Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Samsuzzoha Mondal"'
Autor:
Samsuzzoha Mondal, Karthik Narayan, Samuel Botterbusch, Imania Powers, Jason Zheng, Honey Priya James, Rui Jin, Tobias Baumgart
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-20 (2022)
Here the authors show that protein phase separation is a key mechanism in cellular receptor internalization via fast endophilin mediated endocytosis (FEME). Phase separation facilitates multivalent FEME-protein assembly in this clathrin-independent p
Externí odkaz:
https://doaj.org/article/eb88be9e379b4997bb94720b21511499
Publikováno v:
Bio-Protocol, Vol 13, Iss 12 (2023)
Bin/Amphiphysin/Rvs (BAR) proteins are known as classical membrane curvature generators during endocytosis. Amphiphysin, a member of the N-BAR sub-family of proteins that contain a characteristic amphipathic sequence at the N-terminus of the BAR doma
Externí odkaz:
https://doaj.org/article/b31f0dd281244ee2b8e9e79666c890ac
Autor:
Samsuzzoha Mondal, Tobias Baumgart
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1865:184121
Autor:
Karthik B. Narayan, Samsuzzoha Mondal, Honey Priya James, Laura Baeyens, Jason Zheng, Tobias Baumgart
Publikováno v:
Biophysical Journal. 122:483a
Publikováno v:
Biophysical Journal. 122:30a
Autor:
Samsuzzoha Mondal, Karthik Narayan, Samuel Botterbusch, Imania Powers, Jason Zheng, Honey Priya James, Rui Jin, Tobias Baumgart
A specific group of transmembrane receptors, including the β1-adrenergic receptor (β1-AR), is internalized through a non-clathrin pathway known as Fast Endophilin Mediated Endocytosis (FEME). A key question is: how does the endocytic machinery asse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16f0f5f80498fb7bbfc19cd19914c1f0
https://doi.org/10.1101/2021.12.27.474257
https://doi.org/10.1101/2021.12.27.474257
Publikováno v:
Biophysical Journal. 121:15a-16a
The Bin/Amphiphysin/Rvs (BAR) family protein endophilin plays key roles in membrane curvature generation during endocytosis of cellular receptors. The Src homology 3 (SH3) domain of endophilin interacts with the proline rich third intracellular loop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c37a30bc1e356e0589705b26eab12566
https://doi.org/10.1101/2020.07.11.198937
https://doi.org/10.1101/2020.07.11.198937
Autor:
Samsuzzoha Mondal, Samuel Botterbusch, Karthik Narayan, Imania Powers, Jason Zheng, Tobias Baumgart
Publikováno v:
Biophysical Journal. 121:80a
Publikováno v:
The Journal of Biological Chemistry
Endophilin plays key roles during endocytosis of cellular receptors, including generating membrane curvature to drive internalization. Electrostatic interactions between endophilin’s BIN/Amphiphysin/Rvs domain and anionic membrane lipids have been