Relevant bibliographies by topics / Signalosomes

Contents

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

Academic literature on the topic 'Signalosomes'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Signalosomes"

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Kim, Ingyu, Weijun Pan, Sara A. Jones, Youxin Zhang, Xiaowei Zhuang, and Dianqing Wu. "Clathrin and AP2 are required for PtdIns(4,5)P2-mediated formation of LRP6 signalosomes." Journal of Cell Biology 200, no. 4 (2013): 419–28. http://dx.doi.org/10.1083/jcb.201206096.

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Canonical Wnt signaling is initiated by the binding of Wnt proteins to their receptors, low-density lipoprotein-related protein 5 and 6 (LRP5/6) and frizzled proteins, leading to phosphatidylinositol (4,5)bisphosphate (PtdIns(4,5)P2) production, signalosome formation, and LRP phosphorylation. However, the mechanism by which PtdIns(4,5)P2 regulates the signalosome formation remains unclear. Here we show that clathrin and adaptor protein 2 (AP2) were part of the LRP6 signalosomes. The presence of clathrin and AP2 in the LRP6 signalosomes depended on PtdIns(4,5)P2, and both clathrin and AP2 were
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Quinlan, Casey L., Alexandre D. T. Costa, Cinthia L. Costa, Sandrine V. Pierre, Pierre Dos Santos, and Keith D. Garlid. "Conditioning the heart induces formation of signalosomes that interact with mitochondria to open mitoKATPchannels." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 3 (2008): H953—H961. http://dx.doi.org/10.1152/ajpheart.00520.2008.

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Perfusion of the heart with bradykinin triggers cellular signaling events that ultimately cause opening of mitochondrial ATP-sensitive K+(mitoKATP) channels, increased H2O2production, inhibition of the mitochondrial permeability transition (MPT), and cardioprotection. We hypothesized that the interaction of bradykinin with its receptor induces the assembly of a caveolar signaling platform (signalosome) that contains the enzymes of the signaling pathway and that migrates to mitochondria to induce mitoKATPchannel opening. We developed a novel method for isolating and purifying signalosomes from
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Gerlach, Jan P., Ingrid Jordens, Daniele V. F. Tauriello, et al. "TMEM59 potentiates Wnt signaling by promoting signalosome formation." Proceedings of the National Academy of Sciences 115, no. 17 (2018): E3996—E4005. http://dx.doi.org/10.1073/pnas.1721321115.

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Wnt/β-catenin signaling controls development and adult tissue homeostasis by regulating cell proliferation and cell fate decisions. Wnt binding to its receptors Frizzled (FZD) and low-density lipoprotein-related 6 (LRP6) at the cell surface initiates a signaling cascade that leads to the transcription of Wnt target genes. Upon Wnt binding, the receptors assemble into large complexes called signalosomes that provide a platform for interactions with downstream effector proteins. The molecular basis of signalosome formation and regulation remains elusive, largely due to the lack of tools to analy
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Piperno, Anna, Angela Scala, Antonino Mazzaglia, et al. "Cellular Signaling Pathways Activated by Functional Graphene Nanomaterials." International Journal of Molecular Sciences 19, no. 11 (2018): 3365. http://dx.doi.org/10.3390/ijms19113365.

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The paper reviews the network of cellular signaling pathways activated by Functional Graphene Nanomaterials (FGN) designed as a platform for multi-targeted therapy or scaffold in tissue engineering. Cells communicate with each other through a molecular device called signalosome. It is a transient co-cluster of signal transducers and transmembrane receptors activated following the binding of transmembrane receptors to extracellular signals. Signalosomes are thus efficient and sensitive signal-responding devices that amplify incoming signals and convert them into robust responses that can be rel
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Tulsian, Nikhil K., Valerie Jia-En Sin, Hwee-Ling Koh, and Ganesh S. Anand. "Development of Phosphodiesterase–Protein-Kinase Complexes as Novel Targets for Discovery of Inhibitors with Enhanced Specificity." International Journal of Molecular Sciences 22, no. 10 (2021): 5242. http://dx.doi.org/10.3390/ijms22105242.

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Phosphodiesterases (PDEs) hydrolyze cyclic nucleotides to modulate multiple signaling events in cells. PDEs are recognized to actively associate with cyclic nucleotide receptors (protein kinases, PKs) in larger macromolecular assemblies referred to as signalosomes. Complexation of PDEs with PKs generates an expanded active site that enhances PDE activity. This facilitates signalosome-associated PDEs to preferentially catalyze active hydrolysis of cyclic nucleotides bound to PKs and aid in signal termination. PDEs are important drug targets, and current strategies for inhibitor discovery are ba
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Song, Wenxia, Chaohong Liu, Heather Miller, et al. "BCR-induced actin rearrangement provides a driving force for the formation of surface BCR signalosomes (84.1)." Journal of Immunology 184, no. 1_Supplement (2010): 84.1. http://dx.doi.org/10.4049/jimmunol.184.supp.84.1.

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Abstract In response to antigens, the BCR forms surface signalosomes where it initiates signaling cascades and antigen internalization. This study examines the role of the actin cytoskeleton in BCR signalosome formation. Both multi-valent soluble and membrane-associated antigens induce BCR clustering and actin reorganization. Actin is actively polymerized at BCR microclusters upon their formation and surrounding BCR clusters as they are merged into central clusters. Actin regulators, WASP, cofilin and gelsolin, are activated and recruited to BCR clusters. Latrunculin or jasplakinolide treatmen
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Negro, Alejandra, Kimberly Dodge-Kafka, and Michael S. Kapiloff. "Signalosomes as therapeutic targets." Progress in Pediatric Cardiology 25, no. 1 (2008): 51–56. http://dx.doi.org/10.1016/j.ppedcard.2007.11.012.

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Nhieu, Jennifer, Fatimah Najjar, and Li-Na Wei. "CRABP1 Signalosomes in Non-Canonical Actions of Retinoic Acid—Maintaining Health and Preventing Thyroid Dysfunction in Aging." Endocrines 6, no. 2 (2025): 26. https://doi.org/10.3390/endocrines6020026.

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Retinoic acid (RA) exerts biological effects through RA receptors (RARs) to regulate transcription. RA also elicits rapid, RAR-independent (noncanonical) activities mediated by Cellular RA Binding Protein 1 (CRABP1) to modulate cytosolic signaling. CRABP1 functions by forming protein complexes, named CRABP1 signalosomes, to modulate signal propagation in a cell type-specific manner. This review summarizes multiple CRABP1 signalosomes and their physiological functions. CRABP1 knockout (CKO) mice develop multiple phenotypes progressively throughout the lifespan. These include altered brain funct
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Tulsian, Nikhil K., Abhijeet Ghode, and Ganesh S. Anand. "Adenylate control in cAMP signaling: implications for adaptation in signalosomes." Biochemical Journal 477, no. 16 (2020): 2981–98. http://dx.doi.org/10.1042/bcj20200435.

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In cAMP-Protein Kinase A (PKA) signaling, A-kinase anchoring protein scaffolds assemble PKA in close proximity to phosphodiesterases (PDE), kinase-substrates to form signaling islands or ‘signalosomes’. In its basal state, inactive PKA holoenzyme (R2:C2) is activated by binding of cAMP to regulatory (R)-subunits leading to dissociation of active catalytic (C)-subunits. PDEs hydrolyze cAMP-bound to the R-subunits to generate 5′-AMP for termination and resetting the cAMP signaling. Mechanistic basis for cAMP signaling has been derived primarily by focusing on the proteins in isolation. Here, we
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Abdel-Nour, Mena, Leticia A. M. Carneiro, Jeffrey Downey, et al. "The heme-regulated inhibitor is a cytosolic sensor of protein misfolding that controls innate immune signaling." Science 365, no. 6448 (2019): eaaw4144. http://dx.doi.org/10.1126/science.aaw4144.

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Multiple cytosolic innate sensors form large signalosomes after activation, but this assembly needs to be tightly regulated to avoid accumulation of misfolded aggregates. We found that the eIF2α kinase heme-regulated inhibitor (HRI) controls NOD1 signalosome folding and activation through a process requiring eukaryotic initiation factor 2α (eIF2α), the transcription factor ATF4, and the heat shock protein HSPB8. The HRI/eIF2α signaling axis was also essential for signaling downstream of the innate immune mediators NOD2, MAVS, and TRIF but dispensable for pathways dependent on MyD88 or STING. M
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Dissertations / Theses on the topic "Signalosomes"

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Abdessamad, Mahmoud. "Caractérisation moléculaire et fonctionnelle des signalosomes PTEN/MAGI-1b/TRIP6 et PTEN/PTPN13." Paris 7, 2012. http://www.theses.fr/2012PA077048.

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Le suppresseur de tumeurs PTEN est une phosphatase capable de déphosphoryler certains résidus tyrosine, mais également les phosphoinositides produits de la PI3K. Dans son extrémité C- terminale, PTEN comporte un motif d'interaction avec les domaines PDZ. Notre équipe a établi le rôle majeur de l'activité lipide-phosphatase dans la stabilisation des contacts cellulaires et le contrôle de l'invasion. PTEN est recruté vers les jonctions cellulaires E-cadhérine β-caténine, via la molécule à domaines PDZ MAGI-1. Afin d'identifier de nouveaux partenaires de PTEN, nous avons engagé une approche par l
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Enchev, Radoslav Ivanov. "Structural Studies of the C0P9 Signalosome." Thesis, Institute of Cancer Research (University Of London), 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.521848.

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Birol, Melissa. "Le COP9 signalosome : activité et régulation." Thesis, Montpellier 2, 2014. http://www.theses.fr/2014MON20072/document.

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Le COP9 (Constitutive photomorphogenesis 9) signalosome (CSN) est un complexe multiprotéique contenant huit sous-unités (320 kDa), impliqué dans des processus cellulaires divers allant de la progression du cycle cellulaire, à l'expression des gènes et la réparation de l'ADN, à travers sa fonction au sein du système ubiquitine-protéasome. Il s'agit d'un complexe fortement conservé au cours de l'évolution chez les eucaryotes supérieurs chez qui son activité catalytique est essentielle. Au cours des années d'études biologiques et biochimiques qui ont permis d'élucider le rôle du CSN, sa fonction
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Peth, Andreas. "Funktionelle Charakterisierung der Interaktion des COP9-Signalosoms mit dem Mikrotubuli-bindenden Protein EB1." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2007. http://dx.doi.org/10.18452/15686.

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Das COP9-Signalosom (CSN) ist ein evolutionär konservierter Proteinkomplex. Er besteht aus acht Untereinheiten und wird als Paralog des Lid-Subkomplexes des 26S Proteasoms angesehen. Das CSN verfügt über diverse enzymatische Aktivitäten, die es zu einem regulatorischen Faktor des Ubiquitin-Proteasom-Systems (UPS) machen. Das UPS ist für den Abbau von einem Großteil der zellulären Proteine notwendig. Für die Proteolyse bestimmter Proteine werden diese mit einer Polyubiquitinkette markiert. Dies geschieht über eine Enzymkaskade von E1, E2s und E3-Ligasen, wobei die E3s die Substratspezifität bes
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Leppert, Ulrike. "Die Biogenese des COP9 Signalosoms wird durch microRNAs der let-7-Familie reguliert." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2010. http://dx.doi.org/10.18452/16224.

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Das COP9 Signalosom ist ein hochkonservierter Proteinkomplex bestehend, aus acht Untereinheiten. In der vorgelegten Promotionsarbeit konnte ein bislang unbekannter Regulationsmechanismus der Biogenese des COP9 Signalosoms identifiziert werden. Die siRNA-vermittelte Reduktion der CSN1-Expression führte zu einer Reduktion der Expression aller CSN-Untereinheiten. Die Transfektion von His-CSN1 in siCSN1-Zellen induzierte die CSN-Neusynthese und ferner einen Anstieg der c-Myc- und STAT1 Expression. Durch die Stimulation der Zellen mit IFN alpha bzw. IFN gamma konnte die de novo Synthese des CSN-Kom
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Dohmann, Esther Mirjam Natascha. "The role of the Arabidopsis COP9 signalosome in plant development /." Tübingen, 2009. http://opac.nebis.ch/cgi-bin/showAbstract.pl?sys=000276828.

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Busch, Silke. "Amino Acid Biosynthesis and the COP9 Signalosome in Aspergillus nidulans." Doctoral thesis, [S.l.] : [s.n.], 2002. http://hdl.handle.net/11858/00-1735-0000-0006-AE62-6.

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Khatamzas, Elham. "Definition of the early HIV-1 signalosome in dendritic cells." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:e504a1b9-f8c0-455e-a61b-27c29b5adcdf.

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DCs are critical to the early events of HIV-1 infection. They are the first cells that HIV-1 encounters at mucosal surfaces and as sentinel antigen-presenting cells of the immune system these should alarm the immune system and activate innate immune defences to recruit effective adaptive immunity and viral clearance. A peculiar characteristic of HIV – in contrast to other ssRNA viruses – is its ability to completely evade host innate recognition pathways. Additionally, it has the unique ability to manipulate the endo-lysosomal system of DCs and promote transmission via trans-infection to CD4+
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Leblond-Castaing, Julie. "Caractérisation de l’interaction des protéines IMA/MIF2 et CSN5 au niveau moléculaire et physiologique." Thesis, Bordeaux 1, 2011. http://www.theses.fr/2011BOR14466/document.

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Les plantes ont la capacité à former de nouveaux organes grâce à une croissance continue assurée par une réserve de cellules souches au sein de structures spécifiques, les méristèmes. Les méristèmes floraux diffèrent des méristèmes végétatifs par leur caractère déterminé aboutissant à la production des fleurs. Le gène IMA (INHIBITOR OF MERISTEM ACTIVITY) code une protéine contenant un motif «doigt à zinc» (MIF) régulant les processus développementaux de la fleur et des ovules chez la tomate. En effet, IMA inhibe la prolifération cellulaire au cours de la terminaison florale en agissant sur l’e
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Hetfeld, Bettina Kathrin Johanna. "Die Funktionen des COP9-Signalosoms und des assoziierten USP15 im Ubiquitin-Proteasomsystem." Doctoral thesis, [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=980671868.

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Books on the topic "Signalosomes"

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Redox Proteins in Supercomplexes and Signalosomes. Taylor & Francis Group, 2015.

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Louro, Ricardo O., and Irene Diaz-Moreno. Redox Proteins in Supercomplexes and Signalosomes. Taylor & Francis Group, 2016.

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Louro, Ricardo O. Redox Proteins in Supercomplexes and Signalosomes. Taylor & Francis Group, 2023.

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Louro, Ricardo O., and Irene Diaz-Moreno. Redox Proteins in Supercomplexes and Signalosomes. Taylor & Francis Group, 2016.

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Ma, Yi, Kai He, and Gerald A. Berkowitz, eds. From Structure to Signalosomes: New Perspectives About Membrane Receptors and Channels. Frontiers Media SA, 2019. http://dx.doi.org/10.3389/978-2-88945-973-5.

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Book chapters on the topic "Signalosomes"

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Malissen, Bernard, Ying Wang, Michael Mingueneau, and Marie Malissen. "Th2 Lymphoproliferative Disorders Resulting from Defective LAT Signalosomes." In Decoding the Genomic Control of Immune Reactions. John Wiley & Sons, Ltd, 2007. http://dx.doi.org/10.1002/9780470062128.ch9.

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Franciosini, Anna, Giovanna Serino, and Xing-Wang Deng. "Signaling: COP9 Signalosome." In Molecular Biology. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0263-7_13-5.

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Franciosini, Anna, Giovanna Serino, and Xing-Wang Deng. "COP9 Signalosome Network." In Molecular Biology. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-7570-5_13.

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Schmaler, Tilo, and Wolfgang Dubiel. "Control of Deneddylation by the COP9 Signalosome." In Subcellular Biochemistry. Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6676-6_5.

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Hammond, J., and J. L. Balligand. "Signalling Microdomains: The Beta-3 Adrenergic Receptor/NOS Signalosome." In Microdomains in the Cardiovascular System. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-54579-0_11.

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Bech-Otschir, Dawadschargal, Barbara Kapelari, and Wolfgang Dubiel. "The COP9 Signalosome: Its Possible Role in the Ubiquitin System." In Protein Degradation. Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/352760586x.ch13.

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Altosaar, Katrin, Darlaine Pétrin, Dominic Devost, and Terence E. Hébert. "Signalosome Profiling Reveals Allosteric Interactions Between G Protein-Coupled Receptors." In Methods in Pharmacology and Toxicology. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-779-2_7.

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Langelotz, C., B. Hetfeld, W. Schwenk, and W. Dubiel. "Beta-Catenin bildet einen Abbaukomplex mit dem COP9 Signalosom (CSN)." In Chirurgisches Forum 2006. Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-34668-6_45.

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Rao, Feng, Hong Lin, and Yang Su. "Cullin-RING Ligase Regulation by the COP9 Signalosome: Structural Mechanisms and New Physiologic Players." In Advances in Experimental Medicine and Biology. Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1025-0_4.

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Rubio, Vicente, and Xing Wang Deng. "The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles in the Regulation of Plant Development." In Protein Degradation. Wiley-VCH Verlag GmbH & Co. KGaA, 2007. http://dx.doi.org/10.1002/9783527620227.ch3.

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Conference papers on the topic "Signalosomes"

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Valasarajan, C., J. C. P. Laria, N. C. P. Laria, et al. "Targeting ADORA1/PDE10A Signalosome Regulated cAMP Microenvironment as a Novel Therapeutic Approach for Treating Pulmonary Hypertension." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a4392.

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Stinson, Jeffrey Richard, and Andrew L. Snow. "Abstract A56: Spontaneous aggregation and novel signalosome organization of BENTA-associated gain-of-function CARD11 mutants in lymphocytes." In Abstracts: Third AACR International Conference on Frontiers in Basic Cancer Research - September 18-22, 2013; National Harbor, MD. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.fbcr13-a56.

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Ekambaram, Prasanna, Nathaniel Hubel, Jia-Ying Lee та ін. "Abstract 5109: The CARMA3-Bcl10-MALT1 signalosome mediates NF-κB activation and cellular invasion in AGTR1-positive breast cancer". У Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-5109.

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Kang, H., P. Ekambaram, LM McAllister-Lucas, and PC Lucas. "Abstract P6-07-02: The CARMA3-Bcl10-MALT1 signalosome mediates pro-angiogenic IL-6 and IL-8 paracrine signaling in GPCR+ breast cancer." In Abstracts: 2018 San Antonio Breast Cancer Symposium; December 4-8, 2018; San Antonio, Texas. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-p6-07-02.

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Reports on the topic "Signalosomes"

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Chamovitz, Daniel, and Xing-Wang Deng. Morphogenesis and Light Signal Transduction in Plants: The p27 Subunit of the COP9-Complex. United States Department of Agriculture, 1997. http://dx.doi.org/10.32747/1997.7580666.bard.

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Plants monitor environmental signals and modulate their growth and development in a manner optimal for the prevailing light conditions. The mechanisms by which plants transduce light signals and integrate them with other environmental and developmental signals to regulate plant pattern development are beginning to be unraveled. A large body of knowledge has accumulated regarding the roles of specific photoreceptors in perceiving light signals, and about the downstream developmental responses responding to light (Batschauer, 1999; Chamovitz and Deng, 1996; Deng and Quail, 1999). Still, little i
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Chamovitz, Daniel, and Albrecht Von Arnim. Translational regulation and light signal transduction in plants: the link between eIF3 and the COP9 signalosome. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7696515.bard.

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The COP9 signalosome (CSN) is an eight-subunit protein complex that is highly conserved among eukaryotes. Genetic analysis of the signalosome in the plant model species Arabidopsis thaliana has shown that the signalosome is a repressor of light dependent seedling development as mutant Arabidopsis seedlings that lack this complex develop in complete darkness as if exposed to light. These mutant plants die following the seedling stage, even when exposed to light, indicating that the COP9 signalosome also has a central role in the regulation of normal photomorphogenic development. The biochemical
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Chamovitz, Daniel A., and Zhenbiao Yang. Chemical Genetics of the COP9 Signalosome: Identification of Novel Regulators of Plant Development. United States Department of Agriculture, 2011. http://dx.doi.org/10.32747/2011.7699844.bard.

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This was an exploratory one-year study to identify chemical regulators of the COP9 signalosome. Chemical Genetics uses small molecules to modify or disrupt the function of specific genes/proteins. This is in contrast to classical genetics, in which mutations disrupt the function of genes. The underlying concept is that the functions of most proteins can be altered by the binding of a chemical, which can be found by screening large libraries for compounds that specifically affect a biological, molecular or biochemical process. In addition to screens for chemicals which inhibit specific biologic
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Chamovitz, Daniel A., and Xing-Wang Deng. Developmental Regulation and Light Signal Transduction in Plants: The Fus5 Subunit of the Cop9 Signalosome. United States Department of Agriculture, 2003. http://dx.doi.org/10.32747/2003.7586531.bard.

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Plants adjust their growth and development in a manner optimal for the prevailing light conditions. The molecular mechanisms by which light signals are transduced and integrated with other environmental and developmental signals are an area of intense research. (Batschauer, 1999; Quail, 2002) One paradigm emerging from this work is the interconnectedness of discrete physiological responses at the biochemical level, for instance, between auxin and light signaling (Colon-Carmona et al., 2000; Schwechheimer and Deng, 2001; Tian and Reed, 1999) and between light signaling and plant pathogen intera
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Chamovitz, Daniel A., and Albrecht G. Von Arnim. eIF3 Complexes and the eIF3e Subunit in Arabidopsis Development and Translation Initiation. United States Department of Agriculture, 2009. http://dx.doi.org/10.32747/2009.7696545.bard.

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The original working hypothesis of our proposal was that The “e” subunit of eIF3 has multiple functions from both within the nucleus and in the cytoplasm. Within this model, we further hypothesized that the “e” subunit of eIF3 functions in translation as a repressor. We proposed to test these hypotheses along the following specific aims: 1) Determine the subcellular localization of the interaction between eIF3e and other eIF3 subunits, or the COP9 signalosome. 2) Elucidate the biological significance of the varied subcellular localizations of eIF3e through generating Arabidopsis eIF3e alleles
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