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  1. Book: Structural proteomics

    Owens, Raymond J.

    high-throughput methods

    (Methods in molecular biology ; 2305 ; Springer protocols)

    2021  

    Author's details edited by Raymond J. Owens
    Series title Methods in molecular biology ; 2305
    Springer protocols
    Collection
    Language English
    Size xii, 344 Seiten, Illustrationen
    Edition Third edition
    Publisher Humana Press
    Publishing place New York
    Publishing country United States
    Document type Book
    HBZ-ID HT020932610
    ISBN 978-1-0716-1405-1 ; 9781071614068 ; 1-0716-1405-3 ; 1071614061
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -2305- verfügbar in Königswinter Königswinter

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  2. Book: Structural proteomics

    Owens, Raymond J.

    high-throughput methods

    (Methods in molecular biology ; 1261 ; Springer protocols)

    2015  

    Author's details ed. by Raymond J. Owens
    Series title Methods in molecular biology ; 1261
    Springer protocols
    Collection
    Language English
    Size XII, 375 S. : Ill., graph. Darst.
    Edition 2. ed.
    Publisher Humana Press
    Publishing place New York
    Publishing country United States
    Document type Book
    HBZ-ID HT018508585
    ISBN 978-1-4939-2229-1 ; 9781493922307 ; 1-4939-2229-7 ; 1493922300
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -1261- verfügbar in Königswinter Königswinter

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  3. Article: Structural Biology of Nanobodies against the Spike Protein of SARS-CoV-2

    Tang, Qilong / Owens, Raymond J. / Naismith, James H.

    Viruses. 2021 Nov. 03, v. 13, no. 11

    2021  

    Abstract: Nanobodies are 130 amino acid single-domain antibodies (VHH) derived from the unique heavy-chain-only subclass of Camelid immunogloblins. Their small molecular size, facile expression, high affinity and stability have combined to make them unique ... ...

    Abstract Nanobodies are 130 amino acid single-domain antibodies (VHH) derived from the unique heavy-chain-only subclass of Camelid immunogloblins. Their small molecular size, facile expression, high affinity and stability have combined to make them unique targeting reagents with numerous applications in the biomedical sciences. The first nanobody agent has now entered the clinic as a treatment against a blood disorder. The spread of the SARS-CoV-2 virus has seen the global scientific endeavour work to accelerate the development of technologies to try to defeat a pandemic that has now killed over four million people. In a remarkably short period of time, multiple studies have reported nanobodies directed against the viral Spike protein. Several agents have been tested in culture and demonstrate potent neutralisation of the virus or pseudovirus. A few agents have completed animal trials with very encouraging results showing their potential for treating infection. Here, we discuss the structural features that guide the nanobody recognition of the receptor binding domain of the Spike protein of SARS-CoV-2.
    Keywords Camelidae ; Severe acute respiratory syndrome coronavirus 2 ; amino acids ; animals ; hematologic diseases ; molecular weight ; neutralization ; pandemic ; people ; structural biology ; viruses
    Language English
    Dates of publication 2021-1103
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v13112214
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Structural and mechanistic characterization of bifunctional heparan sulfate N-deacetylase-N-sulfotransferase 1.

    Mycroft-West, Courtney J / Abdelkarim, Sahar / Duyvesteyn, Helen M E / Gandhi, Neha S / Skidmore, Mark A / Owens, Raymond J / Wu, Liang

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 1326

    Abstract: Heparan sulfate (HS) polysaccharides are major constituents of the extracellular matrix, which are involved in myriad structural and signaling processes. Mature HS polysaccharides contain complex, non-templated patterns of sulfation and epimerization, ... ...

    Abstract Heparan sulfate (HS) polysaccharides are major constituents of the extracellular matrix, which are involved in myriad structural and signaling processes. Mature HS polysaccharides contain complex, non-templated patterns of sulfation and epimerization, which mediate interactions with diverse protein partners. Complex HS modifications form around initial clusters of glucosamine-N-sulfate (GlcNS) on nascent polysaccharide chains, but the mechanistic basis underpinning incorporation of GlcNS itself into HS remains unclear. Here, we determine cryo-electron microscopy structures of human N-deacetylase-N-sulfotransferase (NDST)1, the bifunctional enzyme primarily responsible for initial GlcNS modification of HS. Our structures reveal the architecture of both NDST1 deacetylase and sulfotransferase catalytic domains, alongside a non-catalytic N-terminal domain. The two catalytic domains of NDST1 adopt a distinct back-to-back topology that limits direct cooperativity. Binding analyses, aided by activity-modulating nanobodies, suggest that anchoring of the substrate at the sulfotransferase domain initiates the NDST1 catalytic cycle, providing a plausible mechanism for cooperativity despite spatial domain separation. Our data shed light on key determinants of NDST1 activity, and describe tools to probe NDST1 function in vitro and in vivo.
    MeSH term(s) Humans ; Cryoelectron Microscopy ; Heparitin Sulfate/metabolism ; Catalytic Domain ; Sulfotransferases/metabolism ; Extracellular Matrix/metabolism
    Chemical Substances Heparitin Sulfate (9050-30-0) ; Sulfotransferases (EC 2.8.2.-)
    Language English
    Publishing date 2024-02-13
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-45419-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Streamlining the production of proteins for structural biology.

    Owens, Raymond J / Gileadi, Opher

    Biophysical reviews

    2019  , Page(s) 533–534

    Language English
    Publishing date 2019-06-27
    Publishing country Germany
    Document type Letter
    ZDB-ID 2486483-3
    ISSN 1867-2469 ; 1867-2450
    ISSN (online) 1867-2469
    ISSN 1867-2450
    DOI 10.1007/s12551-019-00565-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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  6. Article ; Online: Structural Biology of Nanobodies against the Spike Protein of SARS-CoV-2.

    Tang, Qilong / Owens, Raymond J / Naismith, James H

    Viruses

    2021  Volume 13, Issue 11

    Abstract: Nanobodies are 130 amino acid single-domain antibodies ( ... ...

    Abstract Nanobodies are 130 amino acid single-domain antibodies (V
    MeSH term(s) Animals ; Antibodies, Neutralizing/chemistry ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; COVID-19/therapy ; COVID-19/virology ; Epitopes/chemistry ; Humans ; Mutation ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; SARS-CoV-2/chemistry ; SARS-CoV-2/immunology ; Single-Domain Antibodies/chemistry ; Single-Domain Antibodies/immunology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/immunology
    Chemical Substances Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Single-Domain Antibodies ; Spike Glycoprotein, Coronavirus
    Language English
    Publishing date 2021-11-03
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v13112214
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Screening of Membrane Protein Production by Comparison of Transient Expression in Insect and Mammalian Cells.

    Kaipa, Jagan Mohan / Krasnoselska, Ganna / Owens, Raymond J / van den Heuvel, Joop

    Biomolecules

    2023  Volume 13, Issue 5

    Abstract: Membrane proteins are difficult biomolecules to express and purify. In this paper, we compare the small-scale production of six selected eukaryotic integral membrane proteins in insect and mammalian cell expression systems using different techniques for ... ...

    Abstract Membrane proteins are difficult biomolecules to express and purify. In this paper, we compare the small-scale production of six selected eukaryotic integral membrane proteins in insect and mammalian cell expression systems using different techniques for gene delivery. The target proteins were C terminally fused to the green fluorescent marker protein GFP to enable sensitive monitoring. We show that the choice of expression systems makes a considerable difference to the yield and quality of the six selected membrane proteins. Virus-free transient gene expression (TGE) in insect High Five cells combined with solubilization in dodecylmaltoside plus cholesteryl hemisuccinate generated the most homogeneous samples for all six targets. Further, the affinity purification of the solubilized proteins using the Twin-Strep
    MeSH term(s) Animals ; Membrane Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Insecta/metabolism ; Recombinant Proteins ; Mammals/metabolism
    Chemical Substances Membrane Proteins ; Green Fluorescent Proteins (147336-22-9) ; Recombinant Proteins
    Language English
    Publishing date 2023-05-11
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom13050817
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: The solution structure of the heavy chain-only C5-Fc nanobody reveals exposed variable regions that are optimal for COVID-19 antigen interactions.

    Gao, Xin / Thrush, Joseph W / Gor, Jayesh / Naismith, James H / Owens, Raymond J / Perkins, Stephen J

    The Journal of biological chemistry

    2023  Volume 299, Issue 11, Page(s) 105337

    Abstract: Heavy chain-only antibodies can offer advantages of higher binding affinities, reduced sizes, and higher stabilities than conventional antibodies. To address the challenge of SARS-CoV-2 coronavirus, a llama-derived single-domain nanobody C5 was developed ...

    Abstract Heavy chain-only antibodies can offer advantages of higher binding affinities, reduced sizes, and higher stabilities than conventional antibodies. To address the challenge of SARS-CoV-2 coronavirus, a llama-derived single-domain nanobody C5 was developed previously that has high COVID-19 virus neutralization potency. The fusion protein C5-Fc comprises two C5 domains attached to a glycosylated Fc region of a human IgG1 antibody and shows therapeutic efficacy in vivo. Here, we have characterized the solution arrangement of the molecule. Two 1443 Da N-linked glycans seen in the mass spectra of C5-Fc were removed and the glycosylated and deglycosylated structures were evaluated. Reduction of C5-Fc with 2-mercaptoethylamine indicated three interchain Cys-Cys disulfide bridges within the hinge. The X-ray and neutron Guinier R
    MeSH term(s) Humans ; Immunoglobulin G/chemistry ; Immunoglobulin Heavy Chains/chemistry ; Models, Molecular ; Polysaccharides ; SARS-CoV-2 ; Antibodies, Viral/chemistry ; Single-Domain Antibodies/chemistry
    Chemical Substances Immunoglobulin G ; Immunoglobulin Heavy Chains ; Polysaccharides ; Antibodies, Viral ; Single-Domain Antibodies
    Language English
    Publishing date 2023-10-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.105337
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  9. Article ; Online: Structural proteomics: high-throughput methods. Preface.

    Owens, Raymond J

    Methods in molecular biology (Clifton, N.J.)

    2015  Volume 1261, Page(s) v

    MeSH term(s) Humans ; Proteins/chemistry ; Proteins/isolation & purification ; Proteomics/methods
    Chemical Substances Proteins
    Language English
    Publishing date 2015-01-24
    Publishing country United States
    Document type Introductory Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-2230-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Book: Structural proteomics

    Owens, Raymond J

    high-throughput methods

    (Methods in molecular biology, ; 1261 ; Springer protocols)

    2015  

    Author's details edited by Raymond J. Owens
    Series title Methods in molecular biology, ; 1261
    Springer protocols
    MeSH term(s) Proteomics/methods ; Protein Conformation ; Membrane Proteins/ultrastructure
    Language English
    Size xii, 375 pages :, illustrations.
    Edition Second edition.
    Document type Book
    ISBN 9781493922291 ; 9781493922307 ; 1493922297 ; 1493922300
    Database Catalogue of the US National Library of Medicine (NLM)

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

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