G
Gunnar Dittmar
Researcher at University of Luxembourg
Publications - 155
Citations - 13724
Gunnar Dittmar is an academic researcher from University of Luxembourg. The author has contributed to research in topics: Ubiquitin & Biology. The author has an hindex of 35, co-authored 127 publications receiving 11002 citations. Previous affiliations of Gunnar Dittmar include Charité & Cardiff University.
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Journal ArticleDOI
Global quantification of mammalian gene expression control
Björn Schwanhäusser,Dorothea Busse,Na Li,Gunnar Dittmar,Johannes Schuchhardt,Jana Wolf,Wei Chen,Matthias Selbach +7 more
TL;DR: Using a quantitative model, the first genome-scale prediction of synthesis rates of mRNAs and proteins is obtained and it is found that the cellular abundance of proteins is predominantly controlled at the level of translation.
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Translation of CircRNAs
Nagarjuna Reddy Pamudurti,Osnat Bartok,Marvin Jens,Reut Ashwal-Fluss,Christin Stottmeister,Larissa Ruhe,Mor Hanan,Emanuel Wyler,Daniel Pérez-Hernández,Evelyn Ramberger,Shlomo Shenzis,Moshe Samson,Gunnar Dittmar,Markus Landthaler,Marina Chekulaeva,Nikolaus Rajewsky,Sebastian Kadener +16 more
TL;DR: This study provides strong evidence for translation of circRNAs, revealing the existence of an unexplored layer of gene activity.
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Senescence-associated reprogramming promotes cancer stemness
Maja Milanovic,Dorothy N. Y. Fan,Dimitri Belenki,J. Henry M. Däbritz,Zhen Zhao,Yong Yu,Jan Dörr,Lora Dimitrova,Dido Lenze,Inês Am Barbosa,Marco A. Mendoza-Parra,Tamara Kanashova,Marlen Metzner,Katharina Pardon,Maurice Reimann,Andreas Trumpp,Bernd Dörken,Johannes Zuber,Hinrich Gronemeyer,Michael Hummel,Gunnar Dittmar,Soyoung Lee,Clemens A. Schmitt +22 more
TL;DR: Senescence-associated stemness is an unexpected, cell-autonomous feature that exerts its detrimental, highly aggressive growth potential upon escape from cell-cycle blockade, and is enriched in relapse tumours.
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Proteasome subunit Rpn1 binds ubiquitin-like protein domains.
Suzanne Elsasser,Rayappa Reddy Gali,Martin Schwickart,Christopher N. Larsen,David Leggett,Britta Müller,Matthew T. Feng,Fabian Tübing,Gunnar Dittmar,Daniel Finley +9 more
TL;DR: It is shown that Rad23 binds proteasomes by directly interacting with the base subcomplex of the regulatory particle of the proteasome, and it is proposed that the LRR domain of Rpn1 may be positioned in the base to allow the cargo proteins carried by Rad23 to be presented to the proteAsomal ATPases for unfolding.
Journal ArticleDOI
Cell Cycle–Regulated Modification of the Ribosome by a Variant Multiubiquitin Chain
TL;DR: Data suggest a regulatory role for multiubiquitin chains that is reversible and does not function to target the acceptor protein for degradation, and the K63R mutant of ubiquitin displays defects in ribosomal function in vivo and in vitro, including a dramatic sensitivity to translational inhibitors.