Zobrazeno 1 - 10
of 592
pro vyhledávání: '"A. C. Wahl"'
Autor:
Nelly Said, Mark Finazzo, Tarek Hilal, Bing Wang, Tim Luca Selinger, Daniela Gjorgjevikj, Irina Artsimovitch, Markus C. Wahl
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract Transcription termination factor ρ is a hexameric, RNA-dependent NTPase that can adopt active closed-ring and inactive open-ring conformations. The Sm-like protein Rof, a homolog of the RNA chaperone Hfq, inhibits ρ-dependent termination i
Externí odkaz:
https://doaj.org/article/ef0791a398054336b30478c4f1f54dd0
Autor:
Philipp K. Zuber, Nelly Said, Tarek Hilal, Bing Wang, Bernhard Loll, Jorge González-Higueras, César A. Ramírez-Sarmiento, Georgiy A. Belogurov, Irina Artsimovitch, Markus C. Wahl, Stefan H. Knauer
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract RfaH, a paralog of the universally conserved NusG, binds to RNA polymerases (RNAP) and ribosomes to activate expression of virulence genes. In free, autoinhibited RfaH, an α-helical KOW domain sequesters the RNAP-binding site. Upon recruitm
Externí odkaz:
https://doaj.org/article/22619a1bbf0f4160960efd35b3c7e5a0
Autor:
Junqiao Jia, Tarek Hilal, Katherine E. Bohnsack, Aleksandar Chernev, Ning Tsao, Juliane Bethmann, Aruna Arumugam, Lane Parmely, Nicole Holton, Bernhard Loll, Nima Mosammaparast, Markus T. Bohnsack, Henning Urlaub, Markus C. Wahl
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
ASCC3 is a multi-functional helicase that contains two consecutive Ski2-like helicase units. Here, the authors show that ASCC3 can unwind DNA by threading one strand of a substrate duplex through both helicase units, supported by the TRIP4 protein.
Externí odkaz:
https://doaj.org/article/0ee2586a4c9f44dfb7f3b09d1b9bc981
Autor:
Iva Lučić, Léonie Héluin, Pin-Lian Jiang, Alejandro G Castro Scalise, Cong Wang, Andreas Franz, Florian Heyd, Markus C Wahl, Fan Liu, Andrew JR Plested
Publikováno v:
eLife, Vol 12 (2023)
The dodecameric protein kinase CaMKII is expressed throughout the body. The alpha isoform is responsible for synaptic plasticity and participates in memory through its phosphorylation of synaptic proteins. Its elaborate subunit organization and prope
Externí odkaz:
https://doaj.org/article/a541947c4ca64619bd1c3c6202745a66
Autor:
Karen Vester, Marco Preußner, Nicole Holton, Suihan Feng, Carsten Schultz, Florian Heyd, Markus C. Wahl
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-14 (2022)
Through the use of a reversible chemical dimerizer, the splicing factor PRPF38A is re-localized to the nuclear lamina, paving the way for a systematic analysis of spatio-temporal splicing regulation.
Externí odkaz:
https://doaj.org/article/ffdc066451914e1eaef33cc842e71134
Autor:
Viviane Kremling, Bernhard Loll, Szymon Pach, Ismail Dahmani, Christoph Weise, Gerhard Wolber, Salvatore Chiantia, Markus C. Wahl, Nikolaus Osterrieder, Walid Azab
Publikováno v:
Frontiers in Microbiology, Vol 14 (2023)
Cell entry of most alphaherpesviruses is mediated by the binding of glycoprotein D (gD) to different cell surface receptors. Equine herpesvirus type 1 (EHV-1) and EHV-4 gDs interact with equine major histocompatibility complex I (MHC-I) to initiate e
Externí odkaz:
https://doaj.org/article/3f383c03112646479d3bee13a5b7a488
Autor:
Tam Dang, Bernhard Loll, Sebastian Müller, Ranko Skobalj, Julia Ebeling, Timur Bulatov, Sebastian Gensel, Josefine Göbel, Markus C. Wahl, Elke Genersch, Andi Mainz, Roderich D. Süssmuth
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
The authors show that the N-acetyltransferase PamZ acts as a self-resistance factor disabling the antibacterial paenilamicin that is produced by the honey bee larvae pathogen Paenibacillus larvae.
Externí odkaz:
https://doaj.org/article/efd0e34fbaa048d5bbc9b3660ecfcfae
Autor:
Alexandra Bergfort, Marco Preußner, Benno Kuropka, İbrahim Avşar Ilik, Tarek Hilal, Gert Weber, Christian Freund, Tuğçe Aktaş, Florian Heyd, Markus C. Wahl
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Bergfort et al. use biochemistry, cryoEM, structure-guided mutagenesis, transcriptomics and proteomics to reveal how the intrinsically unstructured C9ORF78 protein binds BRR2 and PRPF8, regulating cassette exons and alternative 3’-splice sites.
Externí odkaz:
https://doaj.org/article/9cdd9c825b2e49b8b316d5d1c8d55312
Autor:
Stefanie Jehle, Natalia Kunowska, Nouhad Benlasfer, Jonathan Woodsmith, Gert Weber, Markus C Wahl, Ulrich Stelzl
Publikováno v:
Molecular Systems Biology, Vol 18, Iss 3, Pp 1-17 (2022)
Abstract Protein kinases play an important role in cellular signaling pathways and their dysregulation leads to multiple diseases, making kinases prime drug targets. While more than 500 human protein kinases are known to collectively mediate phosphor
Externí odkaz:
https://doaj.org/article/933ab559b4b04370bec15ae3542245dc
Autor:
Hao-Hong Pei, Tarek Hilal, Zhuo A. Chen, Yong-Heng Huang, Yuan Gao, Nelly Said, Bernhard Loll, Juri Rappsilber, Georgiy A. Belogurov, Irina Artsimovitch, Markus C. Wahl
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
The bacterial helicase-like transcription factor HelD interacts with the RNA polymerase (RNAP) and together with the RNAP δ subunit enhances RNAP cycling. Here, the authors present the cryo-EM structures of the monomeric and dimeric Bacillus subtili
Externí odkaz:
https://doaj.org/article/862de4900b514335855420b64fe9f8ae