Relevant bibliographies by topics / G protein coupled receptor (GPCR)

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'G protein coupled receptor (GPCR)'

Author: Grafiati
Published: 4 June 2021
Last updated: 4 May 2024

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Journal articles on the topic "G protein coupled receptor (GPCR)"

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Jastrzebska, Beata, Yaroslav Tsybovsky, and Krzysztof Palczewski. "Complexes between photoactivated rhodopsin and transducin: progress and questions." Biochemical Journal 428, no. 1 (April 28, 2010): 1–10. http://dx.doi.org/10.1042/bj20100270.

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Activation of GPCRs (G-protein-coupled receptors) leads to conformational changes that ultimately initiate signal transduction. Activated GPCRs transiently combine with and activate heterotrimeric G-proteins resulting in GTP replacement of GDP on the G-protein α subunit. Both the detailed structural changes essential for productive GDP/GTP exchange on the G-protein α subunit and the structure of the GPCR–G-protein complex itself have yet to be elucidated. Nevertheless, transient GPCR–G-protein complexes can be trapped by nucleotide depletion, yielding an empty-nucleotide G-protein–GPCR complex that can be isolated. Whereas early biochemical studies indicated formation of a complex between G-protein and activated receptor only, more recent results suggest that G-protein can bind to pre-activated states of receptor or even couple transiently to non-activated receptor to facilitate rapid responses to stimuli. Efficient and reproducible formation of physiologically relevant, conformationally homogenous GPCR–G-protein complexes is a prerequisite for structural studies designed to address these possibilities.
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Pellissier, Lucie P., Gaël Barthet, Florence Gaven, Elisabeth Cassier, Eric Trinquet, Jean-Philippe Pin, Philippe Marin, et al. "G Protein Activation by Serotonin Type 4 Receptor Dimers." Journal of Biological Chemistry 286, no. 12 (January 19, 2011): 9985–97. http://dx.doi.org/10.1074/jbc.m110.201939.

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The discovery that class C G protein-coupled receptors (GPCRs) function as obligatory dimeric entities has generated major interest in GPCR oligomerization. Oligomerization now appears to be a common feature among all GPCR classes. However, the functional significance of this process remains unclear because, in vitro, some monomeric GPCRs, such as rhodopsin and β2-adrenergic receptors, activate G proteins. By using wild type and mutant serotonin type 4 receptors (5-HT4Rs) (including a 5-HT4-RASSL) expressed in COS-7 cells as models of class A GPCRs, we show that activation of one protomer in a dimer was sufficient to stimulate G proteins. However, coupling efficiency was 2 times higher when both protomers were activated. Expression of combinations of 5-HT4, in which both protomers were able to bind to agonists but only one could couple to G proteins, suggested that upon agonist occupancy, protomers did not independently couple to G proteins but rather that only one G protein was activated. Coupling of a single heterotrimeric Gs protein to a receptor dimer was further confirmed in vitro, using the purified recombinant WT RASSL 5-HT4R obligatory heterodimer. These results, together with previous findings, demonstrate that, differently from class C GPCR dimers, class A GPCR dimers have pleiotropic activation mechanisms.
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Bhattacharya, M., A. V. Babwah, and S. S. G. Ferguson. "Small GTP-binding protein-coupled receptors." Biochemical Society Transactions 32, no. 6 (October 26, 2004): 1040–44. http://dx.doi.org/10.1042/bst0321040.

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Heterotrimeric GPCRs (G-protein-coupled receptors) form the largest group of integral membrane receptor proteins and mediate diverse physiological processes. In addition to signalling via heterotrimeric G-proteins, GPCRs can also signal by interacting with various small G-proteins to regulate downstream effector pathways. The small G-protein superfamily is structurally classified into at least five families: the Ras, Rho/Rac/cdc42, Rab, Sar1/Arf and Ran families. They are monomeric G-proteins with molecular masses over the range 20–30 kDa, which function as molecular switches to control many eukaryotic cell functions. Several studies have provided evidence of crosstalk between GPCRs and small G-proteins. It is well documented that GPCR signalling through heterotrimeric G-proteins can lead to the activation of Ras and Rho GTPases. In addition, RhoA, Rabs, ARFs and ARF GEFs (guanine nucleotide-exchange factors) can associate directly with GPCRs, and GPCRs may also function as GEFs for small GTPases. In this review, we summarize the recent progress made in understanding the interaction between GPCRs and small GTPases, focusing on understanding how the association of small G-proteins with GPCRs and GPCR-regulatory proteins may influence GPCR signalling and intracellular trafficking.
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Erlandson, Sarah C., Conor McMahon, and Andrew C. Kruse. "Structural Basis for G Protein–Coupled Receptor Signaling." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 1–18. http://dx.doi.org/10.1146/annurev-biophys-070317-032931.

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G protein–coupled receptors (GPCRs), which mediate processes as diverse as olfaction and maintenance of metabolic homeostasis, have become the single most effective class of therapeutic drug targets. As a result, understanding the molecular basis for their activity is of paramount importance. Recent technological advances have made GPCR structural biology increasingly tractable, offering views of these receptors in unprecedented atomic detail. Structural and biophysical data have shown that GPCRs function as complex allosteric machines, communicating ligand-binding events through conformational change. Changes in receptor conformation lead to activation of effector proteins, such as G proteins and arrestins, which are themselves conformational switches. Here, we review how structural biology has illuminated the agonist-induced cascade of conformational changes that culminate in a cellular response to GPCR activation.
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Hay, Debbie L., Christopher S. Walker, Joseph J. Gingell, Graham Ladds, Christopher A. Reynolds, and David R. Poyner. "Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins." Biochemical Society Transactions 44, no. 2 (April 11, 2016): 568–73. http://dx.doi.org/10.1042/bst20150237.

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Receptor activity-modifying proteins (RAMPs) are single pass membrane proteins initially identified by their ability to determine the pharmacology of the calcitonin receptor-like receptor (CLR), a family B G protein-coupled receptor (GPCR). It is now known that RAMPs can interact with a much wider range of GPCRs. This review considers recent developments on the structure of the complexes formed between the extracellular domains (ECDs) of CLR and RAMP1 or RAMP2 as these provide insights as to how the RAMPs direct ligand binding. The range of RAMP interactions is also considered; RAMPs can interact with numerous family B GPCRs as well as examples of family A and family C GPCRs. They influence receptor expression at the cell surface, trafficking, ligand binding and G protein coupling. The GPCR–RAMP interface offers opportunities for drug targeting, illustrated by examples of drugs developed for migraine.
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Gupte, Tejas M., Rabia U. Malik, Ruth F. Sommese, Michael Ritt, and Sivaraj Sivaramakrishnan. "Priming GPCR signaling through the synergistic effect of two G proteins." Proceedings of the National Academy of Sciences 114, no. 14 (March 21, 2017): 3756–61. http://dx.doi.org/10.1073/pnas.1617232114.

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Although individual G-protein–coupled receptors (GPCRs) are known to activate one or more G proteins, the GPCR–G-protein interaction is viewed as a bimolecular event involving the formation of a ternary ligand–GPCR–G-protein complex. Here, we present evidence that individual GPCR–G-protein interactions can reinforce each other to enhance signaling through canonical downstream second messengers, a phenomenon we term “GPCR priming.” Specifically, we find that the presence of noncognate Gq protein enhances cAMP stimulated by two Gs-coupled receptors, β2-adrenergic receptor (β2-AR) and D1 dopamine receptor (D1-R). Reciprocally, Gs enhances IP1 through vasopressin receptor (V1A-R) but not α1 adrenergic receptor (α1-AR), suggesting that GPCR priming is a receptor-specific phenomenon. The C terminus of either the Gαs or Gαq subunit is sufficient to enhance Gα subunit activation and cAMP levels. Interaction of Gαs or Gαq C termini with the GPCR increases signaling potency, suggesting an altered GPCR conformation as the underlying basis for GPCR priming. We propose three parallel mechanisms involving (i) sequential G-protein interactions at the cognate site, (ii) G-protein interactions at distinct allosteric and cognate sites on the GPCR, and (iii) asymmetric GPCR dimers. GPCR priming suggests another layer of regulation in the classic GPCR ternary-complex model, with broad implications for the multiplicity inherent in signaling networks.
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N'Diaye, Elsa-Noah, Aylin C. Hanyaloglu, Kimberly K. Kajihara, Manojkumar A. Puthenveedu, Ping Wu, Mark von Zastrow, and Eric J. Brown. "The Ubiquitin-like Protein PLIC-2 Is a Negative Regulator of G Protein-coupled Receptor Endocytosis." Molecular Biology of the Cell 19, no. 3 (March 2008): 1252–60. http://dx.doi.org/10.1091/mbc.e07-08-0775.

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The activity of many signaling receptors is regulated by their endocytosis via clathrin-coated pits (CCPs). For G protein-coupled receptors (GPCRs), recruitment of the adaptor protein arrestin to activated receptors is thought to be sufficient to drive GPCR clustering in CCPs and subsequent endocytosis. We have identified an unprecedented role for the ubiquitin-like protein PLIC-2 as a negative regulator of GPCR endocytosis. Protein Linking IAP to Cytoskeleton (PLIC)-2 overexpression delayed ligand-induced endocytosis of two GPCRs: the V2 vasopressin receptor and β-2 adrenergic receptor, without affecting endocytosis of the transferrin or epidermal growth factor receptor. The closely related isoform PLIC-1 did not affect receptor endocytosis. PLIC-2 specifically inhibited GPCR concentration in CCPs, without affecting membrane recruitment of arrestin-3 to activated receptors or its cellular levels. Depletion of cellular PLIC-2 accelerated GPCR endocytosis, confirming its regulatory function at endogenous levels. The ubiquitin-like domain of PLIC-2, a ligand for ubiquitin-interacting motifs (UIMs), was required for endocytic inhibition. Interestingly, the UIM-containing endocytic adaptors epidermal growth factor receptor protein substrate 15 and Epsin exhibited preferential binding to PLIC-2 over PLIC-1. This differential interaction may underlie PLIC-2 specific effect on GPCR endocytosis. Identification of a negative regulator of GPCR clustering reveals a new function of ubiquitin-like proteins and highlights a cellular requirement for exquisite regulation of receptor dynamics.
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Ayoub, Mohammed Akli, and Ranjit Vijayan. "Hemorphins Targeting G Protein-Coupled Receptors." Pharmaceuticals 14, no. 3 (March 7, 2021): 225. http://dx.doi.org/10.3390/ph14030225.

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Hemorphins are short peptides produced by the proteolysis of the beta subunit of hemoglobin. These peptides have diverse physiological effects especially in the nervous and the renin-angiotensin systems. Such effects occur through the modulation of a diverse range of proteins including enzymes and receptors. In this review, we focus on pharmacological and functional targeting of G protein-coupled receptors (GPCRs) by hemorphins and their implication in physiology and pathophysiology. Among GPCRs, the opioid receptors constitute the first set of targets of hemorphins with implication in analgesia. Subsequently, several other GPCRs have been reported to be directly or indirectly involved in hemorphins’ action. This includes the receptors for angiotensin II, oxytocin, bombesin, and bradykinin, as well as the human MAS-related G protein-coupled receptor X1. Interestingly, both orthosteric activation and allosteric modulation of GPCRs by hemorphins have been reported. This review links hemorphins with GPCR pharmacology and signaling, supporting the implication of GPCRs in hemorphins’ effects. Thus, this aids a better understanding of the molecular basis of the action of hemorphins and further demonstrates that hemorphin-GPCR axis constitutes a valid target for therapeutic intervention in different systems.
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Vidad, Ashley Ryan, Stephen Macaspac, and Ho Leung Ng. "Locating ligand binding sites in G-protein coupled receptors using combined information from docking and sequence conservation." PeerJ 9 (September 24, 2021): e12219. http://dx.doi.org/10.7717/peerj.12219.

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GPCRs (G-protein coupled receptors) are the largest family of drug targets and share a conserved structure. Binding sites are unknown for many important GPCR ligands due to the difficulties of GPCR recombinant expression, biochemistry, and crystallography. We describe our approach, ConDockSite, for predicting ligand binding sites in class A GPCRs using combined information from surface conservation and docking, starting from crystal structures or homology models. We demonstrate the effectiveness of ConDockSite on crystallized class A GPCRs such as the beta2 adrenergic and A2A adenosine receptors. We also demonstrate that ConDockSite successfully predicts ligand binding sites from high-quality homology models. Finally, we apply ConDockSite to predict the ligand binding sites on a structurally uncharacterized GPCR, GPER, the G-protein coupled estrogen receptor. Most of the sites predicted by ConDockSite match those found in other independent modeling studies. ConDockSite predicts that four ligands bind to a common location on GPER at a site deep in the receptor cleft. Incorporating sequence conservation information in ConDockSite overcomes errors introduced from physics-based scoring functions and homology modeling.
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Whorton, Matthew R., Michael P. Bokoch, Søren G. F. Rasmussen, Bo Huang, Richard N. Zare, Brian Kobilka, and Roger K. Sunahara. "A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein." Proceedings of the National Academy of Sciences 104, no. 18 (April 23, 2007): 7682–87. http://dx.doi.org/10.1073/pnas.0611448104.

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G protein-coupled receptors (GPCRs) respond to a diverse array of ligands, mediating cellular responses to hormones and neurotransmitters, as well as the senses of smell and taste. The structures of the GPCR rhodopsin and several G proteins have been determined by x-ray crystallography, yet the organization of the signaling complex between GPCRs and G proteins is poorly understood. The observations that some GPCRs are obligate heterodimers, and that many GPCRs form both homo- and heterodimers, has led to speculation that GPCR dimers may be required for efficient activation of G proteins. However, technical limitations have precluded a definitive analysis of G protein coupling to monomeric GPCRs in a biochemically defined and membrane-bound system. Here we demonstrate that a prototypical GPCR, the β2-adrenergic receptor (β2AR), can be incorporated into a reconstituted high-density lipoprotein (rHDL) phospholipid bilayer particle together with the stimulatory heterotrimeric G protein, Gs. Single-molecule fluorescence imaging and FRET analysis demonstrate that a single β2AR is incorporated per rHDL particle. The monomeric β2AR efficiently activates Gs and displays GTP-sensitive allosteric ligand-binding properties. These data suggest that a monomeric receptor in a lipid bilayer is the minimal functional unit necessary for signaling, and that the cooperativity of agonist binding is due to G protein association with a receptor monomer and not receptor oligomerization.
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Dissertations / Theses on the topic "G protein coupled receptor (GPCR)"

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Sheng, Yinglun. "G protein signaling and G protein coupled receptor (GPCR) pathway in Xenopus oocyte maturation." Thesis, University of Ottawa (Canada), 2005. http://hdl.handle.net/10393/29262.

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Xenopus laevis oocytes are physiologically arrested at the first meiotic prophase. Progesterone reinitiates meiosis (maturation) through inhibition of an oocyte adenylyl cyclase (AC) and reduction of intracellular cAMP. However, the mechanism by which progesterone regulates AC activity and cAMP level still remains unclear. In this thesis, I summarize work I conducted that collectively helps elucidate how high levels of cAMP might be achieved in G2 arrested oocytes. In Chapter 2, I describe our finding that inhibiting endogenous G-protein betagamma subunits, through the use of two structurally distinct Gbetagamma scavengers, causes hormone-independent oocyte maturation. In contrast, overexpression of Xenopus Gbeta1, alone or together with bovine Ggamma2, inhibits progesterone-induced oocyte maturation. These results for the first time implicate that an endogenous G protein coupled receptor system releases a Gbetagamma complex as the dominant meiosis inhibitor. Chapter 3 describes my research aiming to reveal the identity of the oocyte AC responsible for generating meiosis-inhibiting cAMP. I provide further evidence here that the ability of Gbetagamma to inhibit meiosis is attributed to the activation of an endogenous AC, rather than other possible Gbetagamma effectors. Through molecular cloning and biochemical characterization, I discovered that the likely AC candidate is Xenopus AC7, an isoform that is activated by Gbetagamma, but only in the presence of GTP-bound Gsalpha. The identification of xAC7 suggests that the maintenance of high levels of cAMP may require the cooperation of Gsalpha and Gbetagamma. Finally, in Chapter 4, I describe our efforts in identifying the GPCR(s) responsible for activating the cAMP signaling in prophase-arrested oocytes. A screening of known antagonists of GPCR(s) led to the identification of ritanserin, a potent antagonist of serotonin receptors, as a potent maturation inducer in Xenopus oocytes. Pharmacological and molecular studies, however, have ruled out the involvement of a known serotonin receptor in meiosis arrest. Instead, the most likely candidate is a "constitutively activated" GPCR that bears structural similarities to Xenopus serotonin receptor 7.
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Park, Jung Hee. "Crystal structure of ligand-free G-protein-coupled receptor opsin." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2010. http://dx.doi.org/10.18452/16049.

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Rhodopsin ist als Sehpigment der Photorezeptorzellen einer der am aktivsten untersuchten GPCRs. Es besteht aus dem Apoprotein Opsin und dem inversen Agonisten 11-cis-Retinal. Der inaktivierende Ligand ist in der sieben Transmembran- Helix (TM)-Struktur des Rezeptors kovalent gebunden und muss durch Licht cis/trans-isomerisiert werden, um den Rezeptor zu aktivieren. Der aktivierte Rezep-tor katalysiert den Nukleotidaustausch im G-Protein und zerfällt innerhalb von Minuten in Opsin und all-trans-Retinal. Das visuelle Pigment wird dann durch erneute Beladung des Opsins mit 11-cis-Retinal wieder hergestellt. In der vorliegenden Arbeit wird die erfolgreiche Kristallisation des nativen Opsins aus der Stäbchenzelle der Rinderretina und die Bestimmung der Proteinstruktur bei 2.9 Å Auf-lösung dargestellt. Im Vergleich zur bekannten Struktur des inaktiven Rhodopsins zeigt Opsin deutliche Strukturänderungen in den konservierten E(D)RY und NPxxY(x)5,6F Regionen und in TM5-TM7. Auf der intrazellulären Seite ist TM6 ca. 6-7 Å nach außen gekippt, während die TM5 Helix verlängert und näher zu TM6 verschoben ist. Durch die strukturellen Änderungen, von denen einige einem aktiven GPCR Zustand zugeschrieben werden können, wird die leere Retinalbindungstasche reorganisiert, um zwei Öffnungen für Aus- und Eintritt von Retinal bereitzustellen. Die Struktur von Opsin liefert neue Erkenntnisse zur Bindung von hydrophoben Liganden an GPCRs, zur GPCR-Aktivierung und zur Signalübertragung auf das G-Protein.
Rhodopsin as the visual pigment in photoreceptor cells is one of the most actively studied GPCRs. It consists of the apoprotein opsin and the inverse agonist, 11-cis-retinal. The inactivating ligand is bound in the seven-transmembrane helix (TM) bundle and cis/trans-isomerized by light to activate the receptor. The active receptor state is capable of catalyzing nucleotide exchange in the G protein and decays within minutes into opsin and all-trans-retinal. The visual pigment is then restored by reloading opsin with new 11-cis-retinal. In the present work, the successful crystallization of native opsin from bovine retinal rod cells and determination of the protein structure to 2.9 Å resolution is presented. Compared with the known structure of inactive rhodopsin, opsin displays prominent structural changes in the conserved E(D)RY and NPxxY(x)5,6F regions and TM5-TM7. At the cytoplasmic side, TM6 is tilted outwards by 6-7 Å, whereas the helix structure of TM5 is more elongated and close to TM6. These structural changes, of which some are attributed to an active GPCR state, reorganize the empty retinal binding pocket to disclose two openings for exit and entry of retinal. The opsin structure thus sheds new light on binding of hydrophobic ligands to GPCRs, GPCR activation and signal transfer to the G protein.
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Younkin, Jason W. "Allosteric Effects of G-Protein Coupled Receptor Heteromerization: Relevance to Psychosis." VCU Scholars Compass, 2016. http://scholarscompass.vcu.edu/etd/4457.

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G-protein coupled receptors (GPCRs) implicated in disease are the predominant pharmaceutical targets. Growing evidence suggests that GPCRs form homo- and heteromeric complexes, resulting in allosteric functional changes. Ligands targeting one receptor can alter the function of the other receptor or receptors. Knowledge of these functional changes will provide unique opportunities to treat diseases. We examined two GPCR heteromers implicated in psychosis: mGlu2R-5HT2AR and D2R-5HT2AR. Using whole-cell patch clamp, we studied HEK-293 cells stably transfected with mGlu2R and 5HT2AR. Maximal heteromer formation allows inverse agonists to increase the G-protein activity of the opposite receptor, while sub-maximal heteromer formation does not. However, similar results are obtained in sub-maximal heteromer cells by applying a combination of a mGlu2R synthetic agonist with a 5HT2AR anti-psychotic drug. These results confirm our oocyte results, now in a mammalian cell line. Using two-electrode voltage clamp, we also investigated the allosteric changes upon heteromerization of D2R-5HT2AR in oocytes injected with appropriate cRNAs. Heteromer formation in the presence of dopamine or serotonin results in an increase in G-protein activity of each receptor while the simultaneous presence of both neurotransmitters further increases the G-protein activity. The addition of synthetic agonists or anti-psychotics decreases the G-protein activity of the opposite receptor while agonizing or antagonizing its target receptor, respectively. Maximal allosteric effects upon D2R-5HT2AR formation only occur at a specific cRNA injection ratio, but partial effects exist at other ratios. Our data suggest that allosteric functional changes upon heteromerization are physiologically relevant and are mostly different when comparing mGlu2R-5HT2AR to D2R-5HT2AR.
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Kumas, Gozde. "Detecting G-protein Coupled Receptor Interactions Using Enhanced Green Fluorescent Protein Reassembly." Master's thesis, METU, 2012. http://etd.lib.metu.edu.tr/upload/12614136/index.pdf.

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The largest class of cell surface receptors in mammalian genomes is the superfamily of G protein-coupled receptors (GPCRs) which are activated by a wide range of extracellular responses such as hormones, pheromones, odorants, and neurotransmitters. Drugs which have therapeutic effects on a wide range of diseases are act on GPCRs. In contrast to traditional idea, it is recently getting accepted that G-protein coupled receptors can form homo- and hetero-dimers and this interaction could have important role on maturation, internalization, function or/and pharmacology. Bimolecular fluorescence complementation technique (BiFC)
is an innovative approach based on the reassembly of protein fragments which directly report interactions. In our study we implemented this technique for detecting and visualizing the GPCR interactions in yeast cells. The enhanced green fluorescent protein (EGFP) fractionated into two fragments at genetic level which does not possess fluorescent function. The target proteins which are going to be tested in terms of interaction are modified with the non-functional fragments, to produce the fusion proteins. The interaction between two target proteins, in this study Ste2p receptors which are alpha pheromone receptors from Saccharomyces cerevisiae, enable the fragments to come in a close proximity and reassemble. After reassembly, EGFP regains its fluorescent function which provides a direct read-out for the detection of interaction. Further studies are required to determine subcellular localization of the interaction. Moreover, by using the fusion protein partners constructed in this study, effects of agonist/antagonist binding and post-translational modifications such as glycosylation and phosphorylation can be examined. Apart from all, optimized conditions for BiFC technique will guide for revealing new protein-protein interactions.
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Sherrill, Joseph D. "Functional Analysis of the Murine Cytomegalovirus G Protein-coupled Receptor M33." University of Cincinnati / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1225745444.

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Bahena, Silvia. "Computational Methods for the structural and dynamical understanding of GPCR-RAMP interactions." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-416790.

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Protein-protein interaction dominates all major biology processes in living cells. Recent studies suggestthat the surface expression and activity of G protein-coupled receptors (GPCRs), which are the largestfamily of receptors in human cells, can be modulated by receptor activity–modifying proteins (RAMPs). Computational tools are essential to complement experimental approaches for the understanding ofmolecular activity of living cells and molecular dynamics simulations are well suited to providemolecular details of proteins function and structure. The classical atom-level molecular modeling ofbiological systems is limited to small systems and short time scales. Therefore, its application iscomplicated for systems such as protein-protein interaction in cell-surface membrane. For this reason, coarse-grained (CG) models have become widely used and they represent an importantstep in the study of large biomolecular systems. CG models are computationally more effective becausethey simplify the complexity of the protein structure allowing simulations to have longer timescales. The aim of this degree project was to determine if the applications of coarse-grained molecularsimulations were suitable for the understanding of the dynamics and structural basis of the GPCRRAMP interactions in a membrane environment. Results indicate that the study of protein-proteininteractions using CG needs further improvement with a more accurate parameterization that will allowthe study of complex systems.
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Troupiotis-Tsaïlaki, Anastassia. "Lipid-GPCR interactions: from activation of sphingosine-1-phosphate receptors to modulation of vasopressin V2 receptor function." Doctoral thesis, Universite Libre de Bruxelles, 2015. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/216727.

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GPCRs form the largest family of membrane proteins in human genome and mediate signal transmission in a wide panel of essential physiological processes, and they are thus a major source of pharmaceutical targets. Investigating GPCR interactions with their cognate ligands and their membrane environment is crucial to understand their function at a molecular level. While major breakthroughs in the determination of high resolution structures of GPCRs in inactive and active states have shed a new light on the structural basis of GPCR activation process, complementary approaches are needed to investigate its dynamic aspects in the context of a native lipid environment. Our research work falls within this scope and hinges on two main issues: on the one hand, understand which structural features of the agonist underlie the activation of S1P receptors; on the other hand determine if membrane lipids modulate the structure and the function of the vasopressin V2 receptor (V2R). First, we investigated the functional response of S1P1, S1P2, S1P4 and S1P5 receptors expressed in mammalian cells to a series of synthetic derivatives of the native ligand sphingosine-1-phosphate, of variable alkyl chain length. Our data demonstrated that the hydrophobic tail of the ligand is crucial to induce activation in S1P receptors family, and revealed subtype-specificities regarding the influence of the alkyl chain length. Our experimental results combined with molecular dynamics simulation lead us to propose an activation mechanism for S1P receptors family. In the second part of our work, we reconstituted purified V2R into systems of controlled lipid composition, mimicking the membrane bilayer. Structural and functional characterization of the receptor in different lipid environments, using infrared and fluorescence spectroscopy approaches, revealed that the lipid composition affects V2R conformation and its interaction with a specific ligand. Taken together, our research work contributes to a better understanding of GPCRs activation mechanism and its regulation by lipid environment.
Les récepteurs couplés aux protéines G (GPCRs) forment la plus grande famille de protéines membranaires du génome humain et contribuent à une kyrielle de processus physiologiques essentiels, qui leur confèrent un intérêt pharmacologique majeur. Étudier l'interaction de ces protéines avec leurs ligands et leur environnement membranaire est primordial pour appréhender leur fonctionnement à l’échelle moléculaire. Bien que de remarquables avancées dans la détermination de structures à haute résolution de GPCRs à l'état inactif et actif aient permis de comprendre certaines bases structurales du fonctionnement des récepteurs, des approches complémentaires donnant un aperçu des aspects dynamiques et dans un environnement natif sont nécessaires pour cerner pleinement leur mécanisme d'activation. Notre travail de thèse s'inscrit dans cette problématique et s'articule autour de deux sujets: d'une part, comprendre quelles caractéristiques structurales du ligand sous-tendent l'activation de la famille des récepteurs au sphingosine-1-phosphate (S1P); d'autre part, déterminer si les lipides de la membrane plasmique modulent la structure et la fonction du récepteur à la vasopressine V2. Pour répondre à notre première question, nous avons étudié la réponse fonctionnelle en système cellulaire des récepteurs S1P1, S1P2, S1P4 et S1P5 à des composés synthétiques dérivés du S1P, portant des chaînes alkyles de longueur variable. Nos données mettent en évidence que la longueur de la chaîne hydrocarbonée du ligand est un paramètre crucial dans sa capacité d'induire l'activation du récepteur et ce pour l'ensemble des sous-types étudiés. De plus, nos résultats suggèrent que le comportement vis-à-vis de la longueur de chaîne dépend du sous-type de récepteur considéré. Nos résultats expérimentaux, combinés à une approche de modélisation dynamique, ont abouti à proposer un mécanisme d'activation pour la famille des récepteurs au S1P. Dans le second volet de notre travail, nous avons reconstitué le récepteur V2 purifié dans des systèmes de composition lipidique contrôlée, mimant la bicouche membranaire. Nous avons procédé à la caractérisation structurale et fonctionnelle du récepteur inséré dans différentes types de lipides, par des méthodes spectroscopiques infrarouge et de fluorescence. Les données obtenues suggèrent que la composition lipidique affecte la conformation et la fonction du récepteur. L'ensemble de nos travaux contribue ainsi à une meilleure compréhension du mécanisme d'activation des GPCRs et de leur régulation par l'environnement lipidique.
Doctorat en Sciences
info:eu-repo/semantics/nonPublished
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8

Bucco, Olgatina, and olgatina@gmail com. "Preparing, measuring and capturing G-protein coupled receptor (GPCR) signalling complexes for future development of cell-free assay technologies." Flinders University. medicine, 2006. http://catalogue.flinders.edu.au./local/adt/public/adt-SFU20060703.114912.

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G-protein coupled receptors (GPCRs) are integral membrane proteins which represent primary cellular targets for intracellular signalling. Many of these receptors are altered in disease states and hence are the target for over 50% of marketed drugs. Despite their physiological importance, high-throughput, cell-free assays which measure functional or signalling activity are only recently being investigated. The current approach by the pharmaceutical industry to initially screen compounds for functionality is to use heterologous cell-based assay formats. The aim of this work was to reconstitute a cell-free GPCR signalling system on an appropriate platform (surface) as a prototype for future rapid drug screening and other applications. The proof-of-concept approach involved using the �2A-adrenergic receptor (�2A-AR) containing cell membrane preparations as the model GPCR, reconstituted with a set of heterotrimeric G-proteins; G�i1 and �1�2 (the signal transducing complex being termed a �transductosome�). However, other receptors and G-proteins were also investigated. Receptors were initially obtained from natural (tissue) sources, however in the later stages they were expressed in a heterologous system (insect or mammalian expression system). G-proteins were expressed in Spodoptera frugiperida (Sf9) insect cells using the baculovirus expression system. Receptor expression was verified by radioligand binding assays and endogenous G-proteins were removed from membrane preparations using the chaotropic agent urea to allow for reconstitution with purified G-proteins. Signal transduction through the transductosome was measured using the [35S]GTP�S binding assay. Receptor activated [35S]GTP�S binding was used to determine functional reconstitution and to validate that the system was working in the normal physiological manner both on and off a surface (with surface attachment being via histidine attachment on the G�i1 (6xHIS) subunit). Using the captured (surface-attached) transductosomes, the IC50 values for Rauwolscine, Yohimbine (potent �2-AR antagonists), Prazosin (potent �1- AR antagonist) and Propranolol (�-AR antagonist) displayed the appropriate rank order for this class of receptor. This cell-free, surface-attached signalling complex prototype may have use in the future development of drug screening and discovery assay technologies as well as other applications as an alternative to cell-based assays which are not readily amendable to miniaturisation, long term storage and therefore stable robust microarray formats.
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Byrne, Eamon. "Molecular mechanisms of Hedgehog signal transduction by the G-protein coupled receptor smoothened." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:38abef20-ae98-4835-919c-73afc21a6252.

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The Hedgehog signalling pathway is an essential developmental pathway present in all bilaterians that is involved in embryogenesis, body patterning and stem cell homeostasis. Dysregulation of the Hh pathway leads to various kinds of cancer, such as basal cell carcinoma and medulloblastoma. Smoothened (SMO), a Frizzled-type G-protein coupled receptor (GPCR), is the essential transmembrane signal transducer within the Hh pathway, conveying the signal from the upstream transmembrane protein, Patched1 (Ptc1), to the downstream intracellular proteins. The mechanisms by which SMO transmits the Hh signal from the extracellular environment, through the plasma membrane and to the intracellular proteins are not known. In this thesis, I present my work into the structural and functional characterisation of the extracellular and transmembrane domains (TMD) of human SMO in order to better understand the molecular mechanisms of its signal transduction. The extracellular region of SMO contains a highly conserved cysteine-rich domain (CRD) and a linker domain (LD). I present the first crystal structure of the CRD, LD and TMD of SMO, which is also the first crystal structure of a GPCR with a large functional extracellular domain. This structure revealed a domain architecture for SMO that enables regulation of its transmembrane domain by its extracellular domains. It also revealed a cholesterol molecule bound to the CRD, which we subsequently determined to be a new endogenous small-molecule agonist for SMO. I present five further structures of SMO bound to different small molecule agonists and antagonists. Together, these structures demonstrate that the position of the CRD relative to the TMD reflects the activation state of SMO. We also generated nanobodies against the extracellular region of SMO in order to stabilise its conformation. These studies not only improve our understanding of the workings of a key transmembrane protein within a fundamental signalling pathway but will also aid efforts to develop better therapeutics for an important cancer target.
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Gata, Gabriel. "Regulated export of G-protein coupled receptors." Thesis, Paris 5, 2014. http://www.theses.fr/2014PA05T066.

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La plus grande famille de récepteurs membranaires est constituée par des récepteurs à sept domaines transmembranaires couplés aux protéines G (RCPG). Ces récepteurs sont impliqués dans un grand nombre de réponses cellulaires physiologiques et pathologiques et représentent la ciblé de une grande majorité des produits thérapeutiques. La fonction d’un récepteur est déterminée par la quantité de récepteur fonctionnel à la surface cellulaire, qui dépend de différents paramètres comme le niveau de biosynthèse, l’export vers la surface cellulaire à partir de stocks intracellulaires, l’endocytose et les modifications post-transcriptionelles (ex. phosphorylation). Le nouveau concept d’export régulé pour les RCPG présent l’importance physiologique de la rétention de récepteurs, leur relargage, leur interaction avec les partenaires chaperonnes et les escortes. Les études présentées ici concernent les mécanismes d’export régulé de deux RCPG, le récepteur métabotropique de l’acide γ-amino butyrique (GABAB) et le récepteur de chimiokines CC 5 (CCR5). GABAB est un récepteur constitué de deux sous-unités GB1 et GB2 et CCR5 est probablement un homo-dimer. GB1 ainsi que CCR sont retenus dans des compartiments intracellulaire (RE et appareil Golgi) d’où ils sont relâchés en réponse à un signal extern (CCR5) ou/et en interagissant avec protéines d’escorte (comme CD4 pour CCR5 et GB2 pour GB1). L’objectif de ces études était de comprendre le mécanisme de rétention de ces récepteurs et leur régulation. Dans ce contexte, nous avons déterminé en utilisant des approches biophysiques et biochimiques que ces récepteurs interagissent de façon spécifique avec les membres de Prenylated Rab Acceptors Family (PRAF). Ces protéines sont résidentes dans le RE (PRAF2 et PRAF3) et dans le appareil Golgi (PRAF1) où elles fonctionnent comme de gatekeepers pour les récepteurs. Nous avons pu démontrer que PRAF2 interagie de manière spécifique avec des motifs de rétention connus pour leur implication dans la rétention de récepteurs. Cette interaction détermine une rétention au niveau de RE donc régule de façon négatif l’export vers la membrane cellulaire. Dans le cas de récepteur GABAB, l’interaction de GB2 avec GB1 permet la libération de GB1 de sa rétention par PRAF2 par simple compétition. La modification de l’équilibre stoichiométrique entre les gatekeepers PRAF et les protéines d’escorte pour les récepteurs induit des modifications de la fonction du récepteur in vitro et in vivo. Les PRAFs sont ubiquitaires et peuvent interagir avec plusieurs RCPG représentant dans ce cas des régulateurs majors de la fonction de RCPG dans des conditions physiologiques et pathologiques
The largest family of membrane receptors is constituted by conserved seven-membrane domain spanning receptors, the G-protein coupled receptors (GPCRs). They are involved in numerous cell responses and diseases thus being a major drug target. Receptor function is determined by the amount of active receptors at the cell surface, which depends on various parameters, such as the biosynthetic rate, the export to the cell surface from internal stores, the endocytosis and post-transcriptional modifications (i.e. phosphorylation). Only recently, the importance of the regulated export has emerged, shedding new light on the physiological role of receptor retention, release, chaperoning and escorting. This work concerns the regulated export mechanisms of two members of the GPCRs family, the chemokine receptor 5 (CCR5) and the metabotropic receptor of the g amino butyric acid (GABAB). Whereas CCR5 is likely a homo-dimer of 2 identical protomers, GABAB is an obligatory hetero-dimer of 2 distinct subunit known as GB1 and GB2. Both CCR5 and GB1 are retained in intracellular compartments (the ER and the Golgi) from which they are released in response to external signals (CCR5) and/or interaction with “private escort proteins” (CD4 for CCR5 and GB2 for GB1). The main goal of our work was to understand the mechanism of retention of these receptors and its regulation. In this context, we determined using biochemical and biophysical approaches that these GPCRs specifically interact with the members of the Prenylated Rab Acceptor Family (PRAF). These proteins are resident either in the ER (PRAF2 and PRAF3) or in the Golgi apparatus (PRAF1) where they function as receptor gatekeepers. Indeed, we could document for PRAF2 that this protein likely interacts directly with previously identified receptor retention motifs and inhibits receptor egress from the ER and subsequent trafficking to the plasma membrane. In the context of the GABAB receptor, PRAF2-dependent retention of GB1 can be overridden by GB2 via simple competition. Perturbing the stoichiometry of PRAF gatekeepers respective to that of receptors significantly perturbs receptor function both in vitro and in vivo. Because PRAFs are ubiquitous and seem to interact with many other GPCRs, they might represent major regulators of receptor function both in physiological and pathological conditions
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Books on the topic "G protein coupled receptor (GPCR)"

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Annette, Gilchrist, ed. GPCR molecular pharmacology and drug targeting: Shifting paradigms and new directions. Hoboken, N.J: Wiley, 2010.

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R, George Susan, and O'Dowd Brian Francis 1950-, eds. G protein-coupled receptor-protein interactions. Hoboken, N.J: Wiley-Liss, 2005.

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Herrick-Davis, Katharine, Graeme Milligan, and Giuseppe Di Giovanni, eds. G-Protein-Coupled Receptor Dimers. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8.

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Stevens, Craig W., ed. G Protein-Coupled Receptor Genetics. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-779-2.

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Gurevich, Vsevolod V., Eugenia V. Gurevich, and John J. G. Tesmer, eds. G Protein-Coupled Receptor Kinases. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3798-1.

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Tiberi, Mario, ed. G Protein-Coupled Receptor Signaling. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9121-1.

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Martins, Sofia Aires M., and Duarte Miguel F. Prazeres, eds. G Protein-Coupled Receptor Screening Assays. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1221-7.

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Prazeres, Duarte Miguel F., and Sofia Aires M. Martins, eds. G Protein-Coupled Receptor Screening Assays. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2336-6.

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Adhesion-GPCRs structure to function. New York, N.Y: Springer Science+Business Media, 2010.

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Running, Mark P., ed. G Protein-Coupled Receptor Signaling in Plants. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-532-3.

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Book chapters on the topic "G protein coupled receptor (GPCR)"

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Grinde, Ellinor, and Katharine Herrick-Davis. "Class A GPCR: Serotonin Receptors." In G-Protein-Coupled Receptor Dimers, 129–72. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_6.

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Gingell, Joseph J., Christopher S. Walker, and Debbie L. Hay. "Class B GPCR: Receptors and RAMPs." In G-Protein-Coupled Receptor Dimers, 289–305. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_11.

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Ferré, Sergi. "Allosterism Within GPCR Oligomers: Back to Symmetry." In G-Protein-Coupled Receptor Dimers, 433–50. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_17.

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Fan, Qing R., William Y. Guo, Yong Geng, and Marisa G. Evelyn. "Class C GPCR: Obligatory Heterodimerization of GABAB Receptor." In G-Protein-Coupled Receptor Dimers, 307–25. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_12.

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Harikumar, Kaleeckal G., and Laurence J. Miller. "Secretin Receptor Dimerization. Prototypic of Class B GPCR Behavior." In G-Protein-Coupled Receptor Dimers, 273–87. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_10.

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Sleno, Rory, Dominic Devost, and Terence E. Hébert. "Understanding the Physiological Significance of GPCR Dimers and Oligomers." In G-Protein-Coupled Receptor Dimers, 451–65. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_18.

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Hanyaloglu, Aylin C., F. Fanelli, and K. C. Jonas. "Class A GPCR: Di/Oligomerization of Glycoprotein Hormone Receptors." In G-Protein-Coupled Receptor Dimers, 207–31. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_8.

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Knapp, Barbara, and Uwe Wolfrum. "Adhesion GPCR-Related Protein Networks." In Adhesion G Protein-coupled Receptors, 147–78. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-41523-9_8.

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Jastrzebska, Beata. "Class A GPCR: Light Sensing G Protein-Coupled Receptor – Focus on Rhodopsin Dimer." In G-Protein-Coupled Receptor Dimers, 79–97. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_4.

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Hamann, Jörg, and Alexander G. Petrenko. "Introduction: History of the Adhesion GPCR Field." In Adhesion G Protein-coupled Receptors, 1–11. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-41523-9_1.

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Conference papers on the topic "G protein coupled receptor (GPCR)"

1

Fang, Ye, Anthony G. Frutos, and Joydeep Lahiri. "G protein-coupled receptor (GPCR) microarrays." In International Symposium on Biomedical Optics, edited by Darryl J. Bornhop, David A. Dunn, Raymond P. Mariella, Jr., Catherine J. Murphy, Dan V. Nicolau, Shuming Nie, Michelle Palmer, and Ramesh Raghavachari. SPIE, 2002. http://dx.doi.org/10.1117/12.472073.

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Sadova, A. A., D. A. Dmitrieva, N. A. Safronova, M. B. Shevtsov, T. S. Kurkin, V. I. Borshevskiy, and A. V. Mishin. "PREPARATION OF GPCR ANTIBODY COMPLEX SAMPLES FOR CRYO-ELECTRON MICROSCOPY." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-211.

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G-protein-coupled receptors are extremely important therapeutic targets, and their study represents the primary task of modern structural biology. Obtaining GPCR structures is fraught with many difficulties, which can be overcome by the formation of receptor and antibody fragments complexes. In this work, we obtained 4 antibody fragments, previously successfully used for the determination of GPCR structures, which we plan to use in the future to solve structures of the receptors studied in our laboratory.
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Voli, Florida, Hangyu Yi, Estrella Gonzales-Aloy, and Jenny Yingzi Wang. "Abstract 3906: Targeting a novel G-protein coupled receptor (GPCR) for elimination of leukemia stem cells (LSC)." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3906.

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Martins, SAM, J. Mateus, V. Chu, DMF Prazeres, and JP Conde. "Thin-film amorphous silicon photodiodes with integrated fluorescent filters for monitoring live-cell G-protein coupled receptors (GPCR)." In 2014 IEEE Sensors. IEEE, 2014. http://dx.doi.org/10.1109/icsens.2014.6985298.

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Jala, Venkatakrishna R., Haribabu Bodduluri, Brandie Radde, and Carolyn M. Klinge. "Abstract 4548: The role of GPR30/G-protein coupled estrogen receptor (GPER) in lung cancer development." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4548.

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Guillamat Prats, R., P. Goncalves Romeu, G. Li, and S. Steffens. "G-protein coupled receptor (GPR)55 deficiency affects neutrophil function and regulates lung injury in mice." In ERS Lung Science Conference 2023 abstracts. European Respiratory Society, 2023. http://dx.doi.org/10.1183/23120541.lsc-2023.196.

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Castillo, Maryann, Angelique M. Wimbley, Jacob J. Mayfield, Jenifer C. Lascano, and Kevin D. Houston. "Abstract 1305: Activation of G-protein coupled estrogen receptor (GPER) inhibits ELT-3 uterine leiomyoma cell proliferation." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1305.

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Lv, Xiangmin, Guohua Hua, Chunbo He, John S. Davis, and Cheng Wang. "Abstract B82: G-protein coupled estrogen receptor (GPER) agonist G-1 inhibits growth of human granulosa cell tumor cells via blocking microtubule assembly." In Abstracts: AACR Special Conference on Advances in Ovarian Cancer Research: From Concept to Clinic; September 18-21, 2013; Miami, FL. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1078-0432.ovca13-b82.

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Wang, Cheng, Chao Jiang, Xiangmin Lv, Lan Fu, and John S. Davis. "Abstract 3920: Off-target effects of the putative G-protein coupled estrogen receptor 1 (GPER) agonist G1 in ovarian and breast cancer cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3920.

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Natale, Chris, Tina Garyantes, and Todd Ridky. "Abstract 1225: LNS8801: A novel, enantiomerically pure, small molecule agonist of the G protein-coupled estrogen receptor (GPER) for the treatment of cancer." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1225.

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Reports on the topic "G protein coupled receptor (GPCR)"

1

Rafaeli, Ada, Russell Jurenka, and Daniel Segal. Isolation, Purification and Sequence Determination of Pheromonotropic-Receptors. United States Department of Agriculture, July 2003. http://dx.doi.org/10.32747/2003.7695850.bard.

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Moths constitute a major group of pest insects in agriculture. Pheromone blends are utilised by a variety of moth species to attract conspecific mates, which is under circadian control by the neurohormone, PBAN (pheromone-biosynthesis-activating neuropeptide). Our working hypothesis was that, since the emission of sex-pheromone is necessary to attract a mate, then failure to produce and emit pheromone is a potential strategy for manipulating adult moth behavior. The project aimed at identifying, characterising and determining the sequence of specific receptors responsible for the interaction with pheromonotropic neuropeptide/s using two related moth species: Helicoverpa armigera and H. lea as model insects. We established specific binding to a membrane protein estimated at 50 kDa in mature adult females using a photoaffinity-biotin probe for PBAN. We showed that JH is required for the up-regulation of this putative receptor protein. In vitro studies established that the binding initiates a cascade of second messengers including channel opening for calcium ions and intracellular cAMP production. Pharmacological studies (using sodium fluoride) established that the receptor is coupled to a G-protein, that is, the pheromone-biosynthesis-activating neuropeptide receptor (PBAN-R) belongs to the family of G protein-coupled receptor (GPCR)'s. We showed that PBAN-like peptides are present in Drosophila melanogaster based on bioassay and immunocytochemical data. Using the annotated genome of D. melanogaster to search for a GPCR, we found that some were similar to neuromedin U- receptors of vertebrates, which contain a similar C-terminal ending as PBAN. We established that neuromedin U does indeed induce pheromone biosynthesis and cAMP production. Using a PCR based cloning strategy and mRNA isolated from pheromone glands of H. zea, we successfully identified a gene encoding a GPCR from pheromone glands. The full-length PBAN-R was subsequently cloned and expressed in Sf9 insect cells and was shown to mobilize calcium in response to PBAN in a dose-dependent manner. The successful progress in the identification of a gene, encoding a GPCR for the neurohormone, PBAN, provides a basis for the design of a novel battery of compounds that will specifically antagonize pheromone production. Furthermore, since PBAN belongs to a family of insect neuropeptides with more than one function in different life stages, this rationale may be extended to other physiological key-regulatory processes in different insects.
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Rafaeli, Ada, and Russell Jurenka. Molecular Characterization of PBAN G-protein Coupled Receptors in Moth Pest Species: Design of Antagonists. United States Department of Agriculture, December 2012. http://dx.doi.org/10.32747/2012.7593390.bard.

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The proposed research was directed at determining the activation/binding domains and gene regulation of the PBAN-R’s thereby providing information for the design and screening of potential PBAN-R-blockers and to indicate possible ways of preventing the process from proceeding to its completion. Our specific aims included: (1) The identification of the PBAN-R binding domain by a combination of: (a) in silico modeling studies for identifying specific amino-acid side chains that are likely to be involved in binding PBAN with the receptor and; (b) bioassays to verify the modeling studies using mutant receptors, cell lines and pheromone glands (at tissue and organism levels) against selected, designed compounds to confirm if compounds are agonists or antagonists. (2) The elucidation ofthemolecular regulationmechanisms of PBAN-R by:(a) age-dependence of gene expression; (b) the effect of hormones and; (c) PBAN-R characterization in male hair-pencil complexes. Background to the topic Insects have several closely related G protein-coupled receptors (GPCRs) belonging to the pyrokinin/PBAN family, one with the ligand pheromone biosynthesis activating neuropeptide or pyrokinin-2 and another with diapause hormone or pyrokinin-1 as a ligand. We were unable to identify the diapause hormone receptor from Helicoverpa zea despite considerable effort. A third, related receptor is activated by a product of the capa gene, periviscerokinins. The pyrokinin/PBAN family of GPCRs and their ligands has been identified in various insects, such as Drosophila, several moth species, mosquitoes, Triboliumcastaneum, Apis mellifera, Nasoniavitripennis, and Acyrthosiphon pisum. Physiological functions of pyrokinin peptides include muscle contraction, whereas PBAN regulates pheromone production in moths plus other functions indicating the pleiotropic nature of these ligands. Based on the alignment of annotated genomic sequences, the primary and secondary structures of the pyrokinin/PBAN family of receptors have similarity with the corresponding structures of the capa or periviscerokinin receptors of insects and the neuromedin U receptors found in vertebrates. Major conclusions, solutions, achievements Evolutionary trace analysisof receptor extracellular domains exhibited several class-specific amino acid residues, which could indicate putative domains for activation of these receptors by ligand recognition and binding. Through site-directed point mutations, the 3rd extracellular domain of PBAN-R was shown to be critical for ligand selection. We identified three receptors that belong to the PBAN family of GPCRs and a partial sequence for the periviscerokinin receptor from the European corn borer, Ostrinianubilalis. Functional expression studies confirmed that only the C-variant of the PBAN-R is active. We identified a non-peptide agonist that will activate the PBAN-receptor from H. zea. We determined that there is transcriptional control of the PBAN-R in two moth species during the development of the pupa to adult, and we demonstrated that this transcriptional regulation is independent of juvenile hormone biosynthesis. This transcriptional control also occurs in male hair-pencil gland complexes of both moth species indicating a regulatory role for PBAN in males. Ultimate confirmation for PBAN's function in the male tissue was revealed through knockdown of the PBAN-R using RNAi-mediated gene-silencing. Implications, both scientific and agricultural The identification of a non-peptide agonist can be exploited in the future for the design of additional compounds that will activate the receptor and to elucidate the binding properties of this receptor. The increase in expression levels of the PBAN-R transcript was delineated to occur at a critical period of 5 hours post-eclosion and its regulation can now be studied. The mysterious role of PBAN in the males was elucidated by using a combination of physiological, biochemical and molecular genetics techniques.
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Liu, Mingyao. Role of a Novel Prostate-Specific G-Protein Coupled Receptor (PSGR) in Prostate Tumor Development. Fort Belvoir, VA: Defense Technical Information Center, February 2003. http://dx.doi.org/10.21236/ada415521.

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Ye, Libin, Christopher Andrew Neale, Adnan Sljoka, Brent Lyda, Dmitry Pichugin, Nobuyuki Tsuchimura, Sacha T. Larda, et al. Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations. Office of Scientific and Technical Information (OSTI), April 2018. http://dx.doi.org/10.2172/1434450.

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