Academic literature on the topic 'POLYAMINE RECEPTORS'

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Journal articles on the topic "POLYAMINE RECEPTORS"

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WILLIAMS, Keith. "Interactions of polyamines with ion channels." Biochemical Journal 325, no. 2 (July 15, 1997): 289–97. http://dx.doi.org/10.1042/bj3250289.

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Endogenous polyamines, in particular spermine, have been found to cause block and modulation of a number of types of ion channel. Intracellular spermine is responsible for intrinsic gating and rectification of strong inward rectifier K+ channels by directly plugging the ion channel pore. These K+ channels control the resting membrane potential in both excitable and non-excitable cells, and control the excitability threshold in neurons and muscle cells. Intracellular spermine causes inward rectification at some subtypes of Ca2+-permeable glutamate receptors in the central nervous system, again by plugging the receptor channel pore, and spermine can even permeate the ion channel of these receptors. Extracellular spermine has multiple effects at the N-methyl-D-aspartate (NMDA) subtype of glutamate receptor, including stimulation that increases the size of NMDA receptor currents, and voltage-dependent block. A number of polyamine-conjugated arthropod toxins and synthetic polyamine analogues are potent antagonists of glutamate receptors, and represent new tools with which to study these receptors. Interactions of polyamines with other types of cation channels have been reported. This area of research represents a new biology and a new pharmacology of polyamines.
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Liu, Lan, Rachel Santora, Jaladanki N. Rao, Xin Guo, Tongtong Zou, Huifang M. Zhang, Douglas J. Turner, and Jian-Ying Wang. "Activation of TGF-β-Smad signaling pathway following polyamine depletion in intestinal epithelial cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 285, no. 5 (November 2003): G1056—G1067. http://dx.doi.org/10.1152/ajpgi.00151.2003.

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Smad proteins are transcription activators that are critical for transmitting transforming growth factor-β (TGF-β) superfamily signals from the cell surface receptors to the nucleus. Our previous studies have shown that cellular polyamines are essential for normal intestinal mucosal growth and that a decreased level of polyamines inhibits intestinal epithelial cell proliferation, at least partially, by increasing expression of TGF-β/TGF-β receptors. The current study went further to determine the possibility that Smads are the downstream intracellular effectors of activated TGF-β/TGF-β receptor signaling following polyamine depletion. Studies were conducted in IEC-6 cells derived from rat small intestinal crypts. Depletion of cellular polyamines by α-difluoromethylornithine (DFMO) increased basal levels of Smad3 and Smad4 proteins, induced their nuclear translocation, and stimulated Smad sequence-specific DNA-binding activity. Polyamine depletion-induced Smads were also associated with a significant increase in transcription activation as measured by luciferase reporter gene activity of Smad-dependent promoters. Inhibition of Smads by a dominant-negative mutant Smad4 in the DFMO-treated cells prevented the increased Smad transcription activation. Polyamine-deficient cells highly expressed TGF-β and were growth-arrested at the G1 phase. Inhibition of TGF-β by treatment with either immunoneutralizing anti-TGF-β antibody or TGF-β antisense oligodeoxyribonucleotides not only blocked the induction of Smad activity but also decreased the Smad-mediated transcriptional activation in polyamine-depleted cells. These findings suggest that Smads are involved in the downstream cellular processes mediated by cellular polyamines and that increased TGF-β/TGF-β receptor signaling following polyamine depletion activates Smads, thus resulting in the stimulation of Smad target gene expression.
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Santos, M. F., M. J. Viar, S. A. McCormack, and L. R. Johnson. "Polyamines are important for attachment of IEC-6 cells to extracellular matrix." American Journal of Physiology-Gastrointestinal and Liver Physiology 273, no. 1 (July 1, 1997): G175—G183. http://dx.doi.org/10.1152/ajpgi.1997.273.1.g175.

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The inhibition of ornithine decarboxylase, a rate-limiting enzyme of polyamine biosynthesis, with alpha-difluoromethylornithine in IEC-6 cells (small intestinal crypt cell line) reduces cell migration by 70%, inhibits protein cross-linking, and affects the cytoskeletal assembly. The current study examines the effects of intracellular polyamine depletion on attachment of IEC-6 cells to different matrices. Polyamine deficiency inhibited cell attachment to plastic, laminin, fibronectin, collagen IV, and Matrigel by different extents. Intracellular putrescine restored attachment to all matrices. The presence of a specific inhibitor of protein cross-linking also inhibited attachment to laminin in a dose-dependent manner. The inhibition of cell attachment to plastic and Matrigel was correlated with the inhibition of cell migration. Immunofluorescence studies showed that polyamines are essential for the correct expression of the integrin subunit alpha 2 but not for the expression of the alpha 1-subunit. This study demonstrates that polyamines are important for cell attachment and expression of the integrin alpha 2 beta 1, a putative receptor for collagen and laminin. The impairment of protein cross-linking and the inhibition of the expression of cell surface receptors that bind extracellular matrix (ECM) proteins may be part of the mechanism by which polyamine deficiency retards cell migration in the small intestine.
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Sedwick, Caitlin. "Uncorking AMPA receptors." Journal of General Physiology 150, no. 1 (December 12, 2017): 1. http://dx.doi.org/10.1085/jgp.201711966.

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Maeda, Yutaka, Christophe Rachez, Leo Hawel, Craig V. Byus, Leonard P. Freedman, and Frances M. Sladek. "Polyamines Modulate the Interaction between Nuclear Receptors and Vitamin D Receptor-Interacting Protein 205." Molecular Endocrinology 16, no. 7 (July 1, 2002): 1502–10. http://dx.doi.org/10.1210/mend.16.7.0883.

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Abstract Nuclear receptors (NR) activate transcription by interacting with several different coactivator complexes, primarily via LXXLL motifs (NR boxes) of the coactivator that bind a common region in the ligand binding domain of nuclear receptors (activation function-2, AF–2) in a ligand-dependent fashion. However, how nuclear receptors distinguish between different sets of coactivators remains a mystery, as does the mechanism by which orphan receptors such as hepatocyte nuclear factor 4α (HNF4α) activate transcription. In this study, we show that HNF4α interacts with a complex containing vitamin D receptor (VDR)-interacting proteins (DRIPs) in the absence of exogenously added ligand. However, whereas a full-length DRIP205 construct enhanced the activation by HNF4α in vivo, it did not interact well with the HNF4α ligand binding domain in vitro. In investigating this discrepancy, we found that the polyamine spermine significantly enhanced the interaction between HNF4α and full-length DRIP205 in an AF-2, NR-box-dependent manner. Spermine also enhanced the interaction of DRIP205 with the VDR even in the presence of its ligand, but decreased the interaction of both HNF4α and VDR with the p160 coactivator glucocorticoid receptor interacting protein 1 (GR1P1). We also found that GR1P1 and DRIP205 synergistically activated HNF4α-mediated transcription and that a specific inhibitor of polyamine biosynthesis, α-difluoromethylornithine (DFMO), decreased the ability of HNF4α to activate transcription in vivo. These results lead us to propose a model in which polyamines may facilitate the switch between different coactivator complexes binding to NRs.
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Pina, Fernando, M. Alexandra Bernardo, and Enrique García-España. "Fluorescent Chemosensors Containing Polyamine Receptors." European Journal of Inorganic Chemistry 2000, no. 10 (October 2000): 2143–57. http://dx.doi.org/10.1002/1099-0682(200010)2000:10<2143::aid-ejic2143>3.0.co;2-3.

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Grzelakowska-Sztabert, B., M. Dudkowska, and M. Manteuffel-Cymborowska. "Nuclear and membrane receptor-mediated signalling pathways modulate polyamine biosynthesis and interconversion." Biochemical Society Transactions 35, no. 2 (March 20, 2007): 386–90. http://dx.doi.org/10.1042/bst0350386.

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Polyamines play an important role in cell growth and differentiation, while their overproduction has potentially oncogenic consequences. Polyamine homoeostasis, a critical determinant of cell fate, is precisely tuned at the level of biosynthesis, degradation and transport. The enzymes ODC (ornithine decarboxylase), AdoMetDC (S-adenosylmethionine decarboxylase) and SSAT (spermidine/spermine N1-acetyltransferase) are critical for polyamine pool maintenance. Our experiments were designed to examine the expression of these enzymes in testosterone-induced hypertrophic and antifolate-induced hyperplastic mouse kidney, characterized by activation of AR (androgen receptor) and HGF (hepatocyte growth factor) membrane receptor c-Met respectively. The expression of these key enzymes was up-regulated by antifolate CB 3717 injury-evoked activation of HGF/c-Met signalling. In contrast, activation of the testosterone/AR pathway remarkably induced a selective increase in ODC expression without affecting other enzymes. Studies in catecholamine-depleted kidneys point to a synergistic interaction between the signalling pathways activated via cell membrane catecholamine receptors and AR, as well as c-Met. We found that this cross-talk modulated the expression of ODC and AdoMetDC, enzymes limiting polyamine biosynthesis, but not SSAT. This is in contrast with the antagonistic cross-talk between AR- and c-Met-mediated signalling which negatively regulated the expression of ODC, but affected neither AdoMetDC nor SSAT.
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Chen, Jie, Jaladanki N. Rao, Tongtong Zou, Lan Liu, Bernard S. Marasa, Lan Xiao, Xing Zeng, Douglas J. Turner, and Jian-Ying Wang. "Polyamines are required for expression of Toll-like receptor 2 modulating intestinal epithelial barrier integrity." American Journal of Physiology-Gastrointestinal and Liver Physiology 293, no. 3 (September 2007): G568—G576. http://dx.doi.org/10.1152/ajpgi.00201.2007.

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The Toll-like receptors (TLRs) allow mammalian intestinal epithelium to detect various microbes and activate innate immunity after infection. TLR2 and TLR4 have been identified in intestinal epithelial cells (IECs) as fundamental components of the innate immune response to bacterial pathogens, but the exact mechanism involved in control of TLR expression remains unclear. Polyamines are implicated in a wide variety of biological functions, and regulation of cellular polyamines is a central convergence point for the multiple signaling pathways driving different epithelial cell functions. The current study determined whether polyamines regulate TLR expression, thereby modulating intestinal epithelial barrier function. Depletion of cellular polyamines by inhibiting ornithine decarboxylase (ODC) with α-difluoromethylornithine decreased levels of TLR2 mRNA and protein, whereas increased polyamines by ectopic overexpression of the ODC gene enhanced TLR2 expression. Neither intervention changed basal levels of TLR4. Exposure of normal IECs to low-dose (5 μg/ml) LPS increased ODC enzyme activity and stimulated expression of TLR2 but not TLR4, while polyamine depletion prevented this LPS-induced TLR2 expression. Decreased TLR2 in polyamine-deficient cells was associated with epithelial barrier dysfunction. In contrast, increased TLR2 by the low dose of LPS enhanced epithelial barrier function, which was abolished by inhibition of TLR2 expression with specific, small interfering RNA. These results indicate that polyamines are necessary for TLR2 expression and that polyamine-induced TLR2 activation plays an important role in regulating epithelial barrier function.
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Wu, Guoyao, Nick E. Flynn, and Darrell A. Knabe. "Enhanced intestinal synthesis of polyamines from proline in cortisol-treated piglets." American Journal of Physiology-Endocrinology and Metabolism 279, no. 2 (August 1, 2000): E395—E402. http://dx.doi.org/10.1152/ajpendo.2000.279.2.e395.

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This study was conducted to determine a role for cortisol in regulating intestinal ornithine decarboxylase (ODC) activity and to identify the metabolic sources of ornithine for intestinal polyamine synthesis in suckling pigs. Thirty-two 21-day-old suckling pigs were randomly assigned to one of four groups with eight animals each and received daily intramuscular injections of vehicle solution (sesame oil; control), hydrocortisone 21-acetate (HYD; 25 mg/kg body wt), RU-486 (10 mg/kg body wt, a potent blocker of glucocorticoid receptors), or HYD plus RU-486 for two consecutive days. At 29 days of age, pigs were killed for preparation of jejunal enterocytes. The cytosolic fraction was prepared for determining ODC activity. For metabolic studies, enterocytes were incubated for 45 min at 37°C in 2 ml of Krebs-bicarbonate buffer (pH 7.4) containing 1 mM [U-14C]arginine, 1 mM [U-14C]ornithine, 1 mM [U-14C]glutamine, or 1 mM [U-14C]proline plus 1 mM glutamine. Cortisol administration increased intestinal ODC activity by 230%, polyamine (putrescine, spermidine, and spermine) synthesis from ornithine and proline by 75–180%, and intracellular polyamine concentrations by 45–83%. Polyamine synthesis from arginine was not detected in enterocytes of control pigs but was induced in cells of cortisol-treated pigs. There was no detectable synthesis of polyamines from glutamine in enterocytes of all groups of pigs. The stimulating effects of cortisol on intestinal ODC activity and polyamine synthesis were abolished by coadministration of RU-486. Our data indicate that an increase in plasma cortisol concentrations stimulates intestinal polyamine synthesis via a glucocorticoid receptor-mediated mechanism and that proline (an abundant amino acid in milk) is a major source of ornithine for intestinal polyamine synthesis in suckling neonates.
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Wilding, Timothy J., Kevin Chen, and James E. Huettner. "Fatty acid modulation and polyamine block of GluK2 kainate receptors analyzed by scanning mutagenesis." Journal of General Physiology 136, no. 3 (August 30, 2010): 339–52. http://dx.doi.org/10.1085/jgp.201010442.

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RNA editing of kainate receptor subunits at the Q/R site determines their susceptibility to inhibition by cis-unsaturated fatty acids as well as block by cytoplasmic polyamines. Channels comprised of unedited (Q) subunits are strongly blocked by polyamines, but insensitive to fatty acids, such as arachidonic acid (AA) and docosahexaenoic acid (DHA), whereas homomeric edited (R) channels resist polyamine block but are inhibited by AA and DHA. In the present study, we have analyzed fatty acid modulation of whole-cell currents mediated by homomeric recombinant GluK2 (formerly GluR6) channels with individual residues in the pore-loop, M1 and M3 transmembrane helices replaced by scanning mutagenesis. Our results define three abutting surfaces along the M1, M2, and M3 helices where gain-of-function substitutions render GluK2(Q) channels susceptible to fatty acid inhibition. In addition, we identify four locations in the M3 helix (F611, L614, S618, and T621) at the level of the central cavity where Arg substitution increases relative permeability to chloride and eliminates polyamine block. Remarkably, for two of these positions, L614R and S618R, exposure to fatty acids reduces the apparent chloride permeability and potentiates whole-cell currents ∼5 and 2.5-fold, respectively. Together, our results suggest that AA and DHA alter the orientation of M3 in the open state, depending on contacts at the interface between M1, M2, and M3. Moreover, our results demonstrate the importance of side chains within the central cavity in determining ionic selectivity and block by cytoplasmic polyamines despite the inverted orientation of GluK2 as compared with potassium channels and other pore-loop family members.
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Dissertations / Theses on the topic "POLYAMINE RECEPTORS"

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Shao, Zuoyi. "The effect of polyamine amide toxins and polyamines in nicotinic acetylcholine receptors of the TE671 cell line." Thesis, University of Nottingham, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338532.

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Brackley, Philip T. H. "Properties of vertebrate glutamate receptors expressed In Xenopus oocytes and their interactions with polyamine-containing toxins." Thesis, University of Nottingham, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335702.

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Ring, Joshua Roderick. "SYNTHETIC AROMATIC AGMATINE ANALOGS AS ALLOSTERIC MODULATORS OF THE N-METHYL-D-ASPARTATE (NMDA) RECEPTOR CHANNEL." UKnowledge, 2006. http://uknowledge.uky.edu/gradschool_diss/413.

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The N-methyl-D-aspartate (NMDA) receptors are highly regulated ligand-gated ion channels, which are affected by many substrates. Overactivation of the NMDA receptor can lead to hyperexcitability and a number of neurotoxic effects and neurological diseases. Agmatine has been demonstrated to act allosterically as an inhibitory modulator at the polyamine recognition sites of the NMDA receptor complex. The present study synthesized and evaluated a library of agmatine analogs for their ability to displace tritiated MK-801 from NMDARs in P2 membrane preparations from rat brains at ligand concentrations of 1 mM and 50 uM. A full dose-response curve was generated for the most active compounds, in the presence and absence of a pathological level of spermidine (100 uM). A forty-five member subset of arylidenamino-guanidino compounds was synthesized and all were demonstrated to be NMDA receptor inhibitory modulators in the above assay. Three of these compounds generated biphasic curves, indicating activity at two binding sites: the postulated high-affinity agmatine binding site, and a low-affinity site (perhaps the channel itself). (4-Chlorobenzylidenamino)-guanidine hydrochloride demonstrated an IC50 of 3.6 uM at the former site and 124.5 uM at the latter. Several computer models were generated to direct further synthesis. Based on the structure-activity relationship of the arylidenamino-guanidino compounds, a pharmacophore model of the agmatine binding site of the NMDAR was proposed.
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O'Sullivan, M. C. "Synthesis of certain polyamines and their application in polyamine-receptor studies." Thesis, University of Newcastle Upon Tyne, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233291.

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Fenniri, Hicham. "Polyamines macrocycliques : recepteurs et catalyseurs biomimetiques." Université Louis Pasteur (Strasbourg) (1971-2008), 1994. http://www.theses.fr/1994STR13014.

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Les proprietes physico-chimiques des polyamines macrocycliques font de cette classe de molecules les candidats de choix pour la mise au point de recepteurs et de catalyseurs biomimetiques. Les deux premiers chapitres de cette these, introduisent les concepts de la catalyse supramoleculaire et les proprietes des polyamines. Le troisieme chapitre est consacre a l'etude des proprietes de complexation d'une nouvelle sonde fluorescente pour l'atp, qui s'est averee etre aussi un excellent recepteur pour le nadph. Nous avons egalement mis au point un systeme dans lequel une kinase artificielle fonctionne in situ avec des enzymes naturelles, par couplage energetique; cette etude constitue le premier exemple de couplage entre une enzyme artificielle et des enzymes naturelles; ces etudes ainsi que d'autres sur le mecanisme de transfert de phosphoryle catalyse par la kinase artificielle ont fait l'objet du quatrieme chapitre. Dans les cinquieme et sixieme chapitres nous avons demontre que les polyamines macrocycliques pouvaient activer des molecules tels que le malonate, le pyruvate, et l'acetoacetate, par des mecanismes biomimetiques. L'echange proton/deuterium du malonate a pu etre accelere plus de deux cent cinquante mille fois, et celui du pyruvate plus de huit mille fois
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Mitchinson, Andrew. "New synthetic routes to polyamines and their use in receptor studies." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.481468.

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Davachi, David Hadi. "Intracellular polyamines cause the voltage-dependent block of nicotine acetylcholine receptors in native neurons." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=32988.

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The polyamines spermine and spermidine are found ubiquitously in all mammalian cells where they play a role in a variety of cellular processes. In recent years, the interaction of polyamines with a number of structurally and functionally distinct cation channels has been described. These studies have shown that intracellular polyamines cause a voltage-dependent block of currents from inwardly rectifying K+ channels, AMPA and kainate type glutamate receptors, and neuronal nicotinic acetylcholine receptors. As result of the voltage-dependent polyamine block, these channels conduct current at negative membrane potentials but do not conduct current at positive membrane potentials. This property is termed inward rectification and likely plays an important role in the function of these channels.
The focus of my thesis has been to study the polyamine mediated inward rectification of neuronal nicotinic acetylcholine receptors (nAChRs).
To determine whether spermine causes the rectification of nAChRs in native neurons, I used the Gyro mouse model that lacks spermine due to a deletion in the gene coding for spermine synthase, the enzyme that catalyzes the production of spermine. (Abstract shortened by UMI.)
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Brier, Timothy James. "The interaction of polyamine-amides with the nicotinic acetylcholine receptor of the TE671 cell lines." Thesis, University of Nottingham, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.247142.

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Daeffler, Laurent. "Agonistes inverses et ligands des proteines g, modulation de l'activite constitutive des recepteurs muscariniques m2 (doctorat : pharmacologie)." Strasbourg 1, 1998. http://www.theses.fr/1998STR15070.

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Busse, Leigh Anne. "Characterization of the interaction of putrescine and the adenosine-3' ,5'-cyclic monophosphate-cAMP receptor protein complex in the regulation of the speC gene encoding ornithine decarboxylase in Escherichia coli." Thesis, This resource online, 1988. http://scholar.lib.vt.edu/theses/available/etd-04122010-083645/.

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Book chapters on the topic "POLYAMINE RECEPTORS"

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Usherwood, P. N. R. "Targeting Locust Muscle Glutamate Receptors with Polyamine-Containing Toxins." In Natural and Engineered Pest Management Agents, 259–67. Washington, DC: American Chemical Society, 1993. http://dx.doi.org/10.1021/bk-1994-0551.ch018.

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Koenig, Harold, Jerome J. Trout, Alfred D. Goldstone, and Chung Y. Lu. "NMDA Receptors Mediate Activation of Polyamine Synthesis and Blood-Brain Barrier Breakdown after Cold Injury." In The Role of Neurotransmitters in Brain Injury, 279–83. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3452-5_42.

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Kashiwagi, Keiko, Keith Williams, and Kazuei Igarashi. "Regulation of N-Methyl-d-Aspartate Receptors by Spermine and Ifenprodil." In Polyamines, 243–53. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-55212-3_20.

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Bowie, D., R. Bähring, and M. L. Mayer. "Block of AMPA and Kainate Receptors by Polyamines and Arthropod Toxins." In Ionotropic Glutamate Receptors in the CNS, 251–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-662-08022-1_7.

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Iqbal, Zafar. "Excitatory amino acid receptor-mediated neuronal signal transduction: modulation by polyamines and calcium." In Signal Transduction Mechanisms, 233–40. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2015-3_25.

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Mehta, R. A., D. Zhou, M. Tucker, A. Handa, T. Solomos, and A. K. Mattoo. "Ethylene in Higher Plants: Biosynthetic Interactions with Polyamines and High-Temperature-Mediated Differential Induction of Nr versus TAE1 Ethylene Receptor." In Biology and Biotechnology of the Plant Hormone Ethylene II, 387–93. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4453-7_70.

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Koenig, Harold, A. D. Goldstone, Chung Y. Lu, Zafar Iqbal, C. C. Fan, and J. J. Trout. "Polyamines, Hormone Receptors, and Calcium Fluxes." In The Physiology of Polyamines, 57–81. CRC Press, 2021. http://dx.doi.org/10.1201/9781003210436-5.

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Conference papers on the topic "POLYAMINE RECEPTORS"

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Li, Yang, John Gallagher, Bogdan Olenyuk, Bangyan Stiles, and Ankeste Kassa. "Abstract 2430: Targeting estrogen-related receptor alpha using pyrrole-imidazole polyamide." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2430.

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