Littérature scientifique sur le sujet « 19S regulatory particle »
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Articles de revues sur le sujet "19S regulatory particle"
Ehlinger, Aaron, et Kylie J. Walters. « Structural Insights into Proteasome Activation by the 19S Regulatory Particle ». Biochemistry 52, no 21 (14 mai 2013) : 3618–28. http://dx.doi.org/10.1021/bi400417a.
Texte intégralLim, Hyun-Suk, Chase T. Archer et Thomas Kodadek. « Identification of a Peptoid Inhibitor of the Proteasome 19S Regulatory Particle ». Journal of the American Chemical Society 129, no 25 (juin 2007) : 7750–51. http://dx.doi.org/10.1021/ja072027p.
Texte intégralRosenzweig, Rina, Pawel A. Osmulski, Maria Gaczynska et Michael H. Glickman. « The central unit within the 19S regulatory particle of the proteasome ». Nature Structural & ; Molecular Biology 15, no 6 (30 mai 2008) : 573–80. http://dx.doi.org/10.1038/nsmb.1427.
Texte intégralGreer, Susanna, Nagini Maganti, Meghna Thakkar et Agnieszka Truax. « 19S ATPase subunits of the 26S proteasome play critical roles in transcription elongation. (167.7) ». Journal of Immunology 188, no 1_Supplement (1 mai 2012) : 167.7. http://dx.doi.org/10.4049/jimmunol.188.supp.167.7.
Texte intégralMendes, Marta L., et Gunnar Dittmar. « Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry ». Biomolecules 11, no 4 (27 mars 2021) : 505. http://dx.doi.org/10.3390/biom11040505.
Texte intégralShibahara, Tadashi, Hiroshi Kawasaki et Hisashi Hirano. « Identification of the 19S regulatory particle subunits from the rice 26S proteasome ». European Journal of Biochemistry 269, no 5 (1 mars 2002) : 1474–83. http://dx.doi.org/10.1046/j.1432-1033.2002.02792.x.
Texte intégralStanhill, Ariel, Cole M. Haynes, Yuhong Zhang, Guangwei Min, Matthew C. Steele, Juliya Kalinina, Enid Martinez, Cecile M. Pickart, Xiang-Peng Kong et David Ron. « An Arsenite-Inducible 19S Regulatory Particle-Associated Protein Adapts Proteasomes to Proteotoxicity ». Molecular Cell 23, no 6 (septembre 2006) : 875–85. http://dx.doi.org/10.1016/j.molcel.2006.07.023.
Texte intégralIsono, Erika, Kiyoshi Nishihara, Yasushi Saeki, Hideki Yashiroda, Naoko Kamata, Liying Ge, Takashi Ueda et al. « The Assembly Pathway of the 19S Regulatory Particle of the Yeast 26S Proteasome ». Molecular Biology of the Cell 18, no 2 (février 2007) : 569–80. http://dx.doi.org/10.1091/mbc.e06-07-0635.
Texte intégralOliveri, Franziska, Steffen Johannes Keller, Heike Goebel, Gerardo Omar Alvarez Salinas et Michael Basler. « The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo ». Life Science Alliance 6, no 6 (3 avril 2023) : e202201760. http://dx.doi.org/10.26508/lsa.202201760.
Texte intégralBrockmann, Florian, Nicola Catone, Christine Wünsch, Fabian Offensperger, Martin Scheffner, Gunter Schmidtke et Annette Aichem. « FAT10 and NUB1L cooperate to activate the 26S proteasome ». Life Science Alliance 6, no 8 (15 mai 2023) : e202201463. http://dx.doi.org/10.26508/lsa.202201463.
Texte intégralThèses sur le sujet "19S regulatory particle"
Kaiser, Marie-Luise [Verfasser], et Karin B. [Akademischer Betreuer] Römisch. « A sec61 mutant defective in 19S regulatory particle binding / Marie-Luise Kaiser. Betreuer : Karin B. Römisch ». Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2015. http://d-nb.info/1069289922/34.
Texte intégralPathare, Ganesh [Verfasser], Wolfgang [Akademischer Betreuer] Baumeister et Sevil [Akademischer Betreuer] Weinkauf. « Structural and functional studies of 19S regulatory particle subunits of the 26S proteasome / Ganesh Pathare. Gutachter : Sevil Weinkauf ; Wolfgang Baumeister. Betreuer : Wolfgang Baumeister ». München : Universitätsbibliothek der TU München, 2014. http://d-nb.info/1063090210/34.
Texte intégralLainé, Claudianne. « Caractérisation moléculaire et fonctionnelle de la protéine AAA-ATPase PbRpt3 de Plasmodium berghei : étude de sa fonction régulatrice de PP1c et analyse de son réseau d'interactions chez le parasite ». Electronic Thesis or Diss., Université de Lille (2022-....), 2023. http://www.theses.fr/2023ULILS043.
Texte intégralMalaria, caused by the Plasmodium parasite, is the most lethal parasitosis in the world, with more than 600,000 deaths in 2021, and mostly affects children under the age of 5, mainly in Africa. The RTS,S/A01 vaccine against this infectious disease has been recommended by the WHO since 2021. However, its relative efficacy, combined with the parasite's resistance to artemisinin-based chemo-therapeutic combinations (Artemisinin Combined Therapies) and the vector's resistance to insecticides, implies that further research is needed to gain a better understanding of the parasite's biology and design new anti-parasitic molecules. Reversible protein phosphorylation plays a crucial role in the development of the parasite. For example, it has recently been shown that the serine/threonine phosphatase PP1 is essential during the late stages of schizogony, particularly during the egress phase of the red blood cell. Our team studies the regulators of the catalytic subunit of the phosphatase (PP1c). Two PP1c interactome studies in Plasmodium berghei, have led our team to observe a potential interaction between PP1c and various proteins belonging to the parasite proteasome, including the AAA-ATPase PbRpt3 (PBANKA_0715600), which possesses two RVxF motifs, described as being predominantly present in proteins interacting with PP1c. Furthermore, using global approaches, Rpt3 was predicted to be essential in P. falciparum, whereas in P. berghei parasites deficient for this ATPase show a slow phenotype. The 26S proteasome is a protein complex involved in protein degradation, contributing to homeostasis and the stress response in eukaryotic cells. It is composed of a 20S complex carrying the catalytic activity, associated with one or two 19S regulatory complexes composed of ATPase (Rpt) and non-ATPase (Rpn) proteins. The PbRpt3 protein is thought to belong to the 19S complex of the parasite proteasome. During my thesis, I characterised the PbRpt3 regulatory subunit, demonstrated that it interacts with PP1c in vitro, and that it activates the phosphatase function of PP1c both in vitro and in a heterologous model of Xenopus oocytes. Using a site-directed mutagenesis approach, we observed that the RVxF motifs of PbRpt3 were involved in its binding to PP1c, and in the regulatory function towards this phosphatase. We built a 3D model of the PbRpt3 protein by comparative homology, which enabled us to predict the amino acids involved in ATP stabilisation. The mutation of these amino acids, combined with the Xenopus oocyte approach, led us to show that the enzymatic activity of PbRpt3 would be involved in the activation of the PP1c phosphatase. Using reverse genetics studies, we suggest an essential role for Rpt3 during the intra-erythrocytic stages in P. berghei, as no PbRpt3-deficient parasites were obtained in mice despite numerous cloning attempts and the use of the PlasmoGem system. A Knock-in approach, using the mCherry tag, enabled the protein to be located during the intra-erythrocytic cycle, showing a presence in the cytoplasm during the trophozoite to schizont stages, and a localised concentration in the nucleus in gametocytes. Finally, immunoprecipitation followed by mass spectrometry analysis enabled us to characterise the PbRpt3 interactome in the parasite during the schizont stage. We confirmed that PbRpt3 belongs to the 19S proteasome complex and observed that this ATPase associates with several proteins known to bind to membrane phospholipids. These observations suggest that PbRpt3 could play a direct role, or indirect, through interacting with partners, in the membrane dynamics of P. berghei
Chapitres de livres sur le sujet "19S regulatory particle"
DeMartino, George N., et Cezary Wojcik. « Proteasome Regulator, PA700 (19S Regulatory Particle) ». Dans Protein Degradation, 288–316. Weinheim, FRG : Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/352760586x.ch11.
Texte intégralDeMartino, George N. « Reconstitution of PA700, the 19S Regulatory Particle, from Purified Precursor Complexes ». Dans Methods in Molecular Biology, 443–52. Totowa, NJ : Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-474-2_31.
Texte intégral« 19S Proteasome Regulatory Particle ». Dans Encyclopedia of Cancer, 3817. Berlin, Heidelberg : Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_100015.
Texte intégralHo, Maurice K. C., et Yung H. Wong. « Adenylyl cyclases and cyclic AMP ». Dans Signal Transduction, 223–53. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780199637218.003.0009.
Texte intégralActes de conférences sur le sujet "19S regulatory particle"
Volkanovski, Andrija, Antonio Ballesteros Avila et Miguel Peinador Veira. « Results of the Loss of Offsite Power Events Analysis ». Dans 2016 24th International Conference on Nuclear Engineering. American Society of Mechanical Engineers, 2016. http://dx.doi.org/10.1115/icone24-60153.
Texte intégralRapports d'organisations sur le sujet "19S regulatory particle"
Vargas-Herrera, Hernando, Juan Jose Ospina-Tejeiro, Carlos Alfonso Huertas-Campos, Adolfo León Cobo-Serna, Edgar Caicedo-García, Juan Pablo Cote-Barón, Nicolás Martínez-Cortés et al. Monetary Policy Report - April de 2021. Banco de la República de Colombia, juillet 2021. http://dx.doi.org/10.32468/inf-pol-mont-eng.tr2-2021.
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