Relevant bibliographies by topics / GPCR

Academic literature on the topic 'GPCR'

Author: Grafiati
Published: 4 June 2021
Last updated: 24 August 2024

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Journal articles on the topic "GPCR"

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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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González-Guede, Irene, María López-Ramos, Luis Rodríguez-Rodríguez, Lydia Abasolo, Arkaitz Mucientes, and Benjamín Fernández-Gutiérrez. "Dysregulation of Glypicans and Notum in Osteoarthritis: Plasma Levels, Bone Marrow Mesenchymal Stromal Cells and Osteoblasts." Cells 13, no. 10 (May 16, 2024): 852. http://dx.doi.org/10.3390/cells13100852.

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In this study of the alterations of Glypicans 1 to 6 (GPCs) and Notum in plasma, bone marrow mesenchymal stromal cells (BM-MSCs) and osteoblasts in Osteoarthritis (OA), the levels of GPCs and Notum in the plasma of 25 patients and 24 healthy subjects were measured. In addition, BM-MSCs from eight OA patients and eight healthy donors were cultured over a period of 21 days using both a culture medium and an osteogenic medium. Protein and gene expression levels of GPCs and Notum were determined using ELISA and qPCR at 0, 7, 14 and 21 days. GPC5 and Notum levels decreased in the plasma of OA patients, while the BM-MSCs of OA patients showed downexpression of GPC6 and upregulation of Notum. A decrease in GPC5 and Notum proteins and an increase in GPC3 were found. During osteogenic differentiation, elevated GPCs 2, 4, 5, 6 and Notum mRNA levels and decreased GPC3 were observed in patients with OA. Furthermore, the protein levels of GPC2, GPC5 and Notum decreased, while the levels of GPC3 increased. Glypicans and Notum were altered in BM-MSCs and during osteogenic differentiation from patients with OA. The alterations found point to GPC5 and Notum as new candidate biomarkers of OA pathology.
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Tany, Ryosuke, Yuhei Goto, Yohei Kondo, and Kazuhiro Aoki. "Quantitative live-cell imaging of GPCR downstream signaling dynamics." Biochemical Journal 479, no. 8 (April 21, 2022): 883–900. http://dx.doi.org/10.1042/bcj20220021.

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G-protein-coupled receptors (GPCRs) play an important role in sensing various extracellular stimuli, such as neurotransmitters, hormones, and tastants, and transducing the input information into the cell. While the human genome encodes more than 800 GPCR genes, only four Gα-proteins (Gαs, Gαi/o, Gαq/11, and Gα12/13) are known to couple with GPCRs. It remains unclear how such divergent GPCR information is translated into the downstream G-protein signaling dynamics. To answer this question, we report a live-cell fluorescence imaging system for monitoring GPCR downstream signaling dynamics. Genetically encoded biosensors for cAMP, Ca2+, RhoA, and ERK were selected as markers for GPCR downstream signaling, and were stably expressed in HeLa cells. GPCR was further transiently overexpressed in the cells. As a proof-of-concept, we visualized GPCR signaling dynamics of five dopamine receptors and 12 serotonin receptors, and found heterogeneity between GPCRs and between cells. Even when the same Gα proteins were known to be coupled, the patterns of dynamics in GPCR downstream signaling, including the signal strength and duration, were substantially distinct among GPCRs. These results suggest the importance of dynamical encoding in GPCR signaling.
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Baidya, Mithu, Punita Kumari, Hemlata Dwivedi-Agnihotri, Shubhi Pandey, Badr Sokrat, Silvia Sposini, Madhu Chaturvedi, et al. "Genetically encoded intrabody sensors report the interaction and trafficking of β-arrestin 1 upon activation of G-protein–coupled receptors." Journal of Biological Chemistry 295, no. 30 (May 21, 2020): 10153–67. http://dx.doi.org/10.1074/jbc.ra120.013470.

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Agonist stimulation of G-protein–coupled receptors (GPCRs) typically leads to phosphorylation of GPCRs and binding to multifunctional proteins called β-arrestins (βarrs). The GPCR–βarr interaction critically contributes to GPCR desensitization, endocytosis, and downstream signaling, and GPCR–βarr complex formation can be used as a generic readout of GPCR and βarr activation. Although several methods are currently available to monitor GPCR–βarr interactions, additional sensors to visualize them may expand the toolbox and complement existing methods. We have previously described antibody fragments (FABs) that recognize activated βarr1 upon its interaction with the vasopressin V2 receptor C-terminal phosphopeptide (V2Rpp). Here, we demonstrate that these FABs efficiently report the formation of a GPCR–βarr1 complex for a broad set of chimeric GPCRs harboring the V2R C terminus. We adapted these FABs to an intrabody format by converting them to single-chain variable fragments and used them to monitor the localization and trafficking of βarr1 in live cells. We observed that upon agonist simulation of cells expressing chimeric GPCRs, these intrabodies first translocate to the cell surface, followed by trafficking into intracellular vesicles. The translocation pattern of intrabodies mirrored that of βarr1, and the intrabodies co-localized with βarr1 at the cell surface and in intracellular vesicles. Interestingly, we discovered that intrabody sensors can also report βarr1 recruitment and trafficking for several unmodified GPCRs. Our characterization of intrabody sensors for βarr1 recruitment and trafficking expands currently available approaches to visualize GPCR–βarr1 binding, which may help decipher additional aspects of GPCR signaling and regulation.
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Chattopadhyay, Amitabha. "GPCRs: Lipid-Dependent Membrane Receptors That Act as Drug Targets." Advances in Biology 2014 (October 2, 2014): 1–12. http://dx.doi.org/10.1155/2014/143023.

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G protein-coupled receptors (GPCRs) are the largest class of molecules involved in signal transduction across cell membranes and represent major targets in the development of novel drug candidates in all clinical areas. Although there have been some recent leads, structural information on GPCRs is relatively rare due to the difficulty associated with crystallization. A specific reason for this is the intrinsic flexibility displayed by GPCRs, which is necessary for their functional diversity. Since GPCRs are integral membrane proteins, interaction of membrane lipids with them constitutes an important area of research in GPCR biology. In particular, membrane cholesterol has been reported to have a modulatory role in the function of a number of GPCRs. The role of membrane cholesterol in GPCR function is discussed with specific example of the serotonin1A receptor. Recent results show that GPCRs are characterized with structural motifs that preferentially associate with cholesterol. An emerging and important concept is oligomerization of GPCRs and its role in GPCR function and signaling. The role of membrane cholesterol in GPCR oligomerization is highlighted. Future research in GPCR biology would offer novel insight in basic biology and provide new avenues for drug discovery.
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Liu, Samuel, Preston J. Anderson, Sudarshan Rajagopal, Robert J. Lefkowitz, and Howard A. Rockman. "G Protein-Coupled Receptors: A Century of Research and Discovery." Circulation Research 135, no. 1 (June 21, 2024): 174–97. http://dx.doi.org/10.1161/circresaha.124.323067.

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GPCRs (G protein-coupled receptors), also known as 7 transmembrane domain receptors, are the largest receptor family in the human genome, with ≈800 members. GPCRs regulate nearly every aspect of human physiology and disease, thus serving as important drug targets in cardiovascular disease. Sharing a conserved structure comprised of 7 transmembrane α-helices, GPCRs couple to heterotrimeric G-proteins, GPCR kinases, and β-arrestins, promoting downstream signaling through second messengers and other intracellular signaling pathways. GPCR drug development has led to important cardiovascular therapies, such as antagonists of β-adrenergic and angiotensin II receptors for heart failure and hypertension, and agonists of the glucagon-like peptide-1 receptor for reducing adverse cardiovascular events and other emerging indications. There continues to be a major interest in GPCR drug development in cardiovascular and cardiometabolic disease, driven by advances in GPCR mechanistic studies and structure-based drug design. This review recounts the rich history of GPCR research, including the current state of clinically used GPCR drugs, and highlights newly discovered aspects of GPCR biology and promising directions for future investigation. As additional mechanisms for regulating GPCR signaling are uncovered, new strategies for targeting these ubiquitous receptors hold tremendous promise for the field of cardiovascular medicine.
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Kapolka, Nicholas J., Jacob B. Rowe, Geoffrey J. Taghon, William M. Morgan, Corin R. O’Shea, and Daniel G. Isom. "Proton-gated coincidence detection is a common feature of GPCR signaling." Proceedings of the National Academy of Sciences 118, no. 28 (July 6, 2021): e2100171118. http://dx.doi.org/10.1073/pnas.2100171118.

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The evolutionary expansion of G protein-coupled receptors (GPCRs) has produced a rich diversity of transmembrane sensors for many physical and chemical signals. In humans alone, over 800 GPCRs detect stimuli such as light, hormones, and metabolites to guide cellular decision-making primarily using intracellular G protein signaling networks. This diversity is further enriched by GPCRs that function as molecular sensors capable of discerning multiple inputs to transduce cues encoded in complex, context-dependent signals. Here, we show that many GPCRs are coincidence detectors that couple proton (H+) binding to GPCR signaling. Using a panel of 28 receptors covering 280 individual GPCR-Gα coupling combinations, we show that H+ gating both positively and negatively modulates GPCR signaling. Notably, these observations extend to all modes of GPCR pharmacology including ligand efficacy, potency, and cooperativity. Additionally, we show that GPCR antagonism and constitutive activity are regulated by H+ gating and report the discovery of an acid sensor, the adenosine A2a receptor, which can be activated solely by acidic pH. Together, these findings establish a paradigm for GPCR signaling, biology, and pharmacology applicable to acidified microenvironments such as endosomes, synapses, tumors, and ischemic vasculature.
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Southern, Craig, Jennifer M. Cook, Zaynab Neetoo-Isseljee, Debra L. Taylor, Catherine A. Kettleborough, Andy Merritt, Daniel L. Bassoni, et al. "Screening β-Arrestin Recruitment for the Identification of Natural Ligands for Orphan G-Protein–Coupled Receptors." Journal of Biomolecular Screening 18, no. 5 (February 8, 2013): 599–609. http://dx.doi.org/10.1177/1087057113475480.

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A variety of G-protein–coupled receptor (GPCR) screening technologies have successfully partnered a number of GPCRs with their cognate ligands. GPCR-mediated β-arrestin recruitment is now recognized as a distinct intracellular signaling pathway, and ligand-receptor interactions may show a bias toward β-arrestin over classical GPCR signaling pathways. We hypothesized that the failure to identify native ligands for the remaining orphan GPCRs may be a consequence of biased β-arrestin signaling. To investigate this, we assembled 10 500 candidate ligands and screened 82 GPCRs using PathHunter β-arrestin recruitment technology. High-quality screening assays were validated by the inclusion of liganded receptors and the detection and confirmation of these established ligand-receptor pairings. We describe a candidate endogenous orphan GPCR ligand and a number of novel surrogate ligands. However, for the majority of orphan receptors studied, measurement of β-arrestin recruitment did not lead to the identification of cognate ligands from our screening sets. β-Arrestin recruitment represents a robust GPCR screening technology, and ligand-biased signaling is emerging as a therapeutically exploitable feature of GPCR biology. The identification of cognate ligands for the orphan GPCRs and the extent to which receptors may exist to preferentially signal through β-arrestin in response to their native ligand remain to be determined.
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Ju, Man-Seok, and Sang Taek Jung. "Antigen Design for Successful Isolation of Highly Challenging Therapeutic Anti-GPCR Antibodies." International Journal of Molecular Sciences 21, no. 21 (November 3, 2020): 8240. http://dx.doi.org/10.3390/ijms21218240.

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G-protein-coupled receptors (GPCR) transmit extracellular signals into cells to regulate a variety of cellular functions and are closely related to the homeostasis of the human body and the progression of various types of diseases. Great attention has been paid to GPCRs as excellent drug targets, and there are many commercially available small-molecule chemical drugs against GPCRs. Despite this, the development of therapeutic anti-GPCR antibodies has been delayed and is challenging due to the difficulty in preparing active forms of GPCR antigens, resulting from their low cellular expression and complex structures. Here, we focus on anti-GPCR antibodies that have been approved or are subject to clinical trials and present various technologies to prepare active GPCR antigens that enable the isolation of therapeutic antibodies to proceed toward clinical validation.
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Yan, Huan, Jingling Zhang, Kam-Tong Leung, Kwok-Wai Lo, Jun Yu, Ka-Fai To, and Wei Kang. "An Update of G-Protein-Coupled Receptor Signaling and Its Deregulation in Gastric Carcinogenesis." Cancers 15, no. 3 (January 25, 2023): 736. http://dx.doi.org/10.3390/cancers15030736.

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G-protein-coupled receptors (GPCRs) belong to a cell surface receptor superfamily responding to a wide range of external signals. The binding of extracellular ligands to GPCRs activates a heterotrimeric G protein and triggers the production of numerous secondary messengers, which transduce the extracellular signals into cellular responses. GPCR signaling is crucial and imperative for maintaining normal tissue homeostasis. High-throughput sequencing analyses revealed the occurrence of the genetic aberrations of GPCRs and G proteins in multiple malignancies. The altered GPCRs/G proteins serve as valuable biomarkers for early diagnosis, prognostic prediction, and pharmacological targets. Furthermore, the dysregulation of GPCR signaling contributes to tumor initiation and development. In this review, we have summarized the research progress of GPCRs and highlighted their mechanisms in gastric cancer (GC). The aberrant activation of GPCRs promotes GC cell proliferation and metastasis, remodels the tumor microenvironment, and boosts immune escape. Through deep investigation, novel therapeutic strategies for targeting GPCR activation have been developed, and the final aim is to eliminate GPCR-driven gastric carcinogenesis.
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Dissertations / Theses on the topic "GPCR"

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Blankenship, Elise. "Conserved solvent networks in GPCR activation." Case Western Reserve University School of Graduate Studies / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=case1458221506.

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Poudel, Sagar. "GPCR-Directed Libraries for High Throughput Screening." Thesis, University of Skövde, School of Humanities and Informatics, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:his:diva-29.

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Guanine nucleotide binding protein (G-protein) coupled receptors (GPCRs), the largest receptor family, is enormously important for the pharmaceutical industry as they are the target of 50-60% of all existing medicines. Discovery of many new GPCR receptors by the “human genome project”, open up new opportunities for developing novel therapeutics. High throughput screening (HTS) of chemical libraries is a well established method for finding new lead compounds in drug discovery. Despite some success this approach has suffered from the near absence of more focused and specific targeted libraries. To improve the hit rates and to maximally exploit the full potential of current corporate screening collections, in this thesis work, identification and analysis of the critical drug-binding positions within the GPCRs were done, based on their overall sequence, their transmembrane regions and their drug binding fingerprints. A proper classification based on drug binding fingerprints on the basis for a successful pharmacophore modelling and virtual screening were done, which facilities in the development of more specific and focused targeted libraries for HTS.

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Majin, Wodu. "Mathematical modelling of GPCR-mediated calcium signalling." Thesis, University of Nottingham, 2012. http://eprints.nottingham.ac.uk/12451/.

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Ca2+ is an important messenger which mediates several physiological functions, including muscle contraction, fertilisation, heart regulation and gene transcription. One major way its cytosolic level is raised is via a G-protein coupled receptor (GPCR)- mediated release from intracellular stores. GPCR’s are the target of approximately 50% of all drugs in clinical use. Hence, understanding the underlying mechanisms of signalling in this pathway could lead to improved therapy in disease conditions associated with abnornmal Ca2+ signalling, and to the identification of new drug targets. To gain such insight, this thesis builds and analyses a detailed mathematical model of key processes leading to Ca2+ mobilisation. Ca2+ signalling is considered in the particular context of the M3 muscarinic receptor system. Guided by available data, the Ca2+ mobilisation model is assembled, first by analysing a base G-protein activation model, and subsequently extending it with downstream details. Computationally efficient designs of a global parameter sensitivity analysis method are used to identify the key controlling parameters with respect to the main features of the Ca2+ data. The underlying mechanism behind the experimentally observed, rapid, amplified Ca2+ response is shown to be a rapid rate of inositol trisphosphate (IP3) formation from Phosphatidylinositol 4,5-bisphosphate (PIP2) hydrolysis. Using the same results, potential drug targets (apart fromthe GPCR) are identified, including the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and PIP2. Moreover, possible explanations for therapeutic failures were found when some parameters exerted a biphasic effect on the relative Ca2+ increase. The sensitivity analysis results are used to simplify the process of parameter estimation by a significant reduction of the parameter space of interest. An evolutionary algorithm is used to successfully fit the model to a significant portion of the Ca2+ data. Subsequent sensitivity analyses of the best-fitting parameter sets suggest that mechanistic modelling of kinase-mediated GPCR desensitisation, and SERCA dynamics may be required for a comprehensive representation of the data.
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Tang, Lisa Sarah. "GPCR expressions in Saccharomyces cerevisiae : engineering transductions." Thesis, University of Leeds, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.423190.

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Mishra, Satyakam. "Frequent Subgraph Mining Analysis of GPCR Activation." Case Western Reserve University School of Graduate Studies / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=case1613575702373053.

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Kiess, Alexandra. "Funktionelle Relevanz intrazellulärer Splicevarianten des Brain-specific Angiogenesis Inhibitor 2 (BAI2)." Doctoral thesis, Universitätsbibliothek Leipzig, 2014. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-156171.

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BAI2 gehört zu den Adhesion-G-Protein-gekoppelten Rezeptoren (aGPCR). Diese bisher wenig untersuchte Klasse von ca. 30 GPCR ist charakterisiert durch eine komplexe genomische Struktur, sehr große extrazelluläre Domänen und eine Vielzahl von Splicevarianten. Bisher ist bei den meisten aGPCR, wie auch bei BAI2, wenig über ihre Signaltransduktion und Funktion bekannt. Zum Verständnis der physiologischen Relevanz und zur Suche nach dem endogenen Agonist sind Kenntnisse über Proteinstruktur, Splicevarianten und Signaltransduktion essentiell. Ziel dieser Arbeit war es, mittels verschiedener in vitro-Methoden die Proteinstruktur des BAI2 in den transmembranären und intrazellulären Domänen näher zu untersuchen, sowie die natürlichen Splicevarianten in diesem Bereich, deren evolutionäre Konservierung, Gewebespezifität und Quantität zu erfassen. Für beide gefundenen Splicevarianten, eine im dritten intrazellulären Loop (ICL3) und eine im C-Terminus, konnte eine evolutionäre Konservierung auf Aminosäure- und genomischer Organisationsebene, sowie ihre Entstehung durch Exonskipping nachgewiesen werden. Nachfolgend wurden die Splicevarianten auf mögliche Interaktionen mit intrazellulären Komponenten untersucht. In dieser Arbeit konnte gezeigt werden, dass beide ICL3-Splicevarianten natürlicherweise in einem definierten Verhältnis auftreten. Außerdem konnte gezeigt werden, dass die lange ICL3-Variante des BAI2 nicht zu einer Änderung der Membrantopologie des Rezeptors, einer Homodimerisierung über die zusätzliche Aminosäuresequenz oder zu einer Interaktion mit dem C-Terminus führt. Die Splicevariante im humanen C-Terminus des BAI2 konnte als eine variable, durch Exonskipping entstandene Calcium-unabhängige Calmodulin-Bindungsstelle identifiziert werden. Diese Arbeit belegt die Existenz mehrerer BAI2-Isoformen in vivo. Die Struktur dieser Isoformen lässt unterschiedliche Funktionalitäten vermuten. Auch wenn erste Untersuchungen zwischen den beiden ICL3-Varianten keinen Unterschied ergaben, sind diese Erkenntnisse für die weitere Analyse der Signaltransduktion und Ligandensuche bedeutend. Es ist z.B. denkbar, dass sich die beiden ICL3-Varianten in der G-Protein-Kopplung oder bei der Rekrutierung von intrazellulären Interaktionspartnern unterscheiden oder dass die Splicevariante im C-Terminus zu einer Scaffold- Funktion des Calmodulins führt und/oder die Signaltransduktion durch eine permanente Bindung des Calmodulins an einer Isoform moduliert wird.
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Sladek, Barbara. "Structural studies of integral membrane GPCR accessory proteins." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:09bf7ada-8e58-49f4-a979-bcd0cec95e8b.

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GPCR accessory proteins regulate the strength, efficiency and specificity of signal transfer upon receptor activation. Due to the inherent difficulties of studying membrane proteins in vitro and in vivo, little is known about the structure and topology of these small accessory proteins. Two examples of GPCR accessory proteins are the Melanocortin-2 receptor accessory protein (MRAP) and the Receptor-activity-modifying protein (RAMP) family. MRAP and RAMP1 are the main focus of this thesis in which they are thoroughly characterised by solution-state NMR and further biophysical techniques. The single-pass transmembrane domain protein MRAP regulates the class A GPCR melanocortin receptors. It is specifically required for trafficking the melanocortin-2-receptor from the endoplasmic reticulum to the cell surface and subsequent receptor activation. A remarkable characteristic of MRAP is its proposed native dual-topology, which leads to an antiparallel homodimeric conformation. Investigation of the biochemical and biophysical properties of MRAP revealed an α-helical transmembrane domain, and an α-helical N-terminal LD(Y/I)L-motif. Further efforts concentrated on establishing the homodimeric conformation of MRAP in vitro. RAMP1 facilitates receptor trafficking and alters the ligand specificity of the GPCR Class B receptors calcitonin receptors and calcitonin receptor-like receptors. Moreover, RAMP1 is required to act as a Calcitonin-gene-related peptide (CGRP) receptor (RAMP1). RAMP1 has been shown to form stable parallel homodimers in the absence of its cognate receptor. Its dimerisation and the possible dimerisation motif PxxxxP-motif were studied extensively. With the goal of understanding the mechanism of dimerisation and the role of GPCR accessory proteins I have used solution-state NMR in detergent micelles as my main technique. NMR provides unique possibilities for understanding the structure and dynamics of such small membrane proteins.
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Richardson, Kathryn. "Mechanisms of GPCR signal regulation in fission yeast." Thesis, University of Warwick, 2014. http://wrap.warwick.ac.uk/63554/.

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Cells communicate with each other and respond to environmental cues by sending and receiving signals. Many external signals (ligands) are detected through G protein-coupled receptors (GPCRs), a major class of transmembrane proteins. GPCRs transduce these external signals into appropriate intracellular responses, enabling the cell to adapt to its environment. Malfunctions in these signalling pathways can lead to a range of human diseases and hence GPCRs have become attractive candidates for pharmacological design. The activation of a single receptor has the ability to induce numerous intracellular responses. Coupling this with the great number of different GPCR-types expressed in human cells means that understanding the basic principles of signal transduction and termination in humans is complicated. This study utilises the more simplistic eukaryotic yeast Schizosaccharomyces pombe (S. pombe) to overcome this complexity, as it contains only two GPCR types and hence the cross-talk between pathways is greatly reduced, whilst the structure and signalling functions of GPCRs are often evolutionarily conserved between yeast and humans. Mathematical modelling was used to aid the understanding of GPCR signalling in S. pombe and to inform experimental design. Speci�cally, an ordinary differential equation model �rst developed by Croft et al. (2013) was extended to include all known downstream signal transduction, regulation and termination events. This model is the �rst of its kind to describe a whole GPCR signalling pathway within S. pombe. Although it accurately predicts the cellular response to GPCR signalling it could only reproduce the biological plateau in temporal response with the addition of a 'yet unknown mechanism' GPCR degradation term. This motivated the investigation of how GPCRs in S. pombe are internalised from the plasma membrane in response to ligand stimulation. The primary mechanism for signal termination is via internalisation of the GPCR. This study identi�ed three potential casein kinases (Cki1, Cki2 and Cki3) that promote internalisation of the S. pombe GPCR Mam2. Microscopy analyses in combination with quantitative transcriptional, cell growth and cell cycle position assays uncovered a novel role for these kinases: that Cki2 regulates cell size during vegetative growth, Cki1 and Cki3 regulate the GPCR-response pathway and that Cki3 is essential for completing cytokinesis in S. pombe that have already undergone formation of a conjugation tube in response to ligand. Confocal microscopy of uorescent labelled Mam2 indicated a role for Cki2 in the internalisation and hence termination of the GPCR-response pathway. These findings add to the growing body of evidence that casein kinases are implicated in GPCR desensitisation.
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Goddard, Alan David. "Functional analysis of GPCR signalling cascades in Schizosaccharomyces pombe." Thesis, University of Warwick, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.437696.

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Koyama, Hiroyuki. "Comprehensive Profiling of GPCR Expression in Ghrelin-producing Cells." Kyoto University, 2016. http://hdl.handle.net/2433/215953.

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Books on the topic "GPCR"

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Gilchrist, Annette, ed. GPCR Molecular Pharmacology and Drug Targeting. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470627327.

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Heifetz, Alexander, ed. Computational Methods for GPCR Drug Discovery. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7465-8.

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Dupré, Denis J., Terence E. Hébert, and Ralf Jockers, eds. GPCR Signalling Complexes – Synthesis, Assembly, Trafficking and Specificity. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4765-4.

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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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Yona, Simon, and Martin Stacey, eds. Adhesion-GPCRs. Boston, MA: Springer US, 2010. http://dx.doi.org/10.1007/978-1-4419-7913-1.

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Strasser, Andrea, and Hans-Joachim Wittmann. Modelling of GPCRs. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-4596-4.

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Lebon, Guillaume, ed. Structure and Function of GPCRs. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-24591-7.

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Strasser, Andrea. Modelling of GPCRs: A Practical Handbook. Dordrecht: Springer Netherlands, 2013.

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S, Baker Gregory, and Jol H. M, eds. Stratigraphic analyses using GPR. Boulder, Colo: Geological Society of America, 2007.

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Bourne, H., R. Horuk, J. Kuhnke, and H. Michel, eds. GPCRs: From Deorphanization to Lead Structure Identification. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-48982-5.

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Book chapters on the topic "GPCR"

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Manji, Husseini K., Jorge Quiroz, R. Andrew Chambers, Anthony Absalom, David Menon, Patrizia Porcu, A. Leslie Morrow, et al. "GPCR." In Encyclopedia of Psychopharmacology, 561. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1464.

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Jones, Roger D., and Alan M. Jones. "A Proposed Mechanism for in vivo Programming Transmembrane Receptors." In Communications in Computer and Information Science, 123–37. Cham: Springer Nature Switzerland, 2024. http://dx.doi.org/10.1007/978-3-031-57430-6_11.

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AbstractTransmembrane G-protein coupled receptors (GPCRs) are ideal drug targets because they resemble, in function, molecular microprocessors for which outcomes (e.g. disease pathways) can be controlled by inputs (extracellular ligands). The inputs here are ligands in the extracellular fluid and possibly chemical signals from other sources in the cellular environment that modify the states of molecular switches, such as phosphorylation sites, on the intracellular domains of the receptor. Like in an engineered microprocessor, these inputs control the configuration of output switch states that control the generation of downstream responses to the inputs.Many diseases with heterogeneous prognoses including, for example, cancer and diabetic kidney disease, require precise individualized treatment. The success of precision medicine to treat and cure disease is through its ability to alter the microprocessor outputs in a manner to improve disease outcomes. We previously established ab initio a model based on maximal information transmission and rate of entropy production that agrees with experimental data on GPCR performance and provides insight into the GPCR process. We use this model to suggest new and possibly more precise ways to target GPCRs with potential new drugs.We find, within the context of the model, that responses downstream of the GPCRs can be controlled, in part, by drug ligand concentration, not just whether the ligand is bound to the receptor. Specifically, the GPCRs encode the maximum ligand concentration the GPCR experiences in the number of active phosphorylation or other switch sites on the intracellular domains of the GPCR. This process generates a memory in the GPCR of the maximum ligand concentration seen by the GPCR. Each configuration of switch sites can generate a distinct downstream response bias. This implies that cellular response to a ligand may be programmable by controlling drug concentration. The model addresses the observation paradox that the amount of information appearing in the intracellular region is greater than amount of information stored in whether the ligand binds to the receptor. This study suggests that at least some of the missing information can be generated by the ligand concentration. We show the model is consistent with assay and information-flow experiments.In contrast to the current view of switch behavior in GPCR signaling, we find that switches exist in three distinct states: inactive (neither off nor on), actively on, or actively off. Unlike the inactive state, the active state supports a chemical flux of receptor configurations through the switch, even when the switch state is actively off. Switches are activated one at a time as ligand concentration reaches threshold values and does not reset because the ligand concentration drops below the thresholds. These results have clinical relevance. Treatment with drugs that target GPCR-mediated pathways can have increased precision for outputs by controlling switch configurations. The model suggests that, to see the full response spectrum, fully native receptors should be used in assay experiments rather than chimera receptors.Inactive states allow the possibility for novel adaptations. This expands the search space for natural selection beyond the space determined by pre-specified active switches.
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Wu, Yiran, Jiahui Tong, Kang Ding, Qingtong Zhou, and Suwen Zhao. "GPCR Allosteric Modulator Discovery." In Advances in Experimental Medicine and Biology, 225–51. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-8719-7_10.

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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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Butcher, Adrian J., Andrew B. Tobin, and Kok Choi Kong. "Examining Site-Specific GPCR Phosphorylation." In Methods in Molecular Biology, 237–49. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-126-0_12.

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Gilchrist, Annette, and Maria R. Mazzoni. "Traditional GPCR Pharmacology and Beyond." In Signal Transduction: Pathways, Mechanisms and Diseases, 3–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-02112-1_1.

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Strasser, Andrea, and Hans-Joachim Wittmann. "Special Topics in GPCR Research." In Modelling of GPCRs, 105–20. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4596-4_8.

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Miljus, Tamara, David A. Sykes, Clare R. Harwood, Ziva Vuckovic, and Dmitry B. Veprintsev. "GPCR Solubilization and Quality Control." In Methods in Molecular Biology, 105–27. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0373-4_8.

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Zhao, Qi, Amanda Chapman, Yan Huang, Mary Ferguson, Shannon McBride, Meghan Kelly, Michael Weiner, and Xiaofeng Li. "Ligand-Directed GPCR Antibody Discovery." In Methods in Molecular Biology, 319–42. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1811-0_19.

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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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Conference papers on the topic "GPCR"

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Xie, X. "GPCR-targeted drug discovery." In 67th International Congress and Annual Meeting of the Society for Medicinal Plant and Natural Product Research (GA) in cooperation with the French Society of Pharmacognosy AFERP. © Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-3399677.

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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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Bekhouche, Safia, and Yamina Mohamed Ben Ali. "Optimizing the identification of GPCR function." In SMC '19: The Second Conference of the Moroccan Classification Society. New York, NY, USA: ACM, 2019. http://dx.doi.org/10.1145/3314074.3314082.

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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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Robleto, Valeria, Ya Zhuo, Joseph Crecelius, and Adriano Marchese. "Regulation of GPCR Signaling by Sorting Nexins." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.276700.

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Franchini, Luca, Lindsay R. Watkins, and Cesare Orlandi. "Enhanced cAMP-based assay for GPCR deorphanization." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.148500.

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Qiu, Wang-Ren, Xuan Xiao, and Zhen-Yu Zhang. "Using AdaboostSVM to Predict the GPCR Functional Classes." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5515639.

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WÜTHRICH, KURT. "STUDIES OF GPCR CONFORMATIONS IN NON-CRYSTALLINE MILIEUS." In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0026.

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ROTH, BRYAN L. "THE HIDDEN PHARMACOLOGY OF THE HUMAN GPCR-OME." In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0029.

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Brooks, Charles L. "De novo modeling of GPCR class A structures." In Distributed Processing (IPDPS). IEEE, 2009. http://dx.doi.org/10.1109/ipdps.2009.5160868.

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Reports on the topic "GPCR"

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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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Campos, D. Ground penetrating radar (GPR) methods. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 2012. http://dx.doi.org/10.4095/291772.

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Karp, Brad, and H. T. Kung. GPSR: Greedy Perimeter Stateless Routing for Wireless Networks. Fort Belvoir, VA: Defense Technical Information Center, January 2005. http://dx.doi.org/10.21236/ada440078.

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Nelson, S. D. EM modeling for GPIR using 3D FDTD modeling codes. Office of Scientific and Technical Information (OSTI), October 1994. http://dx.doi.org/10.2172/93462.

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Dubcovsky, Jorge, Tzion Fahima, and Ann Blechl. Positional cloning of a gene responsible for high grain protein content in tetraploid wheat. United States Department of Agriculture, September 2003. http://dx.doi.org/10.32747/2003.7695875.bard.

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High Grain Protein Content (GPC) is a desirable trait in breadmaking and pasta wheat varieties because of its positive effects on quality and nutritional value. However, selection for GPC is limited by our poor understanding of the genes involved in the accumulation of protein in the grain. The long-term goal of this project is to provide a better understanding of the genes controlling GPC in wheat. The specific objectives of this project were: a) to develop a high-density genetic map of the GPC gene in tetraploid wheat, b) to construct a T. turgidum Bacterial Artificial Chromosome (BAC) library, c) to construct a physical map of the GPC gene and identify a candidate for the GPC gene. A gene with a large effect on GPC was detected in Triticum turgidum var. dicoccoides and was previously mapped in the short arm of chromosome 6B. To define better the position of the Gpc-B1 locus we developed homozygous recombinant lines with recombination events within the QTL region. Except for the 30-cM region of the QTL these RSLs were isogenic for the rest of the genome minimizing the genetic variability. To minimize the environmental variability the RSLs were characterized using 10 replications in field experiments organized in a Randomized Complete Block Design, which were repeated three times. Using this strategy, we were able to map this QTL as a single Mendelian locus (Gpc-B1) on a 2.6-cM region flanked by RFLP markers Xcdo365 and Xucw67. All three experiments showed that the lines carrying the DIC allele had an average absolute increase in GPC of 14 g/kg. Using the RFLP flanking markers, we established the microcolinearity between a 2.l-cM region including the Gpc-B1 gene in wheat chromosome 6BS and a 350-kb region on rice chromosome 2. Rice genes from this region were used to screen the Triticeae EST collection, and these ESTs were used to saturate the Gpc-B1 region with molecular markers. With these new markers we were able to map the Gpc-B1 locus within a 0.3-cM region flanked by PCR markers Xucw83 and Xucw71. These flanking markers defined a 36-kb colinear region with rice, including one gene that is a potential candidate for the Gpc-B1 gene. To develop a physical map of the Gpc-B1 region in wheat we first constructed a BAC library of tetraploid wheat, from RSL#65 including the high Gpc-B1 allele. We generated half- million clones with an average size of l3l-kb (5.1 X genome equivalents for each of the two genomes). This coverage provides a 99.4% probability of recovering any gene from durum wheat. We used the Gpc-BI flanking markers to screen this BAC library and then completed the physical map by chromosome walking. The physical map included two overlapping BACs covering a region of approximately 250-kb, including two flanking markers and the Gpc-B1 gene. Efforts are underway to sequence these two BACs to determine if additional wheat genes are present in this region. Weare also developing new RSLs to further dissect this region. We developed PCR markers for flanking loci Xucw79andXucw71 to facilitate the introgression of this gene in commercial varieties by marker assisted selection (httQ://maswheat.ucdavis.edu/ orotocols/HGPC/index.hlm). Using these markers we introgressed the Gpc-B1 gene in numerous pasta and common wheat breeding lines.
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Cook, Samantha, Marissa Torres, Nathan Lamie, Lee Perren, Scott Slone, and Bonnie Jones. Automated ground-penetrating-radar post-processing software in R programming. Engineer Research and Development Center (U.S.), September 2022. http://dx.doi.org/10.21079/11681/45621.

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Ground-penetrating radar (GPR) is a nondestructive geophysical technique used to create images of the subsurface. A major limitation of GPR is that a subject matter expert (SME) needs to post-process and interpret the data, limiting the technique’s use. Post-processing is time-intensive and, for detailed processing, requires proprietary software. The goal of this study is to develop automated GPR post-processing software, compatible with Geophysical Survey Systems, Inc. (GSSI) data, in open-source R programming. This would eliminate the need for an SME to process GPR data, remove proprietary software dependencies, and render GPR more accessible. This study collected GPR profiles by using a GSSI SIR4000 control unit, a 100 MHz antenna, and a Trimble GPS. A standardized method for post-processing data was then established, which includes static data removal, time-zero correction, distance normalization, data filtering, and stacking. These steps were scripted and automated in R programming, excluding data filtering, which was used from an existing package, RGPR. The study compared profiles processed using GSSI software to profiles processed using the R script developed here to ensure comparable functionality and output. While an SME is currently still necessary for interpretations, this script eliminates the need for one to post-process GSSI GPR data.
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Kositsky, Joel, and Peyman Milanfar. A Forward-Looking High-Resolution GPR System. Fort Belvoir, VA: Defense Technical Information Center, April 1999. http://dx.doi.org/10.21236/ada461034.

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Reynolds, R. Michael, and Ernie Lewis. Marine ARM GPCI Investigation of Clouds Psychrometer Field Campaign Report. Office of Scientific and Technical Information (OSTI), September 2016. http://dx.doi.org/10.2172/1324981.

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Lewis, Ernie R. Marine ARM GPCI Investigation of Clouds (MAGIC) Field Campaign Report. Office of Scientific and Technical Information (OSTI), December 2016. http://dx.doi.org/10.2172/1343577.

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Dubcovsky, Jorge, Tzion Fahima, Ann Blechl, and Phillip San Miguel. Validation of a candidate gene for increased grain protein content in wheat. United States Department of Agriculture, January 2007. http://dx.doi.org/10.32747/2007.7695857.bard.

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High Grain Protein Content (GPC) of wheat is important for improved nutritional value and industrial quality. However, selection for this trait is limited by our poor understanding of the genes involved in the accumulation of protein in the grain. A gene with a large effect on GPC was detected on the short arm of chromosome 6B in a Triticum turgidum ssp. dicoccoides accession from Israel (DIC, hereafter). During the previous BARD project we constructed a half-million clones Bacterial Artificial Chromosome (BAC) library of tetraploid wheat including the high GPC allele from DIC and mapped the GPC-B1 locus within a 0.3-cM interval. Our long-term goal is to provide a better understanding of the genes controlling grain protein content in wheat. The specific objectives of the current project were to: (1) complete the positional cloning of the GPC-B1 candidate gene; (2) characterize the allelic variation and (3) expression profile of the candidate gene; and (4) validate this gene by using a transgenic RNAi approach to reduce the GPC transcript levels. To achieve these goals we constructed a 245-kb physical map of the GPC-B1 region. Tetraploid and hexaploid wheat lines carrying this 245-kb DIC segment showed delayed senescence and increased GPC and grain micronutrients. The complete sequencing of this region revealed five genes. A high-resolution genetic map, based on approximately 9,000 gametes and new molecular markers enabled us to delimit the GPC-B1 locus to a 7.4-kb region. Complete linkage of the 7.4-kb region with earlier senescence and increase in GPC, Zn, and Fe concentrations in the grain suggested that GPC-B1 is a single gene with multiple pleiotropic effects. The annotation of this 7.4-kb region identified a single gene, encoding a NAC transcription factor, designated as NAM-B1. Allelic variation studies demonstrated that the ancestral wild wheat allele encodes a functional NAC transcription factor whereas modern wheat varieties carry a non-functional NAM-B1 allele. Quantitative PCR showed that transcript levels for the multiple NAMhomologues were low in flag leaves prior to anthesis, after which their levels increased significantly towards grain maturity. Reduction in RNA levels of the multiple NAMhomologues by RNA interference delayed senescence by over three weeks and reduced wheat grain protein, Zn, and Fe content by over 30%. In the transgenic RNAi plants, residual N, Zn and Fe in the dry leaves was significantly higher than in the control plants, confirming a more efficient nutrient remobilization in the presence of higher levels of GPC. The multiple pleiotropic effects of NAM genes suggest a central role for these genes as transcriptional regulators of multiple processes during leaf senescence, including nutrient remobilization to the developing grain. The cloning of GPC-B1 provides a direct link between the regulation of senescence and nutrient remobilization and an entry point to characterize the genes regulating these two processes. This may contribute to their more efficient manipulation in crops and translate into food with enhanced nutritional value. The characterization of the GPC-B1 gene will have a significant impact on wheat production in many regions of the world and will open the door for the identification of additional genes involved in the accumulation of protein in the grain.
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