Cryo‐EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States - Pospich - 2021 - Angewandte Chemie International Edition - Wiley Online Library

PDF) High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism

Veselin Nasufovic – Postdoctoral Researcher – Max Planck Institute for Medical Research

PDF) Cryo-EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States

Angewandte Chemie: Vol 133, No 16

4polar-STORM polarized super-resolution imaging of actin filament organization in cells

Bending forces and nucleotide state jointly regulate F-actin structure

PDF) Cryo-EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States

Origin and arrangement of actin filaments for gliding motility in apicomplexan parasites revealed by cryo-electron tomography

Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain

Synthesis and Structure−Activity Correlation of Natural-Product Inspired Cyclodepsipeptides Stabilizing F-Actin

Cryo-EM Structures of the Actin:Tropomyosin Filament Reveal the Mechanism for the Transition from C- to M-State - ScienceDirect

Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides

Correlative cryo-ET identifies actin/tropomyosin filaments that mediate cell–substrate adhesion in cancer cells and mechanosensitivity of cell proliferation