Zobrazeno 1 - 10
of 512
pro vyhledávání: '"Bernd Bukau"'
Autor:
Melania Minoia, Jany Quintana-Cordero, Katharina Jetzinger, Ilgin Eser Kotan, Kathryn Jane Turnbull, Michela Ciccarelli, Anna E. Masser, Dorina Liebers, Eloïse Gouarin, Marius Czech, Vasili Hauryliuk, Bernd Bukau, Günter Kramer, Claes Andréasson
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated chaperone, Chp1, that rewires the cotranslational folding machinery to
Externí odkaz:
https://doaj.org/article/f23814c7fcb4463299135165d37e841c
Autor:
Areeb Jawed, Chi-Ting Ho, Tomas Grousl, Aseem Shrivastava, Thomas Ruppert, Bernd Bukau, Axel Mogk
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2023)
To counteract proteotoxic stress and cellular aging, protein quality control (PQC) systems rely on the refolding, degradation and sequestration of misfolded proteins. In Saccharomyces cerevisiae the Hsp70 chaperone system plays a central role in prot
Externí odkaz:
https://doaj.org/article/867016d3b1be48c79c1a0ad93d7010c0
Autor:
Jonathan Bohlen, Liza Harbrecht, Saioa Blanco, Katharina Clemm von Hohenberg, Kai Fenzl, Günter Kramer, Bernd Bukau, Aurelio A. Teleman
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Upon stress, translation of ATF4 is induced by reinitiating ribosomes following translation of short upstream open reading frames (uORFs). Here the authors show that translation re-initiation of ATF4 is mediated by the DENR-MCTS1 complex which acts o
Externí odkaz:
https://doaj.org/article/6f5c73c82bd545db83b3c936664b634c
Autor:
Chi-ting Ho, Tomas Grousl, Oren Shatz, Areeb Jawed, Carmen Ruger-Herreros, Marije Semmelink, Regina Zahn, Karsten Richter, Bernd Bukau, Axel Mogk
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
The sequestration of misfolded proteins into large assemblies by sequestrases is now considered as the third pillar in protein quality control besides chaperones and proteases. Here the authors characterise the functions of the sequestrases Hsp42 and
Externí odkaz:
https://doaj.org/article/046a4baa20df4aac872c48bb40ab57d6
Autor:
Fabian den Brave, Lucas V. Cairo, Chandhuru Jagadeesan, Carmen Ruger-Herreros, Axel Mogk, Bernd Bukau, Stefan Jentsch
Publikováno v:
Cell Reports, Vol 31, Iss 9, Pp - (2020)
Summary: The formation of insoluble inclusions in the cytosol and nucleus is associated with impaired protein homeostasis and is a hallmark of several neurodegenerative diseases. Due to the absence of the autophagic machinery, nuclear protein aggrega
Externí odkaz:
https://doaj.org/article/1bce3ea995b94ff6894220e79aaecc63
Autor:
Johanna Zemva, Christoph Andreas Fink, Thomas Henry Fleming, Leonard Schmidt, Anne Loft, Stephan Herzig, Robert André Knieß, Matthias Mayer, Bernd Bukau, Peter Paul Nawroth, Jens Tyedmers
Publikováno v:
Redox Biology, Vol 13, Iss C, Pp 674-686 (2017)
Energy production is inevitably linked to the generation of toxic metabolites, such as reactive oxygen and carbonyl species, known as major contributors to ageing and degenerative diseases. It remains unclear how cells can adapt to elevated energy fl
Externí odkaz:
https://doaj.org/article/8aeca16a48664371be95eb4093fd15d0
Publikováno v:
Cell Reports, Vol 27, Iss 12, Pp 3433-3446.e4 (2019)
Summary: AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and threading activities are regulated and intertwined
Externí odkaz:
https://doaj.org/article/1437e116bee14ff49e614571aa503d64
Autor:
Mohammed Jamshad, Timothy J Knowles, Scott A White, Douglas G Ward, Fiyaz Mohammed, Kazi Fahmida Rahman, Max Wynne, Gareth W Hughes, Günter Kramer, Bernd Bukau, Damon Huber
Publikováno v:
eLife, Vol 8 (2019)
In bacteria, the translocation of proteins across the cytoplasmic membrane by the Sec machinery requires the ATPase SecA. SecA binds ribosomes and recognises nascent substrate proteins, but the molecular mechanism of nascent substrate recognition is
Externí odkaz:
https://doaj.org/article/03c1fc4e168e4c638fbfaa1f143e7620
Autor:
Sophia Ungelenk, Fatemeh Moayed, Chi-Ting Ho, Tomas Grousl, Annette Scharf, Alireza Mashaghi, Sander Tans, Matthias P. Mayer, Axel Mogk, Bernd Bukau
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Small heat shock proteins (sHsps) contribute to cellular recovery and survival following stress causing elevated levels of misfolded or unfolded proteins. Here the authors demonstrate that sHsps function by maintaining aggregating proteins in close-t
Externí odkaz:
https://doaj.org/article/d064b25e594849efb795495f07d85f93