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  1. Article ; Online: Functional diversity of the superfamily of K⁺ transporters to meet various requirements.

    Diskowski, Marina / Mikusevic, Vedrana / Stock, Charlott / Hänelt, Inga

    Biological chemistry

    2015  Volume 396, Issue 9-10, Page(s) 1003–1014

    Abstract: The superfamily of K+ transporters unites proteins from plants, fungi, bacteria, and archaea that translocate K+ and/or Na+ across membranes. These proteins are key components in osmotic regulation, pH homeostasis, and resistance to high salinity and ... ...

    Abstract The superfamily of K+ transporters unites proteins from plants, fungi, bacteria, and archaea that translocate K+ and/or Na+ across membranes. These proteins are key components in osmotic regulation, pH homeostasis, and resistance to high salinity and dryness. The members of the superfamily are closely related to K+ channels such as KcsA but also show several striking differences that are attributed to their altered functions. This review highlights these functional differences, focusing on the bacterial superfamily members KtrB, TrkH, and KdpA. The functional variations within the family and comparison to MPM-type K+ channels are discussed in light of the recently solved structures of the Ktr and Trk systems.
    MeSH term(s) Animals ; Humans ; Models, Molecular ; Potassium Channels/chemistry ; Potassium Channels/metabolism
    Chemical Substances Potassium Channels
    Language English
    Publishing date 2015-09
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1334659-3
    ISSN 1437-4315 ; 1431-6730 ; 1432-0355
    ISSN (online) 1437-4315
    ISSN 1431-6730 ; 1432-0355
    DOI 10.1515/hsz-2015-0123
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs

    Hellwig, Nils / Peetz, Oliver / Ahdash, Zainab / Tascón, Igor / Booth, Paula J. / Mikusevic, Vedrana / Diskowski, Marina / Politis, Argyris / Hellmich, Yvonne / Hänelt, Inga / Reading, Eamonn / Morgner, Nina

    Chemical communications. 2018 Dec. 4, v. 54, no. 97 p.13702-13705

    2018  

    Abstract: Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, ...

    Abstract Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, allowing determination of oligomeric states of membrane proteins of different functionality directly from the native nanodiscs.
    Keywords chemical reactions ; lipid bilayers ; maleic acid ; mass spectrometry ; membrane proteins ; styrene
    Language English
    Dates of publication 2018-1204
    Size p. 13702-13705.
    Publishing place The Royal Society of Chemistry
    Document type Article ; Online
    Note Resource is Open Access
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c8cc06284f
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs.

    Hellwig, Nils / Peetz, Oliver / Ahdash, Zainab / Tascón, Igor / Booth, Paula J / Mikusevic, Vedrana / Diskowski, Marina / Politis, Argyris / Hellmich, Yvonne / Hänelt, Inga / Reading, Eamonn / Morgner, Nina

    Chemical communications (Cambridge, England)

    2018  Volume 54, Issue 97, Page(s) 13702–13705

    Abstract: Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, ...

    Abstract Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, allowing determination of oligomeric states of membrane proteins of different functionality directly from the native nanodiscs.
    MeSH term(s) Lipid Bilayers/chemistry ; Lipids/chemistry ; Maleates/chemistry ; Mass Spectrometry ; Membrane Proteins/analysis ; Models, Molecular ; Particle Size ; Styrene/chemistry
    Chemical Substances Lipid Bilayers ; Lipids ; Maleates ; Membrane Proteins ; Styrene (44LJ2U959V) ; maleic acid (91XW058U2C)
    Language English
    Publishing date 2018-11-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c8cc06284f
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Helical jackknives control the gates of the double-pore K

    Diskowski, Marina / Mehdipour, Ahmad Reza / Wunnicke, Dorith / Mills, Deryck J / Mikusevic, Vedrana / Bärland, Natalie / Hoffmann, Jan / Morgner, Nina / Steinhoff, Heinz-Jürgen / Hummer, Gerhard / Vonck, Janet / Hänelt, Inga

    eLife

    2017  Volume 6

    Abstract: Ion channel gating is essential for cellular homeostasis and is tightly controlled. In some eukaryotic and most bacterial ligand-gated ... ...

    Abstract Ion channel gating is essential for cellular homeostasis and is tightly controlled. In some eukaryotic and most bacterial ligand-gated K
    Language English
    Publishing date 2017-05-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.24303
    Database MEDical Literature Analysis and Retrieval System OnLINE

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