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  1. Article: FAVOURITE PAPERS. Prof. U. Benjamin Kaupp discusses "Physics of Chemoreception"

    Kaupp, U. Benjamin

    Futura

    2021  Volume 36, Issue 2, Page(s) 7

    Language German ; English
    Document type Article
    ZDB-ID 382906-6
    ISSN 0179-6372
    Database Current Contents Medicine

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  2. Article: WHO'S WHO AT BIF. Prof. U. Benjamin Kaupp answers the BIF questionnaire

    Kaupp, U. Benjamin

    Futura

    2013  Volume 28, Issue 1, Page(s) 34

    Language German ; English
    Document type Article
    ZDB-ID 382906-6
    ISSN 0179-6372
    Database Current Contents Medicine

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  3. Article: WHO'S WHO AT BIF? Prof U. Benjamin Kaupp answers tlie BIF questionnaire

    Kaupp, U. Benjamin

    Futura

    2013  Volume 28, Issue 1, Page(s) 34

    Language German ; English
    Document type Article
    ZDB-ID 382906-6
    ISSN 0179-6372
    Database Current Contents Medicine

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  4. Article ; Online: The structure of cyclic nucleotide-gated channels in rod and cone photoreceptors.

    Barret, Diane C A / Kaupp, U Benjamin / Marino, Jacopo

    Trends in neurosciences

    2022  Volume 45, Issue 10, Page(s) 763–776

    Abstract: Cyclic nucleotide-gated (CNG) channels play a central role in rod and cone photoreceptors of the vertebrate retina. In photoreceptors, light triggers a series of biochemical reactions that ultimately close CNG channels and evoke a brief voltage pulse, a ... ...

    Abstract Cyclic nucleotide-gated (CNG) channels play a central role in rod and cone photoreceptors of the vertebrate retina. In photoreceptors, light triggers a series of biochemical reactions that ultimately close CNG channels and evoke a brief voltage pulse, a signal that is later passed on to the brain. Malfunction of CNG channels can lead to loss of vision. Thus, understanding their function in atomic and mechanistic detail is important. Because of the complex subunit stoichiometry of these channels, elucidation of their structure has proved challenging. Recently, several cryoelectron microscopy (EM) structures of rod and cone CNG channels revealed unexpected structural features. We compare these structures side by side and highlight similarities and differences in key structural elements. We discuss the implications of the channels' structure for questions about their gating, ion permeation, and modulation. These results inform new strategies to further characterize the structural basis of CNG channels functioning in rods and cones.
    MeSH term(s) Cryoelectron Microscopy ; Cyclic Nucleotide-Gated Cation Channels ; Humans ; Nucleotides, Cyclic ; Retina ; Retinal Cone Photoreceptor Cells/physiology
    Chemical Substances Cyclic Nucleotide-Gated Cation Channels ; Nucleotides, Cyclic
    Language English
    Publishing date 2022-08-05
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 282488-7
    ISSN 1878-108X ; 0378-5912 ; 0166-2236
    ISSN (online) 1878-108X
    ISSN 0378-5912 ; 0166-2236
    DOI 10.1016/j.tins.2022.07.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Control of intracellular pH and bicarbonate by CO

    Grahn, Elena / Kaufmann, Svenja V / Askarova, Malika / Ninov, Momchil / Welp, Luisa M / Berger, Thomas K / Urlaub, Henning / Kaupp, U Benjamin

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 5395

    Abstract: The reaction of ... ...

    Abstract The reaction of CO
    MeSH term(s) Humans ; Male ; Bicarbonates ; Carbon Dioxide ; Semen ; Sperm Motility ; Spermatozoa ; Hydrogen-Ion Concentration
    Chemical Substances Bicarbonates ; Carbon Dioxide (142M471B3J)
    Language English
    Publishing date 2023-09-05
    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/s41467-023-40855-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Larry Cohen-50 ways to DYE your science.

    Strünker, Timo / Kaupp, U Benjamin

    Neurophotonics

    2015  Volume 2, Issue 2, Page(s) 21004

    Language English
    Publishing date 2015-05-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2781943-7
    ISSN 2329-4248 ; 2329-423X
    ISSN (online) 2329-4248
    ISSN 2329-423X
    DOI 10.1117/1.NPh.2.2.021004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: A Stable Chemokine Gradient Controls Directional Persistence of Migrating Dendritic Cells.

    Quast, Thomas / Zölzer, Karolin / Guu, Donald / Alvarez, Luis / Küsters, Carsten / Kiermaier, Eva / Kaupp, U Benjamin / Kolanus, Waldemar

    Frontiers in cell and developmental biology

    2022  Volume 10, Page(s) 943041

    Abstract: Navigation of dendritic cells (DCs) from the site of infection to lymphoid organs is guided by concentration gradients of CCR7 ligands. How cells interpret chemokine gradients and how they couple directional sensing to polarization and persistent ... ...

    Abstract Navigation of dendritic cells (DCs) from the site of infection to lymphoid organs is guided by concentration gradients of CCR7 ligands. How cells interpret chemokine gradients and how they couple directional sensing to polarization and persistent chemotaxis has remained largely elusive. Previous experimental systems were limited in the ability to control fast
    Language English
    Publishing date 2022-08-09
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2022.943041
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Structural basis of the partially open central gate in the human CNGA1/CNGB1 channel explained by additional density for calmodulin in cryo-EM map.

    Barret, Diane C A / Schertler, Gebhard F X / Kaupp, U Benjamin / Marino, Jacopo

    Journal of structural biology

    2021  Volume 214, Issue 1, Page(s) 107828

    Abstract: The recently reported structure of the human CNGA1/CNGB1 CNG channel in the open state (Xue et al., 2021a) shows that one CNGA1 and one CNGB1 subunit do not open the central hydrophobic gate completely upon cGMP binding. This is different from what has ... ...

    Abstract The recently reported structure of the human CNGA1/CNGB1 CNG channel in the open state (Xue et al., 2021a) shows that one CNGA1 and one CNGB1 subunit do not open the central hydrophobic gate completely upon cGMP binding. This is different from what has been reported for CNGA homomeric channels (Xue et al., 2021b; Zheng et al., 2020). In seeking to understand how this difference is due to the presence of the CNGB1 subunit, we find that the deposited density map (Xue et al., 2021a) (EMDB 24465) contains an additional density not reported in the images of the original publication. This additional density fits well the structure of calmodulin (CaM), and it unambiguously connects the newly identified D-helix of CNGB1 to one of the CNGA1 helices (A1
    MeSH term(s) Binding Sites ; Calmodulin/metabolism ; Cryoelectron Microscopy ; Cyclic Nucleotide-Gated Cation Channels/chemistry ; Cyclic Nucleotide-Gated Cation Channels/metabolism ; Humans ; Retinal Rod Photoreceptor Cells/metabolism
    Chemical Substances CNGA1 protein, human ; CNGB1 protein, human ; Calmodulin ; Cyclic Nucleotide-Gated Cation Channels
    Language English
    Publishing date 2021-12-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1032718-6
    ISSN 1095-8657 ; 1047-8477
    ISSN (online) 1095-8657
    ISSN 1047-8477
    DOI 10.1016/j.jsb.2021.107828
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods.

    Barret, Diane C A / Schertler, Gebhard F X / Kaupp, U Benjamin / Marino, Jacopo

    Nature structural & molecular biology

    2021  Volume 29, Issue 1, Page(s) 32–39

    Abstract: In rod photoreceptors of the retina, the cyclic nucleotide-gated (CNG) channel is composed of three CNGA and one CNGB subunits, and it closes in response to light activation to generate an electrical signal that is conveyed to the brain. Here we report ... ...

    Abstract In rod photoreceptors of the retina, the cyclic nucleotide-gated (CNG) channel is composed of three CNGA and one CNGB subunits, and it closes in response to light activation to generate an electrical signal that is conveyed to the brain. Here we report the cryo-EM structure of the closed state of the native rod CNG channel isolated from bovine retina. The structure reveals differences between CNGA1 and CNGB1 subunits. Three CNGA1 subunits are tethered at their C terminus by a coiled-coil region. The C-helix in the cyclic nucleotide-binding domain of CNGB1 features a different orientation from that in the three CNGA1 subunits. The arginine residue R994 of CNGB1 reaches into the ionic pathway and blocks the pore, thus introducing an additional gate, which is different from the central hydrophobic gate known from homomeric CNGA channels. These results address the long-standing question of how CNGB1 subunits contribute to the function of CNG channels in visual and olfactory neurons.
    MeSH term(s) Amino Acid Sequence ; Animals ; Cattle ; Conserved Sequence ; Cyclic Nucleotide-Gated Cation Channels/chemistry ; Cyclic Nucleotide-Gated Cation Channels/ultrastructure ; Models, Molecular ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Retinal Rod Photoreceptor Cells/metabolism ; Retinal Rod Photoreceptor Cells/ultrastructure
    Chemical Substances Cyclic Nucleotide-Gated Cation Channels ; Protein Subunits
    Language English
    Publishing date 2021-12-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-021-00700-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Olfactory signalling in vertebrates and insects: differences and commonalities.

    Kaupp, U Benjamin

    Nature reviews. Neuroscience

    2010  Volume 11, Issue 3, Page(s) 188–200

    Abstract: Vertebrates and insects have evolved complex repertoires of chemosensory receptors to detect and distinguish odours. With a few exceptions, vertebrate chemosensory receptors belong to the family of G protein-coupled receptors that initiate a cascade of ... ...

    Abstract Vertebrates and insects have evolved complex repertoires of chemosensory receptors to detect and distinguish odours. With a few exceptions, vertebrate chemosensory receptors belong to the family of G protein-coupled receptors that initiate a cascade of cellular signalling events and thereby electrically excite the neuron. Insect receptors, which are structurally and genetically unrelated to vertebrate receptors, are a complex of two distinct molecules that serves both as a receptor for the odorant and as an ion channel that is gated by binding of the odorant. Metabotropic signalling in vertebrates provides a rich panoply of positive and negative regulation, whereas ionotropic signalling in insects enhances processing speed.
    MeSH term(s) Animals ; Insecta/physiology ; Odorants ; Olfactory Pathways/physiology ; Olfactory Receptor Neurons/physiology ; Pheromones ; Receptors, Odorant/physiology ; Signal Transduction/physiology ; Smell/physiology ; Vertebrates/physiology
    Chemical Substances Pheromones ; Receptors, Odorant
    Language English
    Publishing date 2010-03
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2034150-7
    ISSN 1471-0048 ; 1471-0048 ; 1471-003X
    ISSN (online) 1471-0048
    ISSN 1471-0048 ; 1471-003X
    DOI 10.1038/nrn2789
    Database MEDical Literature Analysis and Retrieval System OnLINE

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