Language English
    Publishing date 2023-11-13
    Publishing country England
    Document type Review ; Journal Article
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwad092
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3150: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Antifreeze protein complements cryoprotective dehydration in the freeze-avoiding springtail Megaphorura arctica.

    Graham, Laurie A / Boddington, Marie E / Holmstrup, Martin / Davies, Peter L

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 3047

    Abstract: The springtail, Megaphorura arctica, is freeze-avoiding and survives sub-zero temperatures by cryoprotective dehydration. At the onset of dehydration there is some supercooling of body fluids, and the danger of inoculative freezing, which would be lethal. ...

    Abstract The springtail, Megaphorura arctica, is freeze-avoiding and survives sub-zero temperatures by cryoprotective dehydration. At the onset of dehydration there is some supercooling of body fluids, and the danger of inoculative freezing, which would be lethal. To see if the springtails are protected by antifreeze proteins in this pre-equilibrium phase, we examined extracts from cold-acclimated M. arctica and recorded over 3 °C of freezing point depression. Proteins responsible for this antifreeze activity were isolated by ice affinity. They comprise isoforms ranging from 6.5 to 16.9 kDa, with an amino acid composition dominated by glycine (>35 mol%). Tryptic peptide sequences were used to identify the mRNA sequence coding for the smallest isoform. This antifreeze protein sequence has high similarity to one characterized in Hypogastrura harveyi, from a different springtail order. If these two antifreeze proteins are true homologs, we suggest their origin dates back to the Permian glaciations some 300 million years ago.
    MeSH term(s) Amino Acid Sequence ; Animals ; Antifreeze Proteins/chemistry ; Antifreeze Proteins/metabolism ; Arthropods/physiology ; Cryoprotective Agents/metabolism ; Crystallization ; DNA, Complementary/genetics ; Dehydration/metabolism ; Freezing ; Glycine/metabolism ; Models, Molecular ; Protein Isoforms/metabolism
    Chemical Substances Antifreeze Proteins ; Cryoprotective Agents ; DNA, Complementary ; Protein Isoforms ; Glycine (TE7660XO1C)
    Language English
    Publishing date 2020-02-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-60060-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: One-Step Selective Labeling of Native Cell Surface Sialoglycans by Exogenous α2,8-Sialylation.

    Babulic, Jonathan L / Kofsky, Joshua M / Boddington, Marie E / Kim, Youjin / Leblanc, Emmanuelle V / Cook, Madeleine G / Garnier, Cole R / Emberley-Korkmaz, Sophie / Colpitts, Che C / Capicciotti, Chantelle J

    ACS chemical biology

    2023  Volume 18, Issue 11, Page(s) 2418–2429

    Abstract: Exo-enzymatic glycan labeling strategies have emerged as versatile tools for efficient and selective installation of terminal glyco-motifs onto live cell surfaces. Through employing specific enzymes and nucleotide-sugar probes, cells can be equipped with ...

    Abstract Exo-enzymatic glycan labeling strategies have emerged as versatile tools for efficient and selective installation of terminal glyco-motifs onto live cell surfaces. Through employing specific enzymes and nucleotide-sugar probes, cells can be equipped with defined glyco-epitopes for modulating cell function or selective visualization and enrichment of glycoconjugates. Here, we identify
    MeSH term(s) Sialyltransferases/metabolism ; Cell Membrane/metabolism ; Polysaccharides/metabolism ; Glycoconjugates ; Epitopes
    Chemical Substances Sialyltransferases (EC 2.4.99.-) ; Polysaccharides ; Glycoconjugates ; Epitopes
    Language English
    Publishing date 2023-11-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.3c00475
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Mass Spectrometry-Based Shotgun Glycomics Using Labeled Glycan Libraries

    Bui, Duong T. / Jung, Jaesoo / Kitova, Elena N. / Li, Zhixiong / Willows, Steven D. / Boddington, Marie E. / Kitov, Pavel I. / Mason, Andrew L. / Capicciotti, Chantelle J. / Mahal, Lara K. / Macauley, Matthew S. / Klassen, John S.

    Analytical chemistry. 2022 Mar. 18, v. 94, no. 12

    2022  

    Abstract: Mass spectrometry-based shotgun glycomics (MS-SG) is a rapid, sensitive, label-, and immobilization-free approach for the discovery of natural ligands of glycan-binding proteins (GBPs). To perform MS-SG, natural libraries of glycans derived from ... ...

    Abstract Mass spectrometry-based shotgun glycomics (MS-SG) is a rapid, sensitive, label-, and immobilization-free approach for the discovery of natural ligands of glycan-binding proteins (GBPs). To perform MS-SG, natural libraries of glycans derived from glycoconjugates in cells or tissues are screened against a target GBP using catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS). Because glycan concentrations are challenging to determine, ligand affinities cannot be directly measured. In principle, relative affinities can be ranked by combining CaR-ESI-MS data with relative concentrations established by hydrophilic interaction liquid chromatography (HILIC) performed on the fluorophore-labeled glycan library. To validate this approach, as well as the feasibility of performing CaR-ESI-MS directly on labeled glycans, libraries of labeled N-glycans extracted from the human monocytic U937 cells or intestinal tissues were labeled with 2-aminobenzamide (2-AB), 2-aminobenzoic acid (2-AA), or procainamide (proA). The libraries were screened against plant and human GBPs with known specificities for α2-3- and α2-6-linked sialosides and quantified by HILIC. Dramatic differences, in some cases, were found for affinity rankings obtained with libraries labeled with different fluorophores, as well as those produced using the combined unlabeled/labeled library approach. The origin of these differences could be explained by differential glycan labeling efficiencies, the impact of specific labels on glycan affinities for the GBPs, and the relative efficiency of release of ligands from GBPs in CaR-ESI-MS. Overall, the results of this study suggest that the 2-AB(CaR-ESI-MS)/2-AB(HILIC) combination provides the most reliable description of the binding specificities of GBPs for N-glycans and is recommended for MS-SG applications.
    Keywords analytical chemistry ; electrospray ionization mass spectrometry ; fluorescent dyes ; glycoconjugates ; glycomics ; humans ; hydrophilic interaction chromatography ; intestines ; ligands ; polysaccharides
    Language English
    Dates of publication 2022-0318
    Size p. 4997-5005.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.1c04779
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 4' 52/94: Show issues
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  6. Article ; Online: Mass Spectrometry-Based Shotgun Glycomics Using Labeled Glycan Libraries.

    Bui, Duong T / Jung, Jaesoo / Kitova, Elena N / Li, Zhixiong / Willows, Steven D / Boddington, Marie E / Kitov, Pavel I / Mason, Andrew L / Capicciotti, Chantelle J / Mahal, Lara K / Macauley, Matthew S / Klassen, John S

    Analytical chemistry

    2022  Volume 94, Issue 12, Page(s) 4997–5005

    Abstract: Mass spectrometry-based shotgun glycomics (MS-SG) is a rapid, sensitive, label-, and immobilization-free approach for the discovery of natural ligands of glycan-binding proteins (GBPs). To perform MS-SG, natural libraries of glycans derived from ... ...

    Abstract Mass spectrometry-based shotgun glycomics (MS-SG) is a rapid, sensitive, label-, and immobilization-free approach for the discovery of natural ligands of glycan-binding proteins (GBPs). To perform MS-SG, natural libraries of glycans derived from glycoconjugates in cells or tissues are screened against a target GBP using catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS). Because glycan concentrations are challenging to determine, ligand affinities cannot be directly measured. In principle, relative affinities can be ranked by combining CaR-ESI-MS data with relative concentrations established by hydrophilic interaction liquid chromatography (HILIC) performed on the fluorophore-labeled glycan library. To validate this approach, as well as the feasibility of performing CaR-ESI-MS directly on labeled glycans, libraries of labeled
    MeSH term(s) Carrier Proteins/metabolism ; Chromatography, Liquid ; Fluorescent Dyes/chemistry ; Glycomics/methods ; Humans ; Ligands ; Polysaccharides/chemistry ; Proteins/metabolism ; Spectrometry, Mass, Electrospray Ionization/methods
    Chemical Substances Carrier Proteins ; Fluorescent Dyes ; Ligands ; Polysaccharides ; Proteins
    Language English
    Publishing date 2022-03-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.1c04779
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4033: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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