• Login
    View Item 
    •   Home
    • Research
    • Articles
    • View Item
    •   Home
    • Research
    • Articles
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of KAUSTCommunitiesIssue DateSubmit DateThis CollectionIssue DateSubmit Date

    My Account

    Login

    Quick Links

    Open Access PolicyORCID LibguidePlumX LibguideSubmit an Item

    Statistics

    Display statistics

    Interaction of amylin species with transition metals and membranes

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    1-s2.0-S0162013418304409-main.pdf
    Size:
    1.016Mb
    Format:
    PDF
    Description:
    Accepted Manuscript
    Download
    Thumbnail
    Name:
    1-s2.0-S0162013418304409-ga1.jpg
    Size:
    15.37Kb
    Format:
    JPEG image
    Description:
    Graphical abstract
    Image viewer
    Download
    Type
    Article
    Authors
    Alghrably, Mawadda
    Czaban, Iwona
    Jaremko, Lukasz cc
    Jaremko, Mariusz cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Date
    2018-11-10
    Online Publication Date
    2018-11-10
    Print Publication Date
    2019-02
    Permanent link to this record
    http://hdl.handle.net/10754/629864
    
    Metadata
    Show full item record
    Abstract
    Islet Amyloid Polypeptide (IAPP), also known as amylin, is a 37-amino-acid peptide hormone that is secreted by pancreatic islet β-cells. Amylin is complementary to insulin in regulating and maintaining blood glucose levels in the human body. The misfolding and aggregation of amylin is primarily associated with type 2 diabetes mellitus, which is classified as an amyloid disease. Recently, the interactions between amylin and specific metal ions, e.g., copper(II), zinc(II), and iron(II), were found to impact its performance and aggregation processes. Therefore, the focus in this review will be on how the chemistry and structural properties of amylin are affected by these interactions. In addition, the impact of amylin and other amyloidogenic peptides interacting with metal ions on the cell membranes is discussed. In particular, recent studies on the interactions of amylin with copper, zinc, iron, nickel, gold, ruthenium, and vanadium are discussed.
    Citation
    Alghrably M, Jaremko Ł, Czaban I, Jaremko M (2018) Interaction of amylin species with transition metals and membranes. Journal of Inorganic Biochemistry. Available: http://dx.doi.org/10.1016/j.jinorgbio.2018.11.004.
    Sponsors
    Authors would like to thank King Abdullah University of Science and Technology (KAUST) for financial support.
    Publisher
    Elsevier BV
    Journal
    Journal of Inorganic Biochemistry
    DOI
    10.1016/j.jinorgbio.2018.11.004
    Additional Links
    https://www.sciencedirect.com/science/article/pii/S0162013418304409
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.jinorgbio.2018.11.004
    Scopus Count
    Collections
    Articles; Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program

    entitlement

     
    DSpace software copyright © 2002-2021  DuraSpace
    Quick Guide | Contact Us | KAUST University Library
    Open Repository is a service hosted by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items. For anonymous users the allowed maximum amount is 50 search results.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.