Artigos de revistas sobre o tema "19S regulatory particle"
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Ehlinger, Aaron, e Kylie J. Walters. "Structural Insights into Proteasome Activation by the 19S Regulatory Particle". Biochemistry 52, n.º 21 (14 de maio de 2013): 3618–28. http://dx.doi.org/10.1021/bi400417a.
Texto completo da fonteLim, Hyun-Suk, Chase T. Archer e Thomas Kodadek. "Identification of a Peptoid Inhibitor of the Proteasome 19S Regulatory Particle". Journal of the American Chemical Society 129, n.º 25 (junho de 2007): 7750–51. http://dx.doi.org/10.1021/ja072027p.
Texto completo da fonteRosenzweig, Rina, Pawel A. Osmulski, Maria Gaczynska e Michael H. Glickman. "The central unit within the 19S regulatory particle of the proteasome". Nature Structural & Molecular Biology 15, n.º 6 (30 de maio de 2008): 573–80. http://dx.doi.org/10.1038/nsmb.1427.
Texto completo da fonteGreer, Susanna, Nagini Maganti, Meghna Thakkar e Agnieszka Truax. "19S ATPase subunits of the 26S proteasome play critical roles in transcription elongation. (167.7)". Journal of Immunology 188, n.º 1_Supplement (1 de maio de 2012): 167.7. http://dx.doi.org/10.4049/jimmunol.188.supp.167.7.
Texto completo da fonteMendes, Marta L., e Gunnar Dittmar. "Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry". Biomolecules 11, n.º 4 (27 de março de 2021): 505. http://dx.doi.org/10.3390/biom11040505.
Texto completo da fonteShibahara, Tadashi, Hiroshi Kawasaki e Hisashi Hirano. "Identification of the 19S regulatory particle subunits from the rice 26S proteasome". European Journal of Biochemistry 269, n.º 5 (1 de março de 2002): 1474–83. http://dx.doi.org/10.1046/j.1432-1033.2002.02792.x.
Texto completo da fonteStanhill, Ariel, Cole M. Haynes, Yuhong Zhang, Guangwei Min, Matthew C. Steele, Juliya Kalinina, Enid Martinez, Cecile M. Pickart, Xiang-Peng Kong e David Ron. "An Arsenite-Inducible 19S Regulatory Particle-Associated Protein Adapts Proteasomes to Proteotoxicity". Molecular Cell 23, n.º 6 (setembro de 2006): 875–85. http://dx.doi.org/10.1016/j.molcel.2006.07.023.
Texto completo da fonteIsono, 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, n.º 2 (fevereiro de 2007): 569–80. http://dx.doi.org/10.1091/mbc.e06-07-0635.
Texto completo da fonteOliveri, Franziska, Steffen Johannes Keller, Heike Goebel, Gerardo Omar Alvarez Salinas e Michael Basler. "The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo". Life Science Alliance 6, n.º 6 (3 de abril de 2023): e202201760. http://dx.doi.org/10.26508/lsa.202201760.
Texto completo da fonteBrockmann, Florian, Nicola Catone, Christine Wünsch, Fabian Offensperger, Martin Scheffner, Gunter Schmidtke e Annette Aichem. "FAT10 and NUB1L cooperate to activate the 26S proteasome". Life Science Alliance 6, n.º 8 (15 de maio de 2023): e202201463. http://dx.doi.org/10.26508/lsa.202201463.
Texto completo da fonteKimura, Yayoi, Yasushi Saeki, Hideyoshi Yokosawa, Bogdan Polevoda, Fred Sherman e Hisashi Hirano. "N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome". Archives of Biochemistry and Biophysics 409, n.º 2 (janeiro de 2003): 341–48. http://dx.doi.org/10.1016/s0003-9861(02)00639-2.
Texto completo da fonteSaeki, Yasushi, Akio Toh-e, Tai Kudo, Hitomi Kawamura e Keiji Tanaka. "Multiple Proteasome-Interacting Proteins Assist the Assembly of the Yeast 19S Regulatory Particle". Cell 137, n.º 5 (maio de 2009): 900–913. http://dx.doi.org/10.1016/j.cell.2009.05.005.
Texto completo da fonteZhang, Xiaonan, Stig Linder e Martina Bazzaro. "Drug Development Targeting the Ubiquitin–Proteasome System (UPS) for the Treatment of Human Cancers". Cancers 12, n.º 4 (7 de abril de 2020): 902. http://dx.doi.org/10.3390/cancers12040902.
Texto completo da fonteBailly, Eric, e 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, n.º 10 (1 de outubro de 1999): 6872–90. http://dx.doi.org/10.1128/mcb.19.10.6872.
Texto completo da fontePeng, Zhaohua, Jeffrey M. Staub, Giovanna Serino, Shing F. Kwok, Jasmina Kurepa, Barry D. Bruce, Richard D. Vierstra, Ning Wei e 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, n.º 2 (fevereiro de 2001): 383–92. http://dx.doi.org/10.1091/mbc.12.2.383.
Texto completo da fonteRosenzweig, Rina, e Michael H. Glickman. "Chaperone-driven proteasome assembly". Biochemical Society Transactions 36, n.º 5 (19 de setembro de 2008): 807–12. http://dx.doi.org/10.1042/bst0360807.
Texto completo da fonteBuneeva, O. A., A. T. Kopylov e 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, n.º 4 (2022): 250–62. http://dx.doi.org/10.18097/pbmc20226804250.
Texto completo da fonteLe Tallec, Benoît, Marie-Bénédicte Barrault, Raphaël Guérois, Thibault Carré e Anne Peyroche. "Hsm3/S5b Participates in the Assembly Pathway of the 19S Regulatory Particle of the Proteasome". Molecular Cell 33, n.º 3 (fevereiro de 2009): 389–99. http://dx.doi.org/10.1016/j.molcel.2009.01.010.
Texto completo da fonteWinkler, L. L., J. Hwang e R. F. Kalejta. "Ubiquitin-Independent Proteasomal Degradation of Tumor Suppressors by Human Cytomegalovirus pp71 Requires the 19S Regulatory Particle". Journal of Virology 87, n.º 8 (13 de fevereiro de 2013): 4665–71. http://dx.doi.org/10.1128/jvi.03301-12.
Texto completo da fonteSteinberger, Shirel, Julia Adler e Yosef Shaul. "Method of Monitoring 26S Proteasome in Cells Revealed the Crucial Role of PSMA3 C-Terminus in 26S Integrity". Biomolecules 13, n.º 6 (15 de junho de 2023): 992. http://dx.doi.org/10.3390/biom13060992.
Texto completo da fonteMarquez-Lona, Esther Magdalena, Ana Lilia Torres-Machorro, Frankie R. Gonzales, Lorraine Pillus e Gentry N. Patrick. "Phosphorylation of the 19S regulatory particle ATPase subunit, Rpt6, modifies susceptibility to proteotoxic stress and protein aggregation". PLOS ONE 12, n.º 6 (29 de junho de 2017): e0179893. http://dx.doi.org/10.1371/journal.pone.0179893.
Texto completo da fonteFerdous, Anwarul, Fernando Gonzalez, Liping Sun, Thomas Kodadek e Stephen Albert Johnston. "The 19S Regulatory Particle of the Proteasome Is Required for Efficient Transcription Elongation by RNA Polymerase II". Molecular Cell 7, n.º 5 (maio de 2001): 981–91. http://dx.doi.org/10.1016/s1097-2765(01)00250-7.
Texto completo da fonteTruax, Agnieszka Dorota, e 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, n.º 1_Supplement (1 de abril de 2007): S6. http://dx.doi.org/10.4049/jimmunol.178.supp.35.26.
Texto completo da fonteBoehringer, Jonas, Christiane Riedinger, Konstantinos Paraskevopoulos, Eachan O. D. Johnson, Edward D. Lowe, Christina Khoudian, Dominique Smith, Martin E. M. Noble, Colin Gordon e Jane A. Endicott. "Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation". Biochemical Journal 448, n.º 1 (18 de outubro de 2012): 55–65. http://dx.doi.org/10.1042/bj20120542.
Texto completo da fonteKao, Athit, Arlo Randall, Yingying Yang, Vishal R. Patel, Wynne Kandur, Shenheng Guan, Scott D. Rychnovsky, Pierre Baldi e Lan Huang. "Mapping the Structural Topology of the Yeast 19S Proteasomal Regulatory Particle Using Chemical Cross-linking and Probabilistic Modeling". Molecular & Cellular Proteomics 11, n.º 12 (30 de abril de 2012): 1566–77. http://dx.doi.org/10.1074/mcp.m112.018374.
Texto completo da fonteOtsubo, Ryota, Hitomi Mimuro, Hiroshi Ashida, Jun Hamazaki, Shigeo Murata e Chihiro Sasakawa. "Shigellaeffector IpaH4.5 targets 19S regulatory particle subunit RPN13 in the 26S proteasome to dampen cytotoxic T lymphocyte activation". Cellular Microbiology 21, n.º 3 (5 de dezembro de 2018): e12974. http://dx.doi.org/10.1111/cmi.12974.
Texto completo da fonteDivald, Andras, Shaye Kivity, Ping Wang, Edith Hochhauser, Beth Roberts, Saul Teichberg, Aldrin V. Gomes e 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, n.º 12 (25 de junho de 2010): 1829–38. http://dx.doi.org/10.1161/circresaha.110.219485.
Texto completo da fonteBai, Minghui, Xian Zhao, Kazutaka Sahara, Yuki Ohte, Yuko Hirano, Takeumi Kaneko, Hideki Yashiroda e Shigeo Murata. "In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals". Biomolecules 9, n.º 6 (31 de maio de 2019): 213. http://dx.doi.org/10.3390/biom9060213.
Texto completo da fonteMatias, Ana C., Paula C. Ramos e R. Jürgen Dohmen. "Chaperone-assisted assembly of the proteasome core particle". Biochemical Society Transactions 38, n.º 1 (19 de janeiro de 2010): 29–33. http://dx.doi.org/10.1042/bst0380029.
Texto completo da fonteTonoki, Ayako, Erina Kuranaga, Takeyasu Tomioka, Jun Hamazaki, Shigeo Murata, Keiji Tanaka e Masayuki Miura. "Genetic Evidence Linking Age-Dependent Attenuation of the 26S Proteasome with the Aging Process". Molecular and Cellular Biology 29, n.º 4 (15 de dezembro de 2008): 1095–106. http://dx.doi.org/10.1128/mcb.01227-08.
Texto completo da fonteSun, Shuangwu, Sisi Liu, Zhengmao Zhang, Wang Zeng, Chuang Sun, Tao Tao, Xia Lin e Xin-Hua Feng. "Phosphatase UBLCP1 controls proteasome assembly". Open Biology 7, n.º 5 (maio de 2017): 170042. http://dx.doi.org/10.1098/rsob.170042.
Texto completo da fonteYue, 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 (agosto de 2017): 29–50. http://dx.doi.org/10.1016/j.bcp.2017.04.032.
Texto completo da fonteTakahashi, M., H. Iwasaki, H. Inoue e K. Takahashi. "Reverse Genetic Analysis of the Caenorhabditis elegans 26S Proteasome Subunits by RNA Interference". Biological Chemistry 383, n.º 7-8 (27 de agosto de 2002): 1263–66. http://dx.doi.org/10.1515/bc.2002.140.
Texto completo da fonteBustamante, 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, n.º 3 (23 de março de 2020): 777. http://dx.doi.org/10.3390/cells9030777.
Texto completo da fonteLiu, 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, n.º 1 (16 de dezembro de 2019): 328–36. http://dx.doi.org/10.1073/pnas.1912531117.
Texto completo da fonteLim, Hyun-Suk, Di Cai, Chase T. Archer e 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, n.º 43 (outubro de 2007): 12936–37. http://dx.doi.org/10.1021/ja075469+.
Texto completo da fonteShibahara, Tadashi, Hiroshi Kawasaki e 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, n.º 1 (janeiro de 2004): 34–41. http://dx.doi.org/10.1016/j.abb.2003.10.013.
Texto completo da fonteGu, Yanyan, Benjamin G. Barwick, Mala Shanmugam, Craig C. Hofmeister, Jonathan L. Kaufman, Ajay K. Nooka, Vikas A. Gupta, Madhav V. Dhodapkar, Lawrence H. Boise e Sagar Lonial. "The Role of Proteasome Activator PA28α in Multiple Myeloma". Blood 134, Supplement_1 (13 de novembro de 2019): 5499. http://dx.doi.org/10.1182/blood-2019-128216.
Texto completo da fonteDiao, Wentao, Xue Yang e 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, n.º 5 (15 de abril de 2014): 611–15. http://dx.doi.org/10.1107/s2053230x14006815.
Texto completo da fonteSong, Yan, Arghya Ray, Deepika Sharma DAS, Dharminder Chauhan e Kenneth C. Anderson. "Targeting 19S-Proteasome Deubiquitinase Rpn11/POH1/PSMD14 in Multiple Myeloma". Blood 126, n.º 23 (3 de dezembro de 2015): 1811. http://dx.doi.org/10.1182/blood.v126.23.1811.1811.
Texto completo da fonteKuo, Chueh-Ling, e 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, n.º 17 (10 de abril de 2017): E3404—E3413. http://dx.doi.org/10.1073/pnas.1701734114.
Texto completo da fonteXia, Xue, Chun-Meng Tang, Gu-Zi Chen e Jia-Jia Han. "Proteasome Dysfunction Leads to Suppression of the Hypoxic Response Pathway in Arabidopsis". International Journal of Molecular Sciences 23, n.º 24 (18 de dezembro de 2022): 16148. http://dx.doi.org/10.3390/ijms232416148.
Texto completo da fonteSahu, Indrajit, e Michael H. Glickman. "Proteasome in action: substrate degradation by the 26S proteasome". Biochemical Society Transactions 49, n.º 2 (17 de março de 2021): 629–44. http://dx.doi.org/10.1042/bst20200382.
Texto completo da fonteMuller, 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, n.º 2 (15 de janeiro de 2006): 250–58. http://dx.doi.org/10.1242/jcs.02743.
Texto completo da fonteCekała, Katarzyna, Karolina Trepczyk, Julia Witkowska, Elżbieta Jankowska e 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, n.º 9 (25 de abril de 2024): 4663. http://dx.doi.org/10.3390/ijms25094663.
Texto completo da fonteMcDonald, Heather B., Astrid Hoes Helfant, Erin M. Mahony, Shaun K. Khosla e 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, n.º 2 (1 de outubro de 2002): 705–20. http://dx.doi.org/10.1093/genetics/162.2.705.
Texto completo da fonteLi, Shuyu, Robert A. Spooner, Stuart C. H. Allen, Christopher P. Guise, Graham Ladds, Tina Schnöder, Manfred J. Schmitt, J. Michael Lord e 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, n.º 15 (agosto de 2010): 2543–54. http://dx.doi.org/10.1091/mbc.e09-08-0743.
Texto completo da fonteMcPherson, Ann, e Tania Watts. "The role of TRAF1 in stabilizing TRAF2 from proteasome mediated degradation downstream of 4-1BB signaling (138.1)". Journal of Immunology 184, n.º 1_Supplement (1 de abril de 2010): 138.1. http://dx.doi.org/10.4049/jimmunol.184.supp.138.1.
Texto completo da fonteLokireddy, Sudarsanareddy, Nikolay Vadimovich Kukushkin e 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, n.º 52 (15 de dezembro de 2015): E7176—E7185. http://dx.doi.org/10.1073/pnas.1522332112.
Texto completo da fonteSong, Yan, Arghya Ray, Dharminder Chauhan e Kenneth Anderson. "Blockade of Ubiquitin Receptor PSMD4/Rpn10 Triggers Cytotoxicity and Overcomes Bortezomib-Resistance in Multiple Myeloma". Blood 132, Supplement 1 (29 de novembro de 2018): 3211. http://dx.doi.org/10.1182/blood-2018-99-114767.
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