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281por Laliotis, Georgios I., Chavdoula, Evangelia, Paraskevopoulou, Maria D., Kaba, Abdul, La Ferlita, Alessandro, Singh, Satishkumar, Anastas, Vollter, Nair, Keith A., Orlacchio, Arturo, Taraslia, Vasiliki, Vlachos, Ioannis, Capece, Marina, Hatzigeorgiou, Artemis, Palmieri, Dario, Tsatsanis, Christos, Alaimo, Salvatore, Sehgal, Lalit, Carbone, David P., Coppola, Vincenzo, Tsichlis, Philip N.Enlace del recurso
Publicado 2022
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282por Izumikawa, Keiichi, Nobe, Yuko, Ishikawa, Hideaki, Yamauchi, Yoshio, Taoka, Masato, Sato, Ko, Nakayama, Hiroshi, Simpson, Richard J, Isobe, Toshiaki, Takahashi, Nobuhiro“…Depletion of TDP-43, in contrast, shifted the localization of these C/D scaRNAs, mainly into the nucleolus, as well as destabilizing scaRNA2, and reduced the site-specific 2′-O-methylation of U1 and U2 snRNAs, including at 70A in U1 snRNA and, 19G, 25G, 47U and 61C in U2 snRNA. …”
Publicado 2019
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283“…We present here a very rare case with PMF and PNH with JAK2 V617F, U2AF1 and SETBP1 mutations at the time of diagnosis. …”
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284“…Recent work has identified cancer-associated U2AF35 missense mutations in two zinc-finger (ZnF) domains, but little is known about Q157R/P substitutions within the second ZnF. …”
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285“…To investigate the role of the RING domain of Mdm2 and MdmX, an analysis of the distinct functionalities of individual RING domains of the Mdm proteins on p53 regulation was conducted in human osteosarcoma (U2OS) cell line. Mdm2 RING domain was observed mainly localized in the cell nucleus, contrasting the localization of MdmX RING domain in the cytoplasm. …”
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286por Lu, Ko-Hsiu, Wu, Heng-Hsiung, Lin, Renn-Chia, Lin, Ya-Chiu, Lu, Peace Wun-Ang, Yang, Shun-Fa, Yang, Jia-Sin“…L48H37 decreased the phosphorylation of STAT3, JAK1, JAK2, and JAK3 in U2OS cells, but did not affect the phosphorylation of ERK, JNK, p38, and Akt. …”
Publicado 2020
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287por Ortuño-Pineda, Carlos, Galindo-Rosales, José Manuel, Calderón-Salinas, José Victor, Villegas-Sepúlveda, Nicolás, Saucedo-Cárdenas, Odila, De Nova-Ocampo, Mónica, Valdés, Jesús“…Our results evidenced novel hnRNP H and U2AF65 functions: respectively, U2AF65-recruiting to a 5'ss in humans and the hnRNP H-displacing function from two juxtaposed GGGG codes.…”
Publicado 2012
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288“…The first stable complex formed during the assembly of spliceosomes onto pre-mRNA substrates in mammals includes U1 snRNP, which recognizes the 5′ splice site, and the splicing factors SF1 and U2AF, which bind the branch point sequence, polypyrimidine tract, and 3′ splice site. …”
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289por Niehus, Svenja E., Allister, Aldrige B., Hoffmann, Andrea, Wiehlmann, Lutz, Tamura, Teruko, Tran, Doan Duy Hai“…The second intron did not splice out in a U2 dependent manner and EVA1A mRNA is not exported. …”
Publicado 2019
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290“…Next, our experiments found that circFOXP1 upregulated U2AF2 expression via sponging miR-423-5p in RCC cells. …”
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291“…The dysregulation of U2 Small Nuclear RNA Auxiliary Factor 2 (U2AF2) is associated with malignant behaviors of multiple types of tumors. …”
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292por Schneider, Cornelius, Agafonov, Dmitry E., Schmitzová, Jana, Hartmuth, Klaus, Fabrizio, Patrizia, Lührmann, Reinhard“…A comparison of the B(act) crosslinking pattern versus that of B* and C complexes revealed that U2 and RES protein interactions with the intron are dynamic. …”
Publicado 2015
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293por Li, Xiaomeng, Roselló, Yannick, Yao, Yang-Rong, Zhuang, Jiaxin, Zhang, Xingxing, Rodríguez-Fortea, Antonio, de Graaf, Coen, Echegoyen, Luis, Poblet, Josep M., Chen, Ning“…For the first time, an actinide nitride clusterfullerene, U(2)N@I(h)(7)-C(80), is synthesized and fully characterized by X-ray single crystallography and multiple spectroscopic methods. …”
Publicado 2020
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294“…All three RNA site mutations of SmD3 were lethal in cells lacking the U2 snRNP subunit Lea1. Benign C-terminal truncations of SmD3 were dead in the absence of Mud2 or Lea1 and barely viable in the absence of Nam8 or Mud1. …”
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295Publicado 2017“…METHODS: Mutational analysis of splicing factor 3B subunit 1 (SF3B1) (K700E), U2 small nuclear RNA auxiliary factor 1 (U2AF1) (S34, Q157P) and serine/arginine-rich splicing factor 2 (SRSF2) (P95) in 118, de novo MDS and related diseases were separately performed by using polymerase chain reaction (PCR) followed by sequence analysis. …”
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300por Niu, Ning-Kui, Wang, Zi-Li, Pan, Shu-Ting, Ding, Hui-Qiang, Au, Giang HT, He, Zhi-Xu, Zhou, Zhi-Wei, Xiao, Guozhi, Yang, Yin-Xue, Zhang, Xueji, Yang, Tianxin, Chen, Xiao-Wu, Qiu, Jia-Xuan, Zhou, Shu-Feng“…This study aimed to investigate the effects of ALS on the cell growth, apoptosis, autophagy, and epithelial to mesenchymal transition (EMT) and the underlying mechanisms in two human OS cell lines U-2 OS and MG-63. The results showed that ALS had potent growth inhibitory, pro-apoptotic, pro-autophagic, and EMT inhibitory effects on U-2 OS and MG-63 cells. …”
Publicado 2015
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