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  1. Book: Bacterial secretion systems

    Journet, Laure / Cascales, Eric

    methods and protocols

    (Methods in molecular biology ; 2715 ; Springer protocols)

    2024  

    Author's details edited by Laure Journet, Eric Cascales
    Series title Methods in molecular biology ; 2715
    Springer protocols
    Collection
    Language English
    Size xvi, 613 Seiten, Illustrationen
    Edition Second edition
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT030590813
    ISBN 978-1-0716-3444-8 ; 9781071634455 ; 1-0716-3444-5 ; 1071634453
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2024 A 75 available for loan (reading room) Lesesaal EG

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  2. Book ; Online: Bacterial Secretion Systems

    Arechaga, Ignacio / Cascales, Eric

    2020  

    Keywords Science: general issues ; Medical microbiology & virology ; Microbiology (non-medical) ; Bacteria ; Secretion ; Membrane ; Transport ; Protein Complex ; Pathogen
    Size 1 electronic resource (292 pages)
    Publisher Frontiers Media SA
    Document type Book ; Online
    Note English ; Open Access
    HBZ-ID HT021230626
    ISBN 9782889639571 ; 2889639576
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  3. Book: Bacterial protein secretion systems

    Journet, Laure / Cascales, Eric

    methods and protocols

    (Methods in molecular biology ; 1615 ; Springer protocols)

    2017  

    Author's details editors Laure Journet and Eric Cascales
    Series title Methods in molecular biology ; 1615
    Springer protocols
    Collection
    Keywords Fractionation ; Lipoproteins ; Peptidoglycan ; Protease ; sub-cellular localisation
    Subject code 570
    Language English
    Size xv, 528 Seiten, Illustrationen, 25.4 cm x 17.8 cm
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT019321098
    ISBN 978-1-4939-7031-5 ; 1-4939-7031-3 ; 9781493970339 ; 149397033X
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -1615- verfügbar in Königswinter Königswinter

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  4. Book ; Online ; E-Book: Protein secretion in bacteria

    Sandkvist, Maria / Cascales, Eric / Christie, Peter J.

    2019  

    Author's details Maria Sandkvist, Eric Cascales and Peter J. Christie
    Keywords Electronic books
    Language English
    Size 1 Online-Ressource (580 Seiten), Illustrationen
    Publisher ASM Press
    Publishing place Washington, DC
    Publishing country United States
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT020383169
    ISBN 978-1-68367-286-9 ; 9781683670278 ; 1-68367-286-0 ; 1683670272
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  5. Article ; Online: Measure of Peptidoglycan Degradation Activity.

    Santin, Yoann G / Cascales, Eric

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

    2023  Volume 2715, Page(s) 197–205

    Abstract: Most bacterial secretion systems are large machines that cross the cell envelope to deliver effectors outside the cell or directly into target cells. The peptidoglycan layer can therefore represent a physical barrier for the assembly of these large ... ...

    Abstract Most bacterial secretion systems are large machines that cross the cell envelope to deliver effectors outside the cell or directly into target cells. The peptidoglycan layer can therefore represent a physical barrier for the assembly of these large machines. Secretion systems and their counterparts such as type IV pili, flagella, and conjugation machines have therefore evolved or hijacked enzymes with peptidoglycan degradation activity. These enzymes are usually glycoside hydrolases that cleave the glycan chains of the peptidoglycan. Their activities are spatially controlled to avoid cell lysis and to create local rearrangement of the cell wall. In addition, peptidoglycan hydrolases may not be only required for the proper assembly of the secretion systems but may directly participate to the release of the effectors. Finally, several antibacterial effectors possess peptidoglycan degradation activity that damage the cell wall once delivered in the target cell. Here, we describe protocols to test the peptidoglycan degradation activity of these proteins in vitro and in solution.
    MeSH term(s) Peptidoglycan ; Anti-Bacterial Agents ; Bacterial Secretion Systems ; Cell Death ; Cell Membrane
    Chemical Substances Peptidoglycan ; Anti-Bacterial Agents ; Bacterial Secretion Systems
    Language English
    Publishing date 2023-11-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3445-5_12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Editorial: Bacterial Secretion Systems, Volume II.

    Arechaga, Ignacio / Cascales, Eric

    Frontiers in microbiology

    2022  Volume 13, Page(s) 917591

    Language English
    Publishing date 2022-05-24
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2022.917591
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Bacterial One- and Two-Hybrid Assays to Monitor Transmembrane Helix Interactions.

    Zoued, Abdelrahim / Duneau, Jean-Pierre / Cascales, Eric

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

    2023  Volume 2715, Page(s) 259–271

    Abstract: In transenvelope multiprotein machines such as bacterial secretion systems, protein-protein interactions not only occur between soluble domains but might also be mediated by helix-helix contacts in the inner membrane. Several assays have been therefore ... ...

    Abstract In transenvelope multiprotein machines such as bacterial secretion systems, protein-protein interactions not only occur between soluble domains but might also be mediated by helix-helix contacts in the inner membrane. Several assays have been therefore developed to test homotypic and heterotypic interactions between transmembrane α-helices in their native membrane environment. Here, we provide detailed protocols for two genetic assays, TOXCAT and GALLEX, which are based on the reconstitution of dimeric regulators allowing the control of expression of reporter genes.
    MeSH term(s) Two-Hybrid System Techniques ; Bacterial Secretion Systems ; Biological Assay ; Genes, Reporter ; Polymers
    Chemical Substances Bacterial Secretion Systems ; Polymers
    Language English
    Publishing date 2023-11-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3445-5_17
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: No fitness cost entailed by type VI secretion system synthesis, assembly, contraction, or disassembly in enteroaggregative

    Taillefer, Boris / Giraud, Julien F / Cascales, Eric

    Journal of bacteriology

    2023  Volume 205, Issue 12, Page(s) e0035723

    Abstract: Importance: Bacteria use weapons to deliver effectors into target cells. One of these weapons, the type VI secretion system (T6SS), assembles a contractile tail acting as a spring to propel a toxin-loaded needle. Due to its size and mechanism of action, ...

    Abstract Importance: Bacteria use weapons to deliver effectors into target cells. One of these weapons, the type VI secretion system (T6SS), assembles a contractile tail acting as a spring to propel a toxin-loaded needle. Due to its size and mechanism of action, the T6SS was intuitively thought to be energetically costly. Here, using a combination of mutants and growth measurements in liquid medium, on plates, and in competition experiments, we show that the T6SS does not entail a growth cost to enteroaggregative
    MeSH term(s) Escherichia coli/genetics ; Type VI Secretion Systems/genetics ; Escherichia coli Proteins/genetics ; Bacterial Proteins
    Chemical Substances Type VI Secretion Systems ; Escherichia coli Proteins ; Bacterial Proteins
    Language English
    Publishing date 2023-11-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/jb.00357-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.50: 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: Editorial

    Ignacio Arechaga / Eric Cascales

    Frontiers in Microbiology, Vol

    Bacterial Secretion Systems, Volume II

    2022  Volume 13

    Keywords secretion systems ; bacteria ; structural biology ; microbiology ; biochemistry ; QR1-502
    Language English
    Publishing date 2022-05-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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  10. Article ; Online: Probing Protein Topology and Conformation by Limited Proteolysis.

    Chabalier, Maïalène / Doan, Thierry / Cascales, Eric

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

    2023  Volume 2715, Page(s) 111–119

    Abstract: Proteases are enzymes that catalyze the hydrolytic degradation of other proteins into peptides or amino acids through the digestion of the peptide bond. Promiscuous proteases that target a wide range of proteins are distinguished from specific proteases ... ...

    Abstract Proteases are enzymes that catalyze the hydrolytic degradation of other proteins into peptides or amino acids through the digestion of the peptide bond. Promiscuous proteases that target a wide range of proteins are distinguished from specific proteases that have a narrow range of substrates. In terms of activity, endoproteases cleave their substrates at specific residues within the target proteins, whereas exoproteases cleave from one extremity and may have processive activities. Proteases are therefore very useful tools to study proteins, notably their structure or conformation. In addition, proteases can be used to probe the topology of bacterial membrane proteins. Here, we describe limited protease accessibility assays to define inner membrane protein topology and conformational changes based on digestion profiles.
    MeSH term(s) Proteolysis ; Peptide Hydrolases ; Endopeptidases ; Membrane Proteins ; Bacterial Proteins
    Chemical Substances Peptide Hydrolases (EC 3.4.-) ; Endopeptidases (EC 3.4.-) ; Membrane Proteins ; Bacterial Proteins
    Language English
    Publishing date 2023-11-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3445-5_8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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