Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Rodolfo Ciuffa"'
Phosphorylation‐linked complex profiling identifies assemblies required for Hippo signal integration
Autor:
Federico Uliana, Rodolfo Ciuffa, Ranjan Mishra, Andrea Fossati, Fabian Frommelt, Sabrina Keller, Martin Mehnert, Eivind Salmorin Birkeland, Frank van Drogen, Nevena Srejic, Matthias Peter, Nicolas Tapon, Ruedi Aebersold, Matthias Gstaiger
Publikováno v:
Molecular Systems Biology, Vol 19, Iss 4, Pp 1-25 (2023)
Abstract While several computational methods have been developed to predict the functional relevance of phosphorylation sites, experimental analysis of the interdependency between protein phosphorylation and Protein–Protein Interactions (PPIs) rema
Externí odkaz:
https://doaj.org/article/87d8299e1ad24511acc6e8b026e4e491
Autor:
Federico Uliana, Matej Vizovišek, Laura Acquasaliente, Rodolfo Ciuffa, Andrea Fossati, Fabian Frommelt, Sandra Goetze, Bernd Wollscheid, Matthias Gstaiger, Vincenzo De Filippis, Ulrich auf dem Keller, Ruedi Aebersold
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
Characterizing proteases in their native environment is still challenging. Here, the authors develop a proteomics workflow for analyzing protease-specific peptides from cell lysates in 96-well format, providing mechanistic insights into blood proteas
Externí odkaz:
https://doaj.org/article/db933c0d43874f78b25c2f9000538975
Autor:
Martin Mehnert, Rodolfo Ciuffa, Fabian Frommelt, Federico Uliana, Audrey van Drogen, Kilian Ruminski, Matthias Gstaiger, Ruedi Aebersold
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-18 (2020)
Diseases can be associated with various mutations of the same gene, but the molecular consequences of specific mutations remain incompletely understood. Here, the authors present an integrated proteomic workflow to determine the molecular response of
Externí odkaz:
https://doaj.org/article/5284796b9f7e4306aca01803fd9b2199
Autor:
Rodolfo Ciuffa, Trond Lamark, Abul K. Tarafder, Audrey Guesdon, Sofia Rybina, Wim J.H. Hagen, Terje Johansen, Carsten Sachse
Publikováno v:
Cell Reports, Vol 11, Iss 5, Pp 748-758 (2015)
The scaffold protein p62/SQSTM1 is involved in protein turnover and signaling and is commonly found in dense protein bodies in eukaryotic cells. In autophagy, p62 acts as a selective autophagy receptor that recognizes and shuttles ubiquitinated prote
Externí odkaz:
https://doaj.org/article/0faae524d02a46d28982a431650aebf1
Autor:
Fabian Frommelt, Andrea Fossati, Federico Uliana, Fabian Wendt, Xue Peng, Moritz Heusel, Bernd Wollscheid, Ruedi Aebersold, Rodolfo Ciuffa, Matthias Gstaiger
Most, if not all, proteins are organized in macromolecular assemblies, which represent key functional units regulating and catalyzing the majority of cellular processes in health and disease. Ever-advancing analytical capabilities promise to pinpoint
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e3010462ac33cec4ef29272a7402e698
https://doi.org/10.1101/2023.03.22.533843
https://doi.org/10.1101/2023.03.22.533843
Autor:
Federico Uliana, Rodolfo Ciuffa, Ranjan Mishra, Andrea Fossati, Fabian Frommelt, Martin Mehnert, Eivind Salmorin Birkeland, Matthias Peter, Nicolas Tapon, Ruedi Aebersold, Matthias Gstaiger
Cellular signaling relies on the temporal and spatial control of the formation of transient protein complexes by post-translational modifications, most notably by phosphorylation. While several computational methods have been developed to predict the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fef5154cd2f5c7628d6dd5f8c5b536f1
https://doi.org/10.1101/2022.03.13.484137
https://doi.org/10.1101/2022.03.13.484137
Autor:
Varun S Sharma, Andrea Fossati, Rodolfo Ciuffa, Marija Buljan, Evan G Williams, Zhen Chen, Wenguang Shao, Patrick G A Pedrioli, Anthony W Purcell, María Rodríguez Martínez, Jiangning Song, Matteo Manica, Ruedi Aebersold, Chen Li
Publikováno v:
Briefings in bioinformatics, vol 23, iss 4
In molecular biology, it is a general assumption that the ensemble of expressed molecules, their activities and interactions determine biological function, cellular states and phenotypes. Stable protein complexes—or macromolecular machines—are, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4cbd6cde1c77e628187d5b66c527662
https://pubmed.ncbi.nlm.nih.gov/35724564
https://pubmed.ncbi.nlm.nih.gov/35724564
Autor:
Rodolfo Ciuffa, Federico Uliana, Jonathan Mannion, Martin Mehnert, Tencho Tenev, Cathy Marulli, Ari Satanowski, Lena Maria Leone Keller, Pilar Natalia Rodilla Ramírez, Alessandro Ori, Matthias Gstaiger, Pascal Meier, Ruedi Aebersold
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 119 (40)
Protein-protein interactions (PPIs) represent the main mode of the proteome organization in the cell. In the last decade, several large-scale representations of PPI networks have captured generic aspects of the functional organization of network comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2ab8d7128be6a326c1ddd82a2d86a9c
Autor:
Pascal Meier, Martin Mehnert, Matthias Gstaiger, Alessandro Ori, Federico Uliana, Pilar Natalia Rodilla Ramirez, Ruedi Aebersold, Ari Satanowski, Cathy Marulli, Rodolfo Ciuffa
Protein-protein interactions (PPI) represent the main mode of the proteome organization in the cell. In the last decade, several large-scale representations of PPI networks have captured generic aspects of the functional organization of network compo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c074c3ad65f933106e9fa33d15889b1
https://doi.org/10.1101/2021.09.18.460902
https://doi.org/10.1101/2021.09.18.460902
Autor:
Vincenzo De Filippis, Andrea Fossati, Bernd Wollscheid, Ruedi Aebersold, Matthias Gstaiger, Laura Acquasaliente, Fabian Frommelt, Federico Uliana, Rodolfo Ciuffa, Ulrich auf dem Keller, Sandra Goetze, Matej Vizovisek
Publikováno v:
Nature Communications
Uliana, F, Vizovišek, M, Acquasaliente, L, Ciuffa, R, Fossati, A, Frommelt, F, Goetze, S, Wollscheid, B, Gstaiger, M, De Filippis, V, auf dem Keller, U & Aebersold, R 2021, ' Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen ', Nature Communications, vol. 12, 1693 . https://doi.org/10.1038/s41467-021-21754-8
Nature Communications, 12 (1)
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
Nature communications, vol 12, iss 1
Uliana, F, Vizovišek, M, Acquasaliente, L, Ciuffa, R, Fossati, A, Frommelt, F, Goetze, S, Wollscheid, B, Gstaiger, M, De Filippis, V, auf dem Keller, U & Aebersold, R 2021, ' Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen ', Nature Communications, vol. 12, 1693 . https://doi.org/10.1038/s41467-021-21754-8
Nature Communications, 12 (1)
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
Nature communications, vol 12, iss 1
Proteases are among the largest protein families and critical regulators of biochemical processes like apoptosis and blood coagulation. Knowledge of proteases has been expanded by the development of proteomic approaches, however, technology for multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2acabc7a0fbf8ca0492abe0f5829d0f6
http://europepmc.org/articles/PMC7966775
http://europepmc.org/articles/PMC7966775