Literatura académica sobre el tema "Cyclic nucleotide-gated channel"
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Artículos de revistas sobre el tema "Cyclic nucleotide-gated channel"
Kaupp, U. Benjamin y Reinhard Seifert. "Cyclic Nucleotide-Gated Ion Channels". Physiological Reviews 82, n.º 3 (7 de enero de 2002): 769–824. http://dx.doi.org/10.1152/physrev.00008.2002.
Texto completoJames, Zachary M. y William N. Zagotta. "Structural insights into the mechanisms of CNBD channel function". Journal of General Physiology 150, n.º 2 (12 de diciembre de 2017): 225–44. http://dx.doi.org/10.1085/jgp.201711898.
Texto completoBecchetti, Andrea, Katia Gamel y Vincent Torre. "Cyclic Nucleotide–Gated Channels". Journal of General Physiology 114, n.º 3 (1 de septiembre de 1999): 377–92. http://dx.doi.org/10.1085/jgp.114.3.377.
Texto completoSanty, Lorraine C. y 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, n.º 6 (1 de diciembre de 1997): E1140—E1148. http://dx.doi.org/10.1152/ajpendo.1997.273.6.e1140.
Texto completoBej, Aritra y James B. Ames. "Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin". International Journal of Molecular Sciences 23, n.º 22 (16 de noviembre de 2022): 14143. http://dx.doi.org/10.3390/ijms232214143.
Texto completoFodor, Anthony A., Sharona E. Gordon y William N. Zagotta. "Mechanism of Tetracaine Block of Cyclic Nucleotide-gated Channels". Journal of General Physiology 109, n.º 1 (1 de enero de 1997): 3–14. http://dx.doi.org/10.1085/jgp.109.1.3.
Texto completoJames, Zachary M., Andrew J. Borst, Yoni Haitin, Brandon Frenz, Frank DiMaio, William N. Zagotta y David Veesler. "CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel". Proceedings of the National Academy of Sciences 114, n.º 17 (10 de abril de 2017): 4430–35. http://dx.doi.org/10.1073/pnas.1700248114.
Texto completoSanty, L. C. y G. Guidotti. "Reconstitution and characterization of two forms of cyclic nucleotide-gated channels from skeletal muscle". American Journal of Physiology-Endocrinology and Metabolism 271, n.º 6 (1 de diciembre de 1996): E1051—E1060. http://dx.doi.org/10.1152/ajpendo.1996.271.6.e1051.
Texto completoPaoletti, Pierre, Edgar C. Young y Steven A. Siegelbaum. "C-Linker of Cyclic Nucleotide–gated Channels Controls Coupling of Ligand Binding to Channel Gating". Journal of General Physiology 113, n.º 1 (1 de enero de 1999): 17–34. http://dx.doi.org/10.1085/jgp.113.1.17.
Texto completoGerhardt, Maximilian J., Siegfried G. Priglinger, Martin Biel y Stylianos Michalakis. "Biology, Pathobiology and Gene Therapy of CNG Channel-Related Retinopathies". Biomedicines 11, n.º 2 (19 de enero de 2023): 269. http://dx.doi.org/10.3390/biomedicines11020269.
Texto completoTesis sobre el tema "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.
Texto completoSunderman, 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.
Texto completoMatulef, 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.
Texto completoLolicato, 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.
Texto completoBecirovic, 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.
Texto completoTanaka, 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.
Texto completoPh.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 y 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.
Texto completoHundal, 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.
Texto completoKimura, 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.
Texto completoArrigoni, 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.
Texto completoLibros sobre el tema "Cyclic nucleotide-gated channel"
Goulding, Evan Hayward. Structure and function of the cyclic nucleotide-gated ion channels. 1994.
Buscar texto completoCapítulos de libros sobre el tema "Cyclic nucleotide-gated channel"
Warren, René y Robert S. Molday. "Regulation of the Rod Photoreceptor Cyclic Nucleotide-Gated Channel". En 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.
Texto completoGrunwald, M. E., H. Zhong y K. W. Yau. "Cyclic Nucleotide-Gated Channels: Classification, Structure and Function, Activators and Inhibitors". En 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.
Texto completoGupta, Vivek K., Ammaji Rajala y Raju V. S. Rajala. "Ras-Associating Domain Proteins: A New Class of Cyclic Nucleotide-Gated Channel Modulators". En Retinal Degenerative Diseases, 777–82. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_99.
Texto completoFitzgerald, J. Browning, Anna P. Malykhina, Muayyad R. Al-Ubaidi y Xi-Qin Ding. "Functional Expression of Cone Cyclic Nucleotide-Gated Channel in Cone Photoreceptor-Derived 661W Cells". En 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.
Texto completoDing, Xi-Qin, Alexander Matveev, Anil Singh, Naoka Komori y Hiroyuki Matsumoto. "Biochemical Characterization of Cone Cyclic Nucleotide-Gated (CNG) Channel Using the Infrared Fluorescence Detection System". En Retinal Degenerative Diseases, 769–75. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_98.
Texto completoDing, Xi-Qin, Alexander Matveev, Anil Singh, Naoka Komori y Hiroyuki Matsumoto. "Exploration of Cone Cyclic Nucleotide-Gated Channel-Interacting Proteins Using Affinity Purification and Mass Spectrometry". En Retinal Degenerative Diseases, 57–65. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-3209-8_8.
Texto completoDing, Xi-Qin, J. Browning Fitzgerald, Alexander B. Quiambao, Cynthia S. Harry y Anna P. Malykhina. "Molecular Pathogenesis of Achromatopsia Associated with Mutations in the Cone Cyclic Nucleotide-Gated Channel CNGA3 Subunit". En Retinal Degenerative Diseases, 245–53. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_28.
Texto completoConley, Shannon M., Xi-Qin Ding y Muna I. Naash. "RDS in Cones Does Not Interact with the Beta Subunit of the Cyclic Nucleotide Gated Channel". En Retinal Degenerative Diseases, 63–70. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_8.
Texto completoMilitante, Julius D. y John B. Lombardini. "Calcium Uptake in the Rat Retina is Dependent on the Function of the Cyclic Nucleotide-Gated Channel: Pharmacologic Evidence". En Advances in Experimental Medicine and Biology, 469–76. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/0-306-46838-7_52.
Texto completoNolan, Matthew F. "Hyperpolarization-Activated Cyclic Nucleotide Gated Channels". En 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.
Texto completoActas de conferencias sobre el tema "Cyclic nucleotide-gated channel"
Chakraborty, Sonhita. "Cyclic Nucleotide-Gated Ion Channel 2 regulates auxin signaling and homeostasis". En ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1052927.
Texto completoRomanenko, A. S., L. A. Lomovatskaya y N. V. Filinova. "SUBCELLULAR LOCALIZATION OF CYCLIC NUCLEOTIDE-GATED ION CHANNELS (CNGCS) IN THE POTATO ROOT CELLS IN THE BIOTIC STRESS". En 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.
Texto completoInformes sobre el tema "Cyclic nucleotide-gated channel"
Miller, Gad y Jeffrey F. Harper. Pollen fertility and the role of ROS and Ca signaling in heat stress tolerance. United States Department of Agriculture, enero de 2013. http://dx.doi.org/10.32747/2013.7598150.bard.
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