Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Abul Arif"'
Autor:
Nickolas B. Reimer, Cynthia B. Alander, Marc F. Hansen, Abul Arif, Hicham Drissi, David K. Monson
Publikováno v:
Techniques in Orthopaedics. 34:275-286
Autor:
Hicham Drissi, Umesh Gangishetti, Pallavi Bhattaram, Sergio Ramirez-Perez, Kyle Jones, Abul Arif
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Scientific Reports
Scientific Reports
Fibroblast-like synoviocytes (FLS) play a critical role in the pathogenesis of rheumatoid arthritis (RA). Chronic inflammation induces transcriptomic and epigenetic modifications that imparts a persistent catabolic phenotype to the FLS, despite their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71c293f4e57921607244f6965946f824
https://doi.org/10.1101/2020.06.27.171348
https://doi.org/10.1101/2020.06.27.171348
Autor:
Dalia Halawani, Jie Chen, Sara C. Kozma, Arnab China, George Thomas, Paul L. Fox, J. Mark Brown, Jie Jia, Xiaoxia Li, Alka A. Potdar, Abul Arif, Jessica Sacks, Kommireddy Vasu, Fulvia Terenzi
Publikováno v:
Nature
Recercat. Dipósit de la Recerca de Catalunya
instname
Dipòsit Digital de la UB
Universidad de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
instname
Dipòsit Digital de la UB
Universidad de Barcelona
Metabolic pathways that contribute to adiposity and ageing are activated by the mammalian target of rapamycin complex 1 (mTORC1) and p70 ribosomal protein S6 kinase 1 (S6K1) axis. However, known mTORC1-S6K1 targets do not account for observed loss-of
Autor:
Myung Hee Kim, Jungwon Hwang, Jae U. Jung, Hyun Kwan Kim, Tae-Hwan Kim, Chul-Ho Lee, Jong-Hwan Kim, Jong-Soo Lee, Abul Arif, Seong Jun Park, Eun-Young Lee, Yong-Hoon Kim, Hyun-Cheol Lee, Sunghoon Kim, Seon-Young Kim, Young Ki Choi, Paul L. Fox, Cheolju Lee, Song Yee Jang, Jae-Hoon Kim
Publikováno v:
Nature immunology, vol 17, iss 11
The mammalian cytoplasmic multi-tRNA synthetase complex (MSC) is a depot system that regulates non-translational cellular functions. Here we found that the MSC component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral inf
Autor:
Paul L. Fox, Stanley L. Hazen, Kommireddy Vasu, Vitaliy Pipich, Peng Yao, Arnab China, Celalettin Topbas, Joseph A. DiDonato, Dalia Halawani, Abul Arif, Valentin Gogonea
Publikováno v:
The journal of biological chemistry 293(23), 8843-8860 (2018). doi:10.1074/jbc.M117.807503
Aminoacyl-tRNA synthetases are ubiquitous, evolutionarily conserved enzymes catalyzing the conjugation of amino acids onto cognate tRNAs. During eukaryotic evolution, tRNA synthetases have been the targets of persistent structural modifications. Thes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::450b027a1f09870ef6b96aa674ff1c2c
https://hdl.handle.net/2128/20157
https://hdl.handle.net/2128/20157
Publikováno v:
Wiley Interdisciplinary Reviews: RNA
The interferon (IFN)-γ-activated inhibitor of translation (GAIT) system directs transcript-selective translational control of functionally related genes. In myeloid cells, IFN-γ induces formation of a multiprotein GAIT complex that binds structural
Publikováno v:
Molecular Cell. 73:446-457.e6
Multisite phosphorylation of kinases can induce on-off or graded regulation of catalytic activity; however, its influence on substrate specificity remains unclear. Here we show multisite phosphorylation of ribosomal protein S6 kinase 1 (S6K1) alters
Autor:
Paul L. Fox, Abul Arif
Publikováno v:
Cell Cycle. 16:2239-2240
Glutamyl(E)-prolyl(P) tRNA Synthetase (EPRS) is an exception to the “one amino acid–one aminoacyl-tRNA synthetase (AARS)” rule. Class I ERS and class II PRS are fused into a single polypeptide that...
Heterotrimeric GAIT Complex Drives Transcript-Selective Translation Inhibition in Murine Macrophages
Publikováno v:
Molecular and Cellular Biology. 32:5046-5055
The gamma interferon (IFN-γ)-activated inhibitor of translation (GAIT) complex in human myeloid cells is heterotetrameric, consisting of glutamyl-prolyl-tRNA synthetase (EPRS), NS1-associated protein 1 (NSAP1), ribosomal protein L13a, and glyceralde
Publikováno v:
Methods (San Diego, Calif.). 113
Phosphorylation of many aminoacyl tRNA synthetases (AARSs) has been recognized for decades, but the contribution of post-translational modification to their primary role in tRNA charging and decryption of genetic code remains unclear. In contrast, ph