Zobrazeno 1 - 10
of 378
pro vyhledávání: '"Alexander, Leitner"'
An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly
Autor:
Daniela Portugal-Calisto, Alexander Gregor Geiger, Julius Rabl, Oscar Vadas, Michaela Oborská-Oplová, Jarosław Mazur, Federica Richina, Purnima Klingauf-Nerurkar, Erich Michel, Alexander Leitner, Daniel Boehringer, Vikram Govind Panse
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract Mechanisms by which G-patch activators tune the processive multi-tasking ATP-dependent RNA helicase Prp43 (DHX15 in humans) to productively remodel diverse RNA:protein complexes remain elusive. Here, a comparative study between a herein and
Externí odkaz:
https://doaj.org/article/971060ff81394f669ef1db98800a9574
Autor:
Lucía Álvarez, Kevin Haubrich, Louisa Iselin, Laurent Gillioz, Vincenzo Ruscica, Karine Lapouge, Sandra Augsten, Ina Huppertz, Nila Roy Choudhury, Bernd Simon, Pawel Masiewicz, Mathilde Lethier, Stephen Cusack, Katrin Rittinger, Frank Gabel, Alexander Leitner, Gracjan Michlewski, Matthias W. Hentze, Frédéric H. T. Allain, Alfredo Castello, Janosch Hennig
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract TRIM25 is an RNA-binding ubiquitin E3 ligase with central but poorly understood roles in the innate immune response to RNA viruses. The link between TRIM25’s RNA binding and its role in innate immunity has not been established. Thus, we ut
Externí odkaz:
https://doaj.org/article/d8245675d28e4b2bbc482fdb79f08563
Autor:
Junsun Park, Hyunmin Kim, Daniel Gestaut, Seyeon Lim, Kwadwo A. Opoku-Nsiah, Alexander Leitner, Judith Frydman, Soung-Hun Roh
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract Proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin-like proteins (PhLPs) to facilitate folding
Externí odkaz:
https://doaj.org/article/b8cf75b24bd047c984b11ca0f74486ab
Autor:
Georg Dorn, Christoph Gmeiner, Tebbe de Vries, Emil Dedic, Mihajlo Novakovic, Fred F. Damberger, Christophe Maris, Esteban Finol, Chris P. Sarnowski, Joachim Kohlbrecher, Timothy J. Welsh, Sreenath Bolisetty, Raffaele Mezzenga, Ruedi Aebersold, Alexander Leitner, Maxim Yulikov, Gunnar Jeschke, Frédéric H.-T. Allain
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract RNA-binding proteins (RBPs) are crucial regulators of gene expression, often composed of defined domains interspersed with flexible, intrinsically disordered regions. Determining the structure of ribonucleoprotein (RNP) complexes involving s
Externí odkaz:
https://doaj.org/article/6ecfd082137440199e61e0254d4f1997
Autor:
Karolina Pavic, Nikhil Gupta, Judit Domènech Omella, Rita Derua, Anna Aakula, Riikka Huhtaniemi, Juha A. Määttä, Nico Höfflin, Juha Okkeri, Zhizhi Wang, Otto Kauko, Roosa Varjus, Henrik Honkanen, Daniel Abankwa, Maja Köhn, Vesa P. Hytönen, Wenqing Xu, Jakob Nilsson, Rebecca Page, Veerle Janssens, Alexander Leitner, Jukka Westermarck
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-18 (2023)
Tumour suppressors are inhibited in cancers and their reactivation could provide novel therapy opportunities. Here, the authors study the structural mechanism by which human tumour suppressor Protein Phosphatase 2A is inhibited in breast cancer cells
Externí odkaz:
https://doaj.org/article/a40d0289287e4365ac202e20daf82ec2
Autor:
Vladyslava Gorbovytska, Seung-Kyoon Kim, Filiz Kuybu, Michael Götze, Dahun Um, Keunsoo Kang, Andreas Pittroff, Theresia Brennecke, Lisa-Marie Schneider, Alexander Leitner, Tae-Kyung Kim, Claus-D. Kuhn
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-22 (2022)
Enhancer RNAs (eRNAs) can stimulate gene transcription through various mechanisms. Here, the authors identify the molecular features within eRNAs that are critical for their action in facilitating RNA Polymerase II release from the paused state.
Externí odkaz:
https://doaj.org/article/6fa17c70dad745c2a97c60a4d135cbda
Autor:
Anna Knörlein, Chris P. Sarnowski, Tebbe de Vries, Moritz Stoltz, Michael Götze, Ruedi Aebersold, Frédéric H.-T. Allain, Alexander Leitner, Jonathan Hall
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Although UV-induced cross-linking is a widely used method to study RNA-protein complexes, the cross-linking reactions are poorly understood. Here, the authors show that π-stacking interactions between nucleobases and aromatic amino acids play a key
Externí odkaz:
https://doaj.org/article/2cd6d485f0bf4ae2b1dfd7988cfbb5cd
Autor:
Stefan Gerhardy, Michaela Oborská-Oplová, Ludovic Gillet, Richard Börner, Rob van Nues, Alexander Leitner, Erich Michel, Janusz J. Petkowski, Sander Granneman, Roland K. O. Sigel, Ruedi Aebersold, Vikram Govind Panse
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Ribosome biogenesis is crucially dependent on proper rRNA folding, a process assisted by chaperones. Here the authors reveal how Puf6 promotes correct rRNA folding at low temperature, a condition where mis-paired RNA folding intermediates frequently
Externí odkaz:
https://doaj.org/article/0bae3de09764483c9083cf74b1da5f94
Autor:
Miranda P. Collier, Karen Betancourt Moreira, Kathy H. Li, Yu-Chan Chen, Daniel Itzhak, Rahul Samant, Alexander Leitner, Alma Burlingame, Judith Frydman
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Abstract The eukaryotic chaperonin TRiC/CCT is a large ATP-dependent complex essential for cellular protein folding. Its subunit arrangement into two stacked eight-membered hetero-oligomeric rings is conserved from yeast to man. A recent breakthrough
Externí odkaz:
https://doaj.org/article/17df211e25b3430283c572003e4f16b8
Autor:
Kevin Sabath, Melanie L. Stäubli, Sabrina Marti, Alexander Leitner, Murielle Moes, Stefanie Jonas
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
The Integrator complex (INT) is responsible for the 3′-end processing of several classes of non-coding RNAs. Here the authors show that the INTS10-INTS13-INTS14 complex forms a distinct submodule of INT and suggest it facilitates RNA substrate targ
Externí odkaz:
https://doaj.org/article/bf3f2057cddb4eac81b86a74bf8c4351