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  1. Article ; Online: Profile of Carolyn R. Bertozzi, Morten Meldal, and K. Barry Sharpless: 2022 Nobel laureates in Chemistry.

    Kiessling, Laura L

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 35, Page(s) e2308367120

    Language English
    Publishing date 2023-08-21
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2308367120
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  2. Article ; Online: ACS Chemical Biology

    Kiessling, Laura L

    ACS chemical biology

    2021  Volume 16, Issue 1, Page(s) 1

    MeSH term(s) Epigenesis, Genetic ; Publishing
    Language English
    Publishing date 2021-01-14
    Publishing country United States
    Document type Editorial
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.0c00961
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Beyond the Crystal Structure of Human Macrophage C-Type Lectin.

    Gabba, Adele / Murphy, Paul V / Kiessling, Laura L / Birrane, Gabriel

    Biochemistry

    2024  Volume 63, Issue 2, Page(s) 191–193

    MeSH term(s) Humans ; Lectins, C-Type/chemistry ; Macrophages/chemistry
    Chemical Substances Lectins, C-Type
    Language English
    Publishing date 2024-01-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.3c00642
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  4. Article ; Online: Special Issue on Chemical Glycobiology.

    Huang, Mia L / Kiessling, Laura L

    ACS chemical biology

    2021  Volume 16, Issue 10, Page(s) 1793–1794

    MeSH term(s) Glycomics ; Humans ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Proteins/metabolism
    Chemical Substances Polysaccharides ; Proteins
    Language English
    Publishing date 2021-07-31
    Publishing country United States
    Document type Editorial ; Introductory Journal Article
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.1c00764
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Advances in glycoscience to understand viral infection and colonization.

    Dugan, Amanda E / Peiffer, Amanda L / Kiessling, Laura L

    Nature methods

    2022  Volume 19, Issue 4, Page(s) 384–387

    MeSH term(s) Glycosylation ; Humans ; Virus Diseases
    Language English
    Publishing date 2022-03-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2169522-2
    ISSN 1548-7105 ; 1548-7091
    ISSN (online) 1548-7105
    ISSN 1548-7091
    DOI 10.1038/s41592-022-01451-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 6022: Show issues Location:
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  6. Article ; Online: Transformative Medical Materials.

    De Laporte, Laura / Kiessling, Fabian

    Advanced healthcare materials

    2023  Volume 12, Issue 20, Page(s) e2301637

    Language English
    Publishing date 2023-07-13
    Publishing country Germany
    Document type Editorial
    ZDB-ID 2649576-4
    ISSN 2192-2659 ; 2192-2640
    ISSN (online) 2192-2659
    ISSN 2192-2640
    DOI 10.1002/adhm.202301637
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    Zs.A 6966: Show issues Location:
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  7. Article ; Online: Chemistry-driven glycoscience.

    Kiessling, Laura L

    Bioorganic & medicinal chemistry

    2018  Volume 26, Issue 19, Page(s) 5229–5238

    Abstract: Carbohydrates are the most prominent features of the cell's exterior-they are the cell's "face" and serve as the cell's identification card. The features of cell surface glycans (e.g. glycoproteins, glycolipids, polysaccharides) can be read by proteins, ... ...

    Abstract Carbohydrates are the most prominent features of the cell's exterior-they are the cell's "face" and serve as the cell's identification card. The features of cell surface glycans (e.g. glycoproteins, glycolipids, polysaccharides) can be read by proteins, other cells, or organisms. In all of these contexts, glycan-binding proteins typically recognize ("read") glycan identity. This recognition mediates important host-microbe interactions, as well as critical physiological functions, including fertilization, development, and immune system function. This article focuses on how proteins recognize glycans with an emphasis on three objectives: 1) to understand the molecular basis for carbohydrate recognition, 2) to implement that understanding to develop functional probes of protein-carbohydrate interactions, and 3) to apply those probes to elucidate and exploit the physiological consequences of protein-carbohydrate interactions. In this context, our group has focused on two key aspects of carbohydrate recognition: CH-π and multivalent interactions. We are applying the foundational knowledge gained from our studies for purposes ranging from illuminating host-microbe interactions to probing immune system function.
    MeSH term(s) Carbon/chemistry ; Cell Adhesion Molecules/chemistry ; Cell Adhesion Molecules/metabolism ; Dendritic Cells/metabolism ; Glycosylation ; Humans ; Hydrogen/chemistry ; Immunity, Active ; Kinetics ; Lectins/chemistry ; Lectins/metabolism ; Lectins, C-Type/chemistry ; Lectins, C-Type/metabolism ; Mycobacterium/physiology ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Protein Binding ; Proteins/chemistry ; Proteins/metabolism ; Receptors, Cell Surface/chemistry ; Receptors, Cell Surface/metabolism
    Chemical Substances Cell Adhesion Molecules ; DC-specific ICAM-3 grabbing nonintegrin ; Lectins ; Lectins, C-Type ; Polysaccharides ; Proteins ; Receptors, Cell Surface ; Carbon (7440-44-0) ; Hydrogen (7YNJ3PO35Z)
    Language English
    Publishing date 2018-09-22
    Publishing country England
    Document type Editorial ; Research Support, N.I.H., Extramural
    ZDB-ID 1161284-8
    ISSN 1464-3391 ; 0968-0896
    ISSN (online) 1464-3391
    ISSN 0968-0896
    DOI 10.1016/j.bmc.2018.09.024
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3815: 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)
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  8. Article ; Online: CH-π Interactions in Glycan Recognition.

    Kiessling, Laura L / Diehl, Roger C

    ACS chemical biology

    2021  Volume 16, Issue 10, Page(s) 1884–1893

    Abstract: Carbohydrate recognition is crucial for biological processes ranging from development to immune system function to host-pathogen interactions. The proteins that bind glycans are faced with a daunting task: to coax these hydrophilic species out of water ... ...

    Abstract Carbohydrate recognition is crucial for biological processes ranging from development to immune system function to host-pathogen interactions. The proteins that bind glycans are faced with a daunting task: to coax these hydrophilic species out of water and into a binding site. Here, we examine the forces underlying glycan recognition by proteins. Our previous bioinformatic study of glycan-binding sites indicated that the most overrepresented side chains are electron-rich aromatic residues, including tyrosine and tryptophan. These findings point to the importance of CH-π interactions for glycan binding. Studies of CH-π interactions show a strong dependence on the presence of an electron-rich π system, and the data indicate binding is enhanced by complementary electronic interactions between the electron-rich aromatic ring and the partial positive charge of the carbohydrate C-H protons. This electronic dependence means that carbohydrate residues with multiple aligned highly polarized C-H bonds, such as β-galactose, form strong CH-π interactions, whereas less polarized residues such as α-mannose do not. This information can guide the design of proteins to recognize sugars and the generation of ligands for proteins, small molecules, or catalysts that bind sugars.
    MeSH term(s) Animals ; Humans ; Hydrophobic and Hydrophilic Interactions ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Protein Binding ; Proteins/chemistry ; Proteins/metabolism ; Static Electricity
    Chemical Substances Polysaccharides ; Proteins
    Language English
    Publishing date 2021-10-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.1c00413
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Biosynthetic incorporation for visualizing bacterial glycans.

    Marando, Victoria M / Kim, Daria E / Kiessling, Laura L

    Methods in enzymology

    2022  Volume 665, Page(s) 135–151

    Abstract: Cell-surface glycans are central to many biological processes, yet methods for their site-selective modification are limited. Strategies for interrogating the structure and function of proteins have been enabled by chemoselective reactions of sidechain ... ...

    Abstract Cell-surface glycans are central to many biological processes, yet methods for their site-selective modification are limited. Strategies for interrogating the structure and function of proteins have been enabled by chemoselective reactions of sidechain functionality for covalent modification, capture, or imaging. However, unlike protein sidechains, glycan building blocks lack distinguishing reactivity. Moreover, glycans are not primary gene products, so encoding glycan variants through genetic manipulation is challenging. Reactive functional groups can be introduced into glycans through metabolic engineering, which involves the generation of modified nucleotide-sugar building blocks. Lipid-linked building blocks, which are also used in glycan biosynthesis, have the advantage that they can be delivered directly to glycosyltransferases to function as surrogate substrates. This process, termed "biosynthetic incorporation," takes advantage of the properties of bacterial glycosyltransferase: they are selective for the products they generate yet promiscuous in their donor preferences. We describe how this strategy can be implemented to label arabinofuranose-containing glycans on the surface of mycobacterial cells. We anticipate that this platform can be expanded to develop chemoselective labeling agents for other important bacterial monosaccharides.
    MeSH term(s) Cell Membrane/metabolism ; Glycosyltransferases/genetics ; Glycosyltransferases/metabolism ; Metabolic Engineering ; Polysaccharides, Bacterial ; Sugars
    Chemical Substances Polysaccharides, Bacterial ; Sugars ; Glycosyltransferases (EC 2.4.-)
    Language English
    Publishing date 2022-01-28
    Publishing country United States
    Document type Journal Article
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2021.12.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Advancing Chemical Microbiology.

    Kiessling, Laura L / Carlson, Erin E

    ACS chemical biology

    2020  Volume 15, Issue 5, Page(s) 1115–1118

    MeSH term(s) Anti-Infective Agents/chemistry ; Anti-Infective Agents/pharmacology ; Bacteria/enzymology ; Bacteria/metabolism ; Biological Products/chemistry ; Biological Products/pharmacology ; Drug Resistance, Microbial ; Fluorescent Dyes/chemistry ; Humans ; Metabolomics ; Mutagenesis ; Optical Imaging/methods ; Peptides/chemistry ; Peptides/pharmacology ; Viruses/metabolism
    Chemical Substances Anti-Infective Agents ; Biological Products ; Fluorescent Dyes ; Peptides
    Keywords covid19
    Language English
    Publishing date 2020-05-14
    Publishing country United States
    Document type Editorial ; Introductory Journal Article
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.0c00330
    Database MEDical Literature Analysis and Retrieval System OnLINE

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