Littérature scientifique sur le sujet « Cyclic nucleotide-gated channel »
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Articles de revues sur le sujet "Cyclic nucleotide-gated channel"
Kaupp, U. Benjamin, et Reinhard Seifert. « Cyclic Nucleotide-Gated Ion Channels ». Physiological Reviews 82, no 3 (7 janvier 2002) : 769–824. http://dx.doi.org/10.1152/physrev.00008.2002.
Texte intégralJames, Zachary M., et William N. Zagotta. « Structural insights into the mechanisms of CNBD channel function ». Journal of General Physiology 150, no 2 (12 décembre 2017) : 225–44. http://dx.doi.org/10.1085/jgp.201711898.
Texte intégralBecchetti, Andrea, Katia Gamel et Vincent Torre. « Cyclic Nucleotide–Gated Channels ». Journal of General Physiology 114, no 3 (1 septembre 1999) : 377–92. http://dx.doi.org/10.1085/jgp.114.3.377.
Texte intégralSanty, Lorraine C., et Guido Guidotti. « Expression of a single gene produces both forms of skeletal muscle cyclic nucleotide-gated channels ». American Journal of Physiology-Endocrinology and Metabolism 273, no 6 (1 décembre 1997) : E1140—E1148. http://dx.doi.org/10.1152/ajpendo.1997.273.6.e1140.
Texte intégralBej, Aritra, et James B. Ames. « Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin ». International Journal of Molecular Sciences 23, no 22 (16 novembre 2022) : 14143. http://dx.doi.org/10.3390/ijms232214143.
Texte intégralFodor, Anthony A., Sharona E. Gordon et William N. Zagotta. « Mechanism of Tetracaine Block of Cyclic Nucleotide-gated Channels ». Journal of General Physiology 109, no 1 (1 janvier 1997) : 3–14. http://dx.doi.org/10.1085/jgp.109.1.3.
Texte intégralJames, Zachary M., Andrew J. Borst, Yoni Haitin, Brandon Frenz, Frank DiMaio, William N. Zagotta et David Veesler. « CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel ». Proceedings of the National Academy of Sciences 114, no 17 (10 avril 2017) : 4430–35. http://dx.doi.org/10.1073/pnas.1700248114.
Texte intégralSanty, L. C., et G. Guidotti. « Reconstitution and characterization of two forms of cyclic nucleotide-gated channels from skeletal muscle ». American Journal of Physiology-Endocrinology and Metabolism 271, no 6 (1 décembre 1996) : E1051—E1060. http://dx.doi.org/10.1152/ajpendo.1996.271.6.e1051.
Texte intégralPaoletti, Pierre, Edgar C. Young et Steven A. Siegelbaum. « C-Linker of Cyclic Nucleotide–gated Channels Controls Coupling of Ligand Binding to Channel Gating ». Journal of General Physiology 113, no 1 (1 janvier 1999) : 17–34. http://dx.doi.org/10.1085/jgp.113.1.17.
Texte intégralGerhardt, Maximilian J., Siegfried G. Priglinger, Martin Biel et Stylianos Michalakis. « Biology, Pathobiology and Gene Therapy of CNG Channel-Related Retinopathies ». Biomedicines 11, no 2 (19 janvier 2023) : 269. http://dx.doi.org/10.3390/biomedicines11020269.
Texte intégralThèses sur le sujet "Cyclic nucleotide-gated channel"
Cukkemane, Abhishek. « Structural and functional studies of a prokaryotic cyclic nucleotide gated channel / ». Jülich : Forschungszentrum, Zentralbibliothek, 2008. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=016779692&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.
Texte intégralSunderman, Elizabeth R. « Single-channel kinetic analysis of the allosteric transition of rod cyclic nucleotide-gated channels / ». Thesis, Connect to this title online ; UW restricted, 1998. http://hdl.handle.net/1773/10526.
Texte intégralMatulef, Kimberly Irene. « Cysteine-scanning mutagenesis of the ligand-binding domain of cyclic nucleotide-gated channels / ». Thesis, Connect to this title online ; UW restricted, 2002. http://hdl.handle.net/1773/5032.
Texte intégralLolicato, M. G. L. « STRUCTURAL STUDIES ON THE REGULATORY DOMAIN OF THREE HCN (HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-GATED) CHANNEL ISOFORMS ». Doctoral thesis, Università degli Studi di Milano, 2012. http://hdl.handle.net/2434/168356.
Texte intégralBecirovic, Elvir. « Role of the CNGB1a Subunit of the Rod Cyclic Nucleotide-Gated Channel in Channel Gating and Pathogenesis of Retinitis Pigmentosa ». Diss., lmu, 2010. http://nbn-resolving.de/urn:nbn:de:bvb:19-119088.
Texte intégralTanaka, Naoto. « A MISSENSE MUTATION IN CONE PHOTORECEPTOR CYCLIC NUCLEOTIDE-GATED CHANNELS ASSOCIATED WITH CANINE DAYLIGHT BLINDNESS OFFERS INSIGHT INTO CHANNEL STRUCTURE AND FUNCTION ». Diss., Temple University Libraries, 2013. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/246634.
Texte intégralPh.D.
Cone cyclic nucleotide-gated (CNG) channels are located in the retinal outer segments, mediating daylight color vision. The channel is a tetramer of A-type (CNGA3) and B-type (CNGB3) subunits. CNGA3 subunits are able to form homotetrameric channels, but CNGB3 exhibits channel function only when co-expressed with CNGA3. Mutations in the genes encoding these cone CNG subunits are associated with achromatopsia, an autosomal recessive genetic disorder which causes incomplete or complete loss of daylight and color vision. A missense mutation, aspartatic acid (Asp) to asparagine (Asn) at position 262 in the canine CNGB3 subunit (cB3-D262N), results in loss of cone function and therefore daylight blindness, highlighting the crucial role of this aspartic acid residue for proper channel biogenesis and/or function. Asp 262 is located in a conserved region of the second transmembrane segment containing three Asp residues designated the Tri-Asp motif. We exploit the conservation of these residues in CNGA3 subunits to examine the motif using a combination of experimental and computational approaches. Mutations of these conserved Asp residues result in a loss of nucleotide-activated currents and mislocalization in heterologous expression. Co-expressing CNGB3 Tri-Asp mutants with wild type CNGA3 results in functional channels, however, their electrophysiological characterization matches the properties of homomeric CNGA3 tetramers. This failure to record heteromeric currents implies that Asp/Asn mutations impact negatively both CNGA3 and CNGB3 subunits. A homology model of canine CNGA3 relaxed in a membrane using molecular dynamics simulations suggests that the Tri-Asp motif is involved in non-specific salt bridge pairings with positive residues of S3 - S4. We propose that the CNGB3-D262N mutation in daylight blind dogs results in the loss of these interactions and leads to an alteration of the electrostatic equilibrium in the S1 - S4 bundle. Because residues analogous to Tri-Asp residues in the voltage-gated Shaker K+ channel superfamily were implicated in monomer folding, we hypothesize that destabilizing these electrostatic interactions might impair the monomer folding state in D262N mutant CNG channels during biogenesis. Another missesnse sense mutation, Arginine (Arg) to tryptophan (Trp) at position 424 in the canine CNGA3 subunit (cA3-R424W), also results in loss of cone function. An amino acid sequence alignment with Shaker K+ channel superfamily indicates that this R424 residue is located in the C-terminal end of the sixth transmembrane segment. A3-R424W mutant channels resulted in no cyclic nucleotide-activated currents and mislocalization with intracellular aggregates. However, the localization of cA3-R424W mutant channels was not affected as severely as the Asp/Asn mutation in S2 Tri-Asp motif, showing a lot of cells with the proper localization of Golgi-like and membrane fluorescence. Moreover, the substitution of Arg 424 to Lysine (Lys), conserving the positive charge, preserved channel function in some cells, which is different from the results of the S2 Tri-Asp motif in which the Asp/Glu substitutions, conserving the negative charge, leads to loss of cyclic nucleotide-activated currents. Even though these missense mutations are both associated with canine daylight blindness, the Arg 424 residue might not be as critical for folding as the Tri-Asp residues in the S2 Tri-Asp motif and might be more of a problem in channel structure and function. The cA3 model relaxed with MD simulations indicated a possible interaction of Arg 424 with the Glu 304 residue in the S4-S5 linker. This hypothesis is supported by electrophysiological data in which the double mutation of reversing these residues, Glu 306 to Arg and Arg 424 to Glu (E306R-R424E) preserves channel function. In the model, this salt bridge appears to contribute to stabilization of the open pore state. The R424W mutation might disrupt the salt bridge formation, leading to deforming and closing the pore region.
Temple University--Theses
Schünke, Sven Verfasser], Dieter [Akademischer Betreuer] [Willbold et Lutz [Akademischer Betreuer] Schmitt. « NMR solution structures of the MloK1 cyclic nucleotide-gated ion channel binding domain / Sven Schünke. Gutachter : Lutz Schmitt. Betreuer : Dieter Willbold ». Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2011. http://d-nb.info/1015434975/34.
Texte intégralHundal, Sukhinder Paul Singh. « Molecular cloning, characterisation and function expression of cyclic nucleotide-gated ion channel genes expressed in sino-atrial node region of heart ». Thesis, University of Leicester, 1994. http://hdl.handle.net/2381/35257.
Texte intégralKimura, Koji. « Hyperpolarization-activated, cyclic nucleotide-gated HCN2 cation channel forms a protein assembly with multiple neuronal scaffold proteins in distinct modes of protein-protein interaction ». Kyoto University, 2004. http://hdl.handle.net/2433/145287.
Texte intégralArrigoni, C. « MODULATION OF PORE GATING BY ¿SENSOR¿ DOMAINS IN VOLTAGE-GATED K+ CHANNELS ». Doctoral thesis, Università degli Studi di Milano, 2013. http://hdl.handle.net/2434/215591.
Texte intégralLivres sur le sujet "Cyclic nucleotide-gated channel"
Goulding, Evan Hayward. Structure and function of the cyclic nucleotide-gated ion channels. 1994.
Trouver le texte intégralChapitres de livres sur le sujet "Cyclic nucleotide-gated channel"
Warren, René, et Robert S. Molday. « Regulation of the Rod Photoreceptor Cyclic Nucleotide-Gated Channel ». Dans Advances in Experimental Medicine and Biology, 205–23. Boston, MA : Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0121-3_12.
Texte intégralGrunwald, M. E., H. Zhong et K. W. Yau. « Cyclic Nucleotide-Gated Channels : Classification, Structure and Function, Activators and Inhibitors ». Dans Pharmacology of Ionic Channel Function : Activators and Inhibitors, 561–79. Berlin, Heidelberg : Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-57083-4_22.
Texte intégralGupta, Vivek K., Ammaji Rajala et Raju V. S. Rajala. « Ras-Associating Domain Proteins : A New Class of Cyclic Nucleotide-Gated Channel Modulators ». Dans Retinal Degenerative Diseases, 777–82. Boston, MA : Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_99.
Texte intégralFitzgerald, J. Browning, Anna P. Malykhina, Muayyad R. Al-Ubaidi et Xi-Qin Ding. « Functional Expression of Cone Cyclic Nucleotide-Gated Channel in Cone Photoreceptor-Derived 661W Cells ». Dans Advances in Experimental Medicine and Biology, 327–34. New York, NY : Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-74904-4_38.
Texte intégralDing, Xi-Qin, Alexander Matveev, Anil Singh, Naoka Komori et Hiroyuki Matsumoto. « Biochemical Characterization of Cone Cyclic Nucleotide-Gated (CNG) Channel Using the Infrared Fluorescence Detection System ». Dans Retinal Degenerative Diseases, 769–75. Boston, MA : Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_98.
Texte intégralDing, Xi-Qin, Alexander Matveev, Anil Singh, Naoka Komori et Hiroyuki Matsumoto. « Exploration of Cone Cyclic Nucleotide-Gated Channel-Interacting Proteins Using Affinity Purification and Mass Spectrometry ». Dans Retinal Degenerative Diseases, 57–65. New York, NY : Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-3209-8_8.
Texte intégralDing, Xi-Qin, J. Browning Fitzgerald, Alexander B. Quiambao, Cynthia S. Harry et Anna P. Malykhina. « Molecular Pathogenesis of Achromatopsia Associated with Mutations in the Cone Cyclic Nucleotide-Gated Channel CNGA3 Subunit ». Dans Retinal Degenerative Diseases, 245–53. New York, NY : Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_28.
Texte intégralConley, Shannon M., Xi-Qin Ding et Muna I. Naash. « RDS in Cones Does Not Interact with the Beta Subunit of the Cyclic Nucleotide Gated Channel ». Dans Retinal Degenerative Diseases, 63–70. New York, NY : Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_8.
Texte intégralMilitante, Julius D., et John B. Lombardini. « Calcium Uptake in the Rat Retina is Dependent on the Function of the Cyclic Nucleotide-Gated Channel : Pharmacologic Evidence ». Dans Advances in Experimental Medicine and Biology, 469–76. Boston, MA : Springer US, 2002. http://dx.doi.org/10.1007/0-306-46838-7_52.
Texte intégralNolan, Matthew F. « Hyperpolarization-Activated Cyclic Nucleotide Gated Channels ». Dans Encyclopedia of Computational Neuroscience, 1413–17. New York, NY : Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-6675-8_231.
Texte intégralActes de conférences sur le sujet "Cyclic nucleotide-gated channel"
Chakraborty, Sonhita. « Cyclic Nucleotide-Gated Ion Channel 2 regulates auxin signaling and homeostasis ». Dans ASPB PLANT BIOLOGY 2020. USA : ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1052927.
Texte intégralRomanenko, A. S., L. A. Lomovatskaya et N. V. Filinova. « SUBCELLULAR LOCALIZATION OF CYCLIC NUCLEOTIDE-GATED ION CHANNELS (CNGCS) IN THE POTATO ROOT CELLS IN THE BIOTIC STRESS ». Dans The Second All-Russian Scientific Conference with international participation "Regulation Mechanisms of Eukariotic Cell Organelle Functions". SIPPB SB RAS, 2018. http://dx.doi.org/10.31255/978-5-94797-318-1-106-108.
Texte intégralRapports d'organisations sur le sujet "Cyclic nucleotide-gated channel"
Miller, Gad, et Jeffrey F. Harper. Pollen fertility and the role of ROS and Ca signaling in heat stress tolerance. United States Department of Agriculture, janvier 2013. http://dx.doi.org/10.32747/2013.7598150.bard.
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