Jeanne C. Stachowiak
Affiliations: | 2008 | University of California, Berkeley, Berkeley, CA, United States |
Google:
"Jeanne Stachowiak"Parents
Sign in to add mentorDaniel A. Fletcher | grad student | 2008 | UC Berkeley | |
(High Reynolds number microfluidic systems for drug delivery.) |
BETA: Related publications
See more...
Publications
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
Lee Y, Yuan F, Cabriales JL, et al. (2024) Transmembrane coupling accelerates the growth of liquid-like protein condensates. Biorxiv : the Preprint Server For Biology |
Xiao K, Park S, Stachowiak J, et al. (2024) Biophysical modeling of membrane curvature generation and curvature sensing by the glycocalyx. Biorxiv : the Preprint Server For Biology |
Yuan F, Gollapudi S, Day KJ, et al. (2024) Ubiquitin-driven protein condensation stabilizes clathrin-mediated endocytosis. Pnas Nexus. 3: pgae342 |
Kamatar A, Bravo JPK, Yuan F, et al. (2024) Lipid droplets as substrates for protein phase separation. Biophysical Journal |
Lee Y, Park S, Yuan F, et al. (2023) Transmembrane coupling of liquid-like protein condensates. Nature Communications. 14: 8015 |
Wilfling F, Kaksonen M, Stachowiak J. (2023) Protein condensates as flexible platforms for membrane traffic. Current Opinion in Cell Biology. 85: 102258 |
Yuan F, Gollapudi S, Day KJ, et al. (2023) Ubiquitin-driven protein condensation promotes clathrin-mediated endocytosis. Biorxiv : the Preprint Server For Biology |
Yuan F, Lee CT, Sangani A, et al. (2023) The ins and outs of membrane bending by intrinsically disordered proteins. Science Advances. 9: eadg3485 |
Maltseva D, Chatterjee S, Yu CC, et al. (2023) Fibril formation and ordering of disordered FUS LC driven by hydrophobic interactions. Nature Chemistry |
Gollapudi S, Jamal S, Kamatar A, et al. (2023) Steric pressure between glycosylated transmembrane proteins inhibits internalization by endocytosis. Proceedings of the National Academy of Sciences of the United States of America. 120: e2215815120 |