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pro vyhledávání: '"Jaclyn Robustelli"'
Autor:
Tobias Baumgart, Jaclyn Robustelli
Publikováno v:
Biochim Biophys Acta Biomembr
Endophilin is an N-BAR protein, which is characterized by a crescent-shaped BAR domain and an amphipathic helix that contributes to the membrane binding of these proteins. The exact function of that H0 helix has been a topic of debate. In mammals, th
Publikováno v:
Biophys J
Phosphatidylinositol-4,5-bisphosphate (PIP2) is an important signaling lipid in eukaryotic cell plasma membranes, playing an essential role in diverse cellular processes. The headgroup of PIP2 is highly negatively charged, and this lipid displays a h
Publikováno v:
Journal of the American Chemical Society. 138:14616-14622
N-BAR proteins such as endophilin are thought to bend lipid membranes via scaffolding (the molding of membranes through the crescent protein shape) and membrane insertion (also called wedging) of amphipathic helices. However, the contributions from t
Autor:
Merve Canyurt, Malcolm J. Daniels, Lily Owei, Jaclyn Robustelli, Tobias Baumgart, Christina L. Cleveland, Rebecca F. Wissner, Conor M. Haney, Harry Ischiropoulos, E. James Petersson, Priscilla Rodriguez
Publikováno v:
Biochemistry
Fibrillar aggregates of the protein α-synuclein (αS) are one of the hallmarks of Parkinson’s disease. Here, we show that measuring the fluorescence polarization (FP) of labels at several sites on αS allows one to monitor changes in the local dyn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c5937f32d619db234ae6a7d9735d21e
https://hdl.handle.net/11693/37311
https://hdl.handle.net/11693/37311
Publikováno v:
Biophysical Journal. 116:495a