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  1. Article ; Online: Selection of Transporter-Targeted Inhibitory Nanobodies by Solid-Supported-Membrane (SSM)-Based Electrophysiology.

    Bärland, Natalie / Perez, Camilo

    Journal of visualized experiments : JoVE

    2021  , Issue 171

    Abstract: Single domain antibodies (nanobodies) have been extensively used in mechanistic and structural studies of proteins and they pose an enormous potential as tools for developing clinical therapies, many of which depend on the inhibition of membrane proteins ...

    Abstract Single domain antibodies (nanobodies) have been extensively used in mechanistic and structural studies of proteins and they pose an enormous potential as tools for developing clinical therapies, many of which depend on the inhibition of membrane proteins such as transporters. However, most of the methods used to determine the inhibition of transport activity are difficult to perform in high-throughput routines and depend on labeled substrates availability thereby complicating the screening of large nanobody libraries. Solid-supported membrane (SSM) electrophysiology is a high-throughput method, used for characterizing electrogenic transporters and measuring their transport kinetics and inhibition. Here we show the implementation of SSM-based electrophysiology to select inhibitory and non-inhibitory nanobodies targeting an electrogenic secondary transporter and to calculate nanobodies inhibitory constants. This technique may be especially useful for selecting inhibitory nanobodies targeting transporters for which labeled substrates are not available.
    MeSH term(s) Cardiac Electrophysiology ; Humans ; Kinetics ; Membrane Proteins/metabolism ; Membrane Transport Proteins/metabolism ; Single-Domain Antibodies
    Chemical Substances Membrane Proteins ; Membrane Transport Proteins ; Single-Domain Antibodies
    Language English
    Publishing date 2021-05-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 2259946-0
    ISSN 1940-087X ; 1940-087X
    ISSN (online) 1940-087X
    ISSN 1940-087X
    DOI 10.3791/62578
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Selection of transporter-targeted inhibitory nanobodies by solid-supported-membrane (ssm)-based electrophysiology

    Bärland, Natalie / Perez, Camilo

    Journal of visualized experiments. 2021 May 03, , no. 171

    2021  

    Abstract: Single domain antibodies (nanobodies) have been extensively used in mechanistic and structural studies of proteins and they pose an enormous potential as tools for developing clinical therapies, many of which depend on the inhibition of membrane proteins ...

    Abstract Single domain antibodies (nanobodies) have been extensively used in mechanistic and structural studies of proteins and they pose an enormous potential as tools for developing clinical therapies, many of which depend on the inhibition of membrane proteins such as transporters. However, most of the methods used to determine the inhibition of transport activity are difficult to perform in high-throughput routines and depend on labeled substrates availability thereby complicating the screening of large nanobody libraries. Solid-supported membrane (SSM) electrophysiology is a high-throughput method, used for characterizing electrogenic transporters and measuring their transport kinetics and inhibition. Here we show the implementation of SSM-based electrophysiology to select inhibitory and non-inhibitory nanobodies targeting an electrogenic secondary transporter and to calculate nanobodies inhibitory constants. This technique may be especially useful for selecting inhibitory nanobodies targeting transporters for which labeled substrates are not available.
    Keywords antibodies ; electrophysiology ; journals ; physiological transport ; screening ; structural proteins ; therapeutics ; transporters
    Language English
    Dates of publication 2021-0503
    Size p. e62578.
    Publishing place Journal of Visualized Experiments
    Document type Article
    ZDB-ID 2259946-0
    ISSN 1940-087X
    ISSN 1940-087X
    DOI 10.3791/62578
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Fast Small-Scale Membrane Protein Purification and Grid Preparation for Single-Particle Electron Microscopy.

    Bärland, Natalie / Perez, Camilo

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

    2020  Volume 2127, Page(s) 275–282

    Abstract: The ongoing development of single-particle cryo-electron microscopy (cryo-EM) is leading to fast data acquisition, data processing, and protein structure elucidation. Quick and reliable methods to go from protein purification and optimization to grid ... ...

    Abstract The ongoing development of single-particle cryo-electron microscopy (cryo-EM) is leading to fast data acquisition, data processing, and protein structure elucidation. Quick and reliable methods to go from protein purification and optimization to grid preparation will significantly improve the reach and power of cryo-EM. Such methods would particularly constitute a tremendous advantage in structural biology of membrane proteins, whose published structures stay still far behind the number of soluble protein structures. Here we describe a fast, low-cost, and user-friendly method for the purification and cryo-EM analysis of a recombinant membrane protein. This method minimizes the amount of starting material and manipulation steps needed to go from purification to grid preparation, and could potentially be expanded to other membrane protein purification systems for its direct application in structure determination by single-particle cryo-EM.
    MeSH term(s) Animals ; Chromatography, Affinity/methods ; Cryoelectron Microscopy/methods ; Freezing ; Humans ; Membrane Proteins/chemistry ; Membrane Proteins/isolation & purification ; Membrane Proteins/metabolism ; Negative Staining/methods ; Protein Conformation ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Single Molecule Imaging/methods ; Specimen Handling/instrumentation ; Specimen Handling/methods ; Time Factors
    Chemical Substances Membrane Proteins ; Recombinant Proteins
    Language English
    Publishing date 2020-02-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-0373-4_18
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mechanistic basis of choline import involved in teichoic acids and lipopolysaccharide modification.

    Bärland, Natalie / Rueff, Anne-Stéphanie / Cebrero, Gonzalo / Hutter, Cedric A J / Seeger, Markus A / Veening, Jan-Willem / Perez, Camilo

    Science advances

    2022  Volume 8, Issue 9, Page(s) eabm1122

    Abstract: Phosphocholine molecules decorating bacterial cell wall teichoic acids and outer-membrane lipopolysaccharide have fundamental roles in adhesion to host cells, immune evasion, and persistence. Bacteria carrying the operon that performs phosphocholine ... ...

    Abstract Phosphocholine molecules decorating bacterial cell wall teichoic acids and outer-membrane lipopolysaccharide have fundamental roles in adhesion to host cells, immune evasion, and persistence. Bacteria carrying the operon that performs phosphocholine decoration synthesize phosphocholine after uptake of the choline precursor by LicB, a conserved transporter among divergent species.
    MeSH term(s) Choline/metabolism ; Cryoelectron Microscopy ; Lipopolysaccharides/metabolism ; Membrane Transport Proteins/metabolism ; Phosphorylcholine/metabolism ; Streptococcus pneumoniae/metabolism ; Teichoic Acids/metabolism
    Chemical Substances Lipopolysaccharides ; Membrane Transport Proteins ; Teichoic Acids ; Phosphorylcholine (107-73-3) ; Choline (N91BDP6H0X)
    Language English
    Publishing date 2022-03-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abm1122
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. 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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  6. Article ; Online: Regioselective para-Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase.

    Payer, Stefan E / Marshall, Stephen A / Bärland, Natalie / Sheng, Xiang / Reiter, Tamara / Dordic, Andela / Steinkellner, Georg / Wuensch, Christiane / Kaltwasser, Susann / Fisher, Karl / Rigby, Stephen E J / Macheroux, Peter / Vonck, Janet / Gruber, Karl / Faber, Kurt / Himo, Fahmi / Leys, David / Pavkov-Keller, Tea / Glueck, Silvia M

    Angewandte Chemie (International ed. in English)

    2017  Volume 56, Issue 44, Page(s) 13893–13897

    Abstract: The utilization of ... ...

    Abstract The utilization of CO
    Language English
    Publishing date 2017-10-02
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201708091
    Database MEDical Literature Analysis and Retrieval System OnLINE

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