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  1. Book ; Thesis: Klinische und radiologische Ergebnisse der konservativen und operativen Behandlung nach Frakturen des Azetabulum

    Lechner, Stefan

    2002  

    Author's details vorgelegt von Stefan Lechner
    Language German
    Size III, 117 S., Ill., graph. Darst., 21 cm
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Regensburg, Univ., Diss., 2002
    HBZ-ID HT013481441
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2002 D 3415 order for loan Magazin

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  2. Article ; Online: Keeping Cool During Lift-out - An Elegant Solution for Preparing Samples in Cryo-FIB.

    Smith, Andrew / Lechner, Lorenz G / Strähle, Stefan / Kleindiek, Stephan

    Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada

    2023  Volume 29, Issue Supplement_1, Page(s) 521–522

    Language English
    Publishing date 2023-08-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 1385710-1
    ISSN 1435-8115 ; 1431-9276
    ISSN (online) 1435-8115
    ISSN 1431-9276
    DOI 10.1093/micmic/ozad067.245
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Shedding light on the contribution of different c-fibre nociceptors to nocifensive behavior.

    Lechner, Stefan G

    Pain

    2017  Volume 158, Issue 12, Page(s) 2281–2282

    Language English
    Publishing date 2017-08-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 193153-2
    ISSN 1872-6623 ; 0304-3959
    ISSN (online) 1872-6623
    ISSN 0304-3959
    DOI 10.1097/j.pain.0000000000001030
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Neue Einsichten in die spinalen und peripheren Signalwege der Schmerzentstehung

    Lechner, Stefan G.

    Neuroforum

    2017  Volume 23, Issue 3, Spec.Iss., Page(s) 173

    Language German
    Document type Article
    ZDB-ID 1238592-x
    ISSN 0947-0875
    Database Current Contents Medicine

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  5. Article ; Online: PKA mediates modality-specific modulation of the mechanically gated ion channel PIEZO2.

    Schaefer, Irina / Verkest, Clement / Vespermann, Lucas / Mair, Thomas / Voß, Hannah / Zeitzschel, Nadja / Lechner, Stefan G

    The Journal of biological chemistry

    2023  Volume 299, Issue 6, Page(s) 104782

    Abstract: PKA is a downstream effector of many inflammatory mediators that induce pain hypersensitivity by increasing the mechanosensitivity of nociceptive sensory afferent. Here, we examine the molecular mechanism underlying PKA-dependent modulation of the ... ...

    Abstract PKA is a downstream effector of many inflammatory mediators that induce pain hypersensitivity by increasing the mechanosensitivity of nociceptive sensory afferent. Here, we examine the molecular mechanism underlying PKA-dependent modulation of the mechanically activated ion channel PIEZO2, which confers mechanosensitivity to many nociceptors. Using phosphorylation site prediction algorithms, we identified multiple putative and highly conserved PKA phosphorylation sites located on intracellular intrinsically disordered regions of PIEZO2. Site-directed mutagenesis and patch-clamp recordings showed that substitution of one or multiple putative PKA sites within a single intracellular domain does not alter PKA-induced PIEZO2 sensitization, whereas mutation of a combination of nine putative sites located on four different intracellular regions completely abolishes PKA-dependent PIEZO2 modulation, though it remains unclear whether all or just some of these nine sites are required. By demonstrating that PIEZO1 is not modulated by PKA, our data also reveal a previously unrecognized functional difference between PIEZO1 and PIEZO2. Moreover, by demonstrating that PKA only modulates PIEZO2 currents evoked by focal mechanical indentation of the cell, but not currents evoked by pressure-induced membrane stretch, we provide evidence suggesting that PIEZO2 is a polymodal mechanosensor that engages different protein domains for detecting different types of mechanical stimuli.
    MeSH term(s) Humans ; Ion Channels/genetics ; Ion Channels/metabolism ; Mechanotransduction, Cellular/genetics ; Pain/physiopathology ; Protein Domains ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Protein Transport/genetics
    Chemical Substances Ion Channels ; PIEZO1 protein, human ; PIEZO2 protein, human ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
    Language English
    Publishing date 2023-05-04
    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 10.1016/j.jbc.2023.104782
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  6. Article ; Online: Intrinsically disordered intracellular domains control key features of the mechanically-gated ion channel PIEZO2.

    Verkest, Clement / Schaefer, Irina / Nees, Timo A / Wang, Na / Jegelka, Juri M / Taberner, Francisco J / Lechner, Stefan G

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 1365

    Abstract: A central question in mechanobiology is how mechanical forces acting in or on cells are transmitted to mechanically-gated PIEZO channels that convert these forces into biochemical signals. Here we examined the role of the intracellular domains of PIEZO2, ...

    Abstract A central question in mechanobiology is how mechanical forces acting in or on cells are transmitted to mechanically-gated PIEZO channels that convert these forces into biochemical signals. Here we examined the role of the intracellular domains of PIEZO2, which account for 25% of the channel, and demonstrate that these domains fine-tune properties such as poking and stretch-sensitivity, velocity coding and single channel conductance. Moreover, we show that the intrinsically disordered linker between the transmembrane helices twelve and thirteen (IDR5) is required for the activation of PIEZO2 by cytoskeleton-transmitted forces. The deletion of IDR5 abolishes PIEZO2-mediated inhibition of neurite outgrowth, while it only partially affected its sensitivity to cell indentation and does not alter its stretch sensitivity. Thus, we propose that PIEZO2 is a polymodal mechanosensor that detects different types of mechanical stimuli via different force transmission pathways, which highlights the importance of utilizing multiple complementary assays when investigating PIEZO function.
    MeSH term(s) Cytoskeleton/metabolism ; Ion Channels/metabolism ; Mechanotransduction, Cellular/physiology
    Chemical Substances Ion Channels
    Language English
    Publishing date 2022-03-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-28974-6
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  7. Article ; Online: Peripheral and spinal circuits involved in mechanical allodynia.

    Arcourt, Alice / Lechner, Stefan G

    Pain

    2015  Volume 156, Issue 2, Page(s) 220–221

    MeSH term(s) Animals ; Humans ; Hyperalgesia/metabolism ; Hyperalgesia/pathology ; Nerve Net/metabolism ; Nerve Net/pathology ; Peripheral Nerves/metabolism ; Peripheral Nerves/pathology ; Spinal Nerves/metabolism ; Spinal Nerves/pathology
    Language English
    Publishing date 2015-01-17
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 193153-2
    ISSN 1872-6623 ; 0304-3959
    ISSN (online) 1872-6623
    ISSN 0304-3959
    DOI 10.1097/01.j.pain.0000460818.62406.38
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Intrinsically disordered intracellular domains control key features of the mechanically-gated ion channel PIEZO2

    Clement Verkest / Irina Schaefer / Timo A. Nees / Na Wang / Juri M. Jegelka / Francisco J. Taberner / Stefan G. Lechner

    Nature Communications, Vol 13, Iss 1, Pp 1-

    2022  Volume 14

    Abstract: A key question in mechanobiology is how mechanical forces are transmitted to PIEZO ion channels. Here, Verkest et al. identify an intracellular channel domain that is required for the activation of PIEZO2 by cytoskeleton-transmitted forces. ...

    Abstract A key question in mechanobiology is how mechanical forces are transmitted to PIEZO ion channels. Here, Verkest et al. identify an intracellular channel domain that is required for the activation of PIEZO2 by cytoskeleton-transmitted forces.
    Keywords Science ; Q
    Language English
    Publishing date 2022-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Neuropathic pain caused by miswiring and abnormal end organ targeting.

    Gangadharan, Vijayan / Zheng, Hongwei / Taberner, Francisco J / Landry, Jonathan / Nees, Timo A / Pistolic, Jelena / Agarwal, Nitin / Männich, Deepitha / Benes, Vladimir / Helmstaedter, Moritz / Ommer, Björn / Lechner, Stefan G / Kuner, Thomas / Kuner, Rohini

    Nature

    2022  Volume 606, Issue 7912, Page(s) 137–145

    Abstract: Nerve injury leads to chronic pain and exaggerated sensitivity to gentle touch (allodynia) as well as a loss of sensation in the areas in which injured and non-injured nerves come ... ...

    Abstract Nerve injury leads to chronic pain and exaggerated sensitivity to gentle touch (allodynia) as well as a loss of sensation in the areas in which injured and non-injured nerves come together
    MeSH term(s) Animals ; Chronic Pain/physiopathology ; Hyperalgesia/physiopathology ; Mechanoreceptors/pathology ; Mice ; Neuralgia/physiopathology ; Nociceptors/pathology ; Skin/innervation ; Skin/physiopathology
    Language English
    Publishing date 2022-05-25
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-04777-z
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  10. Article ; Online: Role of TMEM100 in mechanically insensitive nociceptor un-silencing.

    Nees, Timo A / Wang, Na / Adamek, Pavel / Zeitzschel, Nadja / Verkest, Clement / La Porta, Carmen / Schaefer, Irina / Virnich, Julie / Balkaya, Selin / Prato, Vincenzo / Morelli, Chiara / Begay, Valerie / Lee, Young Jae / Tappe-Theodor, Anke / Lewin, Gary R / Heppenstall, Paul A / Taberner, Francisco J / Lechner, Stefan G

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 1899

    Abstract: Mechanically silent nociceptors are sensory afferents that are insensitive to noxious mechanical stimuli under normal conditions but become sensitized to such stimuli during inflammation. Using RNA-sequencing and quantitative RT-PCR we demonstrate that ... ...

    Abstract Mechanically silent nociceptors are sensory afferents that are insensitive to noxious mechanical stimuli under normal conditions but become sensitized to such stimuli during inflammation. Using RNA-sequencing and quantitative RT-PCR we demonstrate that inflammation upregulates the expression of the transmembrane protein TMEM100 in silent nociceptors and electrophysiology revealed that over-expression of TMEM100 is required and sufficient to un-silence silent nociceptors in mice. Moreover, we show that mice lacking TMEM100 do not develop secondary mechanical hypersensitivity-i.e., pain hypersensitivity that spreads beyond the site of inflammation-during knee joint inflammation and that AAV-mediated overexpression of TMEM100 in articular afferents in the absence of inflammation is sufficient to induce mechanical hypersensitivity in remote skin regions without causing knee joint pain. Thus, our work identifies TMEM100 as a key regulator of silent nociceptor un-silencing and reveals a physiological role for this hitherto enigmatic afferent subclass in triggering spatially remote secondary mechanical hypersensitivity during inflammation.
    MeSH term(s) Animals ; Mice ; Inflammation/metabolism ; Knee Joint ; Nociceptors/metabolism ; Pain/metabolism ; Skin/metabolism
    Chemical Substances Tmem100 protein, mouse
    Language English
    Publishing date 2023-04-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-37602-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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