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  1. Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy
  2. Anti-Infectious Surfaces Achieved by Polymer Modification
  3. Self-assembling DNA–peptide hybrids: morphological consequences of oligonucleotide grafting to a pathogenic amyloid fibrils forming dipeptide
  4. Cationic liposome can interfere mRNA translation in an E. coli cell-free translation system
  5. Chitosanase displayed on liposome can increase its activity and stability
  6. Oxidative/heat stress enhanced production of chitosanase from Streptomyces griseus cells through its interaction with liposome
  7. Characterization of heat-induced interaction of neutral liposome with lipid membrane of Streptomyces griseus cell
  8. Enhanced Release of Chitosanase from Streptomyces griseus through Direct Interaction of Liposome with Cell Membrane under Heat Stress
  9. Liposome Membrane Itself Can Affect Gene Expression in the Escherichia coli Cell-Free Translation System
  10. DNA–Polymer Conjugates: From Synthesis, Through Complex Formation and Self-assembly to Applications
  11. Heat-enhanced production of chitosanase from Streptomyces griseus in the presence of liposome
  12. Video 6. Severing of actin filaments in a cofilin cluster.
  13. Figure 3—figure supplement 2. Actin binding curves of cofilin and cofilin without His tag.
  14. Figure 6—figure supplement 4. Representative still images from Video 12, showing severing in actin filaments decorated with high concentrations of cofilin.
  15. Figure 6—figure supplement 1. Representative still images from Video 9, demonstrating severing of actin filaments by cofilin with His-tag.
  16. Figure 6—figure supplement 2. Representative still images from Video 10, showing severing of actin filaments by cofilin without His-tag.
  17. Table 1. Peak heights and lengths of half helical pitches in bare actin segments neighboring cofilin clusters
  18. Figure 6—figure supplement 3. Representative still images from Video 11, showing severing of actin filaments in the presence and absence of low concentration of cofilin.
  19. Figure 3. Actin filaments with bound cofilin or cofilin-rod fusion protein.
  20. Figure 3—figure supplement 4. Representative still images from Video 1, demonstrating cluster formation and severing function of cofilin-rod without His-tag.
  21. Video 12. Actin filaments decorated with high concentrations of cofilin.
  22. Video 1. Cluster formation and severing functions of cofilin-rod.
  23. Video 10. Severing of actin filaments by cofilin without His-tag.
  24. Figure 1. HS-AFM observation of control and cofilin-bound actin filaments.
  25. Figure 2. Asymmetric structure of bare actin zones neighboring a cofilin cluster.
  26. Figure 4. Growth of cofilin clusters along actin filaments.
  27. Figure 5. Directional preference of the growth of cofilin clusters.
  28. Figure 1—figure supplement 1. Models of control actin filaments and cofilin-decorated filaments on a flat substrate.
  29. Figure 3—figure supplement 1. Co-sedimentation of cofilin (with or without His-tag) with actin filaments.
  30. Figure 3—figure supplement 3. Co-sedimentation of cofilin-rod with (+) and without (−) His-tag.
  31. Video 2. Sparse binding of individual cofilin-rod molecules to actin filaments.
  32. Video 3. Growth of a cofilin cluster toward the pointed end of a filament in F buffer containing 1 mM ADP, 0.1 mM ATP, 20 nM S1, and 75 nM cofilin.
  33. Video 4. Growth of a cofilin cluster toward the pointed end of a filament in F buffer containing 1 mM ADP, 20 nM S1, and 75 nM cofilin.
  34. Video 5. Growth of a cofilin cluster toward the pointed end of a filament in F buffer containing 1 mM ADP, 10 mM Pi, 150 nM S1, and 900 nM cofilin (without His-tag).
  35. Video 7. Severing of actin filaments at or near a boundary between a bare zone and a cofilin cluster.
  36. Video 8. Severing of actin filaments in a bare zone more than one half helix away from a cofilin cluster.
  37. Video 9. Severing of actin filaments by cofilin.
  38. Video 11. Severing of actin filaments in the absence or presence of low concentrations of cofilin.