DOI,IST REx ID,Research Group,Title of publication
10.1103/PhysRevResearch.6.023189,17050,AnSa,Runaway transition in irreversible polymer condensation with cyclization
10.1021/acsnano.4c03839,17239,AnSa,In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures
10.1038/s41567-024-02597-8,17460,"AnSa,MaLo",Self-organization of mortal filaments and its role in bacterial division ring formation
10.15479/at:ista:18661,18661,"GradSch,AnSa",Archaeal membranes : In silico modelling and design
10.1101/2024.10.18.619072,18670,AnSa,Stability vs flexibility: Reshaping archaeal membranes in silico
10.1038/s41567-023-02136-x,13971,"EdHa,AnSa,JePa",Unconventional colloidal aggregation in chiral bacterial baths
10.1140/epje/s10189-023-00354-y,14442,AnSa,Mixtures of self-propelled particles interacting with asymmetric obstacles
10.15479/AT:ISTA:14472,14472,AnSa,Stress granules plug and stabilize damaged endolysosomal membranes
10.1038/s41586-023-06726-w,14610,AnSa,Stress granules plug and stabilize damaged endolysosomal membranes
10.1103/PhysRevLett.131.228401,14655,AnSa,Transverse fluctuations control the assembly of semiflexible filaments
10.1063/5.0134271,12705,AnSa,"Structure and elasticity of model disordered, polydisperse, and defect-free polymer networks"
10.1039/d2sm01562e,12708,AnSa,Steering self-organisation through confinement
10.1126/sciadv.ade5224,12756,AnSa,The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division
10.1021/acs.nanolett.3c00375,13094,AnSa,Wrapping pathways of anisotropic dumbbell particles by Giant Unilamellar Vesicles
10.1038/s42254-023-00598-9,13237,AnSa,Amyloid formation as a protein phase transition
10.1016/j.bpj.2023.02.018,14782,AnSa,Branched actin cortices reconstituted in vesicles sense membrane curvature
10.1083/jcb.202206038,14788,AnSa,Clathrin coats partially preassemble and subsequently bend during endocytosis
10.1021/acs.jpcb.3c04627,14831,AnSa,On kinetic constraints that catalysis imposes on elementary processes
null,15027,AnSa,aggregation_data
10.1073/pnas.2109718119,11841,AnSa,Adsorption free energy predicts amyloid protein nucleation rates