Academic literature on the topic 'Cyclic nucleotide binding domain'

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Journal articles on the topic "Cyclic nucleotide binding domain"

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Matthiesen, Karina, and Jacob Nielsen. "Binding of cyclic nucleotides to phosphodiesterase 10A and 11A GAF domains does not stimulate catalytic activity." Biochemical Journal 423, no. 3 (2009): 401–9. http://dx.doi.org/10.1042/bj20090982.

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To date eleven human PDE (3′,5′-cyclic nucleotide phosphodiesterase) families have been identified. Of these, five families contain non-catalytic tandem GAF (cGMP-specific and -stimulated phosphodiesterases, Anabaenaadenylate cyclases and Escherichia coliFhlA) domains, GAFa and GAFb, in the N-terminal part of the enzyme. For PDE2A, PDE5A and PDE6 the GAF domains have been shown to bind cGMP with high affinity. For PDE2A and PDE5A this ligand binding has been shown to stimulate the catalytic activity of the enzyme. PDE10A and PDE11A are the two most recently described PDEs and it has been sugge
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Lorenz, Robin, Eui-Whan Moon, Jeong Joo Kim, et al. "Mutations of PKA cyclic nucleotide-binding domains reveal novel aspects of cyclic nucleotide selectivity." Biochemical Journal 474, no. 14 (2017): 2389–403. http://dx.doi.org/10.1042/bcj20160969.

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Cyclic AMP and cyclic GMP are ubiquitous second messengers that regulate the activity of effector proteins in all forms of life. The main effector proteins, the 3′,5′-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) and the 3′,5′-cyclic guanosine monophosphate (cGMP)-dependent protein kinase (PKG), are preferentially activated by cAMP and cGMP, respectively. However, the molecular basis of this cyclic nucleotide selectivity is still not fully understood. Analysis of isolated cyclic nucleotide-binding (CNB) domains of PKA regulatory subunit type Iα (RIα) reveals that the C-t
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Lyman, Kyle A., Ye Han, Robert J. Heuermann, et al. "Allostery between two binding sites in the ion channel subunit TRIP8b confers binding specificity to HCN channels." Journal of Biological Chemistry 292, no. 43 (2017): 17718–30. http://dx.doi.org/10.1074/jbc.m117.802256.

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Tetratricopeptide repeat (TPR) domains are ubiquitous structural motifs that mediate protein–protein interactions. For example, the TPR domains in the peroxisomal import receptor PEX5 enable binding to a range of type 1 peroxisomal targeting signal motifs. A homolog of PEX5, tetratricopeptide repeat–containing Rab8b-interacting protein (TRIP8b), binds to and functions as an auxiliary subunit of hyperpolarization-activated cyclic nucleotide (HCN)–gated channels. Given the similarity between TRIP8b and PEX5, this difference in function raises the question of what mechanism accounts for their bin
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Arazi, T., B. Kaplan, R. Sunkar, and H. Fromm. "Cyclic-nucleotide- and Ca2+/calmodulin-regulated channels in plants: targets for manipulating heavy-metal tolerance, and possible physiological roles." Biochemical Society Transactions 28, no. 4 (2000): 471–75. http://dx.doi.org/10.1042/bst0280471.

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Recently we discovered a tobacco protein (designated NtCBP4) that modulates heavy-metal tolerance in transgenic plants. Structurally, NtCBP4 is similar to mammalian cyclic-nucleotide-gated non-selective cation channels containing six putative transmembrane domains, a predicted pore region, a conserved cyclic-nucleotide-binding domain, and a high-affinity calmodulin-binding site that coincides with its cyclic-nucleotide-binding domain. Transgenic tobacco expressing the plasma-membrane-localized NtCBP4 exhibit improved tolerance to Ni2+ and hypersensitivity to Pb2+, which are associated with a d
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Sunderman, Elizabeth R., and William N. Zagotta. "Sequence of Events Underlying the Allosteric Transition of Rod Cyclic Nucleotide–gated Channels." Journal of General Physiology 113, no. 5 (1999): 621–40. http://dx.doi.org/10.1085/jgp.113.5.621.

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Activation of cyclic nucleotide–gated (CNG) ion channels involves a conformational change in the channel protein referred to as the allosteric transition. The amino terminal region and the carboxyl terminal cyclic nucleotide–binding domain of CNG channels have been shown to be involved in the allosteric transition, but the sequence of molecular events occurring during the allosteric transition is unknown. We recorded single-channel currents from bovine rod CNG channels in which mutations had been introduced in the binding domain at position 604 and/or the rat olfactory CNG channel amino termin
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Zbik, Tobias. "Dynamic Conformational Changes in a Cyclic Nucleotide-Binding Domain." Biophysical Journal 112, no. 3 (2017): 203a. http://dx.doi.org/10.1016/j.bpj.2016.11.1122.

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James, Zachary M., Andrew J. Borst, Yoni Haitin, et al. "CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel." Proceedings of the National Academy of Sciences 114, no. 17 (2017): 4430–35. http://dx.doi.org/10.1073/pnas.1700248114.

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Cyclic nucleotide-gated (CNG) and hyperpolarization-activated cyclic nucleotide-regulated (HCN) ion channels play crucial physiological roles in phototransduction, olfaction, and cardiac pace making. These channels are characterized by the presence of a carboxyl-terminal cyclic nucleotide-binding domain (CNBD) that connects to the channel pore via a C-linker domain. Although cyclic nucleotide binding has been shown to promote CNG and HCN channel opening, the precise mechanism underlying gating remains poorly understood. Here we used cryoEM to determine the structure of the intact LliK CNG chan
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Schünke, Sven, Justin Lecher, Matthias Stoldt, U. Benjamin Kaupp, and Dieter Willbold. "Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain." Biomolecular NMR Assignments 4, no. 2 (2010): 147–50. http://dx.doi.org/10.1007/s12104-010-9231-z.

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Schünke, Sven, and Matthias Stoldt. "Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels." Biological Chemistry 394, no. 11 (2013): 1439–51. http://dx.doi.org/10.1515/hsz-2013-0228.

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Abstract Cyclic nucleotide-binding domains (CNBDs) that are present in various channel proteins play crucial roles in signal amplification cascades. Although atomic resolution structures of some of those CNBDs are available, the detailed mechanism by which they confer cyclic nucleotide-binding to the ion channel pore remains poorly understood. In this review, we describe structural insights about cyclic nucleotide-binding-induced conformational changes in CNBDs and their potential coupling with channel gating.
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Paoletti, Pierre, Edgar C. Young, and 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 (1999): 17–34. http://dx.doi.org/10.1085/jgp.113.1.17.

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Cyclic nucleotide–gated channels are composed of a core transmembrane domain, structurally homologous to the voltage-gated K+ channels, and a cytoplasmic ligand-binding domain. These two modules are joined by ∼90 conserved amino acids, the C-linker, whose precise role in the mechanism of channel activation by cyclic nucleotides is poorly understood. We examined cyclic nucleotide–gated channels from bovine photoreceptors and Caenorhabditis elegans sensory neurons that show marked differences in cyclic nucleotide efficacy and sensitivity. By constructing chimeras from these two channels, we iden
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Dissertations / Theses on the topic "Cyclic nucleotide binding domain"

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Matulef, 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.

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Akhavan, Armin. "A conserved determinant of Ion channel trafficking localized to the cyclic nucleotide binding domain : implication for disease." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=84980.

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The Cyclic Nucleotide Binding Domain (CNBD) is conserved in a number of ion channels that belong to three distinct families, the Ether-A-Go-go (EAG); the Cyclic Nucleotide Gated (CNG) and the Hyperpolarization activated Cyclic Nucleotide modulated (HCN) channel families. Extensive biophysical characterizations have established that the function of these channels is directly modulated by cyclic nucleotides in a manner independent of kinase activity and channel phosphorylation. However, the role for this domain in the EAG family is unclear. In addition, although the biophysical properties
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Wu, Albert Ya-Po. "Molecular mechanism of cyclic nucleotide binding to the GAF domains of phosphodiesterases 2 and 5 /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/5012.

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Schünke, Sven Verfasser], Dieter [Akademischer Betreuer] [Willbold, and 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.

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Arrigoni, 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.

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Many proteins in nature show a modular topology, because it is possible to recognize functional modules responsible of distinguishable functions in the protein. Voltage-gated can be considered modular proteins. The superfamily of voltage-gated channels is composed of channels in which a pore-module is in charge of generating an ion conductance across the cell membrane, and other “sensor”-modules perceive different stimuli and transmit them to the pore, readjusting the conductance in response to changes within the cell. The sensor module in voltage-gated channels is the voltage sensing domain.
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Chow, Sarah Sue Wen. "Energetic and structural impact of cyclic nucleotide binding to hyperpolarization-activated cyclic nucleotide-gated channels." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/44980.

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Hyperpolarization-activated Cyclic Nucleotide-gated, HCN, channels contribute to the membrane potential of excitable cells including pacemaker cells of the heart and neurons in the brain. By binding to the inner side of the HCN channel, cAMP facilitates channel opening, but the underlying mechanism has been mainly inferred from relating cAMP concentration to the degree of facilitation. Concentration-response relations reflect the tightly coupled process of cAMP binding and channel opening. The strength of binding and how it is linked to channel opening is not known. Furthermore, cAMP facilit
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Watson, Dorothy M. A. "Cyclic nucleotide binding and oncogene expression in breast cancer." Thesis, University of Edinburgh, 1989. http://hdl.handle.net/1842/19398.

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Kakraba, Samuel. "A Hierarchical Graph for Nucleotide Binding Domain 2." Digital Commons @ East Tennessee State University, 2015. https://dc.etsu.edu/etd/2517.

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One of the most prevalent inherited diseases is cystic fibrosis. This disease is caused by a mutation in a membrane protein, the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is known to function as a chloride channel that regulates the viscosity of mucus that lines the ducts of a number of organs. Generally, most of the prevalent mutations of CFTR are located in one of two nucleotide binding domains, namely, the nucleotide binding domain 1 (NBD1). However, some mutations in nucleotide binding domain 2 (NBD2) can equally cause cystic fibrosis. In this work, a hierarchical gr
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Gao, Enoch N. (Enoch Nuo). "Post-translational lipid modification and nucleotide binding of Myelin 2',3'-Cyclic Nucleotide 3'-Phosphodiesterase (CNP)." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=23889.

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The myelin protein CNP $(2 sp prime,3 sp prime$-Cyclic Nucleotide 3$ sp prime$-Phosphodiesterase) is thio-palmitoylated. Since acylation plays an important role in the protein-membrane interaction, CNP palmitoylation was further investigated. Seven cysteine residues in CNP were individually converted into serines and the palmitoylation was analyzed in either COS-7 cells or an in vitro acylation reaction. No single Cys to Ser mutation could reduce substantially the level of palmitoylation, which may indicate that the turnover of palmitate on CNP is high and that there are multiple palmitoylatio
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Sekharan, Monica R. "Structural studies of the cGMP-binding GAF domain of PDE5A /." Thesis, Connect to this title online; UW restricted, 2004. http://hdl.handle.net/1773/8502.

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Books on the topic "Cyclic nucleotide binding domain"

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Grondin, Ronald Thomas. Expression, purification, refolding, and ATP binding of the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator. National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Abu-Abed, Mona. Characterization of the nucleotide binding domain of the sarco(endo)plasmic reticulum Ca2+-ATPase: Probing effects of nucleotide by NMR. 2004.

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Book chapters on the topic "Cyclic nucleotide binding domain"

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Dever, Thomas E., and William C. Merrick. "The GTP-Binding Domain Revisited." In The Guanine — Nucleotide Binding Proteins. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_4.

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Lee, Vincent T. "Detection of Cyclic Dinucleotide Binding Proteins." In Microbial Cyclic Di-Nucleotide Signaling. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-33308-9_7.

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Chou, Shan-Ho, and Michael Y. Galperin. "Noncanonical Cyclic di-GMP Binding Modes." In Microbial Cyclic Di-Nucleotide Signaling. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-33308-9_8.

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Bellini, Dom, Andrew Hutchin, Odel Soren, Jeremy S. Webb, Ivo Tews, and Martin A. Walsh. "Structure and Regulation of EAL Domain Proteins." In Microbial Cyclic Di-Nucleotide Signaling. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-33308-9_2.

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Dove, Stefan. "Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites." In Non-canonical Cyclic Nucleotides. Springer International Publishing, 2015. http://dx.doi.org/10.1007/164_2015_34.

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Jacquet, Michel, Jacques Camonis, Emmanuelle Boy-Marcotte, Faten Damak, and Hervé Garreau. "The Cyclic Amp Producing Pathway in Saccharomyces Cerevisiae Involves CDC25 and ras Genes Products." In The Guanine — Nucleotide Binding Proteins. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_23.

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Morais-Cabral, João Henrique. "Gating of Potassium Channels by Cyclic Nucleotide Binding." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_473.

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Anborgh, Pieter H., Robbert H. Cool, Eric Jacquet, Michael Jensen, Giuseppe Parlato, and Andrea Parmeggiani. "Structure-Function Relationships of The Gtp-Binding Domain of Elongation Factor Tu." In The Guanine — Nucleotide Binding Proteins. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_7.

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Pingoud, Alfred, Uwe Pieper, Roger Busche, et al. "Structural And Functional Studies on c-P21, v-P21 and the Genetically Engineered Guanine Nucleotide Binding Domain of EF-Tu." In The Guanine — Nucleotide Binding Proteins. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_21.

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Wolfe, Lynn, Terry A. Woodford, Sharron H. Francis, and Jackie D. Corbin. "Direct Involvement of the Cyclic Nucleotide Binding Sites in the Cyclic-Nucleotide-Induced Charge Shift of Protein Kinases." In Activation and Desensitization of Transducing Pathways. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-83618-3_8.

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Conference papers on the topic "Cyclic nucleotide binding domain"

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Liao, Jung-Chi, and George Oster. "The Engines of Biomolecular Motors." In ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46094.

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The majority of biomolecular motors are powered by nucleoside triphosphate (NTP), especially adenosine triphosphate (ATP). These motors consist of a β-sheet with highly conserved motifs and the nucleotide binding domain around it. The highly conserved protein folds are the engines of these motors, which convert the energy of NTP hydrolysis cycle to mechanical work. Although functions of molecular motors are widely diverse, (including cargo movement, DNA unwinding, protein degradation, ion pumping, etc), the nucleotide binding domains are very similar. In the binding site, NTP undergoes a hydro
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Ueno, H., T. Yasunaga, C. Shingyoji, T. Yamaguchi, and K. Hirose. "Dynein Pulls Microtubules Without Rotating Its Stalk." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206430.

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Dynein is a motor protein that hydrolyses ATP and moves toward the minus end of a microtubule (MT). A dynein molecule has one to three heavy chains, each consisting of three domains: a head, a stalk and a tail. ATP is bound and hydrolysed in the head, which has a ring-like structure composed of 6 AAA+ domains. The stalk is an antiparallel coiled-coil, 10–15 nm long, and has a nucleotide-dependent MT-binding domain at the tip (1) (Fig. 1). It has been proposed that the nucleotide-dependent binding affinity of the tubulin-binding site at the tip of the stalk is modulated by the two alpha helices
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Cheung, Tracy M., and George A. Truskey. "Aging Endothelial Cells Exhibit Decreased Response to Atheroprotective Shear Stress." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14402.

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As endothelial cells (ECs) age, morphological and physiological changes occur that may alter macromolecular transport and cause subsequent disease development. ECs in atherosclerotic regions exhibit high cell turnover and high levels of oxidative stress due to transient flow patterns and low and oscillating shear stress. This leads to replicative or stress-induced senescence. Resveratrol indirectly reverses senescence-associated phenotypes via competitive inhibition of cAMP-degrading phosphodiesterases (PDEs). Elevated levels of membrane-associated cAMP activate the cyclic AMP-regulated guanos
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Hsu, You-Ren, Geng-Yen Lee, Jen-Inn Chyi, et al. "Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors." In 2012 IEEE Sensors. IEEE, 2012. http://dx.doi.org/10.1109/icsens.2012.6411277.

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Jakobs, K. H., P. Gierschik, and R. Grandt. "THE ROLE OF GTP-BINDING PROTEINS EXHIBITING GTPase ACTIVITY IN PLATELET ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644773.

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Activation of platelets by agonists acting via cell surface-located receptors apparently involves as an early event in transmembrane signalling an interaction of the agonist-occupied receptor with a guanine nucleotide-binding regulatory protein (G-protein). The activated G-protein, then, transduces the information to the effector molecule, being responsible for the changes in intracellular second messengers. At least two changes in intracellular signal molecules are often found to be associated with platelet activation by agonists, i.e., increases in inositol trisphosphate and diacylglycerol l
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Geddes, V. A., G. V. Louie, G. D. Brayer, and R. T. A. MacGillivray. "MOLECULAR BASIS OF HEMOPHILIA B: IDENTIFICATION OF THE DEFECT IN FACTOR IX VANCOUVER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643872.

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Factor IX Vancouver (fIX-V) is the cause of a moderate form of hemophilia B. An individual presenting with this disorder had 2.6% of normal procoagulant activity in his plasma but had 62% of the normal factor IX antigen level. Specific antibodies showed that fIX-V contains epitopes for both the heavy and light chains of factor IXa. To identify the defect involved, DNA was isolated from the lymphocytes of the male hemophiliac. Southern blot analysis using a full-length factor IX cDNA as a hybridization probe showed no gross differences between the fIX-V gene and the normal factor IX gene. The D
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Stenflo, J., A.-K. öhlin, Å. Lundvall та B. Dahlback. "β-HYDROXY ASPARTIC ACID AND ft-HYDROXYASPARAGINE IN THEEGF-HOMOLOGY REGIONS OF PROTEIN C AND PROTEINS". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643995.

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The amino acid sequence has been determined for all of the vitamin K-dependent proteins and the gene structure is known for some of them. These findings have shown the proteins to consist of four clearly discernible domains, except protein S which has six domains. The protein domains seem to be coded on separate exons (Foster, D. C. et. al. 1985 Proc. Natl. Acad. Sci. USA 82,4673). The vitamin K-dependent γ-carboxyglutamic acid (Gla) containing domain isthe common structural denominator of the members of this protein family. In addition, all of these proteins except prothrombin contain domains
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Beeler, D., L. Fritze, G. Soff, R. Jackman, and R. Rosenberg. "HUMAN THROMBOMODULIN cDNA:SEQUENCE AND TRANSLATED STRUCTURE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643967.

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A 750 bp bovine Thrombomodulin (TM) cDNA fragment was used as an hybridization probe to screen an oligo-dT primed Lambda gtll. cDNA library prepared from human umbilical vein endothelial cell mRNA. A 2.4 kb positive human clone was isolated which showed an 80% nucleotide sequence homology with bovine TM cDNA. This clone and a 550 bp fragment from its 5' end were used to further screen the oligo-dT primed library as well as randomly primed library prepared from the same mRNA. The cDNA clones obtained allow us to describe the overall structure of human TM and reveal that it is extremely similar
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Hawiger, J. "PLATELET RECEPTOR RECOGNITION DOMAINS AND THEIR SYNTHETIC PEPTIDE ANALOGS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643726.

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Adhesive molecules and their receptorsplay an essential role in hemostasis and thrombosis. Platelet thrombi are formed through the interaction of cell adhesion molecules (CAMs) with intercellular adhesion molecules (IAMs)and substrate adhesion molecules (SAMs). Platelet CAMs encompass membrane glycoproteins lb, lib, Ilia,and possibly la and IV, which constitutemembrane receptors for IAMs(e.g., fibrinogen) and for SAMs encompassingvon Willebrand Factor (vWF), fibronectin, vitronectin, collagen, and thrcmbospondin. Receptorfunction of platelet CAMs can be specific,i.e., only one adhesive protein
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Reports on the topic "Cyclic nucleotide binding domain"

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Fluhr, Robert, and Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7697123.bard.

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Innate immune responses in animals and plants involve receptors that recognize microbe-associated molecules. In plants, one set of this defense system is characterized by large families of TIR–nucleotide binding site–leucine-rich repeat (TIR-NBS-LRR) resistance genes. The direct interaction between plant proteins harboring the TIR domain with proteins that transmit and facilitate a signaling pathway has yet to be shown. The Arabidopsis genome encodes TIR-domain containing genes that lack NBS and LRR whose functions are unknown. Here we investigated the functional role of such protein, TLW1 (TI
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Joel, Daniel M., Steven J. Knapp, and Yaakov Tadmor. Genomic Approaches for Understanding Virulence and Resistance in the Sunflower-Orobanche Host-Parasite Interaction. United States Department of Agriculture, 2011. http://dx.doi.org/10.32747/2011.7592655.bard.

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Oroginal Objectives: (i) identify DNA markers linked to the avirulence (Avr) locus and locate the Avr locus through genetic mapping with an inter-race Orobanche cumana population; (ii) develop high-throughput fingerprint DNA markers for genotypingO. cumana races; (iii) identify nucleotide binding domain leucine rich repeat (NB-LRR) genes encoding R proteins conferring resistance to O. cumana in sunflower; (iv) increase the resolution of the chromosomal segment harboring Or₅ and related R genes through genetic and physical mapping in previously and newly developed mapping populations of sunflow
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