Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lorenz Weidenauer"'
Autor:
Kaushik Bhattacharya, Samarpan Maiti, Szabolcs Zahoran, Lorenz Weidenauer, Dina Hany, Diana Wider, Lilia Bernasconi, Manfredo Quadroni, Martine Collart, Didier Picard
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
The molecular chaperone Hsp90 decreases with age but whether organisms can physiologically tune expression is unclear. Here, the authors show that mammalian cells can adjust Hsp90 levels to accumulating cellular stress by translational reprogramming.
Externí odkaz:
https://doaj.org/article/98445de100014006b4ae943b041a9674
Autor:
Kaushik Bhattacharya, Lorenz Weidenauer, Tania Morán Luengo, Ellis C. Pieters, Pablo C. Echeverría, Lilia Bernasconi, Diana Wider, Yashar Sadian, Margreet B. Koopman, Matthieu Villemin, Christoph Bauer, Stefan G. D. Rüdiger, Manfredo Quadroni, Didier Picard
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-21 (2020)
Hop, also known as Stip1 or Sti1, facilitates substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Characterization of proteostasis-related pathways in STIP1 knock-out cell lines reveals that in eukaryotes Stip1 modulates the balance
Externí odkaz:
https://doaj.org/article/82875625c72b4d9c8c7eaaf0131c13bc
Autor:
Lorenz Weidenauer, Manfredo Quadroni
Publikováno v:
Cells, Vol 10, Iss 7, p 1701 (2021)
Hsp90β is a major chaperone involved in numerous cellular processes. Hundreds of client proteins depend on Hsp90β for proper folding and/or activity. Regulation of Hsp90β is critical to coordinate its tasks and is mediated by several post-translat
Externí odkaz:
https://doaj.org/article/3681615970f64bca83e5bcd2c25297fa
Autor:
Manfredo Quadroni, Lorenz Weidenauer
Publikováno v:
Cells, Vol 10, Iss 1701, p 1701 (2021)
Cells
Cells; Volume 10; Issue 7; Pages: 1701
Cells
Cells; Volume 10; Issue 7; Pages: 1701
Hsp90β is a major chaperone involved in numerous cellular processes. Hundreds of client proteins depend on Hsp90β for proper folding and/or activity. Regulation of Hsp90β is critical to coordinate its tasks and is mediated by several post-translat
Publikováno v:
Expert Review of Proteomics. 14:1105-1117
Heat shock protein 90 (HSP90) regulates protein homeostasis in eukaryotes. As a 'professional interactor', HSP90 binds to and chaperones many proteins and has both housekeeping and disease-related functions but its regulation remains in part elusive.
Autor:
Didier Picard, S. G. D. Rüdiger, Lorenz Weidenauer, Kaushik Bhattacharya, Diana Wider, Christoph Ruediger Bauer, Lilia Bernasconi, Pablo Christian Echeverria, Manfredo Quadroni, M. Villemin, T. Moran Luengo
SUMMARYHop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a numb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d38c20ca7fec2711578ee7976a6564f6
Autor:
Horst Vogel, Michel Prudent, Ashwin Thampi, Niels Lion, Luigino Grasso, Romain Wyss, Davide Demurtas, Lorenz Weidenauer
Publikováno v:
Analytical and Bioanalytical Chemistry
Europe PubMed Central
Europe PubMed Central
We report on a generic method to detect and identify the molecular profile of exosomes either derived from cultured cell lines or isolated from biofluids. Exosomes are nanovesicles shed by cells into their microenvironment and carry the molecular ide