DOI,IST REx ID,Research Group,Title of publication
10.1007/978-3-030-81685-8_16,9987,KrCh,Stateless model checking under a reads-value-from equivalence
10.15479/at:ista:9992,9992,"GradSch,JiFr",Wound healing in the Arabidopsis root meristem
10.1038/s41598-021-96932-1,9997,"GradSch,KrCh",The evolution of indirect reciprocity under action and assessment generosity
10.1007/s00029-021-00698-3,9998,TaHa,Quantum K-theory of quiver varieties and many-body systems
10.7554/eLife.66483,9999,CaHe,Apical contacts stemming from incomplete delamination guide progenitor cell allocation through a dragging mechanism
null,10012,JuFi,The local structure of the energy landscape in multiphase mean curvature flow: weak-strong uniqueness and stability of evolutions
null,10022,JaMa,"Evolutionary Γ-convergence of entropic gradient flow structures for Fokker-Planck equations in multiple dimensions"
10.1364/QUANTUM.2020.QTu8A.1,10328,JoFi,New designs and noise channels in electro-optic microwave to optical up-conversion
10.1073/pnas.2007694117,10336,,Physical mechanisms of amyloid nucleation on fluid membranes
10.1039/d0sm00712a,10341,,Characterising the diffusion of biological nanoparticles on fluid and cross-linked membranes
10.1126/sciadv.abc4397,10342,,On the shuttling across the blood-brain barrier via tubule formation: Mechanism and cargo avidity bias
10.1103/physrevlett.125.228101,10344,,Exploring the design rules for efficient membrane-reshaping nanostructures
10.1016/j.bpj.2020.09.013,10346,,Modeling fibrillogenesis of collagen-mimetic molecules
10.1073/pnas.2006684117,10347,,Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
10.1016/j.cell.2020.07.021,10348,,An ESCRT-III polymerization sequence drives membrane deformation and fission
10.1126/science.aaz2532,10349,,"The proteasome controls ESCRT-III–mediated cell division in an archaeon"
10.1039/c9sc06501f,10350,,Identification of on- and off-pathway oligomers in amyloid fibril formation
10.1038/s41557-020-0452-1,10351,,"Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide"
10.1103/physreve.101.022420,10352,,Intrinsically disordered nuclear pore proteins show ideal-polymer morphologies and dynamics
10.1103/physrevlett.124.048102,10353,,Dynamic clustering regulates activity of mechanosensitive membrane channels