Статті в журналах з теми "Ubiquitin-Specific Peptidase 1"
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Raimondi, Marzia, Daniela Cesselli, Carla Di Loreto, Francesco La Marra, Claudio Schneider, and Francesca Demarchi. "USP1 (ubiquitin specific peptidase 1) targets ULK1 and regulates its cellular compartmentalization and autophagy." Autophagy 15, no. 4 (October 29, 2018): 613–30. http://dx.doi.org/10.1080/15548627.2018.1535291.
Повний текст джерелаZhang, Jinghui, Chenchang Liu, and Guofeng You. "Ubiquitin-specific peptidase 8 regulates the trafficking and stability of the human organic anion transporter 1." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 12 (December 2020): 129701. http://dx.doi.org/10.1016/j.bbagen.2020.129701.
Повний текст джерелаShanmugam, Ilanchezhian, Mohammad Abbas, Farhan Ayoub, Susan Mirabal, Manal Bsaili, Erin K. Caulder, David M. Weinstock, Alan E. Tomkinson, Robert Hromas, and Monte Shaheen. "Ubiquitin-specific Peptidase 20 Regulates Rad17 Stability, Checkpoint Kinase 1 Phosphorylation and DNA Repair by Homologous Recombination." Journal of Biological Chemistry 289, no. 33 (June 12, 2014): 22739–48. http://dx.doi.org/10.1074/jbc.m114.550459.
Повний текст джерелаAttaix, Didier, Sophie Ventadour, Audrey Codran, Daniel Béchet, Daniel Taillandier, and Lydie Combaret. "The ubiquitin–proteasome system and skeletal muscle wasting." Essays in Biochemistry 41 (October 1, 2005): 173–86. http://dx.doi.org/10.1042/bse0410173.
Повний текст джерелаNakae, Aya, Michiko Kodama, Toru Okamoto, Makoto Tokunaga, Hiroko Shimura, Kae Hashimoto, Kenjiro Sawada, et al. "Ubiquitin specific peptidase 32 acts as an oncogene in epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate farnesyltransferase 1." Biochemical and Biophysical Research Communications 552 (May 2021): 120–27. http://dx.doi.org/10.1016/j.bbrc.2021.03.049.
Повний текст джерелаOgawa, Masahiro, Tomoya Kitakaze, Naoki Harada, and Ryoichi Yamaji. "Female-specific regulation of skeletal muscle mass by USP19 in young mice." Journal of Endocrinology 225, no. 3 (April 21, 2015): 135–45. http://dx.doi.org/10.1530/joe-15-0128.
Повний текст джерелаYu, Zhongxia, Hui Song, Mutian Jia, Jintao Zhang, Wenwen Wang, Qi Li, Lining Zhang, and Wei Zhao. "USP1–UAF1 deubiquitinase complex stabilizes TBK1 and enhances antiviral responses." Journal of Experimental Medicine 214, no. 12 (November 14, 2017): 3553–63. http://dx.doi.org/10.1084/jem.20170180.
Повний текст джерелаHu, Bin, Chunhua Ge та Chunqing Zhu. "Ubiquitin-specific peptidase 18 negatively regulates and inhibits lipopolysaccharide-induced sepsis by targeting transforming growth factor-β-activated kinase 1 activity". International Immunology 33, № 9 (11 червня 2021): 461–68. http://dx.doi.org/10.1093/intimm/dxab029.
Повний текст джерелаYasunaga, J., F. C. Lin, X. Lu, and K. T. Jeang. "Ubiquitin-Specific Peptidase 20 Targets TRAF6 and Human T Cell Leukemia Virus Type 1 Tax To Negatively Regulate NF- B Signaling." Journal of Virology 85, no. 13 (April 27, 2011): 6212–19. http://dx.doi.org/10.1128/jvi.00079-11.
Повний текст джерелаJingjing, Wu, Guo Wenzheng, Wen Donghua, Hou Guangyu, Zhou Aiping, and Wu Wenjuan. "Deubiquitination and stabilization of programmed cell death ligand 1 by ubiquitin-specific peptidase 9, X-linked in oral squamous cell carcinoma." Cancer Medicine 7, no. 8 (July 10, 2018): 4004–11. http://dx.doi.org/10.1002/cam4.1675.
Повний текст джерелаMeuwissen, Marije E. C., Rachel Schot, Sofija Buta, Grétel Oudesluijs, Sigrid Tinschert, Scott D. Speer, Zhi Li, et al. "Human USP18 deficiency underlies type 1 interferonopathy leading to severe pseudo-TORCH syndrome." Journal of Experimental Medicine 213, no. 7 (June 20, 2016): 1163–74. http://dx.doi.org/10.1084/jem.20151529.
Повний текст джерелаSingh, Rahul, Sonali Deshmukh, Ashwani Kumar, Venuka Durani Goyal, and Ravindra D. Makde. "Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase." Acta Crystallographica Section F Structural Biology Communications 76, no. 10 (September 16, 2020): 488–94. http://dx.doi.org/10.1107/s2053230x20011875.
Повний текст джерелаXu, Gufeng, Xiaojie Tan, Hongmei Wang, Wenjing Sun, Yi Shi, Susan Burlingame, Xue Gu та ін. "Ubiquitin-specific Peptidase 21 Inhibits Tumor Necrosis Factor α-induced Nuclear Factor κB Activation via Binding to and Deubiquitinating Receptor-interacting Protein 1". Journal of Biological Chemistry 285, № 2 (12 листопада 2009): 969–78. http://dx.doi.org/10.1074/jbc.m109.042689.
Повний текст джерелаZhang, Yana, and Deyu Fang. "USP22 controls iNKT immunity partially through MED1-mediated suppression of target-specific histone H2A monoubiquitination." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 78.1. http://dx.doi.org/10.4049/jimmunol.204.supp.78.1.
Повний текст джерелаYu, Wen-Chun, Ren-Yeong Huang, and Tz-Chong Chou. "Oligo-Fucoidan Improves Diabetes-Induced Renal Fibrosis via Activation of Sirt-1, GLP-1R, and Nrf2/HO-1: An In Vitro and In Vivo Study." Nutrients 12, no. 10 (October 8, 2020): 3068. http://dx.doi.org/10.3390/nu12103068.
Повний текст джерелаPark, Jung-Eun, Thị Xuân Thùy Trần, Nayoung Park, Jeonghun Yeom, Kyunggon Kim, and Min-Ji Kang. "The Function of Drosophila USP14 in Endoplasmic Reticulum Stress and Retinal Degeneration in a Model for Autosomal Dominant Retinitis Pigmentosa." Biology 9, no. 10 (October 12, 2020): 332. http://dx.doi.org/10.3390/biology9100332.
Повний текст джерелаWitty, James, Elisa Aguilar-Martinez, and Andrew D. Sharrocks. "SENP1 participates in the dynamic regulation of Elk-1 SUMOylation." Biochemical Journal 428, no. 2 (May 13, 2010): 247–54. http://dx.doi.org/10.1042/bj20091948.
Повний текст джерелаMussell, Ashley, He Shen, Yanmin Chen, Michalis Mastri, Kevin H. Eng, Wiam Bshara, Costa Frangou, and Jianmin Zhang. "USP1 Regulates TAZ Protein Stability Through Ubiquitin Modifications in Breast Cancer." Cancers 12, no. 11 (October 23, 2020): 3090. http://dx.doi.org/10.3390/cancers12113090.
Повний текст джерелаKishi, Kasane, Aya Uchida, Hinako M. Takase, Hitomi Suzuki, Masamichi Kurohmaru, Naoki Tsunekawa, Masami Kanai-Azuma, Stephen A. Wood, and Yoshiakira Kanai. "Spermatogonial deubiquitinase USP9X is essential for proper spermatogenesis in mice." Reproduction 154, no. 2 (August 2017): 135–43. http://dx.doi.org/10.1530/rep-17-0184.
Повний текст джерелаChang, Tsung-Hsien, Songxiao Xu, Prafullakumar Tailor, Tomohiko Kanno, and Keiko Ozato. "The Small Ubiquitin-like Modifier-Deconjugating Enzyme Sentrin-Specific Peptidase 1 Switches IFN Regulatory Factor 8 from a Repressor to an Activator during Macrophage Activation." Journal of Immunology 189, no. 7 (August 31, 2012): 3548–56. http://dx.doi.org/10.4049/jimmunol.1201104.
Повний текст джерелаWatson, Christopher Mark, Laura A. Crinnion, Lindsay Gleghorn, William G. Newman, Rajkumar Ramesar, Peter Beighton, and Gillian A. Wallis. "Identification of a mutation in the ubiquitin-fold modifier 1-specific peptidase 2 gene, UFSP2, in an extended South African family with Beukes hip dysplasia." South African Medical Journal 105, no. 7 (September 21, 2015): 558. http://dx.doi.org/10.7196/samjnew.7917.
Повний текст джерелаZheng, Lewei, Qian Yang, Chengxin Li, Gaoran Xu, Qianqian Yuan, Jinxuan Hou, and Gaosong Wu. "Ubiquitin-Specific Peptidase 8 Modulates Cell Proliferation and Induces Cell Cycle Arrest and Apoptosis in Breast Cancer by Stabilizing Estrogen Receptor Alpha." Journal of Oncology 2023 (January 6, 2023): 1–16. http://dx.doi.org/10.1155/2023/8483325.
Повний текст джерелаWu, Xingxin, Tao Tan, and Qiang Xu. "Metastatic colorectal cancer cells harness nonsense-mediated mRNA decay for immune evasion." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 242.17. http://dx.doi.org/10.4049/jimmunol.204.supp.242.17.
Повний текст джерелаYongganmg, Liu, and Gao Shizheng. "A novel porcine gene, USP7, differentially expressed in the musculus longissimus from Wujin and Large White pigs." Czech Journal of Animal Science 55, No. 1 (January 25, 2010): 37–41. http://dx.doi.org/10.17221/1709-cjas.
Повний текст джерелаShang, Zesen, Jiao Zhao, Qi Zhang, Cheng Cao, Shanshan Tian, Kai Zhang, Ling Liu, Lei Shi, Na Yu, and Shangda Yang. "USP9X-mediated deubiquitination of B-cell CLL/lymphoma 9 potentiates Wnt signaling and promotes breast carcinogenesis." Journal of Biological Chemistry 294, no. 25 (May 9, 2019): 9844–57. http://dx.doi.org/10.1074/jbc.ra119.007655.
Повний текст джерелаChung, Sung Soo, Byung Yong Ahn, Min Kim, Jun Ho Kho, Hye Seung Jung та Kyong Soo Park. "SUMO modification selectively regulates transcriptional activity of peroxisome-proliferator-activated receptor γ in C2C12 myotubes". Biochemical Journal 433, № 1 (15 грудня 2010): 155–61. http://dx.doi.org/10.1042/bj20100749.
Повний текст джерелаLiang, Fengshan, Adam S. Miller, Caroline Tang, David Maranon, Elizabeth A. Williamson, Robert Hromas, Claudia Wiese, Weixing Zhao, Patrick Sung, and Gary M. Kupfer. "The DNA-binding activity of USP1-associated factor 1 is required for efficient RAD51-mediated homologous DNA pairing and homology-directed DNA repair." Journal of Biological Chemistry 295, no. 24 (April 29, 2020): 8186–94. http://dx.doi.org/10.1074/jbc.ra120.013714.
Повний текст джерелаPariano, Marilena, Stefania Pieroni, Antonella De Luca, Rossana G. Iannitti, Monica Borghi, Matteo Puccetti, Stefano Giovagnoli, et al. "Anakinra Activates Superoxide Dismutase 2 to Mitigate Inflammasome Activity." International Journal of Molecular Sciences 22, no. 12 (June 18, 2021): 6531. http://dx.doi.org/10.3390/ijms22126531.
Повний текст джерелаGarcía-Santisteban, Iraia, Sonia Bañuelos, and Jose A. Rodríguez. "A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family." Biochemical Journal 441, no. 1 (December 14, 2011): 209–17. http://dx.doi.org/10.1042/bj20111300.
Повний текст джерелаWu, Suwen, Yutong Cui, Huanqiang Zhao, Xirong Xiao, Lili Gong, Huangfang Xu, Qiongjie Zhou, Duan Ma, and Xiaotian Li. "Trophoblast Exosomal UCA1 Induces Endothelial Injury through the PFN1-RhoA/ROCK Pathway in Preeclampsia: A Human-Specific Adaptive Pathogenic Mechanism." Oxidative Medicine and Cellular Longevity 2022 (September 15, 2022): 1–19. http://dx.doi.org/10.1155/2022/2198923.
Повний текст джерелаMetzendorf, Christoph, Katharina Wineberger, Jenny Rausch, Antonio Cigliano, Kristin Peters, Baodong Sun, Daniela Mennerich, et al. "Transcriptomic and Proteomic Analysis of Clear Cell Foci (CCF) in the Human Non-Cirrhotic Liver Identifies Several Differentially Expressed Genes and Proteins with Functions in Cancer Cell Biology and Glycogen Metabolism." Molecules 25, no. 18 (September 10, 2020): 4141. http://dx.doi.org/10.3390/molecules25184141.
Повний текст джерелаWu, Danyang, Rong Yuan, Lian Zhang, and Meng Sun. "USP13 reduces septic mediated cardiomyocyte oxidative stress and inflammation by inducing Nrf2." Allergologia et Immunopathologia 51, no. 2 (March 1, 2023): 160–67. http://dx.doi.org/10.15586/aei.v51i2.813.
Повний текст джерелаSuzuki, Keisuke, Junko Shibato, Randeep Rakwal, Masahiko Takaura, Ryotaro Hotta, and Yoshinori Masuo. "Biomarkers in the Rat Hippocampus and Peripheral Blood for an Early Stage of Mental Disorders Induced by Water Immersion Stress." International Journal of Molecular Sciences 24, no. 4 (February 5, 2023): 3153. http://dx.doi.org/10.3390/ijms24043153.
Повний текст джерелаDhingra, Rimpy, Inna Rabinovich-Nikitin, Sonny Rothman, Matthew Guberman, Hongying Gang, Victoria Margulets, Davinder S. Jassal, et al. "Proteasomal Degradation of TRAF2 Mediates Mitochondrial Dysfunction in Doxorubicin-Cardiomyopathy." Circulation 146, no. 12 (September 20, 2022): 934–54. http://dx.doi.org/10.1161/circulationaha.121.058411.
Повний текст джерелаKwakkel, J., H. C. van Beeren, M. T. Ackermans, M. C. Platvoet-ter Schiphorst, E. Fliers, W. M. Wiersinga, and A. Boelen. "Skeletal muscle deiodinase type 2 regulation during illness in mice." Journal of Endocrinology 203, no. 2 (August 5, 2009): 263–70. http://dx.doi.org/10.1677/joe-09-0118.
Повний текст джерелаBai, Mixue, Yingying Che, Kun Lu, and Lin Fu. "Analysis of deubiquitinase OTUD5 as a biomarker and therapeutic target for cervical cancer by bioinformatic analysis." PeerJ 8 (June 30, 2020): e9146. http://dx.doi.org/10.7717/peerj.9146.
Повний текст джерелаZhou, Jiangqiao, Tao Qiu, Tianyu Wang, Zhongbao Chen, Xiaoxiong Ma, Long Zhang, and Jilin Zou. "USP4 deficiency exacerbates hepatic ischaemia/reperfusion injury via TAK1 signalling." Clinical Science 133, no. 2 (January 2019): 335–49. http://dx.doi.org/10.1042/cs20180959.
Повний текст джерелаYang, Yanli, Jun Li, and Yinghua Geng. "Exosomes derived from chronic lymphocytic leukaemia cells transfer miR-146a to induce the transition of mesenchymal stromal cells into cancer-associated fibroblasts." Journal of Biochemistry 168, no. 5 (July 10, 2020): 491–98. http://dx.doi.org/10.1093/jb/mvaa064.
Повний текст джерелаXiang, Yijin, Shaoyan Zhang, Jia Lu, Wen Zhang, Min Cai, Dongze Qiu та Dingfang Cai. "USP9X promotes LPS-induced pulmonary epithelial barrier breakdown and hyperpermeability by activating an NF-κBp65 feedback loop". American Journal of Physiology-Cell Physiology 317, № 3 (1 вересня 2019): C534—C543. http://dx.doi.org/10.1152/ajpcell.00094.2019.
Повний текст джерелаPlaué, S., S. Muller, and M. H. van Regenmortel. "A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies." Journal of Experimental Medicine 169, no. 5 (May 1, 1989): 1607–17. http://dx.doi.org/10.1084/jem.169.5.1607.
Повний текст джерелаNiederkorn, Madeline, Melinda Varney, Molly A. Smith, Ruhikanta A. Meetei, and Daniel T. Starczynowski. "Tifab, a Del(5q) MDS/AML Gene, Regulates USP15 Activity and p53." Blood 128, no. 22 (December 2, 2016): 1130. http://dx.doi.org/10.1182/blood.v128.22.1130.1130.
Повний текст джерелаde Oyarzabal, Eleane, Lourdes García-García, Claudia Rangel-Escareño, Leticia Ferreyra-Reyes, Lorena Orozco, María Teresa Herrera, Claudia Carranza, et al. "Expression of USP18 and IL2RA Is Increased in Individuals Receiving Latent Tuberculosis Treatment with Isoniazid." Journal of Immunology Research 2019 (December 6, 2019): 1–13. http://dx.doi.org/10.1155/2019/1297131.
Повний текст джерелаHuang, Limin, Chaoquan Hu, Hui Cao, Xiaoliang Wu, Rongpin Wang, He Lu, Hong Li, and Hui Chen. "MicroRNA-29c Increases the Chemosensitivity of Pancreatic Cancer Cells by Inhibiting USP22 Mediated Autophagy." Cellular Physiology and Biochemistry 47, no. 2 (2018): 747–58. http://dx.doi.org/10.1159/000490027.
Повний текст джерелаAgarwal, Srishti, Priyanka Mishra, Gururaj Shivange, Naveena Kodipelli, María Moros, Jesús M. de la Fuente, and Roy Anindya. "Citrate-capped gold nanoparticles for the label-free detection of ubiquitin C-terminal hydrolase-1." Analyst 140, no. 4 (2015): 1166–73. http://dx.doi.org/10.1039/c4an01935k.
Повний текст джерелаLamback, Elisa Baranski, Carlos Henrique de Azeredo Lima, Renan Lyra Miranda, Alexandro Guterres, Felipe Andreiuolo, Luiz Eduardo Armondi Wildemberg, and Monica Roberto Gadelha. "USP8 Somatic Mutations in Cushing’s Disease and Silent Corticotropinomas." Journal of the Endocrine Society 5, Supplement_1 (May 1, 2021): A651. http://dx.doi.org/10.1210/jendso/bvab048.1328.
Повний текст джерелаZhu, Shaochun, Anna Wuolikainen, Junfang Wu, Anders Öhman, Gunnar Wingsle, Thomas Moritz, Peter M. Andersen, Lars Forsgren, and Miles Trupp. "Targeted Multiple Reaction Monitoring Analysis of CSF Identifies UCHL1 and GPNMB as Candidate Biomarkers for ALS." Journal of Molecular Neuroscience 69, no. 4 (November 12, 2019): 643–57. http://dx.doi.org/10.1007/s12031-019-01411-y.
Повний текст джерелаFunato, Kotaro, Naznin Haq, Yezhou Sun, Jin Chen, Greg Khitrov, Weijia Zhang, and David W. Sternberg. "Translational Regulation of Gene Expression by Cytoplasmic Nucleophosmin in AML: A Global Evaluation of RNA’s Differentially Recruited to Polyribosomes." Blood 110, no. 11 (November 16, 2007): 720. http://dx.doi.org/10.1182/blood.v110.11.720.720.
Повний текст джерелаPimentel, Agustin, Andrea O'Hara, Rosangela de Lima, Suying Xu, Ngoc Toomey, Carlos Brites, Yao-Shan Fan, and Juan Carlos Ramos. "Distinct Patterns of Genomic Alterations in Adult T-Cell Leukemia-Lymphoma Endemic in the Western World." Blood 124, no. 21 (December 6, 2014): 1698. http://dx.doi.org/10.1182/blood.v124.21.1698.1698.
Повний текст джерелаStachorski, Lena, Veera Raghavan Thangapandi, Dirk Reinhardt, and Jan-Henning Klusmann. "Characterization Of Oncogenes On Chromosome 21 Identified By shRNA-Based Viability Screening." Blood 122, no. 21 (November 15, 2013): 1201. http://dx.doi.org/10.1182/blood.v122.21.1201.1201.
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.
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