Zobrazeno 1 - 10
of 634
pro vyhledávání: '"co-translational"'
Autor:
Léa Clusan, Frederic Percevault, Emmanuelle Jullion, Pascale Le Goff, Christophe Tiffoche, Tamara Fernandez‐Calero, Raphaël Métivier, Monica Marin, Farzad Pakdel, Denis Michel, Gilles Flouriot
Publikováno v:
Molecular Oncology, Vol 17, Iss 7, Pp 1302-1323 (2023)
Oestrogen receptor‐alpha (ERα) positivity is intimately associated with the development of hormone‐dependent breast cancers. A major challenge in the treatment of these cancers is to understand and overcome the mechanisms of endocrine resistance
Externí odkaz:
https://doaj.org/article/a18b6851c3da4c85afbc589534d40b27
Autor:
George Allen, Benjamin Weiss, Olesya O. Panasenko, Susanne Huch, Zoltan Villanyi, Benjamin Albert, Daniel Dilg, Marina Zagatti, Paul Schaughency, Susan E. Liao, Jeff Corden, Christine Polte, David Shore, Zoya Ignatova, Vicent Pelechano, Martine A. Collart
Publikováno v:
Genome Biology, Vol 24, Iss 1, Pp 1-27 (2023)
Abstract Background The Ccr4-Not complex is mostly known as the major eukaryotic deadenylase. However, several studies have uncovered roles of the complex, in particular of the Not subunits, unrelated to deadenylation and relevant for translation. In
Externí odkaz:
https://doaj.org/article/23d2ebafa01a4318b68424afd1620c29
Akademický článek
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Akademický článek
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Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 12, p 10049 (2023)
Molecular dynamics simulations of protein folding typically consider the polypeptide chain at equilibrium and in isolation from the cellular components. We argue that in order to understand protein folding as it occurs in vivo, it should be modeled a
Externí odkaz:
https://doaj.org/article/9e9aba575f0f4a1880f4f8c7e253af96
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Co-translational protein folding is one of the central topics in molecular biology. In Escherichia coli, trigger factor (TF) is a primary chaperone that facilitates co-translational folding by directly interacting with nascent polypeptide chains on t
Externí odkaz:
https://doaj.org/article/a35bc38aa070429c99112ac4cf31b346
Autor:
Janire Urrutia, Alejandra Aguado, Carolina Gomis-Perez, Arantza Muguruza-Montero, Oscar R. Ballesteros, Jiaren Zhang, Eider Nuñez, Covadonga Malo, Hee Jung Chung, Aritz Leonardo, Aitor Bergara, Alvaro Villarroel
Publikováno v:
BMC Biology, Vol 19, Iss 1, Pp 1-18 (2021)
Abstract Background The amino acid sequence of proteins generally carries all the necessary information for acquisition of native conformations, but the vectorial nature of translation can additionally determine the folding outcome. Such consideratio
Externí odkaz:
https://doaj.org/article/06cb6d34b83948ddbd9c631e4790026c
Autor:
Leonardo Salicari, Antonio Trovato
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 11, p 9193 (2023)
Entangled motifs are found in one-third of protein domain structures, a reference set that contains mostly globular proteins. Their properties suggest a connection with co-translational folding. Here, we wish to investigate the presence and propertie
Externí odkaz:
https://doaj.org/article/4301eed3b6544d118d323cd20b84ede8
Autor:
Sébastien Meurant, Lorris Mauclet, Marc Dieu, Thierry Arnould, Sven Eyckerman, Patricia Renard
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 11, p 9604 (2023)
Biotin-based proximity labeling approaches, such as BioID, have demonstrated their use for the study of mitochondria proteomes in living cells. The use of genetically engineered BioID cell lines enables the detailed characterization of poorly charact
Externí odkaz:
https://doaj.org/article/168c206f98d8442cb4dbe54d688bf915
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The majority of proteins in nature are composed of multiple domains connected in a single polypeptide. How these long sequences fold into functional structures without forming toxic misfolds or aggregates is poorly understood. Their folding is inextr
Externí odkaz:
https://doaj.org/article/8805b157cdbc4974be5c0941c59556a0