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Academic literature on the topic 'Lunapark'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic "Lunapark"

1

de Almeida-Faria, Juliana, Daniella E. Duque-Guimarães, Thomas P. Ong, Lucas C. Pantaleão, Asha A. Carpenter, Elena Loche, Laura C. Kusinski, et al. "Maternal obesity during pregnancy leads to adipose tissue ER stress in mice via miR-126-mediated reduction in Lunapark." Diabetologia 64, no. 4 (January 27, 2021): 890–902. http://dx.doi.org/10.1007/s00125-020-05357-4.

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Abstract Aims/hypothesis Levels of the microRNA (miRNA) miR-126-3p are programmed cell-autonomously in visceral adipose tissue of adult offspring born to obese female C57BL/6J mice. The spectrum of miR-126-3p targets and thus the consequences of its dysregulation for adipocyte metabolism are unknown. Therefore, the aim of the current study was to identify novel targets of miR-126-3p in vitro and then establish the outcomes of their dysregulation on adipocyte metabolism in vivo using a well-established maternal obesity mouse model. Methods miR-126-3p overexpression in 3T3-L1 pre-adipocytes followed by pulsed stable isotope labelling by amino acids in culture (pSILAC) was performed to identify novel targets of the miRNA. Well-established bioinformatics algorithms and luciferase assays were then employed to confirm those that were direct targets of miR-126-3p. Selected knockdown experiments were performed in vitro to define the consequences of target dysregulation. Quantitative real-time PCR, immunoblotting, histology, euglycaemic–hyperinsulinaemic clamps and glucose tolerance tests were performed to determine the phenotypic and functional outcomes of maternal programmed miR-126-3p levels in offspring adipose tissue. Results The proteomic approach confirmed the identity of known targets of miR-126-3p (including IRS-1) and identified Lunapark, an endoplasmic reticulum (ER) protein, as a novel one. We confirmed by luciferase assay that Lunapark was a direct target of miR-126-3p. Overexpression of miR-126-3p in vitro led to a reduction in Lunapark protein levels and increased Perk (also known as Eif2ak3) mRNA levels and small interference-RNA mediated knockdown of Lunapark led to increased Xbp1, spliced Xbp1, Chop (also known as Ddit3) and Perk mRNA levels and an ER stress transcriptional response in 3T3-L1 pre-adipocytes. Consistent with the results found in vitro, increased miR-126-3p expression in adipose tissue from adult mouse offspring born to obese dams was accompanied by decreased Lunapark and IRS-1 protein levels and increased markers of ER stress. At the whole-body level the animals displayed glucose intolerance. Conclusions/interpretation Concurrently targeting IRS-1 and Lunapark, a nutritionally programmed increase in miR-126-3p causes adipose tissue insulin resistance and an ER stress response, both of which may contribute to impaired glucose tolerance. These findings provide a novel mechanism by which obesity during pregnancy leads to increased risk of type 2 diabetes in the offspring and therefore identify miR-126-3p as a potential therapeutic target. Graphical abstract
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2

Ram, Paul. "Het ‘lunapark’ van Marck Eyck." Huisarts en Wetenschap 51, no. 1 (January 2008): 57–58. http://dx.doi.org/10.1007/bf03086642.

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Tran, Pham-Tue-Hung, Naveed Asghar, Magnus Johansson, and Wessam Melik. "Roles of the Endogenous Lunapark Protein during Flavivirus Replication." Viruses 13, no. 7 (June 22, 2021): 1198. http://dx.doi.org/10.3390/v13071198.

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The endoplasmic reticulum (ER) of eukaryotic cells is a dynamic organelle, which undergoes continuous remodeling. At the three-way tubular junctions of the ER, the lunapark (LNP) protein acts as a membrane remodeling factor to stabilize these highly curved membrane junctions. In addition, during flavivirus infection, the ER membrane is invaginated to form vesicles (Ve) for virus replication. Thus, LNP may have roles in the generation or maintenance of the Ve during flavivirus infection. In this study, our aim was to characterize the functions of LNP during flavivirus infection and investigate the underlying mechanisms of these functions. To specifically study virus replication, we generated cell lines expressing replicons of West Nile virus (Kunjin strain) or Langat virus. By using these replicon platforms and electron microscopy, we showed that depletion of LNP resulted in reduced virus replication, which is due to its role in the generation of the Ve. By using biochemical assays and high-resolution microscopy, we found that LNP is recruited to the Ve and the protein interacts with the nonstructural protein (NS) 4B. Therefore, these data shed new light on the interactions between flavivirus and host factors during viral replication.
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Kriechbaumer, Verena, Emily Breeze, Charlotte Pain, Frances Tolmie, Lorenzo Frigerio, and Chris Hawes. "Arabidopsis Lunapark proteins are involved in ER cisternae formation." New Phytologist 219, no. 3 (May 25, 2018): 990–1004. http://dx.doi.org/10.1111/nph.15228.

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Van Velthoven, Harry. "Signalement van: Het lunapark en andere plekken / Ludo Abicht (2008)." WT. Tijdschrift over de geschiedenis van de Vlaamse beweging 68, no. 1 (January 1, 2009): 105. http://dx.doi.org/10.21825/wt.v68i1.12417.

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Chen, Shuliang, Tanvi Desai, James A. McNew, Patrick Gerard, Peter J. Novick, and Susan Ferro-Novick. "Lunapark stabilizes nascent three-way junctions in the endoplasmic reticulum." Proceedings of the National Academy of Sciences 112, no. 2 (December 29, 2014): 418–23. http://dx.doi.org/10.1073/pnas.1423026112.

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The endoplasmic reticulum (ER) consists of a polygonal network of sheets and tubules interconnected by three-way junctions. This network undergoes continual remodeling through competing processes: the branching and fusion of tubules forms new three-way junctions and new polygons, and junction sliding and ring closure leads to polygon loss. However, little is known about the machinery required to generate and maintain junctions. We previously reported that yeast Lnp1 localizes to ER junctions, and that loss of Lnp1 leads to a collapsed, densely reticulated ER network. In mammalian cells, only approximately half the junctions contain Lnp1. Here we use live cell imaging to show that mammalian Lnp1 (mLnp1) affects ER junction mobility and hence network dynamics. Three-way junctions with mLnp1 are less mobile than junctions without mLnp1. Newly formed junctions that acquire mLnp1 remain stable within the ER network, whereas nascent junctions that fail to acquire mLnp1 undergo rapid ring closure. These findings imply that mLnp1 plays a key role in stabilizing nascent three-way ER junctions.
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Dobryden, Paul. "The institution of pleasure: From display to environment at the Berlin Lunapark." Studies in European Cinema 10, no. 2 (September 1, 2013): 157–78. http://dx.doi.org/10.1386/seci.10.2-3.157_1.

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8

Zhou, Xin, Yu He, Xiaofang Huang, Yuting Guo, Dong Li, and Junjie Hu. "Reciprocal regulation between lunapark and atlastin facilitates ER three-way junction formation." Protein & Cell 10, no. 7 (November 29, 2018): 510–25. http://dx.doi.org/10.1007/s13238-018-0595-7.

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Wang, Songyu, Robert E. Powers, Vicki AM Gold, and Tom A. Rapoport. "The ER morphology-regulating lunapark protein induces the formation of stacked bilayer discs." Life Science Alliance 1, no. 1 (January 2018): e201700014. http://dx.doi.org/10.26508/lsa.201700014.

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Lunapark (Lnp) is a conserved membrane protein that localizes to and stabilizes three-way junctions of the tubular ER network. In higher eukaryotes, phosphorylation of Lnp may contribute to the conversion of the ER from tubules to sheets during mitosis. Here, we report on the reconstitution of purified Lnp with phospholipids. Surprisingly, Lnp induces the formation of stacked membrane discs. Each disc is a bicelle, with Lnp sitting in the bilayer facing both directions. The interaction between bicelles is mediated by the cytosolic domains of Lnp, resulting in a constant distance between the discs. A phosphomimetic Lnp mutant shows reduced bicelle stacking. Based on these results, we propose that Lnp tethers ER membranes in vivo in a cell cycle–dependent manner. Lnp appears to be the first membrane protein that induces the formation of stacked bicelles.
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10

Yuniati, Laurensia, Angela Lauriola, Manouk Gerritsen, Susana Abreu, Eric Ni, Chiara Tesoriero, Jacob O. Onireti, et al. "Ubiquitylation of the ER-Shaping Protein Lunapark via the CRL3KLHL12 Ubiquitin Ligase Complex." Cell Reports 31, no. 7 (May 2020): 107664. http://dx.doi.org/10.1016/j.celrep.2020.107664.

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Dissertations / Theses on the topic "Lunapark"

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Tribulato, Chiara. "Qui in mezzo a noi. I sinti nello spettacolo viaggiante." Doctoral thesis, Università degli studi di Padova, 2019. http://hdl.handle.net/11577/3421864.

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Over the last century, both Italian sinti and other non-sinti travelling entertainers, have occuped the same economical niche and have shared the same itinerant way of life which was structured around seasonal markets and traditional fairs, up to the modern funfairs and circus. Nowadays, funfairs are composite systems characterized by frequent inter-ethnic relations paired with a strong differentiation from the outside world, the gagi’s world. The dichotomy between travelling and settled people strengthens the identity perception of people living in the sphere of funfairs. The marginal condition and the different lifestyle create the illusion of a uniform reality; on the contrary, funfairs are much more complex and multifaceted worlds than one could imagine. Despite sharing the same economic and living space, various and rather dynamic feelings of affiliation are likely to be detected, since they evolve in a daily process of membership self-construction. By employing the ethnografic method, the current study fulfills the purpose to examine how sinti entertainers construct their shared identity starting from some tacit but widely shared reference values.
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Senghaas, Niklas Julius [Verfasser]. "Regulation, biochemistry and functional analysis of the conserved Lunapark protein in central nervous system development / Niklas Julius Senghaas." 2011. http://d-nb.info/1011457067/34.

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Olaleye, Onireti Jacob. "Novel Roles of Cullin-RING Ligases in Cell Signalling and Implications in Health and Disease." Doctoral thesis, 2022. http://hdl.handle.net/11562/1070147.

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Cullin-RING ligases (CRLs) play fundamental functions in key physiological and pathological processes. To identify novel roles of CRLs in cell signalling and their implication in health and diseases, we performed two separate studies: In study 1, we analysed genomic databases to identify CRLs that are hypermutated in cancer. We found that the CRL substrate receptors FBXO24 and DCAF12L2 are hypermutated at critical domains that are necessary for the proper structure/function of the CRL1FBXO24 and CRL4DCAF12L2 complexes, respectively. We showed that the FBXO24(T65P) mutation within the F-box domain as found in cancer disrupts the CRL1FBXO24 complex by blocking the binding of FBXO24 to SKP1. Similarly, we found that DCAF12L2 is hypermutated in cancer at the amino acids sequence positions 334, 335, and 337 within the WD40 repeats that mediate substrate binding. Our affinity purification coupled with mass spectrometry analysis identified MEKK4 and the WDR11 complex as two independent substrates of CRL4DCAF12L2. Moreover, the DCAF12L2(P334L), (R335C), and (R335H) mutations block DCAF12L2 binding to MEKK4 and the WDR11 complex. We also showed that FAM91A1, a component of the WDR11 complex, is ubiquitylated by CRL4DCAF12L2 and proposed that the ubiquitylation of FAM91A1 might be critical in regulating the stability and function of the WDR11 complex. In study 2, we employed a proteomic approach to identify CRL3 complexes activated at the cellular membrane. Our mass spectrometry analysis identified CRL3KLHL12 as a ubiquitin ligase that mediates the ubiquitylation of Lunapark, an endoplasmic reticulum (ER) shaping protein. We show that Lunapark interacts with mechanistic target of rapamycin complex1 (mTORC1) and that the ubiquitylation of Lunapark regulates mTORC1 activation. In addition, we show that the inhibition of Lunapark ubiquitylation leads to neurodevelopmental defects.
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Books on the topic "Lunapark"

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Navarre, Yves. Lunapark. Warszawa: Czytelnik, 1988.

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Zajec, Tomislav. Lunapark. Zagreb: EPH, 2009.

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Gawłowski, Wojciech. Lunapark nieśmiertelności. Sopot: Towarzystwo Przyjaciół Sopotu, 2011.

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Gawłowski, Wojciech. Lunapark nieśmiertelności. Sopot: Towarzystwo Przyjaciół Sopotu, 2011.

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Lunapark kapandı. 3rd ed. Güneşli, İistanbul: Doğan Kitap, 2005.

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6

Grosz, George. Ach knallige Welt, du Lunapark: Gesammelte Gedichte. Munich: Carl Hanser Verlag, 1986.

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Alexander und Renata Camaro Stiftung and Camaro Haus (Berlin Germany), eds. Alexander Camaro: Lunapark : Schaubühne, Budenzauber und Vergnügungswelt. Berlin: Edition q im Be.bra Verlag, 2020.

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8

Het lunapark en andere plekken: Autobiografisch materiaal. Kapellen: Pelckmans, 2008.

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Tatranské (dez)ilúzie: Príbeh našich vel̕hôr alebo ako sa národný park mení na lunapark. Martin: Vydavatel̕stvo Matice Slovenskej, 2010.

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Marec, Anton. Tatranské (dez)ilúzie: Príbeh našich vel̕hôr alebo ako sa národný park mení na lunapark. Martin: Vydavatel̕stvo Matice Slovenskej, 2010.

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Book chapters on the topic "Lunapark"

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"A Cemetery Is Not a Lunapark." In Texts Waiting for History, 47–102. Brill | Rodopi, 2014. http://dx.doi.org/10.1163/9789401211857_004.

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