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Rolf Thermann

Researcher at Vita-Salute San Raffaele University

Publications -  8
Citations -  1516

Rolf Thermann is an academic researcher from Vita-Salute San Raffaele University. The author has contributed to research in topics: Untranslated region & Messenger RNA. The author has an hindex of 8, co-authored 8 publications receiving 1456 citations. Previous affiliations of Rolf Thermann include Humboldt University of Berlin.

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Binary specification of nonsense codons by splicing and cytoplasmic translation

TL;DR: It is demonstrated that cells distinguish a premature termination codon within the β‐globin mRNA from the physiological translation termination codons by a two‐step specification mechanism, and a common principle for nonsense‐mediated decay from yeast to man is proposed.
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Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation

Rolf Thermann, +1 more
- 14 Jun 2007 - 
TL;DR: Results directly show the inhibition of m7GpppG cap-mediated translation initiation as the mechanism of miR2 function, and uncover pseudo-polysomal messenger ribonucleoprotein assemblies that may help to explain earlier findings.
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A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain.

TL;DR: A repetitive motif within Tas3, termed the 'Argonaute hook', is described that is conserved from yeast to humans and binds Ago proteins through their PIWI domains in vitro and in vivo and may be important regulatory components of effector complexes in RNA interference.
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Mechanism of translational regulation by miR-2 from sites in the 5′ untranslated region or the open reading frame

TL;DR: This work shows that specific translational regulation is elicited in vitro and in vivo not only from the 3'UTR, but equally effectively from six Drosophila miR-2-binding sites in the 5' UTR or the ORF.
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microRNA-Mediated Messenger RNA Deadenylation Contributes to Translational Repression in Mammalian Cells

TL;DR: A dual role of deadenylation in miRNA function is suggested: it contributes to translational repression as well as mRNA decay and is thus critically involved in establishing the quantitatively appropriate physiological response to miRNAs.