Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Till Rudack"'
Autor:
Ka Ying Sharon Hung, Sven Klumpe, Markus R. Eisele, Suzanne Elsasser, Geng Tian, Shuangwu Sun, Jamie A. Moroco, Tat Cheung Cheng, Tapan Joshi, Timo Seibel, Duco Van Dalen, Xin-Hua Feng, Ying Lu, Huib Ovaa, John R. Engen, Byung-Hoon Lee, Till Rudack, Eri Sakata, Daniel Finley
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
The interplay of the proteasome and deubiquitinase Ubp6 is crucial for the degradation of ubiquitylated substrates. Here, the authors provide structural insights into the allosteric mechanism by which the activities of both Ubp6 and the proteasome ar
Externí odkaz:
https://doaj.org/article/0db17aeb4b8c4a309992d0d564111f7b
Autor:
Max-Aylmer Dreier, Philipp Althoff, Mohamad Javad Norahan, Stefan Alexander Tennigkeit, Samir F. El-Mashtoly, Mathias Lübben, Carsten Kötting, Till Rudack, Klaus Gerwert
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Dreier et al. reports that the anion channelrhodopsin GtACR1 does not undergo a syn-cycle (light adapted ground state) and thus has a more efficient channel behaviour than CrChR2. They propose that constructing variants lacking syn-cycle could optimi
Externí odkaz:
https://doaj.org/article/e32a077ee10e427a92017a371359e82d
Autor:
Tat Cheung Cheng, Timo Seibel, Daniel Finley, Suzanne Elsasser, Ka Ying Sharon Hung, Till Rudack, Huib Ovaa, John R. Engen, Ying Lu, Byung-Hoon Lee, Markus R. Eisele, Duco Van Dalen, Shuangwu Sun, Tapan Joshi, Xin-Hua Feng, Jamie A. Moroco, Sven Klumpe, Geng Tian, Eri Sakata
The proteasome is the principal cellular protease, and recognizes target proteins that have been covalently marked by ubiquitin chains. The ubiquitin signal is subject to rapid editing at the proteasome, allowing it to reject substrates based on topo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::269104d0fcccb9b12b4cd2a402700a07
https://doi.org/10.1101/2021.07.16.452743
https://doi.org/10.1101/2021.07.16.452743
Autor:
Jörn Güldenhaupt, Marvin Scherlo, Christian Teuber, Mathias Lübben, Klaus Gerwert, Jonas Schartner, Carsten Kötting, Johann P. Klare, Till Rudack
Publikováno v:
Chemical Science
Oncogenic mutated Ras is a key player in cancer, but despite intense and expensive approaches its catalytic center seems undruggable. The Ras dimer interface is a possible alternative drug target. Dimerization at the membrane affects cell growth sign
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9dd101cf11393bf7df82da74072ebbf0
https://pubmed.ncbi.nlm.nih.gov/34194708
https://pubmed.ncbi.nlm.nih.gov/34194708
Autor:
Till Rudack, Tatjana Surdin, Stefan Alexander Tennigkeit, Maiia Shulman, Jan‐Claudius Schwitalla, Dennis Eickelbeck, Klaus Gerwert, Philipp Althoff, Brix Mücher, Stefan Herlitze, Raziye Karapinar, Marvin Scherlo, Melanie D. Mark
Publikováno v:
Chembiochem
Optogenetics uses light‐sensitive proteins, so‐called optogenetic tools, for highly precise spatiotemporal control of cellular states and signals. The major limitations of such tools include the overlap of excitation spectra, phototoxicity, and l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f50956f503258cb2707198e49d03f06
https://doi.org/10.1002/cbic.201900485
https://doi.org/10.1002/cbic.201900485
Autor:
Benjamin D. Engel, Madeline Möller, Till Rudack, Emad Tajkhorshid, Aaron Chan, Raphael Stoll, Julian David Langer, Jan M. Schuller, Pasqual Liauw, Marc M. Nowaczyk, Stefan Bohn, Sandra K. Schuller, Anja Krieger-Liszkay, Oliver Arnolds, Jure Zabret, Jakob Meier-Credo
Publikováno v:
Nature Plants
Nature Plants, 2021, 7 (4), pp.524-538. ⟨10.1038/s41477-021-00895-0⟩
Nature Plants, Nature Publishing Group, 2021, 7 (4), pp.524-538. ⟨10.1038/s41477-021-00895-0⟩
Nat Plants
Nature Plants, 2021, 7 (4), pp.524-538. ⟨10.1038/s41477-021-00895-0⟩
Nature Plants, Nature Publishing Group, 2021, 7 (4), pp.524-538. ⟨10.1038/s41477-021-00895-0⟩
Nat Plants
Biogenesis of photosystem II (PSII), nature’s water-splitting catalyst, is assisted by auxiliary proteins that form transient complexes with PSII components to facilitate stepwise assembly events. Using cryo-electron microscopy, we solved the struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::023ef95ee7aeb33f422f127a02ec7f68
https://hal.science/hal-03406233/document
https://hal.science/hal-03406233/document
Autor:
Aaron Chan, Anja Krieger-Liszkay, Pasqual Liauw, Emad Tajkhorshid, Till Rudack, Stefan Bohn, Julian David Langer, Sandra K. Schuller, Jakob Meier-Credo, Jan M. Schuller, Madeline Möller, Raphael Stoll, Benjamin D. Engel, Jure Zabret, Oliver Arnolds, Marc M. Nowaczyk
Biogenesis of photosystem II (PSII), nature’s water splitting catalyst, is assisted by auxiliary proteins that form transient complexes with PSII components to facilitate stepwise assembly events. Using cryo-electron microscopy, we solved the struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b8c8779c8ea938350b001cd938cd6ada
https://doi.org/10.21203/rs.3.rs-88039/v1
https://doi.org/10.21203/rs.3.rs-88039/v1
Autor:
Jure Zabret, Stefan Bohn, Sandra K. Schuller, Oliver Arnolds, Madeline Möller, Jakob Meier-Credo, Pasqual Liauw, Aaron Chan, Emad Tajkhorshid, Julian D. Langer, Raphael Stoll, Anja Krieger-Liszkay, Benjamin D. Engel, Till Rudack, Jan M. Schuller, Marc M. Nowaczyk
Biogenesis of photosystem II (PSII), nature’s water splitting catalyst, is assisted by auxiliary proteins that form transient complexes with PSII components to facilitate stepwise assembly events. Using cryo-electron microscopy, we solved the struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d12a6418d43d12044c3f2bb88ab53ea
https://doi.org/10.1101/2020.09.14.294884
https://doi.org/10.1101/2020.09.14.294884
Autor:
Steffen Heinz, Karin Gries, Anna Rast, Jürgen M. Plitzko, Justus Niemeyer, Wojciech Wietrzynski, Wataru Sakamoto, Tilak Kumar Gupta, Norikazu Ohnishi, Jörg Nickelsen, Miroslava Schaffer, Till Rudack, Michael Schroda, Mike Strauss, Sven Klumpe, Benjamin D. Engel, Wolfgang Baumeister, Jan M. Schuller
Vesicle-inducing protein in plastids (VIPP1) is essential for the biogenesis and maintenance of thylakoid membranes, which transform light into life. However, it is unknown how VIPP1 performs its vital membrane-shaping function. Here, we use cryo-ele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd17ad02c58984c45961d9885223eeda
https://doi.org/10.1101/2020.08.11.243204
https://doi.org/10.1101/2020.08.11.243204
Autor:
Tilak Kumar Gupta, Norikazu Ohnishi, Benjamin D. Engel, Justus Niemeyer, Wojciech Wietrzynski, Matthias Ostermeier, Miroslava Schaffer, Jan M. Schuller, Steffen Heinz, Joerg Nickelsen, Michael Schroda, Benjamin Spaniol, Jürgen M. Plitzko, Karin Gries, Anna Rast, Michael A. Strauss, Sven Klumpe, Till Rudack, Wataru Sakamoto, Wolfgang Baumeister
Publikováno v:
Cell. 184(14)
Summary Vesicle-inducing protein in plastids 1 (VIPP1) is essential for the biogenesis and maintenance of thylakoid membranes, which transform light into life. However, it is unknown how VIPP1 performs its vital membrane-remodeling functions. Here, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ebab8b6ddb6356e098e55d420ab87a2
https://pubmed.ncbi.nlm.nih.gov/34242559
https://pubmed.ncbi.nlm.nih.gov/34242559