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Relevant bibliographies by topics / Acetylcholine

Academic literature on the topic 'Acetylcholine'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 September 2024

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Journal articles on the topic "Acetylcholine"

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Barman, S. A., E. Senteno, S. Smith, and A. E. Taylor. "Acetylcholine's effect on vascular resistance and compliance in the pulmonary circulation." Journal of Applied Physiology 67, no. 4 (October 1, 1989): 1495–503. http://dx.doi.org/10.1152/jappl.1989.67.4.1495.

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Acetylcholine's effect on the distribution of vascular resistance and compliance in the canine pulmonary circulation was determined under control and elevated vascular tone by the arterial, venous, and double occlusion techniques in isolated blood-perfused dog lungs at both constant flow and constant pressure. Large and small blood vessel resistances and compliances were studied in lungs given concentrations of acetylcholine ranging from 2.0 ng/ml to 200 micrograms/ml. The results of this study indicate that acetylcholine dilates large arteries at low concentrations (less than or equal to 20 ng/ml) and constricts small and large veins at concentrations of at least 2 micrograms/ml. Characterization of acetylcholine's effects at constant pulmonary blood flow indicates that 1) large artery vasodilation may be endothelial-derived relaxing factor-mediated because the dilation is blocked with methylene blue; 2) a vasodilator of the arachidonic acid cascade (blocked by ibuprofen), probably prostacyclin, lessens acetylcholine's pressor effects; 3) when vascular tone was increased, acetylcholine's hemodynamic effects were attenuated; and 4) acetylcholine decreased middle compartment and large vessle compliance under control but not elevated vascular tone. Under constant pressure at control vascular tone acetylcholine increases resistance in all segments except the large artery, and at elevated vascular tone the pressor effects were enhanced, and large artery resistance was increased.

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Xu, Zemin, Chuanyao Tong, and James C. Eisenach. "Acetylcholine Stimulates the Release of Nitric Oxide from Rat Spinal Cord." Anesthesiology 85, no. 1 (July 1, 1996): 107–11. http://dx.doi.org/10.1097/00000542-199607000-00015.

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Background Acetylcholine causes synthesis of nitric oxide in vascular endothelium, and presumptive evidence in vivo suggests spinally released acetylcholine causes antinociception and increased sympathetic nervous system activity via a nitric oxide mechanism. The purpose of this study was to determine, using a recently described bioassay system, whether acetylcholine stimulates nitric oxide release from spinal cord tissue in vitro. Methods Rat thoracolumbar spinal cord slices were incubated in a tissue chamber and perfused with Krebs-Henseleit solution. The perfusate was then passed through endotheliumdenuded rat aortic rings and their tension was measured. Vascular rings were preconstricted with phenylephrine, then were exposed to spinal cord perfusate with increasing concentrations (10(-12)-10(-4)M) of acetylcholine alone or with various antagonists. Results Acetylcholine perfusion of spinal tissue caused concentration-dependent relaxations of the aortic rings, an effect blocked by each of the muscarinic antagonists, atropine, pirenzepine, and AFDX-116. Acetylcholine-induced relaxation also was antagonized by an inhibitor of nitric oxide synthase (N-methyl-L-arginine), a nitric oxide scavenger (hemoglobin) and an inhibitor of guanylate cyclase (methylene blue). Conclusions These results demonstrate release of a vasorelaxant from spinal cord tissue by acetylcholine, which results from an action on muscarinic receptors and exhibits a pharmacology consistent with nitric oxide. Although precise anatomic localization of acetylcholine's action is not possible with this system, these results add to evidence that acetylcholine causes nitric oxide synthesis in the spinal cord.

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&NA;. "Acetylcholine." Reactions Weekly &NA;, no. 1146-1147 (April 2007): 6. http://dx.doi.org/10.2165/00128415-200711460-00018.

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&NA;. "Acetylcholine." Reactions Weekly &NA;, no. 471 (October 1993): 5. http://dx.doi.org/10.2165/00128415-199304710-00021.

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&NA;. "Acetylcholine." Reactions Weekly &NA;, no. 380 (December 1991): 3. http://dx.doi.org/10.2165/00128415-199103800-00006.

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&NA;. "Acetylcholine." Reactions Weekly &NA;, no. 952 (May 2003): 6. http://dx.doi.org/10.2165/00128415-200309520-00019.

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Brown, David A. "Acetylcholine." British Journal of Pharmacology 147, S1 (January 2006): S120—S126. http://dx.doi.org/10.1038/sj.bjp.0706474.

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Doliba, Nicolai M., Wei Qin, Sergei A. Vinogradov, David F. Wilson, and Franz M. Matschinsky. "Palmitic acid acutely inhibits acetylcholine- but not GLP-1-stimulated insulin secretion in mouse pancreatic islets." American Journal of Physiology-Endocrinology and Metabolism 299, no. 3 (September 2010): E475—E485. http://dx.doi.org/10.1152/ajpendo.00072.2010.

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Fatty acids, acetylcholine, and GLP-1 enhance insulin secretion in a glucose-dependent manner. However, the interplay between glucose, fatty acids, and the neuroendocrine regulators of insulin secretion is not well understood. Therefore, we studied the acute effects of PA (alone or in combination with glucose, acetylcholine, or GLP-1) on isolated cultured mouse islets. Two different sets of experiments were designed. In one, a fixed concentration of 0.5 mM of PA bound to 0.15 mM BSA was used; in the other, a PA ramp from 0 to 0.5 mM was applied at a fixed albumin concentration of 0.15 mM so that the molar PA/BSA ratio changed within the physiological range. At a fixed concentration of 0.5 mM, PA markedly inhibited acetylcholine-stimulated insulin release, the rise of intracellular Ca2+, and enhancement of cAMP production but did not influence the effects of GLP-1 on these parameters of islet cell function. 2-ADB, an IP3 receptor inhibitor, reduced the effect of acetylcholine on insulin secretion and reversed the effect of PA on acetylcholine-stimulated insulin release. Islet perfusion for 35–40 min with 0.5 mM PA significantly reduced the calcium storage capacity of ER measured by the thapsigargin-induced Ca2+ release. Oxygen consumption due to low but not high glucose was reduced by PA. When a PA ramp from 0 to 0.5 mM was applied in the presence of 8 mM glucose, PA at concentrations as low as 50 μM significantly augmented glucose-stimulated insulin release and markedly reduced acetylcholine's effects on hormone secretion. We thus demonstrate that PA acutely reduces the total oxygen consumption response to glucose, glucose-dependent acetylcholine stimulation of insulin release, Ca2+, and cAMP metabolism, whereas GLP-1's actions on these parameters remain unaffected or potentiated. We speculate that acute emptying of the ER calcium by PA results in decreased glucose stimulation of respiration and acetylcholine potentiation of insulin secretion.

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Seitz, Andreas, Rutger G. T. Feenstra, Regina E. Konst, Valeria Martínez Pereyra, Sascha Beck, Marcel A. M. Beijk, Tim P. van de Hoef, et al. "Acetylcholine Rechallenge." JACC: Cardiovascular Interventions 15, no. 1 (January 2022): 65–75. http://dx.doi.org/10.1016/j.jcin.2021.10.003.

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Vogt, Nina. "Detecting acetylcholine." Nature Methods 15, no. 9 (August 31, 2018): 648. http://dx.doi.org/10.1038/s41592-018-0131-y.

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Dissertations / Theses on the topic "Acetylcholine"

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Tornoe, Calilla. "Nicotinic acetylcholine receptors in nematodes." Thesis, University of Cambridge, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.363452.

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Bird, Martin Charles. "Immunochemistry of the acetylcholine receptor." Thesis, University of Bath, 1985. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.370159.

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1. Anti-Torpedo marmorata AChR antibody fragments (Fab and F(ab')2) have been prepared from sheep immunised with Torpedo AChR, and exhibiting experimental autoimmune myasthenia gravis. The antibody fragments were labelled with 125I with the retention of antigen binding capacity. Labelled and unlabelled antibody fragments were used to study the antigenicity of soluble and membrane-bound AChR, Anti-receptor antibodies were found to reduce (?-toxin binding to the AChR This was demonstrated to be caused by steric hindrance rather than by direct blockade of the toxin binding site, or by antigenic modulation of the receptor. Removal of carbohydrate residues from the AChR resulted in no decrease in antibody binding, implying that carbohydrate made no direct contribution to the antigenicity of the receptor. Denaturation of the AChR resulted in a decrease in anti-receptor antibody binding of between 60 and 84%. Thus antibodies were directed mainly at conformation-dependent sites on the receptor. Substantial differences between the antigenic sites of soluble and membrane-bound receptors were found. 2. The contribution of antibody-mediated muscle cell lysis in the pathogenesis of myasthenia gravis has been studied, using a novel in vitro cytotoxicity assay based on 3H-carnitine uptake and release by muscle cells in culture. Cytolytic activity toward both chick and human embryonic muscle cell cultures was demonstrated in over 30% of myasthenic sera, suggesting that myolysis may be a major mechanism for AChR loss in myasthenia gravis. Heat-inactivation of the sera abolished their lytic activity, and it was not fully restored by the addition of guinea pig complement. Myolysis may be caused by antibodies other than anti-AChR antibodies present in myasthenic sera.

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Pagan, Augustine J. IV. "Heterosandwich assay of nicotinic acetylcholine receptors." VCU Scholars Compass, 2015. http://scholarscompass.vcu.edu/etd/3815.

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Using the technology afforded by Winschel et al., cyclen-1, a high affinity, strong complexation agent for 8-hydroxypyrene-1,3,6 trisulfonate and derivatives, a new assay has been developed for fluorescently labeling proteins of interest (POIs). Ligation of the endogenous ligand for nicotinic acetylcholine receptors (nAChRs), acetylcholine, using click chemistry afforded the triazole derivative of an alkynyl-acylcholine (compound 1) with 8-azidopyrene-1,3,6 trisulfonate (compound 2). Liposomes encapsulated with Rhodamine B were used to strengthen the initial fluorophore response of compound 2, using an anchored form of cyclen-1 complex. Using a palmitoyl tail as the lipophilic moiety for liposomal amplification, the subsequent response has a fluorophore ratio of up to 1:1 million, compound 2:Rhodamine B molecules. in vitro assay using compound 2 and cyclen-1 anchored liposomes with HEK-293 cells produced a positive binding response, allowing brightly colored fluorescent images of nAChRs upon the cellular membrane. A control for nAChR binding was performed using a co-culture of HEK-293 and endothelial cell lines. Control experiments show compound 2 and liposomes weak binding endothelial cells, however, this could be do to accumulation from another mechanism, more work is necessary to prove whether or not this is correct.

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Burdon, Drew. "Cell growth regulation by muscarinic acetylcholine receptors." Thesis, University of Leicester, 2002. http://hdl.handle.net/2381/29932.

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The growth response of Chinese hamster ovary (CHO) cells to activation of recombinantly expressed G protein-coupled muscarinic M2 or M3 acetylcholine (ACh) receptors has been assessed. Activation of these receptors leads to divergent growth responses: M2 ACh receptor activation causes an increase in DNA synthesis, whereas M3 ACh receptor activation causes a dramatic inhibition of DNA synthesis. The M3 ACh receptor-mediated growth inhibition has been characterised, and shown to comprise a G1-phase cell cycle arrest, involving an increase in p21Cip1/Waf1 protein expression. Further, a receptor-mediated increase in p21Cip1/Waf1 association with cyclin-dependent kinase 2 (CDK2) leads to a decrease in CDK2 activity and an accumulation of hypophosphorylated retinoblastoma protein (pRb). The increase p21Cip1/Waf1 expression is due at least in part to an increase p21Cip1/Waf1 mRNA although no receptor-mediated change in candidate transcription factor activities could be detected. Extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) activation profiles suggested two alternative hypotheses to account for the receptor-mediated growth arrest. However, pharmacological and biochemical data demonstrate that ERK, JNK and p38 MAPK are not involved in the growth regulation, whilst inhibition of PKC partially ablates the growth arrest. Data demonstrate that both M3 ACh receptor-mediated ERK and JNK activities may be dependent on liberated G-protein bg subunits, whilst the growth arrest is not perturbed by bg subunit sequestration. Data presented reveal a MAPK-independent mechanism of growth regulation that may involve coping of the M3 ACh receptor to heterotrimeric G-protein families other than Gq/11.

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Komourian, Jacques. "Alpha-bungarotoxin sensitive neuronal nicotinic acetylcholine receptors." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq29731.pdf.

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Kommalage, Mahinda. "Spinal Acetylcholine Release : Mechanisms and Receptor Involvement." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-5931.

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Schött, Pär A. "Hippocampal galanin and acetylcholine in spatial learning /." Stockholm, 2000. http://diss.kib.ki.se/2000/91-628-4137-8/.

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Spalding, Tracy Anne. "Structural studies on the muscarinic acetylcholine receptor." Thesis, University College London (University of London), 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315419.

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Walsh, Susan. "Search for nicotinic acetylcholine receptors on lymphocytes." Thesis, University of Bath, 1989. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.760593.

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Lotwick, Helen Sylvia. "Anti-(acetylcholine receptor) antibodies in myasthenia gravis." Thesis, University of Bath, 1985. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.351788.

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Levels of anti-(AChR) antibodies were determined in serial serum samples from 14 myasthenic patients over a period of several months, using detergent-solubilized muscle extracts of junctional rat AChR, extra-junctional rat AChR and human adult AChR as antigens. Anti-(AChR) antibody titres obtained using human adult AChR were always higher than those obtained using extra-junctional rat AChR, which were, in turn, always higher than those obtained using junctional rat AChR. Ihe ratios of antibody titres obtained by using the different antigens varied between patients, but were constant for an individual over the period of study. Complementary evidence for the same phenamenon was obtained by other experiments in which an excess of each serum was used to precipitate limited amounts of AChR from muscle extracts. The results obtained by conbining myasthenic sera argue against the suggestion that incomplete precipitation of receptor by certain sera is caused by the absence of particular antibody sub-populations. An alternative explanation, that sera precipitating low amounts of AChR contain toxin-releasing antibodies, is supported by direct measuranents of antibody-mediated toxin loss. The hypothesis that embryonic AChR may constitute the autoimmunogen in MG vas investigated by comparing the interaction of human foetal AChR with BGT and anti-(AChR) antibodies against that established for adult human AChR. Tissue sections and teased muscle fibres fron human adult and foetal muscle were compared immunohistochemically. Detergent extracts of adult and foetal AChRs were canpared in their interaction with radiolabelled BGT by kinetic measurements involving determination of association, dissociation and equilibrium binding constants. AChR was isolated and partially purified frcm human adult and foetal muscle, and their binding to anti-(AChR) antibodies in myasthenic sera and IgG were compared. No significant difference was observed between the binding characteristics of the two receptor types, indicating the absence (at least in 14 - 22 week old foetuses) of ligand binding or antigenic sites unique to foetal AChR.

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Books on the topic "Acetylcholine"

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Skok, V. I., A. A. Selyanko, and V. A. Derkach. Neuronal Acetylcholine Receptors. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-1668-8.

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Dun, Nae J., and Robert L. Perlman, eds. Neurobiology of Acetylcholine. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5266-2.

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Maelicke, Alfred, ed. Nicotinic Acetylcholine Receptor. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71649-2.

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A, Selyanko A., and Derkach V. A, eds. Neuronal acetylcholine receptors. New York: Consultants Bureau, 1989.

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J, Dun Nae, Perlman Robert L, and Karczmar A. G. 1918-, eds. Neurobiology of acetylcholine. New York: Plenum Press, 1987.

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Barrantes, Francisco J., ed. The Nicotinic Acetylcholine Receptor. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-40279-5.

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Li, Ming D., ed. Nicotinic Acetylcholine Receptor Technologies. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3768-4.

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Thany, Steeve Hervé, ed. Insect Nicotinic Acetylcholine Receptors. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6445-8.

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Montréal), International Symposium of the Centre De Recherche En Sciences Neurologiques on Acetylcholine in the Cerebral Cortex (24th 2002 Université de. Acetylcholine in the cerebral cortex. Amsterdam: Elsevier, 2003.

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W, Stone T., ed. CNS neurotransmitters and neuromodulators: Acetylcholine. Boca Raton, Fla: CRC Press, 1995.

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Book chapters on the topic "Acetylcholine"

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Hangay, George, Severiano F. Gayubo, Marjorie A. Hoy, Marta Goula, Allen Sanborn, Wendell L. Morrill, Gerd GÄde, et al. "Acetylcholine." In Encyclopedia of Entomology, 22. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6359-6_30.

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Roffel, Ad F., and Johan Zaagsma. "Acetylcholine." In Airways Smooth Muscle: Neurotransmitters, Amines, Lipid Mediators and Signal Transduction, 81–130. Basel: Birkhäuser Basel, 1995. http://dx.doi.org/10.1007/978-3-0348-7504-2_2.

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Scherrmann, Jean-Michel, Kim Wolff, Christine A. Franco, Marc N. Potenza, Tayfun Uzbay, Lisiane Bizarro, David C. S. Roberts, et al. "Acetylcholine." In Encyclopedia of Psychopharmacology, 8. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_999.

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Tschanz, JoAnn T., and Katherine Treiber. "Acetylcholine." In Encyclopedia of Clinical Neuropsychology, 17. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-0-387-79948-3_1622.

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Brandt, Nicole, and Rachel Flurie. "Acetylcholine." In Encyclopedia of Behavioral Medicine, 18–19. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-39903-0_1351.

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Abrams, David B., J. Rick Turner, Linda C. Baumann, Alyssa Karel, Susan E. Collins, Katie Witkiewitz, Terry Fulmer, et al. "Acetylcholine." In Encyclopedia of Behavioral Medicine, 14–16. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1005-9_1351.

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Tschanz, JoAnn T., and Elizabeth Vernon. "Acetylcholine." In Encyclopedia of Clinical Neuropsychology, 1–2. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-56782-2_1622-2.

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Tschanz, JoAnn, and Elizabeth K. Vernon. "Acetylcholine." In Encyclopedia of Clinical Neuropsychology, 25–26. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-57111-9_1622.

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Kruk, Zygmunt L., and Christopher J. Pycock. "Acetylcholine." In Neurotransmitters and Drugs, 28–49. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3132-2_2.

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Kruk, Zygmunt L., and Christopher J. Pycock. "Acetylcholine." In Neurotransmitters and Drugs, 28–49. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3134-6_2.

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Conference papers on the topic "Acetylcholine"

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Marino, T., and N. Russo. "Molecular dynamics of acetylcholine." In The first European conference on computational chemistry (E.C.C.C.1). AIP, 1995. http://dx.doi.org/10.1063/1.47721.

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Tantry, Evelyne, Joshua Ortiz-Guzman, and Benjamin Arenkiel. "The Impact of Acetylcholine on Basolateral Amygdala Macrocircuits." In 2019 Conference on Cognitive Computational Neuroscience. Brentwood, Tennessee, USA: Cognitive Computational Neuroscience, 2019. http://dx.doi.org/10.32470/ccn.2019.1383-0.

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Sun, Guo-Quan, Jue Wang, Qing Li, Ling-Bo Qian, Zhi-Guo Ye, and Qiang Xia. "Acetylcholine Exerts Cardioprotection by Reducing Reactive Oxygen Species." In 2010 International Conference on Biomedical Engineering and Computer Science (ICBECS). IEEE, 2010. http://dx.doi.org/10.1109/icbecs.2010.5462443.

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Fish, Jordan, Lisa Ossian, and Juyang Weng. "Novelty estimation in developmental networks: Acetylcholine and norepinephrine." In 2013 International Joint Conference on Neural Networks (IJCNN 2013 - Dallas). IEEE, 2013. http://dx.doi.org/10.1109/ijcnn.2013.6706722.

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Perry, Trent. "Interactions of spinosad with insect nicotinic acetylcholine receptors." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.91226.

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Nascimento, Letícia A., Érica C. M. Nascimento, and João B. L. Martins. "Análise da estrutura eletrônica da tacrina e do neurotransmissor acetilcolina." In VIII Simpósio de Estrutura Eletrônica e Dinâmica Molecular. Universidade de Brasília, 2020. http://dx.doi.org/10.21826/viiiseedmol2020150.

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Alzheimer's disease (AD) is a more common neurodegenerative process in the elderly population, characterized by a progressive loss of cognitive abilities, such as memory, language skills, disorientation, attention and depression. Cholinergic hypothesis therapy is the most successful approach for the symptomatic treatment of AD. The therapy consists in the use of drugs with inhibitory action against acetylcholinesterase (AChE) to avoid the decrease of acetylcholine concentration in synaptic clefts. Thus, this research aims to carry out the electronic and structural study of tacrina drug compared to the neurotransmitter acetylcholine, through computational calculations based on theoretical chemistry, using PM6 semi-empirical method jointly to DFT and MP2 methods.

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Herrera, E. G., A. Bonini, F. Vivaldi, B. Melai, P. Salvo, N. Poma, D. Santalucia, A. Kirchhain, and F. Di Francesco. "A Biosensor for the Detection of Acetylcholine and Diazinon." In 2019 41st Annual International Conference of the IEEE Engineering in Medicine & Biology Society (EMBC). IEEE, 2019. http://dx.doi.org/10.1109/embc.2019.8856959.

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Contoli, Marco, Andrea Marcellini, Paolo Casolari, Gaetano Caramori, and Alberto Papi. "Role of the acetylcholine in the virus-induced bronchoconstriction." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa4103.

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Pitikultham, Piyawat, Chakrit Sriprachuabwong, and Pornpimol Sritongkham. "Amperometric acetylcholine biosensor based on graphene-PEDOT:PSS modified electrode." In 2014 7th Biomedical Engineering International Conference (BMEiCON). IEEE, 2014. http://dx.doi.org/10.1109/bmeicon.2014.7017408.

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Shoseyov, David, Rufaida Mruwat, Amjad Horani, Muhamad Natur, and Eitan Kerem. "Acetylcholine Esterase Inhibitors Induced Asthma In A Mouse Model." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3274.

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Reports on the topic "Acetylcholine"

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Cohen, Saul G. Acetylcholinesterase and Acetylcholine Receptor. Fort Belvoir, VA: Defense Technical Information Center, January 1992. http://dx.doi.org/10.21236/ada255623.

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Cohen, Saul G. Acetylcholinesterase and Acetylcholine Receptor. Fort Belvoir, VA: Defense Technical Information Center, January 1985. http://dx.doi.org/10.21236/adb112772.

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Oswald, R. E. Interaction of Opiate and Phencyclidine Derivatives with the Acetylcholine Receptor. Fort Belvoir, VA: Defense Technical Information Center, March 1985. http://dx.doi.org/10.21236/ada155119.

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Johnson, David A. Spatial Relationships between Drug Binding Sites on the Surface of the Acetylcholine Receptor. Fort Belvoir, VA: Defense Technical Information Center, October 1986. http://dx.doi.org/10.21236/ada222751.

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Johnson, David A. Spatial Relationships between Drug Binding Sites on the Surface of the Acetylcholine Receptor. Fort Belvoir, VA: Defense Technical Information Center, February 1989. http://dx.doi.org/10.21236/ada228229.

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Lindstrom, Jon M. Use of Monoclonal Antibodies to Study the Structure and Function of Nicotinic Acetylcholine Receptors on Electric Organ and Muscle and to Determine the Structure of Nicotinic Acetylcholine Receptors on Neurons. Fort Belvoir, VA: Defense Technical Information Center, March 1988. http://dx.doi.org/10.21236/ada198425.

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Musselman, Nicole. Pharmacological characterization of a homomeric nicotinic acetylcholine receptor formed by Ancylostoma caninum ACR-16. Ames (Iowa): Iowa State University, January 2018. http://dx.doi.org/10.31274/cc-20240624-1116.

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Roman, Jesse. Prenatal Exposure to Nicotine and Childhood Asthma: Role of Nicotine Acetylcholine Receptors, Neuropeptides, and Fibronectin Expression in Lung. Fort Belvoir, VA: Defense Technical Information Center, December 2005. http://dx.doi.org/10.21236/ada452269.

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Roman, Jesse. Prenatal Exposure to Nicotine and Childhood Asthma: Role of Nicotine Acetylcholine Receptors, Neuropeptides and Fibronectin Expression in Lung. Fort Belvoir, VA: Defense Technical Information Center, December 2008. http://dx.doi.org/10.21236/ada508588.

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Benton, Bernard J., John H. McDonough, Thomas A. Koviak, and Tsung-Ming A. Shih. Time-Course Effects of GA, GB, GD, GF and VX on Spinal Cord Cholinesterase and Acetylcholine Levels in Six Discrete Areas of the Rat Brain. Fort Belvoir, VA: Defense Technical Information Center, January 2001. http://dx.doi.org/10.21236/ada396059.

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