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Journal articles on the topic 'Molecular receptors'

Author: Grafiati

Published: 4 June 2021

Last updated: 27 April 2022

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1

Brown, Michael, Michael Webb, Elsa Phillips, Elizabeth Skidmore, and Peter McIntyre. "Molecular studies on kinin receptors." Canadian Journal of Physiology and Pharmacology 73, no. 7 (July 1, 1995): 780–86. http://dx.doi.org/10.1139/y95-105.

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We describe the results of functional studies on DNA clones encoding functional bradykinin receptors derived from human, rat, and mouse sources and including both genomic and complementary DNA clones. In both the Xenopus oocyte and the COS cell expression systems, the receptors from human and rat showed the pharmacological properties of B2 receptors, but receptors from mouse displayed both B1- and B2-like pharmacological properties. We further investigated the molecular relationship between the B1 and B2 receptor subtypes expressed by a human fibroblast cell line, and we demonstrate that these

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Szybowska, Patrycja, Ellen Margrethe Haugsten, and Antoni Wiedlocha. "The canonical FGF-FGFR signaling system at the molecular level." Postępy Higieny i Medycyny Doświadczalnej 75, no. 1 (January 1, 2021): 711–19. http://dx.doi.org/10.2478/ahem-2021-0024.

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Abstract Extracellular signaling molecules, among them the fibroblast growth factors (FGFs), enable cells to communicate with neighboring cells. Such signaling molecules that receive and transmit a signal require specific tyrosine kinase receptors located at the cell surface (fibroblast growth factor receptors, FGFRs). The binding of a signaling molecule to its specific receptor results in receptor dimerization and conformational changes in the cytoplasmic part of the receptor. The conformational changes lead to trans-autophosphorylation of the tyrosine kinase domains of the receptors and subs

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Hay, D. L., G. Christopoulos, A. Christopoulos, and P. M. Sexton. "Amylin receptors: molecular composition and pharmacology." Biochemical Society Transactions 32, no. 5 (October 26, 2004): 865–67. http://dx.doi.org/10.1042/bst0320865.

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Several receptors which bind the hormone AMY (amylin) with high affinity have now been identified. The minimum binding unit is composed of the CT (calcitonin) receptor at its core, plus a RAMP (receptor activity modifying protein). The receptors have been named AMY1(a), AMY2(a) and AMY3(a) in accordance with the association of the CT receptor (CT(a)) with RAMP1, RAMP2 and RAMP3 respectively. The challenge is now to determine the localization and pharmacological nature of each of these receptors. Recent attempts to achieve these aims will be briefly discussed.

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Alfimov, Michael V., Olga A. Fedorova, and Sergey P. Gromov. "Photoswitchable molecular receptors." Journal of Photochemistry and Photobiology A: Chemistry 158, no. 2-3 (June 2003): 183–98. http://dx.doi.org/10.1016/s1010-6030(03)00033-9.

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5

Xie, Peng, Junjie Zhang, Baiyu Chen, Xinwei Li, Wenbo Zhang, Mengdan Zhu, Wei Li, Jianqi Li, and Wei Fu. "Computational Methods for Understanding the Selectivity and Signal Transduction Mechanism of Aminomethyl Tetrahydronaphthalene to Opioid Receptors." Molecules 27, no. 7 (March 28, 2022): 2173. http://dx.doi.org/10.3390/molecules27072173.

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Opioid receptors are members of the group of G protein-couple receptors, which have been proven to be effective targets for treating severe pain. The interactions between the opioid receptors and corresponding ligands and the receptor’s activation by different agonists have been among the most important fields in opioid research. In this study, with compound M1, an active metabolite of tramadol, as the clue compound, several aminomethyl tetrahydronaphthalenes were designed, synthesized and assayed upon opioid receptors. With the resultant compounds FW-AII-OH-1 (Ki = 141.2 nM for the κ opioid r

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Breyer, M. D., H. R. Jacobson, and R. M. Breyer. "Functional and molecular aspects of renal prostaglandin receptors." Journal of the American Society of Nephrology 7, no. 1 (January 1996): 8–17. http://dx.doi.org/10.1681/asn.v718.

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The diverse intrarenal effects of the prostaglandins (PG) are mediated by distinct guanine nucleotide regulatory protein (G-protein)-coupled receptors. The cDNA for these receptors have been cloned, their signal transduction mechanisms determined, and their intrarenal distribution mapped. PGE2, the major intrarenal prostaglandin, interacts with at least three distinct E-prostanoid (EP) receptors that are highly expressed in specific regions of the kidney. Each EP receptor not only selectively binds PGE2, but also preferentially couples to different signal transduction pathways, including: stim

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North, R. Alan. "Molecular Physiology of P2X Receptors." Physiological Reviews 82, no. 4 (January 10, 2002): 1013–67. http://dx.doi.org/10.1152/physrev.00015.2002.

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P2X receptors are membrane ion channels that open in response to the binding of extracellular ATP. Seven genes in vertebrates encode P2X receptor subunits, which are 40–50% identical in amino acid sequence. Each subunit has two transmembrane domains, separated by an extracellular domain (∼280 amino acids). Channels form as multimers of several subunits. Homomeric P2X1, P2X2, P2X3, P2X4, P2X5, and P2X7channels and heteromeric P2X2/3and P2X1/5channels have been most fully characterized following heterologous expression. Some agonists (e.g., αβ-methylene ATP) and antagonists [e.g., 2′,3′- O-(2,4,

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Livingstone, C. D., P. G. Strange, and L. H. Naylor. "Molecular modelling of D2-like dopamine receptors." Biochemical Journal 287, no. 1 (October 1, 1992): 277–82. http://dx.doi.org/10.1042/bj2870277.

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Three-dimensional computer models of the rat D2, D3 and D4 dopamine receptor subtypes have been constructed based on the diffraction co-ordinates for bacteriorhodopsin, another membrane-bound protein containing seven transmembrane domains presumed to be arranged in a similar spatial orientation. Models were assembled by aligning the putative transmembrane domains of the dopamine receptors with those of bacteriorhodopsin using sequence similarities, and then superimposing these modelled alpha-helices on to the bacteriorhodopsin-derived co-ordinates. These models explore the potential hydrogen b

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9

Behzadi, Payam, Herney Andrés García-Perdomo, and Tomasz M. Karpiński. "Toll-Like Receptors: General Molecular and Structural Biology." Journal of Immunology Research 2021 (May 29, 2021): 1–21. http://dx.doi.org/10.1155/2021/9914854.

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Background/Aim. Toll-like receptors (TLRs) are pivotal biomolecules in the immune system. Today, we are all aware of the importance of TLRs in bridging innate and adaptive immune system to each other. The TLRs are activated through binding to damage/danger-associated molecular patterns (DAMPs), microbial/microbe-associated molecular patterns (MAMPs), pathogen-associated molecular patterns (PAMPs), and xenobiotic-associated molecular patterns (XAMPs). The immunogenetic molecules of TLRs have their own functions, structures, coreceptors, and ligands which make them unique. These properties of TL

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10

Bettler, Bernhard, Klemens Kaupmann, Johannes Mosbacher, and Martin Gassmann. "Molecular Structure and Physiological Functions of GABAB Receptors." Physiological Reviews 84, no. 3 (July 2004): 835–67. http://dx.doi.org/10.1152/physrev.00036.2003.

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GABAB receptors are broadly expressed in the nervous system and have been implicated in a wide variety of neurological and psychiatric disorders. The cloning of the first GABAB receptor cDNAs in 1997 revived interest in these receptors and their potential as therapeutic targets. With the availability of molecular tools, rapid progress was made in our understanding of the GABAB system. This led to the surprising discovery that GABAB receptors need to assemble from distinct subunits to function and provided exciting new insights into the structure of G protein-coupled receptors (GPCRs) in genera

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11

Brown, E. J., and J. L. Goodwin. "Fibronectin receptors of phagocytes. Characterization of the Arg-Gly-Asp binding proteins of human monocytes and polymorphonuclear leukocytes." Journal of Experimental Medicine 167, no. 3 (March 1, 1988): 777–93. http://dx.doi.org/10.1084/jem.167.3.777.

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We have defined the cell surface molecules of human monocytes and PMN that bind to the chymotryptic cell binding domain of Fn and to a synthetic peptide, KYAVTGRGDS, based on the sequence of Fn, by affinity chromatography. Monocytes express two receptors that differ in their affinity for CBD-Sepharose and peptide-Sepharose, but that both recognize the RGD sequence. Only a single receptor is purified from PMN, which resembles the monocyte surface molecule that binds to peptide-Sepharose. These receptors are not part of the Mac-1, LFA-1, p(150,95) family, but do have homology to the platelet Fn

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Mahmod Al-Qattan, Mohammed Nooraldeen, and Mohd Nizam Mordi. "Molecular Basis of Modulating Adenosine Receptors Activities." Current Pharmaceutical Design 25, no. 7 (June 17, 2019): 817–31. http://dx.doi.org/10.2174/1381612825666190304122624.

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Modulating cellular processes through extracellular chemical stimuli is medicinally an attractive approach to control disease conditions. GPCRs are the most important group of transmembranal receptors that produce different patterns of activations using intracellular mediators (such as G-proteins and Beta-arrestins). Adenosine receptors (ARs) belong to GPCR class and are divided into A1AR, A2AAR, A2BAR and A3AR. ARs control different physiological activities thus considered valuable target to control neural, heart, inflammatory and other metabolic disorders. Targeting ARs using small molecules

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13

Thomas, Lance R., Ronald L. Johnson, John C. Reed, and Andrew Thorburn. "The C-terminal Tails of Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) and Fas Receptors Have Opposing Functions in Fas-associated Death Domain (FADD) Recruitment and Can Regulate Agonist-specific Mechanisms of Receptor Activation." Journal of Biological Chemistry 279, no. 50 (September 27, 2004): 52479–86. http://dx.doi.org/10.1074/jbc.m409578200.

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Members of the tumor necrosis factor (TNF) superfamily of receptors such as Fas/CD95 and the TNF-related apoptosis-inducing ligand (TRAIL) receptors DR4 and DR5 induce apoptosis by recruiting adaptor molecules and caspases. The central adaptor molecule for these receptors is a death domain-containing protein, FADD, which binds to the activated receptor via death domain-death domain interactions. Here, we show that in addition to the death domain, the C-terminal tails of DR4 and DR5 positively regulate FADD binding, caspase activation and apoptosis. In contrast, the corresponding region in the

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14

HRUBY, VICTOR J., HENRY I. YAMAMURA, and FRANK PORRECA. "Molecular Organization of Receptors." Annals of the New York Academy of Sciences 757, no. 1 (May 1995): 7–22. http://dx.doi.org/10.1111/j.1749-6632.1995.tb17461.x.

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15

Al-Hasani, Ream, and Michael R. Bruchas. "Molecular Mechanisms of Opioid Receptor-dependent Signaling and Behavior." Anesthesiology 115, no. 6 (December 1, 2011): 1363–81. http://dx.doi.org/10.1097/aln.0b013e318238bba6.

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Opioid receptors have been targeted for the treatment of pain and related disorders for thousands of years and remain the most widely used analgesics in the clinic. Mu (μ), kappa (κ), and delta (δ) opioid receptors represent the originally classified receptor subtypes, with opioid receptor like-1 (ORL1) being the least characterized. All four receptors are G-protein coupled and activate inhibitory G proteins. These receptors form homo- and heterodimeric complexes and signal to kinase cascades and scaffold a variety of proteins.The authors discuss classic mechanisms and developments in understa

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Kazantseva, Z. I. "Phosphorylated thiacalixarenes as molecular receptors for QCM sensors of volatile compounds." Functional materials 24, no. 4 (December 18, 2017): 599–606. http://dx.doi.org/10.15407/fm24.04.599.

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17

Hirose, Shigehisa, Hiromi Hagiwara, and Yoshio Takei. "Comparative molecular biology of natriuretic peptide receptors." Canadian Journal of Physiology and Pharmacology 79, no. 8 (August 1, 2001): 665–72. http://dx.doi.org/10.1139/y01-034.

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Analysis of the mammalian natriuretic peptide system has established the presence of three types of receptors with distinct structural and functional features and tissue distributions. To clarify the physiological role of each subtype, we studied the natriuretic peptide system in animals with specialized anatomical and physiological features. In this review, following a brief description of the comparative and evolutionary aspects of the ligands, we will analyze the structure and distribution of natriuretic peptide receptors in lower vertebrates, as well as those of rats with essential and sal

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18

BREDESEN, DALE E., PATRICK MEHLEN, and SHAHROOZ RABIZADEH. "Apoptosis and Dependence Receptors: A Molecular Basis for Cellular Addiction." Physiological Reviews 84, no. 2 (April 2004): 411–30. http://dx.doi.org/10.1152/physrev.00027.2003.

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Bredesen, Dale E., Patrick Mehlen, and Shahrooz Rabizadeh. Apoptosis and Dependence Receptors: A Molecular Basis for Cellular Addiction. Physiol Rev 84: 411–430, 2004; 10.1152/physrev.00027.2003.—Classical signal transduction is initiated by ligand-receptor interactions. We have described an alternative form of signal transduction that is initiated by the withdrawal of ligands from specific receptors referred to as dependence receptors. This process is widespread, featuring in developmental cell death, carcinogenesis (especially metastasis), neurodegeneration, and possibly subapoptotic events

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Woodcock, E. A., S. L. Land, R. K. Andrews, M. Linsenmeyer, and D. M. Woodcock. "A low-affinity, low-molecular-mass endothelin-A receptor in neonatal rat heart." Biochemical Journal 304, no. 1 (November 15, 1994): 113–19. http://dx.doi.org/10.1042/bj3040113.

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Endothelin receptors with endothelin-A (ETa) specificity were present in neonatal rat ventricle. However, in both receptor-binding studies and studies of inositol phosphate accumulation, these receptors had lower affinity for endothelin-1 than ETa receptors on isolated neonatal cardiomyocytes or adult left atria. Receptors in the three myocardial preparations were cross-linked to 125I-endothelin-1 and their molecular masses measured using SDS/PAGE. Receptors on left atria and neonatal cardiomyocytes had the expected molecular mass of 48 kDa, whereas the receptors in neonatal ventricle were sma

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Brooks, Charles L. "Molecular Mechanisms of Prolactin and Its Receptor." Endocrine Reviews 33, no. 4 (August 1, 2012): 504–25. http://dx.doi.org/10.1210/er.2011-1040.

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Prolactin and the prolactin receptors are members of a family of hormone/receptor pairs which include GH, erythropoietin, and other ligand/receptor pairs. The mechanisms of these ligand/receptor pairs have broad similarities, including general structures, ligand/receptor stoichiometries, and activation of several common signaling pathways. But significant variations in the structural and mechanistic details are present among these hormones and their type 1 receptors. The prolactin receptor is particularly interesting because it can be activated by three sequence-diverse human hormones: prolact

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Montell, Craig. "Drosophila sensory receptors—a set of molecular Swiss Army Knives." Genetics 217, no. 1 (January 1, 2021): 1–34. http://dx.doi.org/10.1093/genetics/iyaa011.

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Abstract Genetic approaches in the fruit fly, Drosophila melanogaster, have led to a major triumph in the field of sensory biology—the discovery of multiple large families of sensory receptors and channels. Some of these families, such as transient receptor potential channels, are conserved from animals ranging from worms to humans, while others, such as “gustatory receptors,” “olfactory receptors,” and “ionotropic receptors,” are restricted to invertebrates. Prior to the identification of sensory receptors in flies, it was widely assumed that these proteins function in just one modality such

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Koehler, Melanie, Anny Fis, Hermann J. Gruber, and Peter Hinterdorfer. "AFM-Based Force Spectroscopy Guided by Recognition Imaging: A New Mode for Mapping and Studying Interaction Sites at Low Lateral Density." Methods and Protocols 2, no. 1 (January 8, 2019): 6. http://dx.doi.org/10.3390/mps2010006.

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Ligand binding to receptors is one of the most important regulatory elements in biology as it is the initiating step in signaling pathways and cascades. Thus, precisely localizing binding sites and measuring interaction forces between cognate receptor–ligand pairs leads to new insights into the molecular recognition involved in these processes. Here we present a detailed protocol about applying a technique, which combines atomic force microscopy (AFM)-based recognition imaging and force spectroscopy for studying the interaction between (membrane) receptors and ligands on the single molecule le

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Naval, Javier, Diego de Miguel, Ana Gallego-Lleyda, Alberto Anel, and Luis Martinez-Lostao. "Importance of TRAIL Molecular Anatomy in Receptor Oligomerization and Signaling. Implications for Cancer Therapy." Cancers 11, no. 4 (March 29, 2019): 444. http://dx.doi.org/10.3390/cancers11040444.

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(TNF)-related apoptosis-inducing ligand (TRAIL) is able to activate the extrinsic apoptotic pathway upon binding to DR4/TRAIL-R1 and/or DR5/TRAIL-R2 receptors. Structural data indicate that TRAIL functions as a trimer that can engage three receptor molecules simultaneously, resulting in receptor trimerization and leading to conformational changes in TRAIL receptors. However, receptor conformational changes induced by the binding of TRAIL depend on the molecular form of this death ligand, and not always properly trigger the apoptotic cascade. In fact, TRAIL exhibits a much stronger pro-apoptoti

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Chao, W., and M. S. Olson. "Platelet-activating factor: receptors and signal transduction." Biochemical Journal 292, no. 3 (June 15, 1993): 617–29. http://dx.doi.org/10.1042/bj2920617.

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During the past two decades, studies describing the chemistry and biology of PAF have been extensive. This potent phosphoacylglycerol exhibits a wide variety of physiological and pathophysiological effects in various cells and tissues. PAF acts, through specific receptors and a variety of signal transduction systems, to elicit diverse biochemical responses. Several important future directions can be enumerated for the characterization of PAF receptors and their attendant signalling mechanisms. The recent cloning and sequence analysis of the gene for the PAF receptor will allow a number of impo

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Pardeshi, Sushma, Anupama Kumar, and Rita Dhodapkar. "Molecular Imprinting: Mimicking Molecular Receptors for Antioxidants." Materials Science Forum 675-677 (February 2011): 515–20. http://dx.doi.org/10.4028/www.scientific.net/msf.675-677.515.

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Molecularly imprinted polymers (MIPs) have been demonstrated to be a promising class of biomimetic materials that can be tailored to meet specific end use recognition requirements. Molecular imprinting is achieved by the interaction, either covalent or non-covalent between complementary groups in a template molecule and functional monomer units through polymerization. MIPs have been widely employed for divers applications such as chiral separation, chemical sensing, catalysis, drug screening, chromatographic separations and solid phase extraction. During respiration and metabolism, human body

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Norel, R., H. J. Wolfson, and R. Nussinov. "Small Molecule Recognition: Solid Angles Surface Representation and Molecular Shape Complementarity." Combinatorial Chemistry & High Throughput Screening 2, no. 4 (August 1999): 223–36. http://dx.doi.org/10.2174/1386207302666220204193837.

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Abstract: Here we examine the recognition of small molecules by their protein and DNA receptors. We focus on two questions: First, how well does the solid angle molecular surface representation perform in fitting together the surfaces of small ligands, such as drugs and cofactors to their corresponding receptors; And second, in particular, to what extent does the shape complementarity play a role in the matching (recognition) process of such small molecules. Both questions have been investigated in protein-protein binding: "Critical Points" based on solid angle calculations have been shown to

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Santiago, Luis, and Ravinder Abrol. "Understanding G Protein Selectivity of Muscarinic Acetylcholine Receptors Using Computational Methods." International Journal of Molecular Sciences 20, no. 21 (October 24, 2019): 5290. http://dx.doi.org/10.3390/ijms20215290.

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The neurotransmitter molecule acetylcholine is capable of activating five muscarinic acetylcholine receptors, M1 through M5, which belong to the superfamily of G-protein-coupled receptors (GPCRs). These five receptors share high sequence and structure homology; however, the M1, M3, and M5 receptor subtypes signal preferentially through the Gαq/11 subset of G proteins, whereas the M2 and M4 receptor subtypes signal through the Gαi/o subset of G proteins, resulting in very different intracellular signaling cascades and physiological effects. The structural basis for this innate ability of the M1

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Portoghese, Philip S. "Molecular recognition at kappa opioid receptors." Pure and Applied Chemistry 73, no. 9 (September 1, 2001): 1387–91. http://dx.doi.org/10.1351/pac200173091387.

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Structureactivity relationships are rarely straightforward, and often are more complicated than they appear. For this reason, the use of site-directed mutagenesis as a complementary tool to analyze structureactivity relationships has been invaluable. Here, we illustrate how site-directed mutagenesis has led to greater insight into the molecular basis for molecular recognition of norbinaltorphimine and to the design of novel kappa antagonists. Given the paucity of high-resolution crystal structures for membrane-bound receptors, the use of a coordinated "two-dimensional" paradigm that involves

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Indik, ZK, JG Park, S. Hunter, and AD Schreiber. "The molecular dissection of Fc gamma receptor mediated phagocytosis." Blood 86, no. 12 (December 15, 1995): 4389–99. http://dx.doi.org/10.1182/blood.v86.12.4389.bloodjournal86124389.

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Because hematopoietic cells express multiple Fc gamma receptor isoforms, the role of the individual Fc gamma receptors in phagocytosis has been difficult to define. Transfection of Fc gamma receptors into COS-1 cells, which lack endogeneous Fc gamma receptors but have phagocytic potential, has proved valuable for the study of individual Fc gamma receptor function. Using this model system, we have established that a single class of human Fc gamma receptor mediates phagocytosis in the absence of other Fc receptors and that isoforms from each Fc gamma receptor class mediate phagocytosis, although

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Wajant, Harald. "Death receptors." Essays in Biochemistry 39 (October 1, 2003): 53–71. http://dx.doi.org/10.1042/bse0390053.

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Death receptors [Fas/Apo-1/CD95, TNF-R1 [tumour necrosis factor (TNF) receptor 1], DR3 [death receptor 3], TRAIL-R1 [TNF-related apoptosis-inducing ligand receptor 1], TRAIL-R2, DR6, p75-NGFR [p75-nerve growth factor receptor], EDAR [ectodermal dysplasia receptor]] form a subgroup of the TNF-R superfamily that can induce apoptosis (programmed cell death) via a conserved cytoplasmic signalling module termed the death domain. Although death receptors have been recognized mainly as apoptosis inducers, there is growing evidence that these receptors also fulfil a variety of nonapoptotic functions.

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Lovejoy, David A., Belinda S. W. Chang, Nathan R. Lovejoy, and Jon del Castillo. "MOLECULAR EVOLUTION OF GPCRS: CRH/CRH receptors." Journal of Molecular Endocrinology 52, no. 3 (April 7, 2014): T43—T60. http://dx.doi.org/10.1530/jme-13-0238.

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Corticotrophin-releasing hormone (CRH) is the pivotal neuroendocrine peptide hormone associated with the regulation of the stress response in vertebrates. However, CRH-like peptides are also found in a number of invertebrate species. The origin of this peptide can be traced to a common ancestor of lineages leading to chordates and to arthropods, postulated to occur some 500 million years ago. Evidence indicates the presence of a single CRH-like receptor and a soluble binding protein system that acted to transduce and regulate the actions of the early CRH peptide. In vertebrates, genome duplica

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Gesek, F. A., and K. E. White. "Molecular and functional identification of beta-adrenergic receptors in distal convoluted tubule cells." American Journal of Physiology-Renal Physiology 272, no. 6 (June 1, 1997): F712—F720. http://dx.doi.org/10.1152/ajprenal.1997.272.6.f712.

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Renal nerve stimulation or circulating catecholamines activate the beta-adrenergic receptors that mediate direct effects on tubular transport. Three subtypes of beta-adrenergic receptors have been characterized: beta 1, beta 2, and beta 3. beta-Adrenergic-receptor effects on Na+ and Ca2+ transport in distal convoluted tubules (DCT) have not been established. The focus of this study was to 1) identify the subtypes of beta-adrenergic receptors in DCT cells and 2) examine functional responses to beta-receptor activation on adenosine 3',5'-cyclic monophosphate (cAMP) formation and Na+ and Ca2+ ent

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García, Yaima Henry, Orlando Reyes Zamora, Rosalba Troncoso-Rojas, Martín Ernesto Tiznado-Hernández, María Elena Báez-Flores, Elizabeth Carvajal-Millan, and Agustín Rascón-Chu. "Toward Understanding the Molecular Recognition of Fungal Chitin and Activation of the Plant Defense Mechanism in Horticultural Crops." Molecules 26, no. 21 (October 28, 2021): 6513. http://dx.doi.org/10.3390/molecules26216513.

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Large volumes of fruit and vegetable production are lost during postharvest handling due to attacks by necrotrophic fungi. One of the promising alternatives proposed for the control of postharvest diseases is the induction of natural defense responses, which can be activated by recognizing molecules present in pathogens, such as chitin. Chitin is one of the most important components of the fungal cell wall and is recognized through plant membrane receptors. These receptors belong to the receptor-like kinase (RLK) family, which possesses a transmembrane domain and/or receptor-like protein (RLP)

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Stephenson, F. A. "Structure and trafficking of NMDA and GABAA receptors." Biochemical Society Transactions 34, no. 5 (October 1, 2006): 877–81. http://dx.doi.org/10.1042/bst0340877.

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The fidelity of synaptic function is dependent on the expression of the appropriate neurotransmitter receptor subtype, the targeting and trafficking of receptors to synapses as well as the regulation of the actual number of receptors at synapses. GABAA (γ-aminobutyric acid type A) receptors and NMDA (N-methyl-D-aspartate) receptors are both examples of ligand-gated, heteromeric neurotransmitter receptors whose cell-surface expression is dynamic and tightly regulated. NMDA receptors are localized at excitatory synapses. These synapses are highly structured but dynamic, with the interplay betwee

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Kim, Jong-Hoon, János Marton, Simon Mensah Ametamey, and Paul Cumming. "A Review of Molecular Imaging of Glutamate Receptors." Molecules 25, no. 20 (October 16, 2020): 4749. http://dx.doi.org/10.3390/molecules25204749.

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Molecular imaging with positron emission tomography (PET) and single photon emission computed tomography (SPECT) is a well-established and important in vivo technique to evaluate fundamental biological processes and unravel the role of neurotransmitter receptors in various neuropsychiatric disorders. Specific ligands are available for PET/SPECT studies of dopamine, serotonin, and opiate receptors, but corresponding development of radiotracers for receptors of glutamate, the main excitatory neurotransmitter in mammalian brain, has lagged behind. This state of affairs has persisted despite the c

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Egan, Terrance, Jane Cox, and Mark Voigt. "Molecular Structure of P2X Receptors." Current Topics in Medicinal Chemistry 4, no. 8 (April 1, 2004): 821–29. http://dx.doi.org/10.2174/1568026043451005.

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Hongmao Sun and David Fry. "Molecular Modeling of Melanocortin Receptors." Current Topics in Medicinal Chemistry 7, no. 11 (June 1, 2007): 1042–51. http://dx.doi.org/10.2174/156802607780906573.

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38

Arnaud-Neu, Françoise, and Marie-José Schwing-Weill. "Calixarenes, new selective molecular receptors." Synthetic Metals 90, no. 3 (November 1997): 157–64. http://dx.doi.org/10.1016/s0379-6779(98)80001-5.

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Matsuda, Lisa A. "Molecular Aspects of Cannabinoid Receptors." Critical Reviews™ in Neurobiology 11, no. 2-3 (1997): 143–66. http://dx.doi.org/10.1615/critrevneurobiol.v11.i2-3.30.

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Bandoli, Giuliano, Marino Nicolini, Henri Lumbroso, Antonio Grassi, and Giuseppe C. Pappalardo. "Molecular determinants for drug-receptors." Journal of Molecular Structure 160, no. 3-4 (September 1987): 297–309. http://dx.doi.org/10.1016/0022-2860(87)80070-4.

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Schottelius, Margret, and Hans-Jürgen Wester. "Molecular imaging targeting peptide receptors." Methods 48, no. 2 (June 2009): 161–77. http://dx.doi.org/10.1016/j.ymeth.2009.03.012.

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Jacobson., Kenneth A., Daniel L., Boring Xiao-duo Ji, William Barrington, Vickram Ramkumar, and Gary L. Stiles. "Molecular Probes for Adenosine Receptors." Japanese Journal of Pharmacology 52 (1990): 8. http://dx.doi.org/10.1016/s0021-5198(19)32889-6.

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Yamamura, H. I., E. Varga, X. Li, T. Burkey, R. Quock, E. Malatynska, R. Knapp, et al. "Molecular Pharmacology of Opioid Receptors." Japanese Journal of Pharmacology 73 (1997): 2. http://dx.doi.org/10.1016/s0021-5198(19)33779-5.

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Nakanishi, Shigetada. "Molecular physiology of glutamate receptors." Japanese Journal of Pharmacology 67 (1995): 7. http://dx.doi.org/10.1016/s0021-5198(19)35554-4.

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Enz, Ralf, and Garry R. Cutting. "Molecular composition of GABAC receptors." Vision Research 38, no. 10 (May 1998): 1431–41. http://dx.doi.org/10.1016/s0042-6989(97)00277-0.

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REISINE, TERRY, and GRAEME I. BELL. "Molecular Biology of Somatostatin Receptors*." Endocrine Reviews 16, no. 4 (August 1995): 427–42. http://dx.doi.org/10.1210/edrv-16-4-427.

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Strasser, Ruth H., Renate Ihl-Vahl, and Rainer Marquetant. "Molecular biology of adrenergic receptors." Journal of Hypertension 10, no. 6 (June 1992): 501–6. http://dx.doi.org/10.1097/00004872-199206000-00001.

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Hollmann, Michael, Jim Boulter, Cornelia Maron, and Stephen Heinemann. "Molecular Biology of Glutamate Receptors." Kidney and Blood Pressure Research 17, no. 3-4 (1994): 182–83. http://dx.doi.org/10.1159/000173813.

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Pilpel, Yitzhak, Alona Sosinsky, and Doron Lancet. "Molecular biology of olfactory receptors." Essays in Biochemistry 33 (December 1, 1998): 93–104. http://dx.doi.org/10.1042/bse0330093.

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Bates, Michael D., Jay A. Gingrich, James R. Bunzow, Pierre Falardeau, Allen Dearry, Susan E. Senogles, Olivier Civelli, and Marc G. Caron. "Molecular Characterization of Dopamine Receptors." American Journal of Hypertension 3, no. 6_Pt_2 (June 1990): 29S—33S. http://dx.doi.org/10.1093/ajh/3.6.29s.

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