Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Felix J. Metzner"'
Autor:
Felix J. Metzner, Simon J. Wenzl, Michael Kugler, Stefan Krebs, Karl-Peter Hopfner, Katja Lammens
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Schlafen 11 serves as an antiviral restriction factor and a predictive biomarker in cancer. Here, the authors use cryoelectron microscopy and biochemical assays to understand tRNA endoribonuclease and DNA binding functions of human Schlafen 11.
Externí odkaz:
https://doaj.org/article/9eba48c415644da8a478dd70a5e2db50
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Covalent conjugation of endogenous protein complexes offers many opportunities for fundamental and clinical research. Based on a bacterial protein domain that forms a reactive anhydride in the presence of Ca2+, the authors here develop a system that
Externí odkaz:
https://doaj.org/article/ab5f138f64dd46278658c6e3480f8611
Publikováno v:
Nucleic Acids Research
The Schlafen family belongs to the interferon-stimulated genes and its members are involved in cell cycle regulation, T cell quiescence, inhibition of viral replication, DNA-repair and tRNA processing. Here, we present the cryo-EM structure of full-l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd45a92b1ec8be656cedce52c480490d
https://doi.org/10.1093/nar/gkab1278
https://doi.org/10.1093/nar/gkab1278
Autor:
Franziska Kunert, Felix J. Metzner, James Jung, Markus Höpfler, Stephan Woike, Kevin Schall, Dirk Kostrewa, Manuela Moldt, Jia-Xuan Chen, Susanne Bantele, Boris Pfander, Sebastian Eustermann, Karl-Peter Hopfner
The nucleosomal landscape of chromatin depends on the concerted action of chromatin remodelers. The INO80 remodeler specifically places nucleosomes at the boundary of gene regulatory elements, which is proposed to be the result of an ATP-dependent nu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60725623e1a25ab47c5c56b3736c7da7
https://elib.dlr.de/194225/
https://elib.dlr.de/194225/
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Nature Communications
Nature Communications
The Neisseria meningitidis protein FrpC contains a self-processing module (SPM) undergoing autoproteolysis via an aspartic anhydride. Herein, we establish NeissLock, using a binding protein genetically fused to SPM. Upon calcium triggering of SPM, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90d6053c24ef462697a97e1608392390
https://doi.org/10.1038/s41467-021-20963-5
https://doi.org/10.1038/s41467-021-20963-5