Статті в журналах з теми "SUMO Protease"
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Yang, Wei, Liangli Wang, and Wulf Paschen. "Development of a High-Throughput Screening Assay for Inhibitors of Small Ubiquitin-Like Modifier Proteases." Journal of Biomolecular Screening 18, no. 5 (March 7, 2013): 621–28. http://dx.doi.org/10.1177/1087057113479971.
Повний текст джерелаMukhopadhyay, Debaditya, Ferhan Ayaydin, Nagamalleswari Kolli, Shyh-Han Tan, Tadashi Anan, Ai Kametaka, Yoshiaki Azuma, Keith D. Wilkinson, and Mary Dasso. "SUSP1 antagonizes formation of highly SUMO2/3-conjugated species." Journal of Cell Biology 174, no. 7 (September 21, 2006): 939–49. http://dx.doi.org/10.1083/jcb.200510103.
Повний текст джерелаAlegre, Kamela O., and David Reverter. "Swapping Small Ubiquitin-like Modifier (SUMO) Isoform Specificity of SUMO Proteases SENP6 and SENP7." Journal of Biological Chemistry 286, no. 41 (August 30, 2011): 36142–51. http://dx.doi.org/10.1074/jbc.m111.268847.
Повний текст джерелаLiu, Yan, Yali Shen, Yang Song, Lei Xu, J. Jefferson P. P. Perry, and Jiayu Liao. "Isopeptidase Kinetics Determination by a Real Time and Sensitive qFRET Approach." Biomolecules 11, no. 5 (April 30, 2021): 673. http://dx.doi.org/10.3390/biom11050673.
Повний текст джерелаLee, Jiwon, Yool Lee, Min Joo Lee, Eonyoung Park, Sung Hwan Kang, Chin Ha Chung, Kun Ho Lee, and Kyungjin Kim. "Dual Modification of BMAL1 by SUMO2/3 and Ubiquitin Promotes Circadian Activation of the CLOCK/BMAL1 Complex." Molecular and Cellular Biology 28, no. 19 (July 21, 2008): 6056–65. http://dx.doi.org/10.1128/mcb.00583-08.
Повний текст джерелаShen, Lin Nan, Changjiang Dong, Huanting Liu, James H. Naismith, and Ronald T. Hay. "The structure of SENP1–SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing." Biochemical Journal 397, no. 2 (June 28, 2006): 279–88. http://dx.doi.org/10.1042/bj20052030.
Повний текст джерелаVertegaal, Alfred C. O. "SUMO chains: polymeric signals." Biochemical Society Transactions 38, no. 1 (January 19, 2010): 46–49. http://dx.doi.org/10.1042/bst0380046.
Повний текст джерелаXu, Zheng, So Fun Chau, Kwok Ho Lam, Ho Yin Chan, Tzi Bun Ng, and Shannon W. N. Au. "Crystal structure of the SENP1 mutant C603S–SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease." Biochemical Journal 398, no. 3 (August 29, 2006): 345–52. http://dx.doi.org/10.1042/bj20060526.
Повний текст джерелаDi Bacco, Alessandra, Jian Ouyang, Hsiang-Ying Lee, Andre Catic, Hidde Ploegh, and Grace Gill. "The SUMO-Specific Protease SENP5 Is Required for Cell Division." Molecular and Cellular Biology 26, no. 12 (June 15, 2006): 4489–98. http://dx.doi.org/10.1128/mcb.02301-05.
Повний текст джерелаDorval, Véronique, Matthew J. Mazzella, Paul M. Mathews, Ronald T. Hay та Paul E. Fraser. "Modulation of Aβ generation by small ubiquitin-like modifiers does not require conjugation to target proteins". Biochemical Journal 404, № 2 (14 травня 2007): 309–16. http://dx.doi.org/10.1042/bj20061451.
Повний текст джерелаRoden, Julie, Leah Eardley, Andrew Hotson, Yajuan Cao, and Mary Beth Mudgett. "Characterization of the Xanthomonas AvrXv4 Effector, a SUMO Protease Translocated into Plant Cells." Molecular Plant-Microbe Interactions® 17, no. 6 (June 2004): 633–43. http://dx.doi.org/10.1094/mpmi.2004.17.6.633.
Повний текст джерелаXU, Zheng, and Shannon W. N. AU. "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1." Biochemical Journal 386, no. 2 (February 22, 2005): 325–30. http://dx.doi.org/10.1042/bj20041210.
Повний текст джерелаPeek, Jennifer, Catherine Harvey, Dreux Gray, Danny Rosenberg, Likhitha Kolla, Reuben Levy-Myers, Rui Yin, Jonathan L. McMurry, and Oliver Kerscher. "SUMO targeting of a stress-tolerant Ulp1 SUMO protease." PLOS ONE 13, no. 1 (January 19, 2018): e0191391. http://dx.doi.org/10.1371/journal.pone.0191391.
Повний текст джерелаElmore, Zachary C., Megan Donaher, Brooke C. Matson, Helen Murphy, Jason W. Westerbeck, and Oliver Kerscher. "Sumo-dependent substrate targeting of the SUMO protease Ulp1." BMC Biology 9, no. 1 (2011): 74. http://dx.doi.org/10.1186/1741-7007-9-74.
Повний текст джерелаKroetz, Mary B., Dan Su, and Mark Hochstrasser. "Essential Role of Nuclear Localization for Yeast Ulp2 SUMO Protease Function." Molecular Biology of the Cell 20, no. 8 (April 15, 2009): 2196–206. http://dx.doi.org/10.1091/mbc.e08-10-1090.
Повний текст джерелаCheng, Jialin, Min Su, Yunfeng Jin, Qinghua Xi, Yan Deng, Jie Chen, Wei Wang, et al. "Upregulation of SENP3/SMT3IP1 promotes epithelial ovarian cancer progression and forecasts poor prognosis." Tumor Biology 39, no. 3 (March 2017): 101042831769454. http://dx.doi.org/10.1177/1010428317694543.
Повний текст джерелаAu, S. W., Z. Xu, K. H. Lam, and C. S. F. Chau. "Differential maturation of SUMO precursors by SUMO-specific protease, SENP1." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c208. http://dx.doi.org/10.1107/s0108767305091142.
Повний текст джерелаKang, Heejung, Eui Tae Kim, Hye-Ra Lee, Jung-Jin Park, Yoon Young Go, Cheol Yong Choi, and Jin-Hyun Ahn. "Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein." Journal of General Virology 87, no. 8 (August 1, 2006): 2181–90. http://dx.doi.org/10.1099/vir.0.81787-0.
Повний текст джерелаEl Mchichi, Bouchra, Tarik Regad, Mohamed-Ali Maroui, Manuel S. Rodriguez, Aleksey Aminev, Sylvie Gerbaud, Nicolas Escriou, Laurent Dianoux, and Mounira K. Chelbi-Alix. "SUMOylation Promotes PML Degradation during Encephalomyocarditis Virus Infection." Journal of Virology 84, no. 22 (September 8, 2010): 11634–45. http://dx.doi.org/10.1128/jvi.01321-10.
Повний текст джерелаBailey, Daniel, and Peter O’Hare. "Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease." Journal of General Virology 83, no. 12 (December 1, 2002): 2951–64. http://dx.doi.org/10.1099/0022-1317-83-12-2951.
Повний текст джерелаSchuldt, Alison. "A SUMO protease for stress protection." Nature Reviews Molecular Cell Biology 14, no. 5 (April 18, 2013): 263. http://dx.doi.org/10.1038/nrm3569.
Повний текст джерелаLiu, Linpo, Ying Jiang, Xiaomei Zhang, Xu Wang, Yanbing Wang, Yuzhen Han, George Coupland, et al. "Two SUMO Proteases SUMO PROTEASE RELATED TO FERTILITY1 and 2 Are Required for Fertility in Arabidopsis." Plant Physiology 175, no. 4 (October 24, 2017): 1703–19. http://dx.doi.org/10.1104/pp.17.00021.
Повний текст джерелаItahana, Yoko, Edward T. H. Yeh, and Yanping Zhang. "Nucleocytoplasmic Shuttling Modulates Activity and Ubiquitination-Dependent Turnover of SUMO-Specific Protease 2." Molecular and Cellular Biology 26, no. 12 (June 15, 2006): 4675–89. http://dx.doi.org/10.1128/mcb.01830-05.
Повний текст джерелаNait Achour, Thiziri, Stéphanie Sentis, Catherine Teyssier, Amandine Philippat, Annick Lucas, Laura Corbo, Vincent Cavaillès та Stéphan Jalaguier. "Transcriptional Repression of Estrogen Receptor α Signaling by SENP2 in Breast Cancer Cells". Molecular Endocrinology 28, № 2 (1 лютого 2014): 183–96. http://dx.doi.org/10.1210/me.2013-1376.
Повний текст джерелаHattersley, Neil, Linnan Shen, Ellis G. Jaffray, and Ronald T. Hay. "The SUMO protease SENP6 is a direct regulator of PML nuclear bodies." Molecular Biology of the Cell 22, no. 1 (January 2011): 78–90. http://dx.doi.org/10.1091/mbc.e10-06-0504.
Повний текст джерелаLiu, Yan, Yali Shen, Shasha Zheng, and Jiayu Liao. "A novel robust quantitative Förster resonance energy transfer assay for protease SENP2 kinetics determination against its all natural substrates." Molecular BioSystems 11, no. 12 (2015): 3407–14. http://dx.doi.org/10.1039/c5mb00568j.
Повний текст джерелаAmbaye, Nigus D. "Noncovalent structure of SENP1 in complex with SUMO2." Acta Crystallographica Section F Structural Biology Communications 75, no. 5 (April 24, 2019): 332–39. http://dx.doi.org/10.1107/s2053230x19004266.
Повний текст джерелаVerma, Vivek, Anjil K. Srivastava, Catherine Gough, Alberto Campanaro, Moumita Srivastava, Rebecca Morrell, Joshua Joyce, et al. "SUMO enables substrate selectivity by mitogen-activated protein kinases to regulate immunity in plants." Proceedings of the National Academy of Sciences 118, no. 10 (March 1, 2021): e2021351118. http://dx.doi.org/10.1073/pnas.2021351118.
Повний текст джерелаLi, Shyr-Jiann, and Mark Hochstrasser. "The Ulp1 SUMO isopeptidase." Journal of Cell Biology 160, no. 7 (March 24, 2003): 1069–82. http://dx.doi.org/10.1083/jcb.200212052.
Повний текст джерелаZhang, Faying, Hui Zheng, Yufan Xian, Haoyue Song, Shengchen Wang, Yueli Yun, Li Yi, and Guimin Zhang. "Profiling Substrate Specificity of the SUMO Protease Ulp1 by the YESS–PSSC System to Advance the Conserved Mechanism for Substrate Cleavage." International Journal of Molecular Sciences 23, no. 20 (October 13, 2022): 12188. http://dx.doi.org/10.3390/ijms232012188.
Повний текст джерелаJi, Mingfei, Zongtao Chai, Jie Chen, Gang Li, Qiang Li, Miao Li, Yelei Ding, Shaoyong Lu, Guanqun Ju, and Jianquan Hou. "Insights into the Allosteric Effect of SENP1 Q597A Mutation on the Hydrolytic Reaction of SUMO1 via an Integrated Computational Study." Molecules 27, no. 13 (June 28, 2022): 4149. http://dx.doi.org/10.3390/molecules27134149.
Повний текст джерелаAlonso, Annabel, Sonia D'Silva, Maliha Rahman, Pam B. Meluh, Jacob Keeling, Nida Meednu, Harold J. Hoops, and Rita K. Miller. "The yeast homologue of the microtubule-associated protein Lis1 interacts with the sumoylation machinery and a SUMO-targeted ubiquitin ligase." Molecular Biology of the Cell 23, no. 23 (December 2012): 4552–66. http://dx.doi.org/10.1091/mbc.e12-03-0195.
Повний текст джерелаSmith, Matthew, Vinay Bhaskar, Joseph Fernandez, and Albert J. Courey. "DrosophilaUlp1, a Nuclear Pore-associated SUMO Protease, Prevents Accumulation of Cytoplasmic SUMO Conjugates." Journal of Biological Chemistry 279, no. 42 (August 4, 2004): 43805–14. http://dx.doi.org/10.1074/jbc.m404942200.
Повний текст джерелаMalakhov, Michael P., Michael R. Mattern, Oxana A. Malakhova, Mark Drinker, Stephen D. Weeks, and Tauseef R. Butt. "SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins." Journal of Structural and Functional Genomics 5, no. 1/2 (March 2004): 75–86. http://dx.doi.org/10.1023/b:jsfg.0000029237.70316.52.
Повний текст джерелаBea, Annika, Constanze Kröber-Boncardo, Manpreet Sandhu, Christine Brinker, and Joachim Clos. "The Leishmania donovani SENP Protease Is Required for SUMO Processing but Not for Viability." Genes 11, no. 10 (October 14, 2020): 1198. http://dx.doi.org/10.3390/genes11101198.
Повний текст джерелаVera Rodriguez, Arturo, Steffen Frey, and Dirk Görlich. "Engineered SUMO/protease system identifies Pdr6 as a bidirectional nuclear transport receptor." Journal of Cell Biology 218, no. 6 (April 25, 2019): 2006–20. http://dx.doi.org/10.1083/jcb.201812091.
Повний текст джерелаSun, Xiao-Xin, Yingxiao Chen, Yulong Su, Xiaoyan Wang, Krishna Mohan Chauhan, Juan Liang, Colin J. Daniel, Rosalie C. Sears, and Mu-Shui Dai. "SUMO protease SENP1 deSUMOylates and stabilizes c-Myc." Proceedings of the National Academy of Sciences 115, no. 43 (October 10, 2018): 10983–88. http://dx.doi.org/10.1073/pnas.1802932115.
Повний текст джерелаLau, Yue-Ting K., Vladimir Baytshtok, Tessa A. Howard, Brooke M. Fiala, JayLee M. Johnson, Lauren P. Carter, David Baker, Christopher D. Lima, and Christopher D. Bahl. "Discovery and engineering of enhanced SUMO protease enzymes." Journal of Biological Chemistry 293, no. 34 (July 5, 2018): 13224–33. http://dx.doi.org/10.1074/jbc.ra118.004146.
Повний текст джерелаShin, Eun Ju, Hyun Mi Shin, Eori Nam, Won Seog Kim, Ji‐Hoon Kim, Byung‐Ha Oh, and Yungdae Yun. "DeSUMOylating isopeptidase: a second class of SUMO protease." EMBO reports 13, no. 4 (February 28, 2012): 339–46. http://dx.doi.org/10.1038/embor.2012.3.
Повний текст джерелаMohideen, Firaz, and Christopher D. Lima. "SUMO Takes Control of a Ubiquitin-Specific Protease." Molecular Cell 30, no. 5 (June 2008): 539–40. http://dx.doi.org/10.1016/j.molcel.2008.05.010.
Повний текст джерелаSu, Dan, and Mark Hochstrasser. "A WLM Protein with SUMO-Directed Protease Activity." Molecular and Cellular Biology 30, no. 15 (June 21, 2010): 3734–36. http://dx.doi.org/10.1128/mcb.00673-10.
Повний текст джерелаVethantham, Vasupradha, Nishta Rao, and James L. Manley. "Sumoylation Modulates the Assembly and Activity of the Pre-mRNA 3′ Processing Complex." Molecular and Cellular Biology 27, no. 24 (October 8, 2007): 8848–58. http://dx.doi.org/10.1128/mcb.01186-07.
Повний текст джерелаPsakhye, Ivan, and Dana Branzei. "SMC complexes are guarded by the SUMO protease Ulp2 against SUMO-chain-mediated turnover." Cell Reports 36, no. 5 (August 2021): 109485. http://dx.doi.org/10.1016/j.celrep.2021.109485.
Повний текст джерелаNishida, Tamotsu, and Yoshiji Yamada. "SMT3IP1, a nucleolar SUMO-specific protease, deconjugates SUMO-2 from nucleolar and cytoplasmic nucleophosmin." Biochemical and Biophysical Research Communications 374, no. 2 (September 2008): 382–87. http://dx.doi.org/10.1016/j.bbrc.2008.07.047.
Повний текст джерелаXirodimas, Dimitris P., and David P. Lane. "Targeting a nucleolar SUMO protease for degradation: A mechanism by which ARF induces SUMO conjugation." Cell Cycle 7, no. 21 (November 2008): 3287–91. http://dx.doi.org/10.4161/cc.7.21.7232.
Повний текст джерелаMukhopadhyay, Debaditya, Alexei Arnaoutov, and Mary Dasso. "The SUMO protease SENP6 is essential for inner kinetochore assembly." Journal of Cell Biology 188, no. 5 (March 8, 2010): 681–92. http://dx.doi.org/10.1083/jcb.200909008.
Повний текст джерелаCimarosti, Helena, Emi Ashikaga, Nadia Jaafari, Laura Dearden, Philip Rubin, Kevin A. Wilkinson, and Jeremy M. Henley. "Enhanced SUMOylation and SENP-1 Protein Levels following Oxygen and Glucose Deprivation in Neurones." Journal of Cerebral Blood Flow & Metabolism 32, no. 1 (October 12, 2011): 17–22. http://dx.doi.org/10.1038/jcbfm.2011.146.
Повний текст джерелаBest, Jennifer L., Soula Ganiatsas, Sadhana Agarwal, Austin Changou, Paolo Salomoni, Orian Shirihai, Pamela B. Meluh, Pier Paolo Pandolfi, and Leonard I. Zon. "SUMO-1 Protease-1 Regulates Gene Transcription through PML." Molecular Cell 10, no. 4 (October 2002): 843–55. http://dx.doi.org/10.1016/s1097-2765(02)00699-8.
Повний текст джерелаChung, Sung Soo, Byung Yong Ahn, Min Kim, Hye Hun Choi, Ho Seon Park, Shinae Kang, Sang Gyu Park, et al. "Control of Adipogenesis by the SUMO-Specific Protease SENP2." Molecular and Cellular Biology 30, no. 9 (March 1, 2010): 2135–46. http://dx.doi.org/10.1128/mcb.00852-09.
Повний текст джерелаHu, Chenxi, and Xiaodong Jiang. "The SUMO-specific protease family regulates cancer cell radiosensitivity." Biomedicine & Pharmacotherapy 109 (January 2019): 66–70. http://dx.doi.org/10.1016/j.biopha.2018.10.071.
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