about
Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic StateCryo-electron microscopy structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone.Quaternary structure influences the peroxidase activity of peroxiredoxin 3.Peroxiredoxin is a Versatile Self-Assembling Tecton for Protein NanotechnologyProtein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin filmsPhysicochemical Characterization of Polymer-Stabilized Coacervate ProtocellsAssembly of Protein Stacks With in Situ Synthesized Nanoparticle CargoSelf-assembly of toroidal proteins explored using native mass spectrometryThe hallmarks of living systems: towards creating artificial cells
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Q27707006-1455FA0F-9BA4-458F-BF95-D29B3D5F0801Q41011903-2F5ED93D-884A-49BA-9FDF-FDDCAC5B1D41Q50040222-CE439BD0-EA63-47D3-B855-4E83952BFEBDQ58042213-A8C6612D-FFF8-4468-8D0F-670DD2A89B19Q86552922-2BAE6D94-EE37-415A-9C9A-F690722C415DQ90222582-0B09A23C-D21D-4B39-B59D-F6DBEEAC308AQ90484134-AD0AB2B7-BD8F-4003-AC85-5E23589A2B26Q90843765-71005634-67EA-4C1E-A99A-F3ACD478C740Q93163758-0C86DA5A-F933-42DD-BF21-1751ED6676E7
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description
investigador
@es
researcher
@en
name
N Amy Yewdall
@en
type
label
N Amy Yewdall
@en
prefLabel
N Amy Yewdall
@en
P31
P496
0000-0002-6056-3716