Topic
RNA
About: RNA is a research topic. Over the lifetime, 111695 publications have been published within this topic receiving 5475262 citations. The topic is also known as: ribonucleic acid.
Papers published on a yearly basis
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TL;DR: It is found that transfection of expression constructs for MEG3 and its isoforms results in a significant increase in p53 protein levels and dramatically stimulates p 53-dependent transcription from a p53-responsive promoter, supporting the concept that M EG3 functions as a non-coding RNA.
573 citations
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TL;DR: A comparison study of RNA binding in NMR-based and electrospray Ionization Mass Spectrometry-Based methods found that the former showed superior results while the latter showed better results in relation to the latter.
Abstract: 5.1. Binding Sites of the Aminoglycosides 1185 5.2. Importance of Electrostatic Interactions 1185 5.3. Nonionic Interactions 1185 5.4. Pseudo-Base Pair Interactions 1186 5.5. Water-Mediated Contacts 1186 5.6. Shape Complementarity and Conformational Adaptation 1186 6. Assays for Evaluating RNA Binding 1186 6.1. Methods Utilizing Fluorescently Labeled RNA 1186 6.2. NMR-Based Methods 1187 6.3. Electrospray Ionization Mass Spectrometry-Based Methods 1187
573 citations
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TL;DR: TAP, like its yeast homolog Mex67p, is a bona fide mRNA nuclear export mediator and is the second cellular RNA binding protein shown to be directly involved in the export of its target RNA.
572 citations
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TL;DR: The crystal structures of RNase H are reported and it is concluded that two-metal-ion catalysis is a general feature of the superfamily and the catalytic residues of Argonaute are predicted.
571 citations
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TL;DR: A cryo-electron microscopy structure of the RNA-dependent RNA polymerase of SARS-CoV-2 sheds light on coronavirus replication and enables the analysis of the inhibitory mechanisms of candidate antiviral drugs.
Abstract: The new coronavirus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) uses an RNA-dependent RNA polymerase (RdRp) for the replication of its genome and the transcription of its genes1-3. Here we present a cryo-electron microscopy structure of the SARS-CoV-2 RdRp in an active form that mimics the replicating enzyme. The structure comprises the viral proteins non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template-product duplex. The active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity with conserved residues. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged 'sliding poles'. These sliding poles can account for the known processivity of RdRp that is required for replicating the long genome of coronaviruses3. Our results enable a detailed analysis of the inhibitory mechanisms that underlie the antiviral activity of substances such as remdesivir, a drug for the treatment of coronavirus disease 2019 (COVID-19)4.
571 citations