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pro vyhledávání: '"Ellen, Rieloff"'
Autor:
Ellen Rieloff, Marie Skepö
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 20, p 11058 (2021)
Intrinsically disordered proteins are involved in many biological processes such as signaling, regulation, and recognition. A common strategy to regulate their function is through phosphorylation, as it can induce changes in conformation, dynamics, a
Externí odkaz:
https://doaj.org/article/907c6e3f98bc4d6a839350ae86417c43
Autor:
Ellen Rieloff, Marie Skepö
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 18, p 10174 (2021)
Phosphorylation is a common post-translational modification among intrinsically disordered proteins and regions, which helps regulate function by changing the protein conformations, dynamics, and interactions with binding partners. To fully comprehen
Externí odkaz:
https://doaj.org/article/efa81dbf66894aa48c2d49c1b08d6e8c
Publikováno v:
ACS Omega, Vol 2, Iss 5, Pp 1915-1921 (2017)
Externí odkaz:
https://doaj.org/article/494225493f27417bafc2af0e03669de1
Autor:
Marie Skepö, Ellen Rieloff
Publikováno v:
Journal of Chemical Theory and Computation. 16:1924-1935
Phosphorylation is one of the most abundant types of post-translational modifications of intrinsically disordered proteins (IDPs). This study examines the conformational changes in the 15-residue-long N-terminal fragment of the IDP statherin upon pho
Autor:
Aleksandra P. Dabkowska, Ellen Rieloff, Meina Wang, Linda K. Månsson, Emma Sparr, Jérôme J. Crassous, Jasper N. Immink, Adriana M. Mihut
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America 116(12), 5442-5450 (2019). doi:10.1073/pnas.1807790116
Proceedings of the National Academy of Sciences of the United States of America 116(12), 5442-5450 (2019). doi:10.1073/pnas.1807790116
Significance Soft microgel-based colloids consisting of a responsive polymer network offer an ideal platform for exploring the interactions between nanomaterials and artificial model membranes. Here, we report a modality to pattern and assemble respo
Publikováno v:
Journal of Molecular Biology. 431:511-523
Attractive interactions between intrinsically disordered proteins can be crucial for the functionality or, on the contrary, lead to the formation of harmful aggregates. For obtaining a molecular understanding of intrinsically disordered proteins and
Autor:
Ellen, Rieloff, Marie, Skepö
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2141
There is a great interest within the research community to understand the structure-function relationship for intrinsically disordered proteins (IDPs); however, the heterogeneous distribution of conformations that IDPs can adopt limits the applicabil
Autor:
Ellen Rieloff, Marie Skepö
Publikováno v:
Methods in Molecular Biology ISBN: 9781071605233
There is a great interest within the research community to understand the structure-function relationship for intrinsically disordered proteins (IDPs); however, the heterogeneous distribution of conformations that IDPs can adopt limits the applicabil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9881ad7dace41a00e6f866df92c29411
https://doi.org/10.1007/978-1-0716-0524-0_13
https://doi.org/10.1007/978-1-0716-0524-0_13
Publikováno v:
ACS Omega, Vol 2, Iss 5, Pp 1915-1921 (2017)
ACS Omega
ACS Omega
Bubbles in DNA are involved in many important biological processes. In this work, a coarse-grained model is used for characterizing bubbles formed in DNA melting. The model resorts only to electrostatic interactions at the Debye-Huckel level, in comb
Publikováno v:
'Journal of Molecular Biology ', vol: 430, pages: 2478-2492 (2018)
In this study, we have used the coarse-grained model developed for the intrinsically disordered saliva protein (IDP) Histatin 5, on an experimental selection of monomeric IDPs, and we show that the model is generally applicable when electrostatic int