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PKR activation by noncanonical ligands: a 5′-triphosphate requirement versus antisense contamination
Publikováno v:
RNA
Protein kinase RNA-activated (PKR) is an interferon-inducible kinase that is potently activated by long double-stranded RNA (dsRNA). In a previous study, we found that snoRNAs exhibit increased association with PKR in response to metabolic stress. Wh
Autor:
Elena Plessa, Anthony Bougas, Yury S. Polikanov, George P. Dinos, Maxim S. Svetlov, Marios G. Krokidis, Chih-Wei Chen
Publikováno v:
RNA
The 70S ribosome is a major target for antibacterial drugs. Two of the classical antibiotics, chloramphenicol (CHL) and erythromycin (ERY), competitively bind to adjacent but separate sites on the bacterial ribosome: the catalytic peptidyl transferas
Autor:
Shigeyuki Yokoyama, Sakurako Goto-Ito, Georges Lahoud, Ya-Ming Hou, Ken-ichi Yoshida, Takuhiro Ito
Publikováno v:
RNA. 17:1236-1246
Bacterial TrmD and eukaryotic-archaeal Trm5 form a pair of analogous tRNA methyltransferase that catalyze methyl transfer from S-adenosyl methionine (AdoMet) to N1 of G37, using catalytic motifs that share no sequence or structural homology. Here we
Autor:
Daniel M. Dupont, Frédéric Ducongé, Jeppe B. Madsen, Bertrand Tavitian, Roland K. Hartmann, Jørgen Kjems, Peter A. Andreasen
Publikováno v:
Dupont, D M, Madsen, J B, Hartmann, R K, Tavitian, B, Ducongé, F, Kjems, J & Andreasen, P A 2010, ' Serum-stable RNA aptamers to urokinase-type plasminogen activator blocking receptor binding ', RNA, vol. 16, no. 12, pp. 2360-9 . https://doi.org/10.1261/rna.2338210
The serine proteinase urokinase-type plasminogen activator (uPA) is widely recognized as a potential target for anticancer therapy. Its association with cell surfaces through the uPA receptor (uPAR) is central to its function and plays an important r
Publikováno v:
RNA. 8:1393-1400
Aminoglycosides are known to bind and perturb the function of catalytic RNA. Here we show that they also are potent inhibitors of protein-based catalysis using Escherichia coli Klenow polymerase (pol) and mammalian poly(A)-specific ribonuclease (PARN