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Journal articles on the topic 'Perireceptor events'

Author: Grafiati
Published: 25 January 2025

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1

Pelosi, Paolo. "Perireceptor events in olfaction." Journal of Neurobiology 30, no. 1 (May 1996): 3–19. http://dx.doi.org/10.1002/(sici)1097-4695(199605)30:1<3::aid-neu2>3.0.co;2-a.

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2

Leal, W. S., H. Wojtasek, Jean-Francois Picimbon, S. Kuwaharat, H. Saito, and M. Hasegawa. "Perireceptor Events in Pheromone Perception in Scarab Beetles." Journal of Asia-Pacific Entomology 1, no. 1 (March 1998): 1–8. http://dx.doi.org/10.1016/s1226-8615(08)60001-1.

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3

Carr, William E. S., Richard A. Gleeson, and Henry G. Trapido-Rosenthal. "The role of perireceptor events in chemosensory processes." Trends in Neurosciences 13, no. 6 (June 1990): 212–15. http://dx.doi.org/10.1016/0166-2236(90)90162-4.

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4

Pelosi, P. "The role of perireceptor events in vertebrate olfaction." Cellular and Molecular Life Sciences 58, no. 4 (April 2001): 503–9. http://dx.doi.org/10.1007/pl00000875.

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5

Menco, Bert Ph M. "Ultrastructural aspects of olfactory transduction and perireceptor events." Seminars in Cell Biology 5, no. 1 (February 1994): 11–24. http://dx.doi.org/10.1006/scel.1994.1003.

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6

Kaissling, K. E. "Olfactory Perireceptor and Receptor Events in Moths: A Kinetic Model." Chemical Senses 26, no. 2 (February 1, 2001): 125–50. http://dx.doi.org/10.1093/chemse/26.2.125.

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7

Kaissling, Karl-Ernst. "Olfactory perireceptor and receptor events in moths: a kinetic model revised." Journal of Comparative Physiology A 195, no. 10 (August 21, 2009): 895–922. http://dx.doi.org/10.1007/s00359-009-0461-4.

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8

Heydel, Jean-Marie, Alexandra Coelho, Nicolas Thiebaud, Arièle Legendre, Anne-Marie Le Bon, Philippe Faure, Fabrice Neiers, Yves Artur, Jérôme Golebiowski, and Loïc Briand. "Odorant-Binding Proteins and Xenobiotic Metabolizing Enzymes: Implications in Olfactory Perireceptor Events." Anatomical Record 296, no. 9 (July 31, 2013): 1333–45. http://dx.doi.org/10.1002/ar.22735.

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9

Derby, C. D., H. S. Cate, and L. R. Gentilcore. "Perireception in olfaction: molecular mass sieving by aesthetasc sensillar cuticle determines odorant access to receptor sites in the Caribbean spiny lobster Panulirus argus." Journal of Experimental Biology 200, no. 15 (August 1, 1997): 2073–81. http://dx.doi.org/10.1242/jeb.200.15.2073.

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The responsiveness of chemoreceptor neurons depends on a combination of perireceptor and receptor events. Olfactory neurons of crustaceans are packaged into distinctive cuticular sensilla called aesthetascs. The cuticle of aesthetascs is thin and permeable, even though it does not contain any obvious surface pores or pore tubules. This suggests that this 'spongy' aesthetasc cuticle may act as a molecular sieve that restricts large odorant molecules from entering the sensilla and binding to the olfactory neurons. We examined whether this is so for the aesthetasc cuticle of the Caribbean spiny lobster Panulirus argus. We used a chromatographic column packed with aesthetasc cuticle and connected to a flow-through ultraviolet spectrophotometer to measure the elution times of ultraviolet-absorbent molecular mass markers between 165 and 2 x 10(6) Da. Molecules larger than approximately 8.5 kDa had similar elution times, indicating that they did not penetrate the cuticle. Molecules smaller than 8.5 kDa had longer elution times that were directly and inversely proportional to their molecular mass. These results suggest that aesthetasc cuticle excludes molecules larger than 8.5 kDa from having access to the olfactory receptor neurons. We conclude that the molecular sieving capacity of the aesthetasc cuticle of P. argus is a perireceptor mechanism that is a critical determinant of the types of molecules capable of stimulating its olfactory receptors.
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10

Getchell, Thomas V., and William E. S. Carr. "Perireceptor events: chemical reception involves more than just receptors, G-proteins and second messengers." Chemical Senses 15, no. 2 (1990): 179. http://dx.doi.org/10.1093/chemse/15.2.179.

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11

Rospars, J. P., V. Krivan, and P. Lansky. "Perireceptor and Receptor Events in Olfaction. Comparison of Concentration and Flux Detectors: a Modeling Study." Chemical Senses 25, no. 3 (June 1, 2000): 293–311. http://dx.doi.org/10.1093/chemse/25.3.293.

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12

Leal, Walter Soares. "Molecules and macromolecules involved in chemical communication of scarab beetles." Pure and Applied Chemistry 73, no. 3 (January 1, 2001): 613–16. http://dx.doi.org/10.1351/pac200173030613.

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Chemical communication involves the production and release of specific chemicals (pheromones and other semiochemicals) by the emitter, and the detection and olfactory processing of these signals leading to appropriate behavioral responses in the receiver. In contrast to most of the scarab species investigated to date, the Japanese and Osaka beetles have the ability to detect the allospecific pheromone, which plays a pivotal role in the isolation mechanism between these two species. Each species produces a single enantiomer of japonilure [(Z)-5-(dec1-enyl)oxacyclopentan-2-one], but they have evolved the ability to detect both enantiomers, one as an attractant and the other as a behavioral antagonist (stop signal). There is growing evidence in the literature that the inordinate sensitivity and selectivity of the insect olfactory system is achieved by a combination of various olfactory-specific proteins, namely, odorant-binding proteins (OBPs), odorant receptors (ORs), and odorant-degrading enzymes. The relationship between the pheromone structures and the primary sequences of the proteins suggest that OBPs play a part in the selectivity of the olfactory system in scarab beetles by "filtering" chemical signals during the early olfactory processing (perireceptor events). Nevertheless, it is unlikely that pheromone-binding proteins are "chiral filters" as the Japanese and Osaka beetles each possess only one single binding protein. Upon interaction with negatively charged membranes, OBPs undergo conformational changes that may lead to the release of the ligands.
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13

Boichot, Valentin, Mariam Muradova, Clément Nivet, Alena Proskura, Jean-Marie Heydel, Marie-Chantal Canivenc-Lavier, Francis Canon, Fabrice Neiers, and Mathieu Schwartz. "The role of perireceptor events in flavor perception." Frontiers in Food Science and Technology 2 (October 19, 2022). http://dx.doi.org/10.3389/frfst.2022.989291.

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The sensory perception of food is a complex phenomenon involving the integration of different stimuli (aroma, taste, trigeminal sensations, texture and visual). Flavor compounds activate odorant, taste and trigeminal chemoreceptors, generating a depolarization of the sensory neurons and then the consciousness of food flavor perception. Recent studies are increasingly highlighting the importance of perireceptor events, which include all the molecular events surrounding the receptors, in the modulation of flavor perception. These events affect the quantity and quality of flavor compounds in the environment of chemoreceptors. They include the metabolization of flavor compounds by enzymes present in biological fluids (saliva and mucus) and the oronasal epithelia and noncovalent interactions with binding proteins. Perireceptor mechanisms have been extensively studied in insects and mammals, demonstrating the importance of the entailed processes in the termination of the chemical signal. In humans, research is in full swing. Here, we reviewed the perireceptor mechanisms recently reported in vitro, in biological fluids and in cells and in vivo in humans. These studies indicate that perireceptor mechanisms likely have an important contribution to flavor perception. This mini-review focuses on recent pioneering studies that are paving the way for this new research area. It also suggests that new approaches taking into account the real conditions of food consumption will be required in the future to accurately address this question.
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14

Manzini, Ivan. "Perireceptor events and peripheral modulation of olfactory signals in the olfactory epithelium of vertebrates." Neuroforum, July 8, 2022. http://dx.doi.org/10.1515/nf-2022-0005.

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Abstract The olfactory epithelium (OE) and its associated perireceptor space, i.e., the mucus layer (ML) covering the epithelium, are the most peripheral parts of the vertebrate olfactory system. The olfactory receptor neurons (ORNs), one of the cell types of the OE, are the odorant detectors of the olfactory system. These bipolar neurons extend their apical appendages, which express odorant receptors, into the ML. The binding of odorants to odorant receptors is the initial step of odor processing. The vast majority of research on the peripheral olfactory system has focused on the ORNs and the molecular components of the olfactory transduction cascades. Less attention has been directed to the other cell types of the OE and their physiological functions. For a long time, it was assumed that the olfactory signals detected in the OE are transmitted to the olfactory bulb without preprocessing, but this view turned out to be over-simplistic. It has been shown that the olfactory signals are critically modulated already in the OE. Despite compelling evidence, many descriptions of the olfactory system still ignore the existence of these peripheral modulatory mechanisms. The importance of peripheral modulation of the olfactory signals, the physiological functions of the other epithelial cell types, the extrinsic innervation of the olfactory mucosa, and the perireceptor space are only slowly coming into focus in the olfactory research. Furthermore, several intraepithelial signaling pathways that signal epithelial damage and initiate regenerative processes have recently been discovered. This review provides a concise overview of the current knowledge of peripheral events in the olfactory mucosa and the perireceptor space.
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15

Paesani, Massimiliano, Arthur G. Goetzee, Sanne Abeln, and Halima Mouhib. "Odorant Binding Proteins Facilitate the Gas‐Phase Uptake of Odorants Through the Nasal Mucus." Chemistry – A European Journal, November 7, 2024. http://dx.doi.org/10.1002/chem.202403058.

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Mammalian odorant binding proteins (OBPs) have long been suggested to transport hydrophobic odorant molecules through the aqueous environment of the nasal mucus. While the function of OBPs as odorant transporters is supported by their hydrophobic beta‐barrel structure, no rationale has been provided on why and how these proteins facilitate the uptake of odorants from the gas phase. Here, a multi‐scale computational approach validated through available high‐resolution spectroscopy experiments reveals that the conformational space explored by carvone inside the binding cavity of porcine OBP (pOBP) is much closer to the gas than the aqueous phase, and that pOBP effectively manages to transport odorants by lowering the free energy barrier of odorant uptake. Understanding such perireceptor events is crucial to fully unravel the molecular processes underlying the olfactory sense and move towards the development of protein‐based biomimetic sensor units that can serve as artificial noses.
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