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  1. AU="Moroni, Anna"
  2. AU=Kreger Bridget T.
  3. AU="Woods, Angela L"
  4. AU=Iba Toshiaki
  5. AU="Akberova, N I"
  6. AU="Bolouki Moghaddam, Farzaneh"
  7. AU="Rajeshkannan, Nadarajah"
  8. AU="Noda, Judith"
  9. AU=Loucks Catrina M.
  10. AU="Lachérade, J-C"
  11. AU=Jalali Subhadra AU=Jalali Subhadra
  12. AU="Yang, Yung"
  13. AU="Belt, Brian"
  14. AU="Beckley, Akinpelumi A"
  15. AU="Adams, Tempe"
  16. AU=Wahidi Momen M
  17. AU="Pardis C. Sabeti"
  18. AU=Arkowitz Robert A
  19. AU="Sempoux, Christine"
  20. AU="Selebatso, Moses"
  21. AU=Sountoulides Petros
  22. AU="Huachun Zou"
  23. AU=SHENG Nan AU=SHENG Nan
  24. AU="Gascon, Pierre"
  25. AU="Hoa Phong, Pham Huu Thien"
  26. AU="Guiyan Ni"

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  1. Artikel ; Online: Weak Cation Selectivity in HCN Channels Results From K

    Bauer, Daniel / Wissmann, Jan / Moroni, Anna / Thiel, Gerhard / Hamacher, Kay

    Function (Oxford, England)

    2022  Band 3, Heft 3, Seite(n) zqac019

    Abstract: Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels generate the pacemaker current which plays an important role in the timing of various biological processes like the heart beat. We used umbrella sampling to explore the potential of mean ... ...

    Abstract Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels generate the pacemaker current which plays an important role in the timing of various biological processes like the heart beat. We used umbrella sampling to explore the potential of mean force for the conduction of potassium and sodium through the open HCN4 pore. Our data explain distinct functional features like low unitary conductance and weak selectivity as a result of high energetic barriers inside the selectivity filter of this channel. They exceed the 3-5 kJ/mol threshold which is presumed as maximal barrier for diffusion-limited conductance. Furthermore, simulations provide a thermodynamic explanation for the weak cation selectivity of HCN channels that contain only two ion binding sites in the selectivity filter (SF). We find that sodium ions bind more strongly to the SF than potassium and are easier released by binding of potassium than of another sodium. Hence ion transport and selectivity in HCN channels is not determined by the same mechanism as in potassium-selective channels; it rather relies on sodium as a weak blocker that can only be released by potassium.
    Sprache Englisch
    Erscheinungsdatum 2022-04-22
    Erscheinungsland England
    Dokumenttyp Journal Article
    ISSN 2633-8823
    ISSN (online) 2633-8823
    DOI 10.1093/function/zqac019
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Detection of ligand binding to purified HCN channels using fluorescence-based size exclusion chromatography.

    Saponaro, Andrea / Sharifzadeh, Atiyeh Sadat / Moroni, Anna

    Methods in enzymology

    2021  Band 652, Seite(n) 105–123

    Abstract: Biochemical measurements of ligand binding to eukaryotic membrane proteins are challenging because they can require large amounts of purified protein. For this reason, ligand binding is preferentially evaluated on soluble domains rather than on the full ... ...

    Abstract Biochemical measurements of ligand binding to eukaryotic membrane proteins are challenging because they can require large amounts of purified protein. For this reason, ligand binding is preferentially evaluated on soluble domains rather than on the full length proteins. In this chapter, we describe the use of fluorescence size exclusion chromatography-based thermostability (FSEC-TS) as an assay to monitor ligand binding to the full length mammalian ion channel HCN4. FSEC-TS monitors the effect of the ligand on the thermal denaturation curve of the protein by following the fluorescence of a fused GFP protein. Changes in the melting temperature (Tm) provide a quantitative value for measuring ligand-protein interaction. As a proof of concept, we describe here the protocol for monitoring the binding of the second messenger cAMP and of the known HCN drug Ivabradine to the purified GFP-HCN4 channel. cTMP, a known non-binder of HCN channels, is used as a control. Due to the small amount of protein required, the assay represents a high-throughput screening system for evaluating binding of small molecules to full length proteins.
    Mesh-Begriff(e) Animals ; Chromatography, Gel ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/genetics ; Ligands
    Chemische Substanzen Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; Ligands
    Sprache Englisch
    Erscheinungsdatum 2021-02-27
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2021.01.043
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  3. Artikel ; Online: Structural and functional approaches to studying cAMP regulation of HCN channels.

    Saponaro, Andrea / Thiel, Gerhard / Moroni, Anna

    Biochemical Society transactions

    2021  Band 49, Heft 6, Seite(n) 2573–2579

    Abstract: Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels are primarily activated by voltage and further modulated by cAMP. While cAMP binding alone does not open the channel, its presence facilitates the action of voltage, increasing channel ... ...

    Abstract Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels are primarily activated by voltage and further modulated by cAMP. While cAMP binding alone does not open the channel, its presence facilitates the action of voltage, increasing channel open probability. Functional results indicate that the membrane-based voltage sensor domain (VSD) communicates with the cytosolic cyclic nucleotide-binding domain (CNBD), and vice-versa. Yet, a mechanistic explanation on how this could occur in structural terms is still lacking. In this review, we will discuss the recent advancement in understanding the molecular mechanisms connecting the VSD with the CNBD in the tetrameric organization of HCN channels unveiled by the 3D structures of HCN1 and HCN4. Data show that the HCN domain transmits cAMP signal to the VSD by bridging the cytosolic to the membrane domains. Furthermore, a metal ion coordination site connects the C-linker to the S4-S5 linker in HCN4, further facilitating cAMP signal transmission to the VSD in this isoform.
    Mesh-Begriff(e) Animals ; Cell Membrane/metabolism ; Cyclic AMP/metabolism ; Cytosol/metabolism ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/chemistry ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/metabolism ; Signal Transduction ; Structure-Activity Relationship
    Chemische Substanzen Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; Cyclic AMP (E0399OZS9N)
    Sprache Englisch
    Erscheinungsdatum 2021-12-03
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20210290
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Buch ; Online ; Dissertation / Habilitation: HCN4 pacemaker channels as potential therapeutic targets based on their novel structural properties

    Sharifzadeh, Atiyehsadat [Verfasser] / Thiel, Gerhard [Akademischer Betreuer] / Moroni, Anna [Akademischer Betreuer]

    2023  

    Verfasserangabe Atiyehsadat Sharifzadeh ; Gerhard Thiel, Anna Moroni
    Schlagwörter Biowissenschaften, Biologie ; Life Science, Biology
    Thema/Rubrik (Code) sg570
    Sprache Englisch
    Verlag Universitäts- und Landesbibliothek
    Erscheinungsort Darmstadt
    Dokumenttyp Buch ; Online ; Dissertation / Habilitation
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  5. Artikel: cyclic AMP Regulation and Its Command in the Pacemaker Channel HCN4.

    Porro, Alessandro / Thiel, Gerhard / Moroni, Anna / Saponaro, Andrea

    Frontiers in physiology

    2020  Band 11, Seite(n) 771

    Abstract: Direct regulation of the pacemaker "funny" current ( ... ...

    Abstract Direct regulation of the pacemaker "funny" current (I
    Sprache Englisch
    Erscheinungsdatum 2020-07-07
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2020.00771
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  6. Artikel ; Online: Tailoring baker's yeast Saccharomyces cerevisiae for functional testing of channelrhodopsin.

    Höler, Sebastian / Degreif, Daniel / Stix, Florentine / Yang, Shang / Gao, Shiqiang / Nagel, Georg / Moroni, Anna / Thiel, Gerhard / Bertl, Adam / Rauh, Oliver

    PloS one

    2023  Band 18, Heft 4, Seite(n) e0280711

    Abstract: Channelrhodopsin 2 (ChR2) and its variants are the most frequent tools for remote manipulation of electrical properties in cells via light. Ongoing attempts try to enlarge their functional spectrum with respect to ion selectivity, light sensitivity and ... ...

    Abstract Channelrhodopsin 2 (ChR2) and its variants are the most frequent tools for remote manipulation of electrical properties in cells via light. Ongoing attempts try to enlarge their functional spectrum with respect to ion selectivity, light sensitivity and protein trafficking by mutations, protein engineering and environmental mining of ChR2 variants. A shortcoming in the required functional testing of large numbers of ChR2 variants is the lack of an easy screening system. Baker's yeast, which was successfully employed for testing ion channels from eukaryotes has not yet been used for screening of ChR2s, because they neither produce the retinal chromophore nor its precursor carotenoids. We found that addition of retinal to the external medium was not sufficient for detecting robust ChR activity in yeast in simple growth assays. This obstacle was overcome by metabolic engineering of a yeast strain, which constitutively produces retinal. In proof of concept experiments we functionally express different ChR variants in these cells and monitor their blue light induced activity in simple growth assays. We find that light activation of ChR augments an influx of Na+ with a consequent inhibition of cell growth. In a K+ uptake deficient yeast strain, growth can be rescued in selective medium by the blue light induced K+ conductance of ChR. This yeast strain can now be used as chassis for screening of new functional ChR variants and mutant libraries in simple yeast growth assays under defined selective conditions.
    Mesh-Begriff(e) Saccharomyces cerevisiae/metabolism ; Channelrhodopsins/genetics ; Channelrhodopsins/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Metabolic Engineering ; Mutation ; Fermentation
    Chemische Substanzen Channelrhodopsins ; Saccharomyces cerevisiae Proteins
    Sprache Englisch
    Erscheinungsdatum 2023-04-13
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0280711
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  7. Artikel: HCN channels sense temperature and determine heart rate responses to heat.

    Wu, Yuejin / Wang, Qinchuan / Granger, Jonathan / Gaido, Oscar Reyes / Aguilar, Eric Nunez / Ludwig, Andreas / Moroni, Anna / Bianchet, Mario A / Anderson, Mark E

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Heart rate increases with heat, [1-3] constituting a fundamental physiological relationship in vertebrates. Each normal heartbeat is initiated by an action potential generated in a sinoatrial nodal pacemaker cell. Pacemaker cells are enriched with ... ...

    Abstract Heart rate increases with heat, [1-3] constituting a fundamental physiological relationship in vertebrates. Each normal heartbeat is initiated by an action potential generated in a sinoatrial nodal pacemaker cell. Pacemaker cells are enriched with hyperpolarization activated cyclic nucleotide-gated ion channels (HCN) that deliver cell membrane depolarizing inward current that triggers action potentials. HCN channel current increases due to cAMP binding, a mechanism coupling adrenergic tone to physiological 'fight or flight' heart rate acceleration. However, the mechanism(s) for heart rate response to thermal energy is unknown. We used thermodynamical and homology computational modeling, site-directed mutagenesis and mouse models to identify a concise motif on the S4-S5 linker of the cardiac pacemaker HCN4 channels (M407/Y409) that determines HCN4 current (I
    Sprache Englisch
    Erscheinungsdatum 2023-09-03
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.09.02.556046
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  8. Artikel ; Online: Combination of hydrophobicity and codon usage bias determines sorting of model K

    Engel, Anja J / Paech, Steffen / Langhans, Markus / van Etten, James L / Moroni, Anna / Thiel, Gerhard / Rauh, Oliver

    Traffic (Copenhagen, Denmark)

    2023  Band 24, Heft 11, Seite(n) 533–545

    Abstract: ... When the ... ...

    Abstract When the K
    Mesh-Begriff(e) Animals ; Codon Usage ; Proteins/metabolism ; Mitochondria/metabolism ; Protein Transport ; Endoplasmic Reticulum/metabolism ; Codon/metabolism ; Hydrophobic and Hydrophilic Interactions ; Mammals/genetics ; Mammals/metabolism
    Chemische Substanzen Proteins ; Codon
    Sprache Englisch
    Erscheinungsdatum 2023-08-14
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12915
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

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    Zs.A 5634: Hefte anzeigen Standort:
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  9. Artikel ; Online: A high affinity switch for cAMP in the HCN pacemaker channels.

    Porro, Alessandro / Saponaro, Andrea / Castelli, Roberta / Introini, Bianca / Hafez Alkotob, Anahita / Ranjbari, Golnaz / Enke, Uta / Kusch, Jana / Benndorf, Klaus / Santoro, Bina / DiFrancesco, Dario / Thiel, Gerhard / Moroni, Anna

    Nature communications

    2024  Band 15, Heft 1, Seite(n) 843

    Abstract: Binding of cAMP to Hyperpolarization activated cyclic nucleotide gated (HCN) channels facilitates pore opening. It is unclear why the isolated cyclic nucleotide binding domain (CNBD) displays in vitro lower affinity for cAMP than the full-length channel ... ...

    Abstract Binding of cAMP to Hyperpolarization activated cyclic nucleotide gated (HCN) channels facilitates pore opening. It is unclear why the isolated cyclic nucleotide binding domain (CNBD) displays in vitro lower affinity for cAMP than the full-length channel in patch experiments. Here we show that HCN are endowed with an affinity switch for cAMP. Alpha helices D and E, downstream of the cyclic nucleotide binding domain (CNBD), bind to and stabilize the holo CNBD in a high affinity state. These helices increase by 30-fold cAMP efficacy and affinity measured in patch clamp and ITC, respectively. We further show that helices D and E regulate affinity by interacting with helix C of the CNBD, similarly to the regulatory protein TRIP8b. Our results uncover an intramolecular mechanism whereby changes in binding affinity, rather than changes in cAMP concentration, can modulate HCN channels, adding another layer to the complex regulation of their activity.
    Mesh-Begriff(e) Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/metabolism ; Ion Channel Gating/physiology ; Protein Conformation, alpha-Helical ; Nucleotides, Cyclic ; Cyclic Nucleotide-Gated Cation Channels/genetics ; Cyclic Nucleotide-Gated Cation Channels/metabolism
    Chemische Substanzen Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; Nucleotides, Cyclic ; Cyclic Nucleotide-Gated Cation Channels
    Sprache Englisch
    Erscheinungsdatum 2024-01-29
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-45136-y
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Distinct classes of potassium channels fused to GPCRs as electrical signaling biosensors.

    García-Fernández, M Dolores / Chatelain, Franck C / Nury, Hugues / Moroni, Anna / Moreau, Christophe J

    Cell reports methods

    2021  Band 1, Heft 8, Seite(n) None

    Abstract: Ligand-gated ion channels (LGICs) are natural biosensors generating electrical signals in response to the binding of specific ligands. ... ...

    Abstract Ligand-gated ion channels (LGICs) are natural biosensors generating electrical signals in response to the binding of specific ligands. Creating
    Mesh-Begriff(e) Animals ; Mice ; Receptors, G-Protein-Coupled/genetics ; Signal Transduction ; Ligand-Gated Ion Channels/metabolism ; Ligands ; Biosensing Techniques
    Chemische Substanzen Receptors, G-Protein-Coupled ; Ligand-Gated Ion Channels ; Ligands
    Sprache Englisch
    Erscheinungsdatum 2021-12-20
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2667-2375
    ISSN (online) 2667-2375
    DOI 10.1016/j.crmeth.2021.100119
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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