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| 001 | 830009 | ||
| 005 | 20240619083538.0 | ||
| 024 | 7 | _ | |a 10.1063/1.4979985 |2 doi |
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| 100 | 1 | _ | |a Giani, M. |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Early stages of clathrin aggregation at a membrane in coarse-grained simulations |
| 260 | _ | _ | |a Melville, NY |c 2017 |b American Institute of Physics |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a The self-assembly process of clathrin coated pits during endocytosis has been simulated by combining and extending coarse grained models of the clathrin triskelion, the adaptor protein AP2, and a flexible network membrane. The AP2’s core, upon binding to membrane and cargo, releases a motif that can bind clathrin. In conditions where the core-membrane-cargo binding is weak, the binding of this motif to clathrin can result in a stable complex. We characterize the conditions and mechanisms resulting in the formation of clathrin lattices that curve the membrane, i.e., clathrin coated pits. The mechanical properties of the AP2 β linker appear crucial to the orientation of the curved clathrin lattice relative to the membrane, with wild-type short linkers giving rise to the inward curving buds enabling endocytosis while long linkers produce upside-down cages and outward curving bulges |
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| 700 | 1 | _ | |a den Otter, W. K. |0 P:(DE-HGF)0 |b 1 |e Corresponding author |
| 700 | 1 | _ | |a Briels, Willem |0 P:(DE-Juel1)159317 |b 2 |u fzj |
| 773 | _ | _ | |a 10.1063/1.4979985 |g Vol. 146, no. 15, p. 155102 - |0 PERI:(DE-600)1473050-9 |n 15 |p 155102 - |t The journal of chemical physics |v 146 |y 2017 |x 1089-7690 |
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