Zobrazeno 1 - 10
of 243
pro vyhledávání: '"F. Ulrich Hartl"'
Autor:
Georg Krainer, Raphael P. B. Jacquat, Matthias M. Schneider, Timothy J. Welsh, Jieyuan Fan, Quentin A. E. Peter, Ewa A. Andrzejewska, Greta Šneiderienė, Magdalena A. Czekalska, Hannes Ausserwoeger, Lin Chai, William E. Arter, Kadi L. Saar, Therese W. Herling, Titus M. Franzmann, Vasilis Kosmoliaptsis, Simon Alberti, F. Ulrich Hartl, Steven F. Lee, Tuomas P. J. Knowles
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract The physical characterization of proteins in terms of their sizes, interactions, and assembly states is key to understanding their biological function and dysfunction. However, this has remained a difficult task because proteins are often hi
Externí odkaz:
https://doaj.org/article/a359ec4607614996aebacbbb2897fd7b
Autor:
Nikolas Furthmann, Verian Bader, Lena Angersbach, Alina Blusch, Simran Goel, Ana Sánchez-Vicente, Laura J. Krause, Sarah A. Chaban, Prerna Grover, Victoria A. Trinkaus, Eva M. van Well, Maximilian Jaugstetter, Kristina Tschulik, Rune Busk Damgaard, Carsten Saft, Gisa Ellrichmann, Ralf Gold, Arend Koch, Benjamin Englert, Ana Westenberger, Christine Klein, Lisa Jungbluth, Carsten Sachse, Christian Behrends, Markus Glatzel, F. Ulrich Hartl, Ken Nakamura, Chadwick W. Christine, Eric J. Huang, Jörg Tatzelt, Konstanze F. Winklhofer
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-24 (2023)
Abstract NEMO is a ubiquitin-binding protein which regulates canonical NF-κB pathway activation in innate immune signaling, cell death regulation and host-pathogen interactions. Here we identify an NF-κB-independent function of NEMO in proteostasis
Externí odkaz:
https://doaj.org/article/254c39b4dc224a428f4f65c841b52060
Autor:
Anna Maria Eisele-Bürger, Frederik Eisele, Sandra Malmgren Hill, Xinxin Hao, Kara L. Schneider, Rahmi Imamoglu, David Balchin, Beidong Liu, F. Ulrich Hartl, Peter V. Bozhkov, Thomas Nyström
Publikováno v:
Cell Reports, Vol 42, Iss 11, Pp 113372- (2023)
Summary: Metacaspases are ancestral homologs of caspases that can either promote cell death or confer cytoprotection. Furthermore, yeast (Saccharomyces cerevisiae) metacaspase Mca1 possesses dual biochemical activity: proteolytic activity causing cel
Externí odkaz:
https://doaj.org/article/9af3080157bc43d7b143e62b2b0ce9aa
Autor:
Itika Saha, Patricia Yuste-Checa, Miguel Da Silva Padilha, Qiang Guo, Roman Körner, Hauke Holthusen, Victoria A. Trinkaus, Irina Dudanova, Rubén Fernández-Busnadiego, Wolfgang Baumeister, David W. Sanders, Saurabh Gautam, Marc I. Diamond, F. Ulrich Hartl, Mark S. Hipp
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Tau aggregates are associated with several neurodegenerative disorders. In this work, I. Saha and colleagues show that valosin-containing protein (VCP) recruited to Tau fibrils disaggregates them. However, this process comes at a cost: it generates s
Externí odkaz:
https://doaj.org/article/55b4a135031e4d249c4f455de3857bf8
Autor:
Matthias M. Schneider, Saurabh Gautam, Therese W. Herling, Ewa Andrzejewska, Georg Krainer, Alyssa M. Miller, Victoria A. Trinkaus, Quentin A. E. Peter, Francesco Simone Ruggeri, Michele Vendruscolo, Andreas Bracher, Christopher M. Dobson, F. Ulrich Hartl, Tuomas P. J. Knowles
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Molecular chaperones from the Hsp70 family can break up protein aggregates, including amyloids. Here, the authors utilize microfluidic diffusional sizing to assess the mechanism of α-synuclein (αS) disaggregation by the Hsc70–DnaJB1–Apg2 system
Externí odkaz:
https://doaj.org/article/9d156d4ff127467f8d1a03fe03aed8f5
Autor:
Patricia Yuste-Checa, Victoria A. Trinkaus, Irene Riera-Tur, Rahmi Imamoglu, Theresa F. Schaller, Huping Wang, Irina Dudanova, Mark S. Hipp, Andreas Bracher, F. Ulrich Hartl
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Variants of the extracellular chaperone Clusterin are associated with Alzheimer’s disease (AD) and Clusterin levels are elevated in AD patient brains. Here, the authors show that Clusterin binds to oligomeric Tau, which enhances the seeding capacit
Externí odkaz:
https://doaj.org/article/6817e37ab6504c1fa561f4ad2a667e95
Autor:
Victoria A. Trinkaus, Irene Riera-Tur, Antonio Martínez-Sánchez, Felix J. B. Bäuerlein, Qiang Guo, Thomas Arzberger, Wolfgang Baumeister, Irina Dudanova, Mark S. Hipp, F. Ulrich Hartl, Rubén Fernández-Busnadiego
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
The molecular architecture of α-Synuclein (α-Syn) inclusions, pathognomonic of various neurodegenerative disorders, remains unclear. Here, authors use cryo-electron tomography to image neuronal α-Syn inclusions in situ and find that inclusions con
Externí odkaz:
https://doaj.org/article/84faa4c08a42424bb5304d04db2b7ff0
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
Identifying factors that enable cells to induce a potent stress response to amyloid-like aggregation can provide further insight into the mechanism of stress regulation. Here, the authors express polyglutamine-expanded Huntingtin as a model disease p
Externí odkaz:
https://doaj.org/article/bf06109c704f419bbd81a8c23509df78
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
The Hsp70 system prevents protein aggregation and increases folding yields, but it is unknown whether it also enhances the rate of folding. Here the authors combine refolding assays, FRET and hydrogen/deuterium exchange-mass spectrometry measurements
Externí odkaz:
https://doaj.org/article/6125957e2a10438cac86795beb9c3d88
Autor:
Liang Zhao, Giulia Vecchi, Michele Vendruscolo, Roman Körner, Manajit Hayer-Hartl, F. Ulrich Hartl
Publikováno v:
Cell Reports, Vol 28, Iss 5, Pp 1335-1345.e6 (2019)
Summary: Stress-inducible molecular chaperones have essential roles in maintaining protein homeostasis, but the extent to which they affect overall proteome stability remains unclear. Here, we analyze the effects of the DnaK (Hsp70) system on protein
Externí odkaz:
https://doaj.org/article/5f1789a4b41e4b01b9c1bcb3a2b6d66b