Zeitschriftenartikel zum Thema „19S regulatory particle“
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Ehlinger, Aaron, und Kylie J. Walters. „Structural Insights into Proteasome Activation by the 19S Regulatory Particle“. Biochemistry 52, Nr. 21 (14.05.2013): 3618–28. http://dx.doi.org/10.1021/bi400417a.
Der volle Inhalt der QuelleLim, Hyun-Suk, Chase T. Archer und Thomas Kodadek. „Identification of a Peptoid Inhibitor of the Proteasome 19S Regulatory Particle“. Journal of the American Chemical Society 129, Nr. 25 (Juni 2007): 7750–51. http://dx.doi.org/10.1021/ja072027p.
Der volle Inhalt der QuelleRosenzweig, Rina, Pawel A. Osmulski, Maria Gaczynska und Michael H. Glickman. „The central unit within the 19S regulatory particle of the proteasome“. Nature Structural & Molecular Biology 15, Nr. 6 (30.05.2008): 573–80. http://dx.doi.org/10.1038/nsmb.1427.
Der volle Inhalt der QuelleGreer, Susanna, Nagini Maganti, Meghna Thakkar und Agnieszka Truax. „19S ATPase subunits of the 26S proteasome play critical roles in transcription elongation. (167.7)“. Journal of Immunology 188, Nr. 1_Supplement (01.05.2012): 167.7. http://dx.doi.org/10.4049/jimmunol.188.supp.167.7.
Der volle Inhalt der QuelleMendes, Marta L., und Gunnar Dittmar. „Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry“. Biomolecules 11, Nr. 4 (27.03.2021): 505. http://dx.doi.org/10.3390/biom11040505.
Der volle Inhalt der QuelleShibahara, Tadashi, Hiroshi Kawasaki und Hisashi Hirano. „Identification of the 19S regulatory particle subunits from the rice 26S proteasome“. European Journal of Biochemistry 269, Nr. 5 (01.03.2002): 1474–83. http://dx.doi.org/10.1046/j.1432-1033.2002.02792.x.
Der volle Inhalt der QuelleStanhill, Ariel, Cole M. Haynes, Yuhong Zhang, Guangwei Min, Matthew C. Steele, Juliya Kalinina, Enid Martinez, Cecile M. Pickart, Xiang-Peng Kong und David Ron. „An Arsenite-Inducible 19S Regulatory Particle-Associated Protein Adapts Proteasomes to Proteotoxicity“. Molecular Cell 23, Nr. 6 (September 2006): 875–85. http://dx.doi.org/10.1016/j.molcel.2006.07.023.
Der volle Inhalt der QuelleIsono, 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, Nr. 2 (Februar 2007): 569–80. http://dx.doi.org/10.1091/mbc.e06-07-0635.
Der volle Inhalt der QuelleOliveri, Franziska, Steffen Johannes Keller, Heike Goebel, Gerardo Omar Alvarez Salinas und Michael Basler. „The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo“. Life Science Alliance 6, Nr. 6 (03.04.2023): e202201760. http://dx.doi.org/10.26508/lsa.202201760.
Der volle Inhalt der QuelleBrockmann, Florian, Nicola Catone, Christine Wünsch, Fabian Offensperger, Martin Scheffner, Gunter Schmidtke und Annette Aichem. „FAT10 and NUB1L cooperate to activate the 26S proteasome“. Life Science Alliance 6, Nr. 8 (15.05.2023): e202201463. http://dx.doi.org/10.26508/lsa.202201463.
Der volle Inhalt der QuelleKimura, Yayoi, Yasushi Saeki, Hideyoshi Yokosawa, Bogdan Polevoda, Fred Sherman und Hisashi Hirano. „N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome“. Archives of Biochemistry and Biophysics 409, Nr. 2 (Januar 2003): 341–48. http://dx.doi.org/10.1016/s0003-9861(02)00639-2.
Der volle Inhalt der QuelleSaeki, Yasushi, Akio Toh-e, Tai Kudo, Hitomi Kawamura und Keiji Tanaka. „Multiple Proteasome-Interacting Proteins Assist the Assembly of the Yeast 19S Regulatory Particle“. Cell 137, Nr. 5 (Mai 2009): 900–913. http://dx.doi.org/10.1016/j.cell.2009.05.005.
Der volle Inhalt der QuelleZhang, Xiaonan, Stig Linder und Martina Bazzaro. „Drug Development Targeting the Ubiquitin–Proteasome System (UPS) for the Treatment of Human Cancers“. Cancers 12, Nr. 4 (07.04.2020): 902. http://dx.doi.org/10.3390/cancers12040902.
Der volle Inhalt der QuelleBailly, Eric, und Steven I. Reed. „Functional Characterization of Rpn3 Uncovers a Distinct 19S Proteasomal Subunit Requirement for Ubiquitin-Dependent Proteolysis of Cell Cycle Regulatory Proteins in Budding Yeast“. Molecular and Cellular Biology 19, Nr. 10 (01.10.1999): 6872–90. http://dx.doi.org/10.1128/mcb.19.10.6872.
Der volle Inhalt der QuellePeng, Zhaohua, Jeffrey M. Staub, Giovanna Serino, Shing F. Kwok, Jasmina Kurepa, Barry D. Bruce, Richard D. Vierstra, Ning Wei und Xing-Wang Deng. „The Cellular Level of PR500, a Protein Complex Related to the 19S Regulatory Particle of the Proteasome, Is Regulated in Response to Stresses in Plants“. Molecular Biology of the Cell 12, Nr. 2 (Februar 2001): 383–92. http://dx.doi.org/10.1091/mbc.12.2.383.
Der volle Inhalt der QuelleRosenzweig, Rina, und Michael H. Glickman. „Chaperone-driven proteasome assembly“. Biochemical Society Transactions 36, Nr. 5 (19.09.2008): 807–12. http://dx.doi.org/10.1042/bst0360807.
Der volle Inhalt der QuelleBuneeva, O. A., A. T. Kopylov und A. E. Medvedev. „The key role of the regulatory 19S subunit in changes in the brain proteasome subproteome induced by the neuroprotector isatin“. Biomeditsinskaya Khimiya 68, Nr. 4 (2022): 250–62. http://dx.doi.org/10.18097/pbmc20226804250.
Der volle Inhalt der QuelleLe Tallec, Benoît, Marie-Bénédicte Barrault, Raphaël Guérois, Thibault Carré und Anne Peyroche. „Hsm3/S5b Participates in the Assembly Pathway of the 19S Regulatory Particle of the Proteasome“. Molecular Cell 33, Nr. 3 (Februar 2009): 389–99. http://dx.doi.org/10.1016/j.molcel.2009.01.010.
Der volle Inhalt der QuelleWinkler, L. L., J. Hwang und R. F. Kalejta. „Ubiquitin-Independent Proteasomal Degradation of Tumor Suppressors by Human Cytomegalovirus pp71 Requires the 19S Regulatory Particle“. Journal of Virology 87, Nr. 8 (13.02.2013): 4665–71. http://dx.doi.org/10.1128/jvi.03301-12.
Der volle Inhalt der QuelleSteinberger, Shirel, Julia Adler und Yosef Shaul. „Method of Monitoring 26S Proteasome in Cells Revealed the Crucial Role of PSMA3 C-Terminus in 26S Integrity“. Biomolecules 13, Nr. 6 (15.06.2023): 992. http://dx.doi.org/10.3390/biom13060992.
Der volle Inhalt der QuelleMarquez-Lona, Esther Magdalena, Ana Lilia Torres-Machorro, Frankie R. Gonzales, Lorraine Pillus und Gentry N. Patrick. „Phosphorylation of the 19S regulatory particle ATPase subunit, Rpt6, modifies susceptibility to proteotoxic stress and protein aggregation“. PLOS ONE 12, Nr. 6 (29.06.2017): e0179893. http://dx.doi.org/10.1371/journal.pone.0179893.
Der volle Inhalt der QuelleFerdous, Anwarul, Fernando Gonzalez, Liping Sun, Thomas Kodadek und Stephen Albert Johnston. „The 19S Regulatory Particle of the Proteasome Is Required for Efficient Transcription Elongation by RNA Polymerase II“. Molecular Cell 7, Nr. 5 (Mai 2001): 981–91. http://dx.doi.org/10.1016/s1097-2765(01)00250-7.
Der volle Inhalt der QuelleTruax, Agnieszka Dorota, und Susanna F. Greer. „The role of the 19S ATPase S6a in the transcriptional regulation of major histocompatibility class II (MHC II) genes (35.26)“. Journal of Immunology 178, Nr. 1_Supplement (01.04.2007): S6. http://dx.doi.org/10.4049/jimmunol.178.supp.35.26.
Der volle Inhalt der QuelleBoehringer, Jonas, Christiane Riedinger, Konstantinos Paraskevopoulos, Eachan O. D. Johnson, Edward D. Lowe, Christina Khoudian, Dominique Smith, Martin E. M. Noble, Colin Gordon und Jane A. Endicott. „Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation“. Biochemical Journal 448, Nr. 1 (18.10.2012): 55–65. http://dx.doi.org/10.1042/bj20120542.
Der volle Inhalt der QuelleKao, Athit, Arlo Randall, Yingying Yang, Vishal R. Patel, Wynne Kandur, Shenheng Guan, Scott D. Rychnovsky, Pierre Baldi und Lan Huang. „Mapping the Structural Topology of the Yeast 19S Proteasomal Regulatory Particle Using Chemical Cross-linking and Probabilistic Modeling“. Molecular & Cellular Proteomics 11, Nr. 12 (30.04.2012): 1566–77. http://dx.doi.org/10.1074/mcp.m112.018374.
Der volle Inhalt der QuelleOtsubo, Ryota, Hitomi Mimuro, Hiroshi Ashida, Jun Hamazaki, Shigeo Murata und Chihiro Sasakawa. „Shigellaeffector IpaH4.5 targets 19S regulatory particle subunit RPN13 in the 26S proteasome to dampen cytotoxic T lymphocyte activation“. Cellular Microbiology 21, Nr. 3 (05.12.2018): e12974. http://dx.doi.org/10.1111/cmi.12974.
Der volle Inhalt der QuelleDivald, Andras, Shaye Kivity, Ping Wang, Edith Hochhauser, Beth Roberts, Saul Teichberg, Aldrin V. Gomes und Saul R. Powell. „Myocardial Ischemic Preconditioning Preserves Postischemic Function of the 26S Proteasome Through Diminished Oxidative Damage to 19S Regulatory Particle Subunits“. Circulation Research 106, Nr. 12 (25.06.2010): 1829–38. http://dx.doi.org/10.1161/circresaha.110.219485.
Der volle Inhalt der QuelleBai, Minghui, Xian Zhao, Kazutaka Sahara, Yuki Ohte, Yuko Hirano, Takeumi Kaneko, Hideki Yashiroda und Shigeo Murata. „In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals“. Biomolecules 9, Nr. 6 (31.05.2019): 213. http://dx.doi.org/10.3390/biom9060213.
Der volle Inhalt der QuelleMatias, Ana C., Paula C. Ramos und R. Jürgen Dohmen. „Chaperone-assisted assembly of the proteasome core particle“. Biochemical Society Transactions 38, Nr. 1 (19.01.2010): 29–33. http://dx.doi.org/10.1042/bst0380029.
Der volle Inhalt der QuelleTonoki, Ayako, Erina Kuranaga, Takeyasu Tomioka, Jun Hamazaki, Shigeo Murata, Keiji Tanaka und Masayuki Miura. „Genetic Evidence Linking Age-Dependent Attenuation of the 26S Proteasome with the Aging Process“. Molecular and Cellular Biology 29, Nr. 4 (15.12.2008): 1095–106. http://dx.doi.org/10.1128/mcb.01227-08.
Der volle Inhalt der QuelleSun, Shuangwu, Sisi Liu, Zhengmao Zhang, Wang Zeng, Chuang Sun, Tao Tao, Xia Lin und Xin-Hua Feng. „Phosphatase UBLCP1 controls proteasome assembly“. Open Biology 7, Nr. 5 (Mai 2017): 170042. http://dx.doi.org/10.1098/rsob.170042.
Der volle Inhalt der QuelleYue, Xin, Yinglin Zuo, Hongpeng Ke, Jiaming Luo, Lanlan Lou, Wenjing Qin, Youqiao Wang et al. „Identification of 4-arylidene curcumin analogues as novel proteasome inhibitors for potential anticancer agents targeting 19S regulatory particle associated deubiquitinase“. Biochemical Pharmacology 137 (August 2017): 29–50. http://dx.doi.org/10.1016/j.bcp.2017.04.032.
Der volle Inhalt der QuelleTakahashi, M., H. Iwasaki, H. Inoue und K. Takahashi. „Reverse Genetic Analysis of the Caenorhabditis elegans 26S Proteasome Subunits by RNA Interference“. Biological Chemistry 383, Nr. 7-8 (27.08.2002): 1263–66. http://dx.doi.org/10.1515/bc.2002.140.
Der volle Inhalt der QuelleBustamante, Hianara A., Karina Cereceda, Alexis E. González, Guillermo E. Valenzuela, Yorka Cheuquemilla, Sergio Hernández, Eloisa Arias-Muñoz et al. „The Proteasomal Deubiquitinating Enzyme PSMD14 Regulates Macroautophagy by Controlling Golgi-to-ER Retrograde Transport“. Cells 9, Nr. 3 (23.03.2020): 777. http://dx.doi.org/10.3390/cells9030777.
Der volle Inhalt der QuelleLiu, Xiaoyan, Weidi Xiao, Yanan Zhang, Sandra E. Wiley, Tao Zuo, Yingying Zheng, Natalie Chen et al. „Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function“. Proceedings of the National Academy of Sciences 117, Nr. 1 (16.12.2019): 328–36. http://dx.doi.org/10.1073/pnas.1912531117.
Der volle Inhalt der QuelleLim, Hyun-Suk, Di Cai, Chase T. Archer und Thomas Kodadek. „Periodate-Triggered Cross-Linking Reveals Sug2/Rpt4 as the Molecular Target of a Peptoid Inhibitor of the 19S Proteasome Regulatory Particle“. Journal of the American Chemical Society 129, Nr. 43 (Oktober 2007): 12936–37. http://dx.doi.org/10.1021/ja075469+.
Der volle Inhalt der QuelleShibahara, Tadashi, Hiroshi Kawasaki und Hisashi Hirano. „Mass spectrometric analysis of expression of ATPase subunits encoded by duplicated genes in the 19S regulatory particle of rice 26S proteasome“. Archives of Biochemistry and Biophysics 421, Nr. 1 (Januar 2004): 34–41. http://dx.doi.org/10.1016/j.abb.2003.10.013.
Der volle Inhalt der QuelleGu, Yanyan, Benjamin G. Barwick, Mala Shanmugam, Craig C. Hofmeister, Jonathan L. Kaufman, Ajay K. Nooka, Vikas A. Gupta, Madhav V. Dhodapkar, Lawrence H. Boise und Sagar Lonial. „The Role of Proteasome Activator PA28α in Multiple Myeloma“. Blood 134, Supplement_1 (13.11.2019): 5499. http://dx.doi.org/10.1182/blood-2019-128216.
Der volle Inhalt der QuelleDiao, Wentao, Xue Yang und Hao Zhou. „Purification, crystallization and preliminary X-ray data collection of the N-terminal domain of the 26S proteasome regulatory subunit p27 and its complex with the ATPase domain of Rpt5 fromMus musculus“. Acta Crystallographica Section F Structural Biology Communications 70, Nr. 5 (15.04.2014): 611–15. http://dx.doi.org/10.1107/s2053230x14006815.
Der volle Inhalt der QuelleSong, Yan, Arghya Ray, Deepika Sharma DAS, Dharminder Chauhan und Kenneth C. Anderson. „Targeting 19S-Proteasome Deubiquitinase Rpn11/POH1/PSMD14 in Multiple Myeloma“. Blood 126, Nr. 23 (03.12.2015): 1811. http://dx.doi.org/10.1182/blood.v126.23.1811.1811.
Der volle Inhalt der QuelleKuo, Chueh-Ling, und Alfred Lewis Goldberg. „Ubiquitinated proteins promote the association of proteasomes with the deubiquitinating enzyme Usp14 and the ubiquitin ligase Ube3c“. Proceedings of the National Academy of Sciences 114, Nr. 17 (10.04.2017): E3404—E3413. http://dx.doi.org/10.1073/pnas.1701734114.
Der volle Inhalt der QuelleXia, Xue, Chun-Meng Tang, Gu-Zi Chen und Jia-Jia Han. „Proteasome Dysfunction Leads to Suppression of the Hypoxic Response Pathway in Arabidopsis“. International Journal of Molecular Sciences 23, Nr. 24 (18.12.2022): 16148. http://dx.doi.org/10.3390/ijms232416148.
Der volle Inhalt der QuelleSahu, Indrajit, und Michael H. Glickman. „Proteasome in action: substrate degradation by the 26S proteasome“. Biochemical Society Transactions 49, Nr. 2 (17.03.2021): 629–44. http://dx.doi.org/10.1042/bst20200382.
Der volle Inhalt der QuelleMuller, D. „A molecular link A molecular link between Hairless and Pros26.4, a member of the AAA-ATPase subunits of the proteasome 19S regulatory particle in Drosophila“. Journal of Cell Science 119, Nr. 2 (15.01.2006): 250–58. http://dx.doi.org/10.1242/jcs.02743.
Der volle Inhalt der QuelleCekała, Katarzyna, Karolina Trepczyk, Julia Witkowska, Elżbieta Jankowska und Ewa Wieczerzak. „Rpt5-Derived Analogs Stimulate Human Proteasome Activity in Cells and Degrade Proteins Forming Toxic Aggregates in Age-Related Diseases“. International Journal of Molecular Sciences 25, Nr. 9 (25.04.2024): 4663. http://dx.doi.org/10.3390/ijms25094663.
Der volle Inhalt der QuelleMcDonald, Heather B., Astrid Hoes Helfant, Erin M. Mahony, Shaun K. Khosla und Loretta Goetsch. „Mutational Analysis Reveals a Role for the C Terminus of the Proteasome Subunit Rpt4p in Spindle Pole Body Duplication inSaccharomyces cerevisiae“. Genetics 162, Nr. 2 (01.10.2002): 705–20. http://dx.doi.org/10.1093/genetics/162.2.705.
Der volle Inhalt der QuelleLi, Shuyu, Robert A. Spooner, Stuart C. H. Allen, Christopher P. Guise, Graham Ladds, Tina Schnöder, Manfred J. Schmitt, J. Michael Lord und Lynne M. Roberts. „Folding-competent and Folding-defective Forms of Ricin A Chain Have Different Fates after Retrotranslocation from the Endoplasmic Reticulum“. Molecular Biology of the Cell 21, Nr. 15 (August 2010): 2543–54. http://dx.doi.org/10.1091/mbc.e09-08-0743.
Der volle Inhalt der QuelleMcPherson, Ann, und Tania Watts. „The role of TRAF1 in stabilizing TRAF2 from proteasome mediated degradation downstream of 4-1BB signaling (138.1)“. Journal of Immunology 184, Nr. 1_Supplement (01.04.2010): 138.1. http://dx.doi.org/10.4049/jimmunol.184.supp.138.1.
Der volle Inhalt der QuelleLokireddy, Sudarsanareddy, Nikolay Vadimovich Kukushkin und Alfred Lewis Goldberg. „cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins“. Proceedings of the National Academy of Sciences 112, Nr. 52 (15.12.2015): E7176—E7185. http://dx.doi.org/10.1073/pnas.1522332112.
Der volle Inhalt der QuelleSong, Yan, Arghya Ray, Dharminder Chauhan und Kenneth Anderson. „Blockade of Ubiquitin Receptor PSMD4/Rpn10 Triggers Cytotoxicity and Overcomes Bortezomib-Resistance in Multiple Myeloma“. Blood 132, Supplement 1 (29.11.2018): 3211. http://dx.doi.org/10.1182/blood-2018-99-114767.
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