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  1. Article

    Open Access

    UV-induced G4 DNA structures recruit ZRF1 which prevents UV-induced senescence

    Senescence has two roles in oncology: it is known as a potent tumor-suppressive mechanism, which also supports tissue regeneration and repair, it is also known to contribute to reduced patient resilience, whic...

    Alessio De Magis, Michaela Limmer, Venkat Mudiyam, David Monchaud in Nature Communications (2023)

  2. Article

    Open Access

    Clinical and immunological effects of mRNA vaccines in malignant diseases

    In vitro-transcribed messenger RNA-based therapeutics represent a relatively novel and highly efficient class of drugs. Several recently published studies emphasize the potential efficacy of mRNA vaccines in trea...

    Annkristin Heine, Stefan Juranek, Peter Brossart in Molecular Cancer (2021)

  3. Article

    Open Access

    G-quadruplexes: a promising target for cancer therapy

    DNA and RNA can fold into a variety of alternative conformations. In recent years, a particular nucleic acid structure was discussed to play a role in malignant transformation and cancer development. This stru...

    Nils Kosiol, Stefan Juranek, Peter Brossart, Annkristin Heine in Molecular Cancer (2021)

  4. Article

    Open Access

    Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair

    Nucleic acids can fold into G-quadruplex (G4) structures that can fine-tune biological processes. Proteins are required to recognize G4 structures and coordinate their function. Here we identify Zuo1 as a nove...

    Alessio De Magis, Silvia Götz, Mona Hajikazemi, Enikő Fekete-Szücs in Nature Communications (2020)

  5. Article

    Open Access

    Abstracts of the 52nd Workshop for Pediatric Research

    Rhea van den Bruck, Patrick P. Weil, Thomas Ziegenhals in Molecular and Cellular Pediatrics (2017)

  6. No Access

    Article

    Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I

    The innate immune system relies on a series of specific receptors that recognize RNAs that might come from viruses. The structure of the C terminal domain of one such receptor, RIG-I, in complex with 5'ppp-dsR...

    Yanli Wang, Janos Ludwig, Christine Schuberth in Nature Structural & Molecular Biology (2010)

  7. No Access

    Article

    Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes

    The slicer activity of the RNA-induced silencing complex resides within its Argonaute (Ago) component, in which the PIWI domain provides the catalytic residues governing guide-strand mediated site-specific cle...

    Yanli Wang, Stefan Juranek, Haitao Li, Gang Sheng, Greg S. Wardle, Thomas Tuschl in Nature (2009)

  8. No Access

    Article

    Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex

    Here we report on a 3.0 Å crystal structure of a ternary complex of wild-type Thermus thermophilus argonaute bound to a 5′-phosphorylated 21-nucleotide guide DNA and a 20-nucleotide target RNA containing cleavage...

    Yanli Wang, Stefan Juranek, Haitao Li, Gang Sheng, Thomas Tuschl in Nature (2008)

  9. No Access

    Article

    Structure of the guide-strand-containing argonaute silencing complex

    The slicer activity of the RNA-induced silencing complex is associated with argonaute, the RNase H-like PIWI domain of which catalyses guide-strand-mediated sequence-specific cleavage of target messenger RNA. ...

    Yanli Wang, Gang Sheng, Stefan Juranek, Thomas Tuschl, Dinshaw J. Patel in Nature (2008)

  10. No Access

    Article

    Cell cycle-dependent regulation of telomere tethering in the nucleus

    It is well established that telomeres are tethered in the eukaryotic nucleus, but a detailed analysis of the regulation of telomere attachment throughout the cell cycle is still lacking. We show here that the ...

    Katrin Paeschke, Stefan Juranek, Daniela Rhodes, Hans Joachim Lipps in Chromosome Research (2008)

  11. No Access

    Article

    Telomerase recruitment by the telomere end binding protein-β facilitates G-quadruplex DNA unfolding in ciliates

    The telomeric G-overhangs of the ciliate Stylonychia lemnae fold into a G-quadruplex DNA structure in vivo. Telomeric G-quadruplex formation requires the presence of two telomere end binding proteins, TEBPα and T...

    Katrin Paeschke, Stefan Juranek, Tomas Simonsson in Nature Structural & Molecular Biology (2008)