LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 194

Search options

  1. Article: 2021 Nobel Prize for mechanosensory transduction.

    Martinac, Boris

    Biophysical reviews

    2022  Volume 14, Issue 1, Page(s) 15–20

    Abstract: Written by someone who has worked in the mechanobiology field for close to 40 years, this commentary describes some historical background to the recent award of one-half of the Nobel Prize for Physiology or Medicine to Ardem Patapoutian for his discovery ...

    Abstract Written by someone who has worked in the mechanobiology field for close to 40 years, this commentary describes some historical background to the recent award of one-half of the Nobel Prize for Physiology or Medicine to Ardem Patapoutian for his discovery of the family of mechanosensitive Piezo ion channels, which function as mechanoreceptors feeling the environment in senses such as touch, pain, and proprioception.
    Language English
    Publishing date 2022-02-19
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2486483-3
    ISSN 1867-2469 ; 1867-2450
    ISSN (online) 1867-2469
    ISSN 1867-2450
    DOI 10.1007/s12551-022-00935-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Book: Sensing with ion channels

    Martinac, Boris

    (Springer series in biophysics ; 11)

    2008  

    Author's details Boris Martinac, ed
    Series title Springer series in biophysics ; 11
    Collection
    Keywords Ion Channels / physiology ; Mechanotransduction, Cellular / physiology ; Mechanoreceptors / physiology ; Ionenkanal ; Signaltransduktion
    Subject Signalübertragung ; Signalvermittlung
    Language English
    Size XXII, 304 S. : Ill., graph. Darst., 235 mm x 155 mm
    Publisher Springer
    Publishing place Berlin u.a.
    Publishing country Germany
    Document type Book
    HBZ-ID HT015389713
    ISBN 978-3-540-72683-8 ; 3-540-72683-7
    Database Catalogue ZB MED Medicine, Health

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2008 A 5517 order for loan Magazin

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Mechanisms of PIEZO Channel Inactivation.

    Zhou, Zijing / Martinac, Boris

    International journal of molecular sciences

    2023  Volume 24, Issue 18

    Abstract: PIEZO channels PIEZO1 and PIEZO2 are the newly identified mechanosensitive, non-selective cation channels permeable to ... ...

    Abstract PIEZO channels PIEZO1 and PIEZO2 are the newly identified mechanosensitive, non-selective cation channels permeable to Ca
    Language English
    Publishing date 2023-09-14
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241814113
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article: "Force-From-Lipids" Dependence of the MscCG Mechanosensitive Channel Gating on Anionic Membranes.

    Nakayama, Yoshitaka / Rohde, Paul R / Martinac, Boris

    Microorganisms

    2023  Volume 11, Issue 1

    Abstract: Mechanosensory transduction ... ...

    Abstract Mechanosensory transduction in
    Language English
    Publishing date 2023-01-12
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms11010194
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: The force-from-lipid principle and its origin, a '

    Martinac, Boris / Kung, Ching

    Journal of neurogenetics

    2022  Volume 36, Issue 2-3, Page(s) 44–54

    Abstract: The force-from-lipid (FFL) principle states that it is the lateral stretch force from the lipid membrane that ultimately opens mechanosensitive (MS) channels, not the external tether nor the internal cytoskeleton. Piezo channels for certain touch or ... ...

    Abstract The force-from-lipid (FFL) principle states that it is the lateral stretch force from the lipid membrane that ultimately opens mechanosensitive (MS) channels, not the external tether nor the internal cytoskeleton. Piezo channels for certain touch or proprioception and the hair-cell channels for hearing or balance apparently obey this principle, which is based on the idea that the lipid bilayer is an amphipathic compartment with a distinct internal force-distribution profile. Physical stretch or insertion of chemical impurities alters this profile, driving channel shape change to conform to the new environment. Thus, FFL governs all dynamic proteins embedded in membrane, including Kv's and TRPs. This article retraces the humble origin of the FFL concept.
    MeSH term(s) Animals ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Escherichia coli Proteins/metabolism ; Elephants/metabolism ; Ion Channels ; Mechanotransduction, Cellular ; RNA/metabolism ; Adenosine Triphosphate/metabolism
    Chemical Substances Lipid Bilayers ; Escherichia coli Proteins ; Ion Channels ; RNA (63231-63-0) ; Adenosine Triphosphate (8L70Q75FXE) ; MscL protein, E coli
    Language English
    Publishing date 2022-07-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 605543-6
    ISSN 1563-5260 ; 0167-7063
    ISSN (online) 1563-5260
    ISSN 0167-7063
    DOI 10.1080/01677063.2022.2097674
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1878: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article: A novel force transduction pathway from a tension sensor to the gate in the mechano-gating of MscL channel.

    Sawada, Yasuyuki / Nomura, Takeshi / Martinac, Boris / Sokabe, Masahiro

    Frontiers in chemistry

    2023  Volume 11, Page(s) 1175443

    Abstract: The bacterial mechanosensitive channel of large conductance MscL is activated exclusively by increased tension in the membrane bilayer. Despite many proposed models for MscL opening, its precise mechano-gating mechanism, particularly how the received ... ...

    Abstract The bacterial mechanosensitive channel of large conductance MscL is activated exclusively by increased tension in the membrane bilayer. Despite many proposed models for MscL opening, its precise mechano-gating mechanism, particularly how the received force at the tension sensor transmits to the gate remains incomplete. Previous studies have shown that along with amphipathic
    Language English
    Publishing date 2023-06-06
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2711776-5
    ISSN 2296-2646
    ISSN 2296-2646
    DOI 10.3389/fchem.2023.1175443
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Single-molecule FRET studies of ion channels.

    Martinac, Boris

    Progress in biophysics and molecular biology

    2017  Volume 130, Issue Pt B, Page(s) 192–197

    Abstract: Different types of fluorescence spectroscopy approaches have over the last two decades become important techniques in studies of ion channel structure and dynamics. Many fluorescence methods have been used to examine a huge variety of ion channels. Any ... ...

    Abstract Different types of fluorescence spectroscopy approaches have over the last two decades become important techniques in studies of ion channel structure and dynamics. Many fluorescence methods have been used to examine a huge variety of ion channels. Any fluorescence study of ion channels requires the presence of fluorophores, which may be intrinsic to the channel protein, attached either extrinsically to the protein, or be simply located nearby the channel to monitor local conditions such as for many of the ion-sensitive dyes. Many ion channel studies utilize protein-bound or intrinsic protein fluorophores. Single-molecule Förster resonance energy transfer (smFRET) spectroscopy has been particularly useful in gaining detailed structural information for multimeric membrane proteins including ion channels. This technique presents a major advancement in studies of structural dynamics of these membrane proteins. Although it has required different approaches to protein labelling, control of the protein state, as well as careful analysis of the orientations, geometries, and number of fluorescent probes, the smFRET methodology provides an excellent tool for studying the structure of ion channels.
    MeSH term(s) Fluorescence Resonance Energy Transfer/methods ; Humans ; Ion Channels/chemistry ; Ion Channels/metabolism
    Chemical Substances Ion Channels
    Language English
    Publishing date 2017-06-23
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 209302-9
    ISSN 1873-1732 ; 0079-6107
    ISSN (online) 1873-1732
    ISSN 0079-6107
    DOI 10.1016/j.pbiomolbio.2017.06.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.281: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Fishing for Links Between Omega-3 Fatty Acids and Atrial Fibrillation.

    Fatkin, Diane / Cox, Charles D / Martinac, Boris

    Circulation

    2022  Volume 145, Issue 14, Page(s) 1037–1039

    MeSH term(s) Humans ; Atrial Fibrillation/drug therapy ; Fatty Acids, Omega-3/therapeutic use
    Chemical Substances Fatty Acids, Omega-3
    Language English
    Publishing date 2022-04-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80099-5
    ISSN 1524-4539 ; 0009-7322 ; 0069-4193 ; 0065-8499
    ISSN (online) 1524-4539
    ISSN 0009-7322 ; 0069-4193 ; 0065-8499
    DOI 10.1161/CIRCULATIONAHA.121.058596
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ui IV Zs.60: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: “Force-From-Lipids” Dependence of the MscCG Mechanosensitive Channel Gating on Anionic Membranes

    Yoshitaka Nakayama / Paul R. Rohde / Boris Martinac

    Microorganisms, Vol 11, Iss 194, p

    2023  Volume 194

    Abstract: Mechanosensory transduction in Corynebacterium glutamicum plays a major role in glutamate efflux for industrial MSG, whose production depends on the activation of MscCG-type mechanosensitive channels. Dependence of the MscCG channel activation by ... ...

    Abstract Mechanosensory transduction in Corynebacterium glutamicum plays a major role in glutamate efflux for industrial MSG, whose production depends on the activation of MscCG-type mechanosensitive channels. Dependence of the MscCG channel activation by membrane tension on the membrane lipid content has to date not been functionally characterized. Here, we report the MscCG channel patch clamp recording from liposomes fused with C. glutamicum membrane vesicles as well as from proteoliposomes containing the purified MscCG protein. Our recordings demonstrate that mechanosensitivity of MscCG channels depends significantly on the presence of negatively charged lipids in the proteoliposomes. MscCG channels in liposome preparations fused with native membrane vesicles exhibited the activation threshold similar to the channels recorded from C. glutamicum giant spheroplasts. In comparison, the activation threshold of the MscCG channels reconstituted into azolectin liposomes was higher than the activation threshold of E. coli MscL, which is gated by membrane tension close to the bilayer lytic tension. The spheroplast-like activation threshold was restored when the MscCG channels were reconstituted into liposomes made of E. coli polar lipid extract. In liposomes made of polar lipids mixed with synthetic phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin, the activation threshold of MscCG was significantly reduced compared to the activation threshold recorded in azolectin liposomes, which suggests the importance of anionic lipids for the channel mechanosensitivity. Moreover, the micropipette aspiration technique combined with patch fluorometry demonstrated that membranes containing anionic phosphatidylglycerol are softer than membranes containing only polar non-anionic phosphatidylcholine and phosphatidylethanolamine. The difference in mechanosensitivity between C. glutamicum MscCG and canonical MscS of E. coli observed in proteoliposomes explains the evolutionary tuning of the force from lipids sensing in various ...
    Keywords bacterial mechanosensing ; bacterial electrophysiology ; patch fluorometry ; micropipette aspiration ; membrane stiffness ; Corynebacterium glutamicum ; Biology (General) ; QH301-705.5
    Subject code 572
    Language English
    Publishing date 2023-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  10. Article ; Online: A novel force transduction pathway from a tension sensor to the gate in the mechano-gating of MscL channel

    Yasuyuki Sawada / Takeshi Nomura / Boris Martinac / Masahiro Sokabe

    Frontiers in Chemistry, Vol

    2023  Volume 11

    Abstract: The bacterial mechanosensitive channel of large conductance MscL is activated exclusively by increased tension in the membrane bilayer. Despite many proposed models for MscL opening, its precise mechano-gating mechanism, particularly how the received ... ...

    Abstract The bacterial mechanosensitive channel of large conductance MscL is activated exclusively by increased tension in the membrane bilayer. Despite many proposed models for MscL opening, its precise mechano-gating mechanism, particularly how the received force at the tension sensor transmits to the gate remains incomplete. Previous studies have shown that along with amphipathic N-terminus located near the cytoplasmic surface of the membrane, Phe78 residue near the outer surface also acts as a “tension sensor,” while Gly22 is a central constituent of the “hydrophobic gate.” Present study focused on elucidating the force transmission mechanism from the sensor Phe78 in the outer transmembrane helix (TM2) to the gate in the inner transmembrane helix (TM1) of MscL by applying the patch clamp and molecular dynamics (MD) simulations to the wild type MscL channel and its single mutants at the sensor (F78N), the gate (G22N) and their combination (G22N/F78N) double mutant. F78N MscL resulted in a severe loss-of-function, while G22N MscL caused a gain-of-function channel exhibiting spontaneous openings at the resting membrane tension. We initially speculated that the spontaneous opening in G22N mutant might occur without tension acting on Phe78 residue. To test this hypothesis, we examined the (G22N/F78N) double mutant, which unexpectedly exhibited neither spontaneous activity nor activity by a relatively high membrane tension. To understand the underlying mechanism, we conducted MD simulations and analyzed the force transduction pathway. Results showed that the mutation at the tension sensor (F78N) in TM2 caused decreased interaction of this residue not only with lipids, but also with a group of amino acids (Ile32-Leu36-Ile40) in the neighboring TM1 helix, which resulted in an inefficient force transmission to the gate-constituting amino acids on TM1. This change also induced a slight tilting of TM1 towards the membrane plane and decreased the size of the channel pore at the gate, which seems to be the major mechanism for the ...
    Keywords mechanosensitive channel ; E-coli ; MscL ; gating mechanism ; patch clamp ; molecular dynamics ; Chemistry ; QD1-999
    Subject code 612
    Language English
    Publishing date 2023-06-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top