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  1. Article ; Online: Association of insulin resistance with the accumulation of saturated intramyocellular lipid: A comparison with other fat stores.

    Azhar, Mueed / Watson, Laura P E / De Lucia Rolfe, Emanuella / Ferraro, Michele / Carr, Katherine / Worsley, Jieniean / Boesch, Chris / Hodson, Leanne / Chatterjee, Krishna K / Kemp, Graham J / Savage, David B / Sleigh, Alison

    NMR in biomedicine

    2024  , Page(s) e5117

    Abstract: It has been shown using proton magnetic resonance spectroscopy ( ...

    Abstract It has been shown using proton magnetic resonance spectroscopy (
    Language English
    Publishing date 2024-02-14
    Publishing country England
    Document type Journal Article
    ZDB-ID 1000976-0
    ISSN 1099-1492 ; 0952-3480
    ISSN (online) 1099-1492
    ISSN 0952-3480
    DOI 10.1002/nbm.5117
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: HDX-MS and deletion analysis of the type 4 secretion system protein TraF from the Escherichia coli F plasmid.

    Lento, Cristina / Ferraro, Michele / Wilson, Derek / Audette, Gerald F

    FEBS letters

    2016  Volume 590, Issue 3, Page(s) 376–386

    Abstract: Conjugative DNA transfer by the F-plasmid is achieved through a type IV secretion system (T4SS) encoded within the plasmid's transfer region; TraF is one of several F-T4SS proteins essential for F-pilus assembly. In order to identify regions of the ... ...

    Abstract Conjugative DNA transfer by the F-plasmid is achieved through a type IV secretion system (T4SS) encoded within the plasmid's transfer region; TraF is one of several F-T4SS proteins essential for F-pilus assembly. In order to identify regions of the protein important for TraF function, a series of deletion mutants were assessed for their ability to recover conjugative transfer in a traF knockout. Interestingly, modification of any region of TraF abolishes pilus synthesis, resulting in a loss of rescue of conjugative function. Dynamic analysis of TraF by time-resolved hydrogen-deuterium exchange revealed that the C-terminal region containing the predicted thioredoxin-like domain is quite structured, while the N-terminal region, predicted to interact with TraH in the intact F-T4SS, was more dynamic.
    MeSH term(s) Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Conjugation, Genetic ; Deuterium Exchange Measurement ; Escherichia coli/physiology ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Fimbriae, Bacterial/physiology ; Gene Deletion ; Gene Knockout Techniques ; Homologous Recombination ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Plasmids/chemistry ; Plasmids/metabolism ; Protein Conformation ; Protein Interaction Domains and Motifs ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Spectrometry, Mass, Electrospray Ionization ; Type IV Secretion Systems/chemistry ; Type IV Secretion Systems/genetics ; Type IV Secretion Systems/metabolism
    Chemical Substances Bacterial Proteins ; Escherichia coli Proteins ; Nuclear Proteins ; Peptide Fragments ; Recombinant Fusion Proteins ; TraF protein, E coli ; TraH protein, Bacteria ; Type IV Secretion Systems
    Language English
    Publishing date 2016-02
    Publishing country England
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.12066
    Database MEDical Literature Analysis and Retrieval System OnLINE

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