Relevant bibliographies by topics / Receptor assembly

Academic literature on the topic 'Receptor assembly'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Receptor assembly"

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Ahring, Philip Kiær, Vivian Wan Yu Liao, and Thomas Balle. "Concatenated nicotinic acetylcholine receptors: A gift or a curse?" Journal of General Physiology 150, no. 3 (January 30, 2018): 453–73. http://dx.doi.org/10.1085/jgp.201711846.

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Nicotinic acetylcholine receptors (nAChRs) belong to the Cys-loop receptor family and are vital for normal mammalian brain function. Cys-loop receptors are pentameric ligand-gated ion channels formed from five identical or homologous subunits oriented around a central ion-conducting pore, which result in homomeric or heteromeric receptors, respectively. Within a given Cys-loop receptor family, many different heteromeric receptors can assemble from a common set of subunits, and understanding the properties of these heteromeric receptors is crucial for the continuing quest to generate novel treatments for human diseases. Yet this complexity also presents a hindrance for studying Cys-loop receptors in heterologous expression systems, where full control of the receptor stoichiometry and assembly is required. Therefore, subunit concatenation technology is commonly used to control receptor assembly. In theory, this methodology should facilitate full control of the stoichiometry. In reality, however, we find that commonly used constructs do not yield the expected receptor stoichiometries. With ternary or more complex receptors, concatenated subunits must assemble uniformly in only one orientation; otherwise, the resulting receptor pool will consist of receptors with mixed stoichiometries. We find that typically used constructs of α4β2 nAChR dimers, tetramers, and pentamers assemble readily in both the clockwise and the counterclockwise orientations. Consequently, we investigate the possibility of successfully directing the receptor assembly process using concatenation. We begin by investigating the three-dimensional structures of the α4β2 nAChR. Based on this, we hypothesize that the minimum linker length required to bridge the C terminus of one subunit to the N terminus of the next is shortest in the counterclockwise orientation. We then successfully express receptors with a uniform stoichiometry by systematically shortening linker lengths, proving the hypothesis correct. Our results will significantly aid future studies of heteromeric Cys-loop receptors and enable clarification of the current contradictions in the literature.
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Bollan, K., L. A. Robertson, H. Tang, and C. N. Connolly. "Multiple assembly signals in γ-aminobutyric acid (type A) receptor subunits combine to drive receptor construction and composition." Biochemical Society Transactions 31, no. 4 (August 1, 2003): 875–79. http://dx.doi.org/10.1042/bst0310875.

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Mammalian γ-aminobutyric acid type A (GABAA) receptors are constructed from a large repertoire of subunits (α1–α6, β1–β3, γ1–γ3, δ, ∊, θ and π) into a pentameric ion channel. GABAA receptor assembly occurs within the endoplasmic reticulum (ER) and involves interactions with chaperone molecules. Only specific subunit combinations can produce functional surface receptors (with a fixed stoichiometry); other subunit combinations are retained within the ER and degraded. Thus, receptor assembly occurs by defined pathways to limit the diversity of GABAA receptors. The key to understanding how receptor diversity is achieved and controlled is the identification of assembly signals capable of distinguishing between other subunit partners. Analysis of an assembly box in α1 (residues 57–68) has revealed an absolute requirement for this region in the assembly of αβ receptors. Furthermore, a selective requirement for a single amino acid (R66) is observed for the assembly of α1β2, but not α1β1 or α1β3, receptors. In addition, we have characterized an assembly signal in the β3 subunit that is capable of driving the assembly of β3, γ2β3 and α1β3 receptors. Interestingly, this signal does not appear to utilize the α1 assembly box, suggesting the presence of alternative assembly signals within the α1 subunit. Although this β3 signal is sufficient to permit the formation of βγ receptors it is not necessary, suggesting that alternative assembly signals also exist within the β3 subunit. These findings support the belief that GABAA receptor assembly occurs via multiple defined pathways that may be determined by subunit availability.
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Sarto-Jackson, Isabella, Roman Furtmueller, Margot Ernst, Sigismund Huck, and Werner Sieghart. "Spontaneous Cross-link of Mutated α1 Subunits during GABAA Receptor Assembly." Journal of Biological Chemistry 282, no. 7 (December 4, 2006): 4354–63. http://dx.doi.org/10.1074/jbc.m609676200.

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γ-Aminobutyric acid, type A (GABAA) receptor α1 subunits containing a cysteine mutation at a position in the channel mouth (H109C) surprisingly formed a spontaneous cross-link with each other in receptors composed of α1H109C, β3, and γ2 subunits. Cross-linking of two α1H109C subunits did not significantly change the affinity of [3H]muscimol or [3H]Ro15-1788 binding in α1H109Cβ3γ2 receptors, but GABA displayed a reduced potency for activating chloride currents. On reduction of the disulfide bond, however, GABA activation as well as diazepam modulation was similar in mutated and wild-type receptors, suggesting that these receptors exhibited the same subunit stoichiometry and arrangement. Disulfide bonds could not be reoxidized by copper phenanthroline after having been reduced in completely assembled receptors, suggesting that cross-linking can only occur at an early stage of assembly. The cross-link of α1H109C subunits and the subsequent transport of the resulting homodimers to the cell surface caused a reduction of the intracellular pool of α1H109C subunits and a reduced formation of completely assembled receptors. The formation of α1H109C homodimers as well as of correctly assembled GABAA receptors containing cross-linked α1H109C subunits could indicate that homodimerization of α1 subunits via contacts located in the channel mouth might be one starting point of GABAA receptor assembly. Alternatively the assembly mechanism might have started with the formation of heterodimers followed by a cross-link of mutated α1 subunits at the heterotrimeric stage. The formation of cross-linked α1H109C homodimers would then have occurred independently in a separate pathway.
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Knudson, C. B. "Hyaluronan receptor-directed assembly of chondrocyte pericellular matrix." Journal of Cell Biology 120, no. 3 (February 1, 1993): 825–34. http://dx.doi.org/10.1083/jcb.120.3.825.

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Initial assembly of extracellular matrix occurs within a zone immediately adjacent to the chondrocyte cell surface termed the cell-associated or pericellular matrix. Assembly within the pericellular matrix compartment requires specific cell-matrix interactions to occur, that are mediated via membrane receptors. The focus of this study is to elucidate the mechanisms of assembly and retention of the cartilage pericellular matrix proteoglycan aggregates important for matrix organization. Assembly of newly synthesized chondrocyte pericellular matrices was inhibited by the addition to hyaluronan hexasaccharides, competitive inhibitors of the binding of hyaluronan to its cell surface receptor. Fully assembled chondrocyte pericellular matrices were displaced using hyaluronan hexasaccharides as well. When exogenous hyaluronan was added to matrix-free chondrocytes in combination with aggrecan, a pericellular matrix equivalent in size to an endogenous matrix formed within 30 min of incubation. Addition of hyaluronan and aggrecan to glutaraldehyde-fixed chondrocytes resulted in matrix assembly comparable to live chondrocytes. These matrices could be inhibited from assembling by the addition of excess hyaluronan hexasaccharides or displaced once assembled by subsequent incubation with hyaluronan hexasaccharides. The results indicate that the aggrecanrich chondrocyte pericellular matrix is not only on a scaffolding of hyaluronan, but actually anchored to the cell surface via the interaction between hyaluronan and hyaluronan receptors.
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Letourneur, F., S. Hennecke, C. Démollière, and P. Cosson. "Steric masking of a dilysine endoplasmic reticulum retention motif during assembly of the human high affinity receptor for immunoglobulin E." Journal of Cell Biology 129, no. 4 (May 15, 1995): 971–78. http://dx.doi.org/10.1083/jcb.129.4.971.

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Signals that can cause retention in the ER have been found in the cytoplasmic domain of individual subunits of multimeric receptors destined to the cell surface. To study how ER retention motifs are masked during assembly of oligomeric receptors, we analyzed the assembly and intracellular transport of the human high-affinity receptor for immunoglobulin E expressed in COS cells. The cytoplasmic domain of the alpha chain contains a dilysine ER retention signal, which becomes nonfunctional after assembly with the gamma chain, allowing transport out of the ER of the fully assembled receptor. Juxtaposition of the cytoplasmic domains of the alpha and gamma subunits during assembly is responsible for this loss of ER retention. Substitution of the gamma chain cytoplasmic domain with cytoplasmic domains of irrelevant proteins resulted in efficient transport out of the ER of the alpha chain, demonstrating that nonspecific steric hindrance by the cytoplasmic domain of the gamma chain accounts for the masking of the ER retention signal present in the cytoplasmic domain of the alpha chain. Such a mechanism allows the ER retention machinery to discriminate between assembled and nonassembled receptors, and thus participates in quality control at the level of the ER.
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Blount, P., and J. P. Merlie. "Mutational analysis of muscle nicotinic acetylcholine receptor subunit assembly." Journal of Cell Biology 111, no. 6 (December 1, 1990): 2613–22. http://dx.doi.org/10.1083/jcb.111.6.2613.

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The structural elements required for normal maturation and assembly of the nicotinic acetylcholine receptor alpha subunit were investigated by expression of mutated subunits in transfected fibroblasts. Normally, the wild-type alpha subunit acquires high affinity alpha bungarotoxin binding in a time-dependent manner; however, mutation of the 128 and/or 142 cysteines to either serine or alanine, as well as deletion of the entire 14 amino acids in this region abolished all detectable high affinity binding. Nonglycosylated subunits that had a serine to glycine mutation in the consensus sequence also did not efficiently attain high affinity binding to toxin. In contrast, mutation of the proline at position 136 to glycine or alanine, or a double mutation of the cysteines at position 192 and 193 to serines had no effect on the acquisition of high affinity toxin binding. These data suggest that a disulfide bridge between cysteines 128 and 142 and oligosaccharide addition at asparagine 141 are required for the normal maturation of alpha subunit as assayed by high affinity toxin binding. The unassembled wild-type alpha subunit expressed in fibroblasts is normally degraded with a t1/2 of 2 h; upon assembly with the delta subunit, the degradation rate slows significantly (t1/2 greater than 13 h). All mutated alpha subunits retained the capacity to assemble with a delta subunit coexpressed in fibroblasts; however, mutated alpha subunits that were not glycosylated or did not acquire high affinity toxin binding were rapidly degraded (t1/2 = 20 min to 2 h) regardless of whether or not they assembled with the delta subunit. Assembly and rapid degradation of nonglycosylated acetylcholine receptor (AChR) subunits and subunit complexes were also observed in tunicamycin-treated BC3H-1 cells, a mouse musclelike cell line that normally expresses functional AChR. Hence, rapid degradation may be one form of regulation assuring that only correctly processed and assembled subunits accumulate, and ultimately make functional receptors in AChR-expressing cells.
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Millar, N. S. "Assembly and subunit diversity of nicotinic acetylcholine receptors." Biochemical Society Transactions 31, no. 4 (August 1, 2003): 869–74. http://dx.doi.org/10.1042/bst0310869.

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Nicotinic acetylcholine receptors (nAChRs) are a diverse family of neurotransmitter-gated ion channels which contain five transmembrane subunits arranged around a central pore. Distinct receptor subtypes are expressed at the vertebrate skeletal neuromuscular junction, in mechanosensory cells and within the central and peripheral nervous systems. A total of 17 nAChR subunits (α1–α10, β1–β4, γ, δ and ∊) have been identified in vertebrate species, which can co-assemble to generate a wide variety of nAChRs. Nicotinic receptors also constitute an abundant and diverse family of receptors in invertebrates. As a consequence of studies which have been conducted with both native and recombinant nAChRs, the subunit composition of nAChRs and the rules governing subunit co-assembly are becoming clearer. In this paper the extent of nAChR subunit diversity and evidence for receptor subunit composition is reviewed.
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Pratt, William B., Mario D. Galigniana, Yoshihiro Morishima, and Patrick J. M. Murphy. "Role of molecular chaperones in steroid receptor action." Essays in Biochemistry 40 (June 1, 2004): 41–58. http://dx.doi.org/10.1042/bse0400041.

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Unliganded steroid receptors are assembled into heterocomplexes with heat-shock protein (hsp) 90 by a multiprotein chaperone machinery. In addition to binding the receptors at the chaperone site, hsp90 binds cofactors at other sites that are part of the assembly machinery, as well as immunophilins that connect the assembled receptor-hsp90 heterocomplexes to a protein trafficking pathway. The hsp90-/hsp70-based chaperone machinery interacts with the unliganded glucocorticoid receptor to open the steroid-binding cleft to access by a steroid, and the machinery interacts in very dynamic fashion with the liganded, transformed receptor to facilitate its translocation along microtubular highways to the nucleus. In the nucleus, the chaperone machinery interacts with the receptor in transcriptional regulatory complexes after hormone dissociation to release the receptor and terminate transcriptional activation. By forming heterocomplexes with hsp90, the chaperone machinery stabilizes the receptor to degradation by the ubiquitin-proteasome pathway of proteolysis.
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Ball, Stephen G., Christopher Bayley, C. Adrian Shuttleworth, and Cay M. Kielty. "Neuropilin-1 regulates platelet-derived growth factor receptor signalling in mesenchymal stem cells." Biochemical Journal 427, no. 1 (March 15, 2010): 29–40. http://dx.doi.org/10.1042/bj20091512.

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Using human MSCs (mesenchymal stem cells) lacking VEGF (vascular endothelial growth factor) receptors, we show that the pro-angiogenic receptor neuropilin-1 associates with phosphorylated PDGFRs [PDGF (platelet-derived growth factor) receptors], thereby regulating cell signalling, migration, proliferation and network assembly. Neuropilin-1 co-immunoprecipitated and co-localized with phosphorylated PDGFRs in the presence of growth factors. Neuropilin-1 knockdown blocked PDGF-AA-induced PDGFRα phosphorylation and migration, reduced PDGF-BB-induced PDGFRβ activation and migration, blocked VEGF-A activation of both PDGFRs, and attenuated proliferation. Neuropilin-1 prominently co-localized with both PDGFRs within MSC networks assembled in Matrigel™ and in the chorioallantoic membrane vasculature microenvironment, and its knockdown grossly disrupted network assembly and decreased PDGFR signalling. Thus neuropilin-1 regulates MSCs by forming ligand-specific receptor complexes that direct PDGFR signalling, especially the PDGFRα homodimer. This receptor cross-talk may control the mobilization of MSCs in neovascularization and tissue remodelling.
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Minamiki, Tsukuru, Yuki Ichikawa, and Ryoji Kurita. "The Power of Assemblies at Interfaces: Nanosensor Platforms Based on Synthetic Receptor Membranes." Sensors 20, no. 8 (April 15, 2020): 2228. http://dx.doi.org/10.3390/s20082228.

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Synthetic sensing materials (artificial receptors) are some of the most attractive components of chemical/biosensors because of their long-term stability and low cost of production. However, the strategy for the practical design of these materials toward specific molecular recognition in water is not established yet. For the construction of artificial material-based chemical/biosensors, the bottom-up assembly of these materials is one of the effective methods. This is because the driving forces of molecular recognition on the receptors could be enhanced by the integration of such kinds of materials at the ‘interfaces’, such as the boundary portion between the liquid and solid phases. Additionally, the molecular assembly of such self-assembled monolayers (SAMs) can easily be installed in transducer devices. Thus, we believe that nanosensor platforms that consist of synthetic receptor membranes on the transducer surfaces can be applied to powerful tools for high-throughput analyses of the required targets. In this review, we briefly summarize a comprehensive overview that includes the preparation techniques for molecular assemblies, the characterization methods of the interfaces, and a few examples of receptor assembly-based chemical/biosensing platforms on each transduction mechanism.
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Dissertations / Theses on the topic "Receptor assembly"

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Sagar, Rajeeve. "Self-assembly via hydrogen bonding." Thesis, University of Warwick, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.247352.

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Atlason, Palmi por. "The folding and assembly of NMDA receptor subunits." Thesis, University of Oxford, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.487137.

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The NMDA receptor is a member of the ionotropic glutamate receptor family, which includes the AMPA and kainate receptors. Functional NMDA receptors are heteromeric and made up from three receptor subunit families; NR1, NR2 and NR3. Currently, the receptor is thought to form in a dimer-of-dimer assembly with two NRI subunits and two NR2 subunits. The NR3 can associate with both NRI and NR2 to form a unique receptor or NRI alone to form an excitatory glycine receptor. The exact assembly pathway and the nature of assembly intermediates are currently unknown. The folding status of NR1, NR2A and NR3A was examined in heterologous systems, both individually expressed and co-expressed. It was found that while NRI appeared to fold well when expressed on its own and contain relatively few free cysteine residues, the NR3A subunit appeared to form aggregates when analysed under non-reducing conditions. BothNR2A and NR3A aggregated when treated with the sulfhydryl crosslinker BMH, indicating mUltiple free cysteine residues and a degree of misfolding. NRI migrated as a dimer when treated with BMH. A small pool of fast degrading NRI was detected but the majority of the protein was very stable in cells. NR2A and NR3A were turned over rapidly when expressed on their own with NR2A showing stabilisation in the presence of NRI. FRAP analysis indicated a degree of misfolding of NR2A and NR3A. NRI readily associated with both NR2A and NR3A but no association of NR2A and NR3A was detected in the absence ofNRl. The analysis of receptor assembly using BiFC confirmed the homodimerization of NRI but failed to give any evidence for homodimerization of either NR2A or NR3A. The BiFC analysis further indicates that the homodimer of NRI is readily disassociable. The robust complementation seen between NRI and NR2A, coupled with the absence of complementation ofNR2A and NR2A in the presence ofNRl suggest the preferential assembly of heterodimers. Possibly, steric constraints prevent complementation in the tetramer, suggesting a 1-2-1-2 symmetry around the pore. A similar constraint due to a coiled-coil domain in NR3A might explain the absence of complementation between NRI and NR3A. . Taken together, the results suggest the central role of NRI in the folding and assembly of the other subunit families. The probable assembly pathway suggests recruitment of NRI from an intracellular pool to associate with newly synthesised NR2 or NR3 to form heterodimers which then assemble to form the functional tetrameric receptor.
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Smith, Miriam Jane. "Studies of GABA_A receptor subunit assembly and processing." Thesis, University College London (University of London), 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.415891.

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Taylor, Pamela Mary. "Identification of assembly determinants in GABA←A receptor subunits." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.394507.

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Goebel, Erich J. "Insights into the Activin Class: Mechanisms of Receptor Assembly and Specificity." University of Cincinnati / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=ucin162316530833396.

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Nadler, Laurie Sue. "GABA(A) receptor subunit expression and assembly in rat cerebellar neurons." Case Western Reserve University School of Graduate Studies / OhioLINK, 1996. http://rave.ohiolink.edu/etdc/view?acc_num=case1057672368.

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Berglund, Jenny. "Structure-function studies of organelle assembly and receptor recognition in organelles assembled via the chaperone/usher pathway /." Uppsala : Dept. of Molecular Biology, Swedish Univ. of Agricultural Sciences, 2004. http://epsilon.slu.se/a441.pdf.

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Blümmel, Anne-Sophie [Verfasser], and Matthias [Akademischer Betreuer] Müller. "Initial assembly steps of the twin-arginine translocation signal peptide receptor complex." Freiburg : Universität, 2016. http://d-nb.info/1135118256/34.

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Legate, Kyle R. Andrews D. W. "Characterization of the beta-subunit of the mammalian SRP receptor and its role in assembly of the SRP receptor /." *McMaster only, 2003.

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Sukumaran, Madhav. "Biophysical investigations of AMPA receptor N-terminal domain structure and function reveal mechanisms underlying receptor assembly, dynamics, and allosteric potential." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708278.

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Books on the topic "Receptor assembly"

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Molecular Mechanisms that Orchestrate the Assembly of Antigen Receptor Loci. Elsevier, 2015. http://dx.doi.org/10.1016/s0065-2776(15)x0005-8.

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Murre, Cornelis. Molecular Mechanisms That Orchestrate the Assembly of Antigen Receptor Loci. Elsevier Science & Technology Books, 2015.

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Jockers, Ralf, Denis J. Dupré, and Terence E. Hébert. GPCR Signalling Complexes - Synthesis, Assembly, Trafficking and Specificity. Springer, 2012.

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Gpcr Signalling Complexes Synthesis Assembly Trafficking And Specificity. Springer, 2012.

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Jockers, Ralf, Denis J. Dupré, and Terence E. Hébert. GPCR Signalling Complexes - Synthesis, Assembly, Trafficking and Specificity. Springer London, Limited, 2012.

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Keith, Chris. The Gospel as Manuscript. Oxford University Press, 2020. http://dx.doi.org/10.1093/oso/9780199384372.001.0001.

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This book offers a new material history of the Jesus tradition. It shows that the introduction of manuscripts to the transmission of the Jesus tradition played an underappreciated but crucial role in the reception history of the tradition that eventuated. It focuses particularly on the competitive textualization of the Jesus tradition, whereby Gospel authors drew attention to the written nature of their tradition, sometimes in attempts to assert superiority to predecessors, and the public reading of the Jesus tradition. Both these processes reveal efforts on the part of early followers of Jesus to place the gospel-as-manuscript on display, whether in the literary tradition or in the assembly. Building upon interdisciplinary work on ancient book cultures, this book traces an early history of the gospel as artifact from the textualization of Mark in the first century until the eventual usage of liturgical reading as a marker of authoritative status in the second and third centuries and beyond. Overall, it reveals a vibrant period of the development of the Jesus tradition, wherein the material status of the tradition frequently played as important a role as the ideas about Jesus that it contained.
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Deaville, James, Siu-Lan Tan, and Ron Rodman, eds. The Oxford Handbook of Music and Advertising. Oxford University Press, 2021. http://dx.doi.org/10.1093/oxfordhb/9780190691240.001.0001.

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The Oxford Handbook of Music and Advertising assembles an array of forty-two pathbreaking chapters on the production, texts, and reception of advertising through music. Uniquely interdisciplinary, the collection’s tripartite structure leads the reader through these stages in the communication of the advertising message as presented by Chris Wharton (2015). The chapters on production study the factors, activities, and people behind the music for the marketing pitch, both past and present. Prominent throughlines in the section include factors influencing the selection of music (and musicians) for advertising, the role of music in corporate branding strategies, the creative forces behind the soundscape of advertising, and industry practices that undergird all aspects of music in commercial contexts. The section on Text focuses on analytic and historical approaches to ads in various media, and includes commentaries on musical genres in ads ranging from Western European art music to American popular genre. Also covered in this section is ad music as used in different ad genres, such as political ads, public service announcements, and television commercials. The analyses used in this section draws from traditional music theory, semiotics, and hermeneutic analysis. Finally, the last section addressing “Reception”—with contributions by researchers in psychology, marketing, and other fields—involves the formulation of models and theories, and implementation of research methods to examine how the presence of music may influence peoples’ attitudes, emotions, thoughts, and behaviors in the context of advertisements and within service environments such as stores, restaurants, and banks. The editors and chapter contributors of this book bring a diversity of perspectives to the topic but share a united aim: to illuminate music’s vital contribution to the advertising message.
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Harris, Laura. Experiments in Exile. Fordham University Press, 2018. http://dx.doi.org/10.5422/fordham/9780823279784.001.0001.

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Comparing the radical aesthetic and social experiments undertaken by two exile intellectuals, James and Oiticica, Harris chart a desire in their work to formulate alternative theories of citizenship, wherein common reception of popular cultural forms is linked to a potentially expanded, non-exclusive polity. By carefully analyzing the materiality of the multiply-lined, multiply voiced writing of the “undocuments” that record these social experiments and relay their prophetic descriptions of and instructions for the new social worlds they wished to forge and inhabit, however, Harris argue that their projects ultimately challenge rather than seek to rehabilitate normative conceptions of citizens and polities as well as authors and artworks. James and Oiticica’s experiments recall the insurgent sociality of “the motley crew” historians Peter Linebaugh and Marcus Rediker describe in The Many-Headed Hydra, their study of the trans-Atlantic, cross-gendered, multi-racial working class of the seventeenth and eighteenth centuries. Reading James’s and Oiticica’s projects against the grain of Linebaugh and Rediker’s inability to find evidence of that sociality’s persistence or futurity, Harris show how James and Oiticica gravitate toward and seek to relay the ongoing renewal of dissident, dissonant social forms, which are for them always also aesthetic forms, in the barrack-yards of Port-of-Spain and the favelas of Rio de Janeiro, the assembly lines of Detroit and the streets of the New York. The formal openness and performative multiplicity that manifests itself at the place where writing and organizing converge invokes that sociality and provokes its ongoing re-invention. Their writing extends a radical, collective Afro-diasporic intellectuality, an aesthetic sociality of blackness, where blackness is understood not as the eclipse, but the ongoing transformative conservation of the motley crew’s multi-raciality. Blackness is further instantiated in the interracial and queer sexual relations, and in a new sexual metaphorics of production and reproduction, whose disruption and reconfiguration of gender structures the collaborations from which James’s and Oiticica’s undocuments emerge, orienting them towards new forms of social, aesthetic and intellectual life.
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Book chapters on the topic "Receptor assembly"

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Jung, Seung-Yong, Edward T. Castellana, Matthew A. Holden, Tinglu Yang, and Paul S. Cremer. "Multivalent Ligand-Receptor Interactions on Planar Supported Membranes An On-Chip Approach." In Nanoscale Assembly, 99–117. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-25656-3_6.

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Thomas, Lance R., Robin Milley Cobb, and Eugene M. Oltz. "Dynamic Regulation of Antigen Receptor Gene Assembly." In Advances in Experimental Medicine and Biology, 103–15. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-0296-2_9.

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Terhorst, C., B. Alarcon, B. Berkhout, R. Blumberg, H. Clevers, K. Georgopoulos, C. Hall, et al. "Assembly of the T Cell Receptor/CD3 Complex." In Progress in Immunology, 33–39. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-83755-5_6.

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Millard, Christopher J., and John W. R. Schwabe. "Assembly and Regulation of Nuclear Receptor Corepressor Complexes." In Nuclear Receptors: From Structure to the Clinic, 155–75. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-18729-7_9.

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Smith, David F., William P. Sullivan, Jill Johnson, and David O. Toft. "In Vitro Assembly of the Avian Progesterone Receptor." In Steroid Hormone Receptors: Basic and Clinical Aspects, 247–60. Boston, MA: Birkhäuser Boston, 1994. http://dx.doi.org/10.1007/978-1-4615-9849-7_9.

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Fox-Loe, Ashley M., Linda P. Dwoskin, and Christopher I. Richards. "Nicotinic Acetylcholine Receptors as Targets for Tobacco Cessation Therapeutics: Cutting-Edge Methodologies to Understand Receptor Assembly and Trafficking." In Nicotinic Acetylcholine Receptor Technologies, 119–32. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3768-4_7.

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Sukumaran, Madhav, Andrew C. Penn, and Ingo H. Greger. "AMPA Receptor Assembly: Atomic Determinants and Built-In Modulators." In Synaptic Plasticity, 241–64. Vienna: Springer Vienna, 2012. http://dx.doi.org/10.1007/978-3-7091-0932-8_11.

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Übelhart, Rudolf, Markus Werner, and Hassan Jumaa. "Assembly and Function of the Precursor B-Cell Receptor." In Current Topics in Microbiology and Immunology, 3–25. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/82_2015_475.

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von Heijne, Gunnar. "Sequence Determinants for Protein Import into Chloroplasts and Thylakoid Membrane Protein Assembly." In Transport and Receptor Proteins of Plant Membranes, 195–99. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3442-6_18.

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Vignali, Dario A. A. "Cooperative Recognition of MHC Class II:Peptide Complexes by the T Cell Receptor and CD4." In MHC Molecules: Expression, Assembly and Function, 207–28. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4684-6462-7_13.

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Conference papers on the topic "Receptor assembly"

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Srinivasan, Visvanathan, Nayan Reddy, Adriana Brasoava, and David L. Wells. "Micro-Embossing of Polymeric Substrates for Fluidic Self-Assembly." In ASME 2006 International Mechanical Engineering Congress and Exposition. ASMEDC, 2006. http://dx.doi.org/10.1115/imece2006-14817.

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Fluidic Self-Assembly™ (FSA)™ has become a routine manufacturing process in the production of radio-frequency identification tags. FSA operates through the self-positioning of micro-devices into pre-prepared matching receptor sites in a substrate. Research at North Dakota State University has focused on extending the applications of FSA well-beyond the current production routine. This pursuit requires, among other modifications, substantive extrapolation of the size, depth, configuration, spacing and spatial density of receptor sites. Three different test wafer patterns (see Figure 5 for patterns having nominal sizes of 1050μ, 1500μ, μ2150 and 3050μ square receptors with different spacing between them) took into account the corner compensation structure dimensions, which are based on thickness of silicon mold wafer feature to be etched (see Figure 2). The embossing tool (silicon wafer) was patterned photo-lithographically and subsequently wet etched in a KOH 2:1 solution. Experiments suggest shorter tool life in the case of closely packed features (spacing ~ 0.5mm). Receptor profiles evaluated using both optical and mechanical inspection (see Figures 3 and 4) suggest that features having larger size (up to nominal size of 3050μ square) and thickness (nominal depths of 110μ and 210μ) can be embossed accurately for use in FSA by slightly increasing the embossing time in case of deeper receptors. It was also noticed that the relative receptor depths attained with respect to the thickness of the feature on the mold wafer was lower while embossing deeper receptor sites, leading to the conclusion that mold wafers must be etched longer in such cases. The embossed receptor sites were subsequently filled with micro-devices in accordance with the standard operating parameters of Fluidic Self-Assembly process. These sample experimental runs suggest receptors slightly deeper than the micro-devices facilitate higher yields (or fill rates) in FSA. However, in cases where the receptors are too deep relative to the micro-device (> 5μ), air-entrapment occurred between the micro-device and the bottom of the receptor site, which caused problems in post-FSA processes due to air expansion. This paper presents comprehensive guidelines for embossing larger and deeper receptors for effective use in FSA.
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Huss, Anja, Omar Ramírez, Felipe Santibáñez, Andrés Couve, Steffen Härtel, and Jörg Enderlein. "SOFI of GABABneurotransmitter receptors in hippocampal neurons elucidates intracellular receptor trafficking and assembly." In SPIE BiOS, edited by Jörg Enderlein, Ingo Gregor, Zygmunt K. Gryczynski, Rainer Erdmann, and Felix Koberling. SPIE, 2013. http://dx.doi.org/10.1117/12.2006215.

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Brasoava, Adriana, Radu Danescu, Visvanathan Srinivasan, and David Wells. "Preferential Orientation of Silicon Blocks During Fluidic Self-Assembly of Microelectronics." In ASME 2005 International Mechanical Engineering Congress and Exposition. ASMEDC, 2005. http://dx.doi.org/10.1115/imece2005-81417.

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Fluidic Self-Assembly (FSA) is a newly developed, high productivity method to assemble millimeter and submillimeter size silicon electronic components (blocks) into circuit boards. Large numbers of thin, truncated pyramid shaped components are released in water and move gravitationally down inclined substrates to fall into indentations (receptors) of complementary shape. To increase the rate of receptor filling and improve the process efficiency, the probability of proper alignment between blocks and receptors must be maximized. The present paper reports an experimental study aimed at determining the preferential orientation of the blocks in a practical FSA process. Blocks ranging in size from 1050 to 3050 microns were tested for: (i) in-plane orientation angle during their motion, and (ii) right-side-up (RSU) versus up-side-down (USD) landing upon dispensing. Results indicate that blocks exhibit a high degree of in-plane angular self-orientation, which depends on the block aspect ratio. Spatial orientation of blocks at the release point is a decisive factor on their correct (RSU) landing on the substrate. Based on this observation, an original dispensing strategy was developed that increased the RSU fraction to values typically over 90%.
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Xiao Zhu Fan, Konstantinos Gerasopoulos, Adam Brown, Nathan Siwak, James Culver, and Reza Ghodssi. "Virus directed assembly of receptor peptides for explosive sensing." In 2010 Ninth IEEE Sensors Conference (SENSORS 2010). IEEE, 2010. http://dx.doi.org/10.1109/icsens.2010.5690229.

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Dominak, Lisa M., Sailaja Paruchuri, Jennifer Leising, Brian D. Southern, and Mitchell Olman. "Urokinase Receptor Ligation Orchestrates Lipid Raft Assembly Leading To Migration." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a6041.

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Duperray, A., A. Troesch, R. Berthier, E. Chagnon, and G. Marguerie. "BIOSYNTHESIS AND ASSEMBLY OF PLATELET GPIIbIIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643958.

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Platelet GPIIbIIIa is a calcium-dependent heterodimer which is constituted of two proteins subunits GPIIb and GPIIIa. The GPIIb is itself made of two disulfide-linked subunits IIba and IIbβ. GPIlia is a single chain protein. GPIIbIIIa serves as a receptor for fibrinogen, fibronectin and von Willebrand factor and is implicated in platelet adhesive reactions. This protein is a member of an adhesion receptor protein family for which the name “cytoadhesins” has been proposed. As a preliminary step in the study of the genetic diversity of the members of this family, we have analysed the biosynthesis and assembly of GPIIbIIIa in human megakaryocytes and in a human megakaryocytic cell line : LAMA-84. Megakaryocytes were isolated from liquid cultures of cryopreserved blood cell concentrates from patients in the chronic phase of chronic myeloid leukemia. Using these cell preparations, we have shown that the a and 3 subunits of GPIIb derive from a common precursor, the pro-GPIIb, which associated in an early step with GP IIIa. In a second set of experiments, we have analysed the expression of the GPIIbIIIa complex in LAMA-84. Only a minority of the native cells were reacting with the anti GPIIIIIa antibodies as tested by immunofluorescent labeling. In contrast, the expression of GPIIbIIIa in these cells was amplified in the presence of the phorbol ester TPA. Metabolic labeling experiments indicated that a large quantity of pro-GPIIb was synthesized in the native cells, while very little of the mature forms of GPIIb and IIIa were detected. After TPA induction, the expression of GPIIIa was greatly enhanced with a simultaneous increase in mature GPIIb. These data indicate that a deficit in GP Ilia results in the biosynthesis of a non-associated pro-GPIIb which cannot be further processed, suggesting that the GPIIIa subunit is a regulatory component in the biosynthesis of the GPIIbIIIa complex.
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Marquerie, G., A. Duperray, G. Uzan, and R. Berthier. "BIOSYNTHETIC PATHWAYS OF THE PLATELET FIBRINOGEN RECEPTOR IN HUMAN MEGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642954.

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Interaction between cells and between cells and extracellular matrices are critical for a number of biological processes, including organ development, cell differenciation, cell motility, and the inimune' response. These interactions are mediated by a family of adhesion receptors that recognize short sequences such as Arg-Gly-Asp (RGD). These receptors share similar structural properties. They are heterodimers composed of a and B subunits and sometime express common epitopes. This suggests that the structural and functional relationship of these receptors may result from the transcription of related genes or may arise from cell specific post-transcriptional events. Thus, analysis of the biosynthesis and processing of these receptors would provide valuable insights into the molecular mechanism which control their expression at the surface,of different cells. Platelet membrane glycoprotein (GP) IIb-IIIa is a member of this receptor family. This protein is a non covalent heterodimer composed of two distinct polypeptides, Glib which consists of two subunits Ilba and IlbB (Mr = 116 kD, Mr = 25 kD) and GPIIIa (Mr = 100 kD, reduced). GPIIb-IIIa functions at site of platelet aggregation and serves as receptor for RGD containing factors including fibrinogen, fibronectin and von Willebrand factor. We report here on the investigation of the biosynthetic pathways of this RGD receptor in human megakaryocytes. High number of megakaryocytic cells from the megakaryoblastic stage to the polyploid mature megakaryocyte were obtained from liquid culture of cryopreserved leukocyte stem cell concentrates from patients with chronic myelogenous leukemia (CML). After sorting, using a FACS IV and indirect immunofluores-cent labeling with monoclonal antibodies anti-GPIIb-IIIa, 95 % of the cells in culture were of the megakaryocytic lineage. These megakarocytes represented an excellent tool to delineate at the molecular level events associated with the biosynthesis of GPIIb-IIIa.Metabolic labeling and pulse-chase experiments indicated that GPIIb and GPIIIa are synthesized from separate mRNA and that the two subunits of GPIIb derive from a common precursor. This was further confirmed by cell-free translation of megakaryocyte mRNA and the identification of separate cDNA containing sequences coding for the pro-GPIIb and for GPIIIa. These cDNA were isolated from a Xgt11 expression library constructed with purified megakaryocyte RNA, and were used to size the messengers coding for the two polypeptides. A single mRNA species of 3.9 kB was found to encode the pro-GPIIb, whereas two different mRNA species of 2.9 kB and 4. 1 kB were identified with the GPIIIa cDNA.The newly synthesized GPIIIa associates early with the pro-GPIIb in the rough endoplasmic reticulum. Examination of the glycosylation pathways with endoglycosidase H, tunicamycin and monensin indicated that high mannose oligosaccharides are added to the GPIIIa and pro-GPIIb polypeptide backbone. The pro-GPIIb is then processed with conversion of high mannose to the complex type carbohydrate, whereas GPIIIa remains endoH sensitive. Glycosylation of pro-GPIIb-IIIa and processing of oligosaccharides are prerequisite for proteolytic maturation of pro-GPIIb and the expression of the mature complex at the surface of the cell. Thus post-translational processing of GPIIb-IIIa requires an early assembly of the complex. This may have important implications in the maturation of megakaryocyte granules and in the molecular mechanism underlying the Glanzmann thrombastenic disease.
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Yahaya, Muhammad, Muhamad Mat Salleh, and Akrajas Ali Umar. "Self-assembly layer of amino fluorenone derivative as optical receptor to detect cyclohexane vapour." In Microtechnologies for the New Millennium 2005, edited by Carles Cane, Jung-Chih Chiao, and Fernando Vidal Verdu. SPIE, 2005. http://dx.doi.org/10.1117/12.608493.

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Stern, David M., Sara Rimon, Todd Scott, and Peter P. Nawroth. "MODULATION OF ENDOTHELIAL CELL COAGULANT PROPERTIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642946.

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As the cells forming the luminal vascular surface, endothelium is strategically located to play a role in the regulation of coagulation. Participation of endothelium in coagulation involves specific receptors on the cell surface functioning at the level of initiation and propagation of hemostatic reactions. In the anticoagulant protein C pathway, for example, the receptor thrombomodulin initiates thrombin-mediated activation of protein C and a binding site for protein S on bovine endothelium promotes assembly of the functional activated protein C/protein S complex. Endothelium also synthesizes, stores and releases functional protein S constitutively and in response to specific stimuli such as norepinephrine.Since activation of protein C requires thrombin formation in proximity to the vessel wall, we have examined procoagulant reactions on the endothelial cell surface. Endothelium provides a receptor for Factor IX/IXa which is relatively selective for the enzyme form and facilitates Factor IXa-VIII-mediated activation of Factor X. Half-maximal Factor Xa formation occurs at a Factor IXa concentration of 0.4nM on endothelium, whereas lOnM is required on liposomes. This concentration of Factor IXa corresponds to that which results in half-maximal occupancy of endothelial cell Factor IXa binding sites in the presence of Factors VIII and X, thus correlating kinetics and binding measurements. Crosslinking and ligand blotting studies have shown that the receptor is a protein with a molecular weight of ∼160,000. The clinical significance of this receptor is suggested by the moderately severe bleeding disorder observed in a patient with hemophilia B due to an abnormal Factor IX molecule, Factor IXalabama (Factor IXala). Although the coagulant activity of Factor IXala is only mildly decreased on phospholipids, it is severely impaired on endothelium. The affinity of Factor IXala for the endothelial cell Factor X activation complex is decreased by 20-fold compared with the normal enzyme and the binding affinity is similarly decreased. Since the molecular defect in Factor IXala has been previously shown to consist of a single point mutation in the growth factor domain, this indicates a role for the growth factor domain in receptor, recognition.The picture of endothelial cell coagulant properties which emerges from these and other studies is one in which endothelium has either an anticoagulant or procoagulant potential, depending on modulation of receptor expression and release of secreted products. In the quiescent state, anticoagulant mechanisms predominate with only limited amounts of procoagulant activity: there is little tissue factor activity and only a basal level of receptors for Factor IX/lXa. Activation of endothelium by Tumor Necrosis Factor (TNF) or Interleukin 1 can shift this balance. Tissue factor synthesis and expression occurs in a dose-dependent manner, being half-maximal at a TNF concentration of about 150pM. TNF also increases the number of Factor IX/lXa binding sites. Concomitant with enhancement of endothelial cell procoagulant properties is a suppression of cell surface cofactor activity for the anticoagulant protein C pathway. Endothelial cell-dependent, thrombin-mediated activated protein C formation is decreased by 70-80% and activated protein C-protein S-mediated Factor Va inactivation decreases by over 90%. Following the in vivo infusion of Interleukin 1, similar changes in endothelial cell coagulant properties were observed on aortic segments with fibrin deposition occurring on the functionally altered, but morphologically intact endothelium. This modulation of endothelial cell coagulant properties could underlie the prothrombotic state associated with inflammatory disorders and could also explain the recently observed selective intravascular thrombosis of tumor vasculature seen in vivo in meth A sarcomas after administration of TNF.Thus, although endothelium was initially felt to be hemostatically inert, this apparent lack of activity actually masks a delicate balance of procoagulant and anticoagulant mechanisms. The balance can be effectively shifted by physiologic mediators, such as monokines, which alter receptor expression on the endothelial cell surface. Changes in endothelial cell hemostatic properties may be an early indicator of vessel wall disease and underlie the pathogenesis of localized thrombotic processes.
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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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Reports on the topic "Receptor assembly"

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Hesterman, Eli, Myles A. Brown, and Yongfeng Shang. Dynamics of Estrogen Receptor Transcription Complex Assembly in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada412699.

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Gafni, Yedidya, and Vitaly Citovsky. Molecular interactions of TYLCV capsid protein during assembly of viral particles. United States Department of Agriculture, April 2007. http://dx.doi.org/10.32747/2007.7587233.bard.

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Tomato yellow leaf curl geminivirus (TYLCV) is a major pathogen of cultivated tomato, causing up to 100% crop loss in many parts of the world. The present proposal, a continuation of a BARD-funded project, expanded our understanding of the molecular mechanisms by which CP molecules, as well as its pre-coat partner V2, interact with each other (CP), with the viral genome, and with cellular proteins during assembly and movement of the infectious virions. Specifically, two major objectives were proposed: I. To study in detail the molecular interactions between CP molecules and between CP and ssDNA leading to assembly of infectious TYLCV virions. II. To study the roles of host cell factors in TYLCV assembly. Our research toward these goals has produced the following major achievements: • Characterization of the CP nuclear shuttling interactor, karyopherin alpha 1, its pattern of expression and the putative involvement of auxin in regulation of its expression. (#1 in our list of publication, Mizrachy, Dabush et al. 2004). • Identify a single amino acid in the capsid protein’s sequence that is critical for normal virus life-cycle. (#2 in our list of publications, Yaakov, Levy et al. in preparation). • Development of monoclonal antibodies with high specificity to the capsid protein of TYLCV. (#3 in our list of publications, Solmensky, Zrachya et al. in press). • Generation of Tomato plants resistant to TYLCV by expressing transgene coding for siRNA targeted at the TYLCV CP. (#4 in our list of publications, Zrachya, Kumar et al. in press). •These research findings provided significant insights into (i) the molecular interactions of TYLCV capsid protein with the host cell nuclear shuttling receptor, and (ii) the mechanism by which TYLCV V2 is involved in the silencing of PTGS and contributes to the virus pathogenicity effect. Furthermore, the obtained knowledge helped us to develop specific strategies to attenuate TYLCV infection, for example, by blocking viral entry into and/or exit out of the host cell nucleus via siRNA as we showed in our publication recently (# 4 in our list of publications). Finally, in addition to the study of TYLCV nuclear import and export, our research contributed to our understanding of general mechanisms for nucleocytoplasmic shuttling of proteins and nucleic acids in plant cells. Also integration for stable transformation of ssDNA mediated by our model pathogen Agrobacterium tumefaciens led to identification of plant specific proteins involved.
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Greene, Geoffrey. Multidomain Assembly of Nuclear Estrogen Receptors: Structural Insights into ER-Positive Breast Cancer Therapeutics. Fort Belvoir, VA: Defense Technical Information Center, April 2012. http://dx.doi.org/10.21236/ada562255.

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Greene, Geoffrey. Multi-Domain Assembly of Nuclear Estrogen Receptors: Structural Insights into ER-Positive Breast Cancer Therapeutics. Fort Belvoir, VA: Defense Technical Information Center, April 2013. http://dx.doi.org/10.21236/ada580416.

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Tzfira, Tzvi, Michael Elbaum, and Sharon Wolf. DNA transfer by Agrobacterium: a cooperative interaction of ssDNA, virulence proteins, and plant host factors. United States Department of Agriculture, December 2005. http://dx.doi.org/10.32747/2005.7695881.bard.

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Agrobacteriumtumefaciensmediates genetic transformation of plants. The possibility of exchanging the natural genes for other DNA has led to Agrobacterium’s emergence as the primary vector for genetic modification of plants. The similarity among eukaryotic mechanisms of nuclear import also suggests use of its active elements as media for non-viral genetic therapy in animals. These considerations motivate the present study of the process that carries DNA of bacterial origin into the host nucleus. The infective pathway of Agrobacterium involves excision of a single-stranded DNA molecule (T-strand) from the bacterial tumor-inducing plasmid. This transferred DNA (T-DNA) travels to the host cell cytoplasm along with two virulence proteins, VirD2 and VirE2, through a specific bacteriumplant channel(s). Little is known about the precise structure and composition of the resulting complex within the host cell and even less is known about the mechanism of its nuclear import and integration into the host cell genome. In the present proposal we combined the expertise of the US and Israeli labs and revealed many of the biophysical and biological properties of the genetic transformation process, thus enhancing our understanding of the processes leading to nuclear import and integration of the Agrobacterium T-DNA. Specifically, we sought to: I. Elucidate the interaction of the T-strand with its chaperones. II. Analyzing the three-dimensional structure of the T-complex and its chaperones in vitro. III. Analyze kinetics of T-complex formation and T-complex nuclear import. During the past three years we accomplished our goals and made the following major discoveries: (1) Resolved the VirE2-ssDNA three-dimensional structure. (2) Characterized VirE2-ssDNA assembly and aggregation, along with regulation by VirE1. (3) Studied VirE2-ssDNA nuclear import by electron tomography. (4) Showed that T-DNA integrates via double-stranded (ds) intermediates. (5) Identified that Arabidopsis Ku80 interacts with dsT-DNA intermediates and is essential for T-DNA integration. (6) Found a role of targeted proteolysis in T-DNA uncoating. Our research provide significant physical, molecular, and structural insights into the Tcomplex structure and composition, the effect of host receptors on its nuclear import, the mechanism of T-DNA nuclear import, proteolysis and integration in host cells. Understanding the mechanical and molecular basis for T-DNA nuclear import and integration is an essential key for the development of new strategies for genetic transformation of recalcitrant plant species. Thus, the knowledge gained in this study can potentially be applied to enhance the transformation process by interfering with key steps of the transformation process (i.e. nuclear import, proteolysis and integration). Finally, in addition to the study of Agrobacterium-host interaction, our research also revealed some fundamental insights into basic cellular mechanisms of nuclear import, targeted proteolysis, protein-DNA interactions and DNA repair.
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