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  1. Article ; Online: Reinhardt Rüdel  : Muscle physiologist, mentor, role model.

    Fahlke, Christoph

    Pflugers Archiv : European journal of physiology

    2023  Volume 476, Issue 1, Page(s) 1–2

    MeSH term(s) Humans ; Mentors ; Muscles
    Language English
    Publishing date 2023-11-28
    Publishing country Germany
    Document type Editorial
    ZDB-ID 6380-0
    ISSN 1432-2013 ; 0031-6768
    ISSN (online) 1432-2013
    ISSN 0031-6768
    DOI 10.1007/s00424-023-02886-w
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  2. Book: Taschenatlas Physiologie

    Fahlke, Christoph / Linke, Wolfgang / Rassler, Beate / Wiesner, Rudolf J.

    mit Grundlagen der Pathophysiologie

    2022  

    Author's details Ch. Fahlke, W. A. Linke, B. Raßler, R. J. Wiesner
    Keywords Physiologie
    Subject Humanphysiologie ; Mensch ; Körperfunktion
    Language German
    Size XXIV, 472 Seiten, Illustrationen, 21 cm x 13.5 cm
    Edition 3. Auflage
    Publisher Elsevier
    Publishing place München
    Publishing country Germany
    Document type Book
    Old title Vorangegangen ist
    HBZ-ID HT021320709
    ISBN 978-3-437-41927-0 ; 3-437-41927-7 ; 9783437096105 ; 3437096109
    Database Catalogue ZB MED Medicine, Health

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  3. Article: Membrane physiology and biophysics-Another milestone.

    Fahlke, Christoph

    Frontiers in physiology

    2022  Volume 13, Page(s) 1081004

    Language English
    Publishing date 2022-11-25
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2022.1081004
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  4. Article ; Online: Regulation of glial glutamate transporters by C-terminal domains.

    Leinenweber, Ariane / Machtens, Jan-Philipp / Begemann, Birgit / Fahlke, Christoph

    The Journal of biological chemistry

    2010  Volume 286, Issue 3, Page(s) 1927–1937

    Abstract: ... expressed in astroglia. Human EAAT2 encompasses eight transmembrane domains and a 74-amino acid C-terminal ... domain that resides in the cytoplasm. We examined the role of this region by studying various C-terminal ... and confocal imaging. Removal of the complete C terminus (K498X EAAT2) results in loss of function ...

    Abstract Excitatory amino acid transporter 2 (EAAT2) is a high affinity glutamate transporter predominantly expressed in astroglia. Human EAAT2 encompasses eight transmembrane domains and a 74-amino acid C-terminal domain that resides in the cytoplasm. We examined the role of this region by studying various C-terminal truncations and mutations using heterologous expression in mammalian cells, whole-cell patch clamp recording and confocal imaging. Removal of the complete C terminus (K498X EAAT2) results in loss of function because of intracellular retention of truncated proteins in the cytoplasm. However, a short stretch of amino acids (E500X EAAT2) within the C terminus results in correctly processed transporters. E500X reduced glutamate transport currents by 90%. Moreover, the voltage and substrate dependence of E500X EAAT2 anion currents was significantly altered. WT and mutant EAAT2 anion channels are modified by external Na(+) in the presence as well as in the absence of L-glutamate. Whereas Na(+) stimulates EAAT2 anion currents in the presence of L-glutamate, increased [Na(+)] reduces such currents without glutamate. In cells internally dialyzed with Na(+), WT, and truncated EAAT2 display comparable Na(+) dependence. With K(+) as main internal cation, E500X drastically increased the apparent dissociation constant for external Na(+). The effects of E500X can be represented by a kinetic model that allows translocation of the empty transporter from the outward- to the inward-facing conformation and stabilization of the inward-facing conformation by internal K(+). Our results demonstrate that the C terminus modifies the glutamate uptake cycle, possibly affecting the movements of the translocation domain of EAAT2 glutamate transporter.
    MeSH term(s) Amino Acid Sequence ; Cell Line ; Excitatory Amino Acid Transporter 2 ; Glutamate Plasma Membrane Transport Proteins/genetics ; Glutamate Plasma Membrane Transport Proteins/metabolism ; Glutamic Acid/metabolism ; Humans ; Models, Biological ; Neuroglia ; Potassium/metabolism ; Protein Structure, Tertiary/physiology ; Sequence Deletion ; Sodium/metabolism
    Chemical Substances Excitatory Amino Acid Transporter 2 ; Glutamate Plasma Membrane Transport Proteins ; SLC1A2 protein, human ; Glutamic Acid (3KX376GY7L) ; Sodium (9NEZ333N27) ; Potassium (RWP5GA015D)
    Language English
    Publishing date 2010-11-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M110.153486
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  5. Article: Membrane Physiology and Biophysics-What Remains to Be Done?

    Fahlke, Christoph

    Frontiers in physiology

    2020  Volume 11, Page(s) 892

    Language English
    Publishing date 2020-07-28
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2020.00892
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  6. Book ; Online ; E-Book: Taschenatlas Physiologie

    Fahlke, Christoph / Linke, Wolfgang A. / Raßler, Beate / Wiesner, Rudolf J.

    mit 44 Tabellen

    2015  

    Keywords Physiologie ; Taschenatlas ; Vorklinik ; Physikum ; Prüfungsvorbereitung
    Subject Humanphysiologie ; Mensch ; Körperfunktion
    Subject code 612.00222
    Language German
    Size 1 Online-Ressource (XXIV, 469 Seiten), Illustrationen
    Edition 2. Auflage
    Publisher Urban & Fischer
    Publishing place München
    Publishing country Germany
    Document type Book ; Online ; E-Book
    Note Lizenzpflichtig
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    HBZ-ID HT018973847
    ISBN 978-3-437-29925-4 ; 9783437419188 ; 3-437-29925-5 ; 3437419188
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  7. Article ; Online: Laudatio. Prof. Dr. med. Dr. h. c. Hans Lippert - Ordinarius für Chirurgie an der Otto-von-Guericke-Universität Magdeburg 1993-2013.

    Ridwelski, Karsten / Manger, Thomas / Pross, Matthias / Fahlke, Jörg

    Zentralblatt fur Chirurgie

    2013  Volume 138, Issue 4, Page(s) 400–402

    Title translation Laudatio. Prof. Dr. med. Dr. h. c. Hans Lippert - professor for surgery at the Magdeburg Otto von Guericke University 1993-2013.
    MeSH term(s) Czechoslovakia ; Faculty, Medical/history ; General Surgery/history ; Germany ; History, 20th Century ; History, 21st Century ; Quality Assurance, Health Care/history ; Societies, Medical/history
    Language German
    Publishing date 2013-08
    Publishing country Germany
    Document type Biography ; Editorial ; Historical Article
    ZDB-ID 200935-3
    ISSN 1438-9592 ; 0044-409X
    ISSN (online) 1438-9592
    ISSN 0044-409X
    DOI 10.1055/s-0033-1350749
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  8. Article: Regulation of Glial Glutamate Transporters by C-terminal Domains

    Leinenweber, Ariane / Machtens, Jan-Philipp / Begemann, Birgit / Fahlke, Christoph

    Journal of biological chemistry. 2011 Jan. 21, v. 286, no. 3

    2011  

    Abstract: ... expressed in astroglia. Human EAAT2 encompasses eight transmembrane domains and a 74-amino acid C-terminal ... domain that resides in the cytoplasm. We examined the role of this region by studying various C-terminal ... and confocal imaging. Removal of the complete C terminus (K498X EAAT2) results in loss of function ...

    Abstract Excitatory amino acid transporter 2 (EAAT2) is a high affinity glutamate transporter predominantly expressed in astroglia. Human EAAT2 encompasses eight transmembrane domains and a 74-amino acid C-terminal domain that resides in the cytoplasm. We examined the role of this region by studying various C-terminal truncations and mutations using heterologous expression in mammalian cells, whole-cell patch clamp recording and confocal imaging. Removal of the complete C terminus (K498X EAAT2) results in loss of function because of intracellular retention of truncated proteins in the cytoplasm. However, a short stretch of amino acids (E500X EAAT2) within the C terminus results in correctly processed transporters. E500X reduced glutamate transport currents by 90%. Moreover, the voltage and substrate dependence of E500X EAAT2 anion currents was significantly altered. WT and mutant EAAT2 anion channels are modified by external Na⁺ in the presence as well as in the absence of L-glutamate. Whereas Na⁺ stimulates EAAT2 anion currents in the presence of L-glutamate, increased [Na⁺] reduces such currents without glutamate. In cells internally dialyzed with Na⁺, WT, and truncated EAAT2 display comparable Na⁺ dependence. With K⁺ as main internal cation, E500X drastically increased the apparent dissociation constant for external Na⁺. The effects of E500X can be represented by a kinetic model that allows translocation of the empty transporter from the outward- to the inward-facing conformation and stabilization of the inward-facing conformation by internal K⁺. Our results demonstrate that the C terminus modifies the glutamate uptake cycle, possibly affecting the movements of the translocation domain of EAAT2 glutamate transporter.
    Language English
    Dates of publication 2011-0121
    Size p. 1927-1937.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database NAL-Catalogue (AGRICOLA)

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  9. Article: Cellular Physiology and Pathophysiology of EAAT Anion Channels.

    Kovermann, Peter / Engels, Miriam / Müller, Frank / Fahlke, Christoph

    Frontiers in cellular neuroscience

    2022  Volume 15, Page(s) 815279

    Abstract: Excitatory amino acid transporters (EAATs) optimize the temporal resolution and energy demand of mammalian excitatory synapses by quickly removing glutamate from the synaptic cleft into surrounding neuronal and glial cells and ensuring low resting ... ...

    Abstract Excitatory amino acid transporters (EAATs) optimize the temporal resolution and energy demand of mammalian excitatory synapses by quickly removing glutamate from the synaptic cleft into surrounding neuronal and glial cells and ensuring low resting glutamate concentrations. In addition to secondary active glutamate transport, EAATs also function as anion channels. The channel function of these transporters is conserved in all homologs ranging from archaebacteria to mammals; however, its physiological roles are insufficiently understood. There are five human EAATs, which differ in their glutamate transport rates. Until recently the high-capacity transporters EAAT1, EAAT2, and EAAT3 were believed to conduct only negligible anion currents, with no obvious function in cell physiology. In contrast, the low-capacity glutamate transporters EAAT4 and EAAT5 are thought to regulate neuronal signaling as glutamate-gated channels. In recent years, new experimental approaches and novel animal models, together with the discovery of a human genetic disease caused by gain-of-function mutations in EAAT anion channels have enabled identification of the first physiological and pathophysiological roles of EAAT anion channels.
    Language English
    Publishing date 2022-01-06
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2452963-1
    ISSN 1662-5102
    ISSN 1662-5102
    DOI 10.3389/fncel.2021.815279
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  10. Book ; Thesis: Alcohol consumption in the rat

    Fahlke, Claudia

    modulaton by adrenal steroids and mesotelencephalic dopamine

    1994  

    Author's details av Claudia Fahlke
    Language English
    Size Getr. Zählung : graph. Darst.
    Publishing country Sweden
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Göteborg, Univ., Diss., 1994
    HBZ-ID HT006312378
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    94 E 1146 order for loan Magazin

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