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  1. Book ; Online ; E-Book: Macromolecular protein complexes / IV

    Harris, James R. / Marles-Wright, Jon

    structure and function

    (Subcellular biochemistry ; 99)

    2022  

    Abstract: This book covers the latest findings of a wide variety of viral, prokaryotic and eukaryotic macromolecular protein complexes and builds upon the solid macromolecular foundations established by previous volumes of the Subcellular Biochemistry series. Thus, ...

    Author's details J. Robin Harris, Jon Marles-Wright editors
    Series title Subcellular biochemistry ; 99
    Macromolecular protein complexes
    Collection Macromolecular protein complexes
    Abstract This book covers the latest findings of a wide variety of viral, prokaryotic and eukaryotic macromolecular protein complexes and builds upon the solid macromolecular foundations established by previous volumes of the Subcellular Biochemistry series. Thus, an almost encyclopaedic coverage of the broad field of protein complex structure and function has been established. The 17 interesting chapters included in this book have been organised into four sections: Soluble Protein Complexes, Membrane Protein Complexes, Fibrous Protein Complexes and Viral Protein Complexes. Significant topics present here are: Fatty Acid Synthase, the Fork Protection Complex, Ribonucleotide Reductase, the Kinetochore, G proteins, the FtsEX Complex, the Kainate Receptor, the Photosystem I-antenna, the Mycobacterial Arabinofuranosyltransferases, the the Bacterial Flagellum, the Actomyosin Complex, Motile Cilia, SLS Collagen Polymorphic Structures, and the Reovirus Capsid and Polymerase. Up-dates/expansion of chapter topics present in earlier volumes are now included in chapters here, e.g., those on Ferritin-like proteins and the Multi-tRNA Synthetase. The book is richly illustrated throughout, which is the result of an impressive integration of structural data from X-ray crystallography with that from cryo-electron microscopy. Functional aspects of protein-protein interactions are also given a high priority.
    Keywords Proteins ; Biomolecules ; Physical biochemistry ; Macromolecules ; Cytology
    Language English
    Size 1 Online-Ressource (viii, 552 Seiten), Illustrationen, Diagramme
    Publishing country Switzerland
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT021584603
    ISBN 978-3-031-00793-4 ; 9783031007927 ; 3-031-00793-X ; 3031007921
    DOI 10.1007/978-3-031-00793-4
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book ; Online ; E-Book: Macromolecular protein complexes / III

    Harris, James R. / Marles-Wright, Jon

    structure and function

    (Subcellular biochemistry ; 96)

    2021  

    Author's details J. Robin Harris, Jon Marles-Wright editors
    Series title Subcellular biochemistry ; 96
    Macromolecular protein complexes
    Collection Macromolecular protein complexes
    Language English
    Size 1 Online-Ressource (viii, 577 Seiten), Illustrationen, Diagramme
    Publishing country Switzerland
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT021584888
    ISBN 978-3-030-58971-4 ; 9783030589707 ; 3-030-58971-4 ; 3030589706
    DOI 10.1007/978-3-030-58971-4
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

    Full text online

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  3. Book ; Online ; E-Book: Macromolecular protein complexes / II

    Harris, James R. / Marles-Wright, Jon

    structure and function

    (Subcellular biochemistry ; 93)

    2019  

    Author's details J. Robin Harris, Jon Marles-Wright editors
    Series title Subcellular biochemistry ; 93
    Macromolecular protein complexes
    Collection Macromolecular protein complexes
    Language English
    Size 1 Online-Ressource (viii, 658 Seiten), Illustrationen, Diagramme
    Publishing country Switzerland
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT021584886
    ISBN 978-3-030-28151-9 ; 9783030281502 ; 3-030-28151-5 ; 3030281507
    DOI 10.1007/978-3-030-28151-9
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

    Full text online

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  4. Book ; Online: Macromolecular protein complexes

    Harris, James R. / Marles-Wright, Jon

    structure and function

    (Subcellular biochemistry)

    2017  

    Author's details J. Robin Harris, Jon Marles-Wright editors
    Series title Subcellular biochemistry
    Keywords Multiprotein Complexes ; Macromolecular Substances ; Models, Molecular ; Life sciences ; Proteins
    Subject code 572.6
    Language English
    Dates of publication 2017-9999
    Size Online-Ressource
    Publisher Springer
    Publishing place Cham
    Publishing country Switzerland
    Document type Book ; Online
    HBZ-ID HT019879955
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  5. Book ; Online ; E-Book: Macromolecular protein complexes / [I]

    Harris, James R. / Marles-Wright, Jon

    structure and function

    (Subcellular biochemistry ; 83)

    2017  

    Author's details J. Robin Harris, Jon Marles-Wright editors
    Series title Subcellular biochemistry ; 83
    Macromolecular protein complexes
    Collection Macromolecular protein complexes
    Language English
    Size 1 Online-Ressource (viii, 572 Seiten), Illustrationen
    Publishing country Switzerland
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT021584854
    ISBN 978-3-319-46503-6 ; 9783319465012 ; 3-319-46503-1 ; 3319465015
    DOI 10.1007/978-3-319-46503-6
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

    Full text online

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  6. Article ; Online: A User's Guide to Golden Gate Cloning Methods and Standards.

    Bird, Jasmine E / Marles-Wright, Jon / Giachino, Andrea

    ACS synthetic biology

    2022  Volume 11, Issue 11, Page(s) 3551–3563

    Abstract: The continual demand for specialized molecular cloning techniques that suit a broad range of applications has driven the development of many different cloning strategies. One method that has gained significant traction is Golden Gate assembly, which ... ...

    Abstract The continual demand for specialized molecular cloning techniques that suit a broad range of applications has driven the development of many different cloning strategies. One method that has gained significant traction is Golden Gate assembly, which achieves hierarchical assembly of DNA parts by utilizing Type IIS restriction enzymes to produce user-specified sticky ends on cut DNA fragments. This technique has been modularized and standardized, and includes different subfamilies of methods, the most widely adopted of which are the MoClo and Golden Braid standards. Moreover, specialized toolboxes tailored to specific applications or organisms are also available. Still, the quantity and range of assembly methods can constitute a barrier to adoption for new users, and even experienced scientists might find it difficult to discern which tools are best suited toward their goals. In this review, we provide a beginner-friendly guide to Golden Gate assembly, compare the different available standards, and detail the specific features and quirks of commonly used toolboxes. We also provide an update on the state-of-the-art in Golden Gate technology, discussing recent advances and challenges to inform existing users and promote standard practices.
    MeSH term(s) Synthetic Biology/methods ; Cloning, Molecular ; DNA Restriction Enzymes/genetics ; DNA/genetics ; Genetic Vectors
    Chemical Substances DNA Restriction Enzymes (EC 3.1.21.-) ; DNA (9007-49-2)
    Language English
    Publishing date 2022-11-02
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ISSN 2161-5063
    ISSN (online) 2161-5063
    DOI 10.1021/acssynbio.2c00355
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Introduction: Protein Oligomerization and the Formation of Macromolecular Assemblies.

    Harris, J Robin / Marles-Wright, Jon

    Sub-cellular biochemistry

    2020  Volume 93, Page(s) 1–22

    Abstract: The ability of biomolecules to link together to form higher order assemblies underlies much of cellular structure and function. Here we emphasise protein oligomerisation and discuss some of the principles of molecular interaction, from early ... ...

    Abstract The ability of biomolecules to link together to form higher order assemblies underlies much of cellular structure and function. Here we emphasise protein oligomerisation and discuss some of the principles of molecular interaction, from early considerations through to the present day. A few protein examples are presented, selected from our research interests, to highlight assembly features, ranging from the hemoglobins, the hemocyanins to the peroxiredoxins, collagen, the encapsulins and ferritins.
    MeSH term(s) Macromolecular Substances/chemistry ; Macromolecular Substances/metabolism ; Protein Multimerization
    Chemical Substances Macromolecular Substances
    Language English
    Publishing date 2020-01-14
    Publishing country United States
    Document type Introductory Journal Article
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-030-28151-9_1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Synthetic biology approaches to copper remediation: bioleaching, accumulation and recycling.

    Giachino, Andrea / Focarelli, Francesca / Marles-Wright, Jon / Waldron, Kevin J

    FEMS microbiology ecology

    2021  Volume 97, Issue 2

    Abstract: One of the current aims of synthetic biology is the development of novel microorganisms that can mine economically important elements from the environment or remediate toxic waste compounds. Copper, in particular, is a high-priority target for ... ...

    Abstract One of the current aims of synthetic biology is the development of novel microorganisms that can mine economically important elements from the environment or remediate toxic waste compounds. Copper, in particular, is a high-priority target for bioremediation owing to its extensive use in the food, metal and electronic industries and its resulting common presence as an environmental pollutant. Even though microbe-aided copper biomining is a mature technology, its application to waste treatment and remediation of contaminated sites still requires further research and development. Crucially, any engineered copper-remediating chassis must survive in copper-rich environments and adapt to copper toxicity; they also require bespoke adaptations to specifically extract copper and safely accumulate it as a human-recoverable deposit to enable biorecycling. Here, we review current strategies in copper bioremediation, biomining and biorecycling, as well as strategies that extant bacteria use to enhance copper tolerance, accumulation and mineralization in the native environment. By describing the existing toolbox of copper homeostasis proteins from naturally occurring bacteria, we show how these modular systems can be exploited through synthetic biology to enhance the properties of engineered microbes for biotechnological copper recovery applications.
    MeSH term(s) Biodegradation, Environmental ; Copper ; Humans ; Metals ; Recycling ; Synthetic Biology
    Chemical Substances Metals ; Copper (789U1901C5)
    Language English
    Publishing date 2021-01-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 283722-5
    ISSN 1574-6941 ; 0168-6496
    ISSN (online) 1574-6941
    ISSN 0168-6496
    DOI 10.1093/femsec/fiaa249
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2967: 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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  9. Article: Versatile Chemo-Biocatalytic Cascade Driven by a Thermophilic and Irreversible C-C Bond-Forming α-Oxoamine Synthase.

    Ashley, Ben / Baslé, Arnaud / Sajjad, Mariyah / El Ashram, Ahmed / Kelis, Panayiota / Marles-Wright, Jon / Campopiano, Dominic J

    ACS sustainable chemistry & engineering

    2023  Volume 11, Issue 21, Page(s) 7997–8002

    Abstract: We report a chemo-biocatalytic cascade for the synthesis of substituted pyrroles, driven by the action of an irreversible, thermostable, pyridoxal 5'-phosphate (PLP)-dependent, C-C bond-forming biocatalyst ( ...

    Abstract We report a chemo-biocatalytic cascade for the synthesis of substituted pyrroles, driven by the action of an irreversible, thermostable, pyridoxal 5'-phosphate (PLP)-dependent, C-C bond-forming biocatalyst (
    Language English
    Publishing date 2023-05-16
    Publishing country United States
    Document type Journal Article
    ISSN 2168-0485
    ISSN 2168-0485
    DOI 10.1021/acssuschemeng.3c00243
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Toxin release by conditional remodelling of ParDE1 from Mycobacterium tuberculosis leads to gyrase inhibition.

    Beck, Izaak N / Arrowsmith, Tom J / Grobbelaar, Matthew J / Bromley, Elizabeth H C / Marles-Wright, Jon / Blower, Tim R

    Nucleic acids research

    2023  Volume 52, Issue 4, Page(s) 1909–1929

    Abstract: Mycobacterium tuberculosis, the causative agent of tuberculosis, is a growing threat to global health, with recent efforts towards its eradication being reversed in the wake of the COVID-19 pandemic. Increasing resistance to gyrase-targeting second-line ... ...

    Abstract Mycobacterium tuberculosis, the causative agent of tuberculosis, is a growing threat to global health, with recent efforts towards its eradication being reversed in the wake of the COVID-19 pandemic. Increasing resistance to gyrase-targeting second-line fluoroquinolone antibiotics indicates the necessity to develop both novel therapeutics and our understanding of M. tuberculosis growth during infection. ParDE toxin-antitoxin systems also target gyrase and are regulated in response to both host-associated and drug-induced stress during infection. Here, we present microbiological, biochemical, structural, and biophysical analyses exploring the ParDE1 and ParDE2 systems of M. tuberculosis H37Rv. The structures reveal conserved modes of toxin-antitoxin recognition, with complex-specific interactions. ParDE1 forms a novel heterohexameric ParDE complex, supported by antitoxin chains taking on two distinct folds. Curiously, ParDE1 exists in solution as a dynamic equilibrium between heterotetrameric and heterohexameric complexes. Conditional remodelling into higher order complexes can be thermally driven in vitro. Remodelling induces toxin release, tracked through concomitant inhibition and poisoning of gyrase activity. Our work aids our understanding of gyrase inhibition, allowing wider exploration of toxin-antitoxin systems as inspiration for potential therapeutic agents.
    MeSH term(s) Humans ; Antitoxins/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/chemistry ; DNA Gyrase/genetics ; Fluoroquinolones ; Mycobacterium tuberculosis ; Pandemics ; Tuberculosis/microbiology ; Bacterial Toxins/metabolism
    Chemical Substances Antitoxins ; Bacterial Proteins ; DNA Gyrase (EC 5.99.1.3) ; Fluoroquinolones ; Bacterial Toxins
    Language English
    Publishing date 2023-12-12
    Publishing country England
    Document type Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkad1220
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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