All Stories

  1. Water bend–libration as a cellular Raman imaging probe of hydration
  2. The N terminus of α-synuclein dictates fibril formation
  3. Defining an amyloid link Between Parkinson’s disease and melanoma
  4. Unroofing site-specific α-synuclein–lipid interactions at the plasma membrane
  5. Modulating functional amyloid formation via alternative splicing of the premelanosomal protein PMEL17
  6. Terminal Alkynes as Raman Probes of α‐Synuclein in Solution and in Cells
  7. pH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence
  8. Structural Insights into α-Synuclein Fibril Polymorphism: Effects of Parkinson's Disease-Related C-Terminal Truncations
  9. N-Terminal Acetylation Affects α-Synuclein Fibril Polymorphism
  10. C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson's disease
  11. Interplay between α-synuclein amyloid formation and membrane structure
  12. Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures
  13. Probing Membrane Association of α-Synuclein Domains with VDAC Nanopore Reveals Unexpected Binding Pattern
  14. Segmental 13 C-Labeling and Raman Microspectroscopy of α-Synuclein Amyloid Formation
  15. Segmental 13 C-Labeling and Raman Microspectroscopy of α-Synuclein Amyloid Formation
  16. Why Study Functional Amyloids? Lessons from the Repeat Domain of Pmel17
  17. Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules
  18. Effects of phosphatidylcholine membrane fluidity on the conformation and aggregation of N-terminally acetylated α-synuclein
  19. Raman fingerprints of amyloid structures
  20. Structural features of α-synuclein amyloid fibrils revealed by Raman spectroscopy
  21. Taking a Bite Out of Amyloid: Mechanistic Insights into α-Synuclein Degradation by Cathepsin L
  22. Physical Chemistry in Biomedical Research: From Cuvettes toward Cellular Insights
  23. Reversing the Amyloid Trend: Mechanism of Fibril Assembly and Dissolution of the Repeat Domain from a Human Functional Amyloid
  24. Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers
  25. Apolipoprotein C-III Nanodiscs Studied by Site-Specific Tryptophan Fluorescence
  26. Single-Particle Tracking of Human Lipoproteins
  27. Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III
  28. Cysteine cathepsins are essential in lysosomal degradation of α-synuclein
  29. α-Synuclein Shows High Affinity Interaction with Voltage-dependent Anion Channel, Suggesting Mechanisms of Mitochondrial Regulation and Toxicity in Parkinson Disease
  30. Dissociation of glucocerebrosidase dimer in solution by its co-factor, saposin C
  31. Lysophospholipid-Containing Membranes Modulate the Fibril Formation of the Repeat Domain of a Human Functional Amyloid, Pmel17
  32. Structural Features of Membrane-bound Glucocerebrosidase and α-Synuclein Probed by Neutron Reflectometry and Fluorescence Spectroscopy
  33. Molecular Origin of pH-Dependent Fibril Formation of a Functional Amyloid
  34. Amyloid Triangles, Squares, and Loops of Apolipoprotein C-III
  35. Alpha-Synuclein Lipid-Dependent Membrane Binding and Translocation through the α-Hemolysin Channel
  36. Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners
  37. Emerging insights into the mechanistic link between α-synuclein and glucocerebrosidase in Parkinson's disease
  38. Membrane Remodeling by α-Synuclein and Effects on Amyloid Formation
  39. Saposin C Protects Glucocerebrosidase against α-Synuclein Inhibition
  40. NMR Structure of Calmodulin Complexed to an N-Terminally Acetylated α-Synuclein Peptide
  41. Membrane-bound α-synuclein interacts with glucocerebrosidase and inhibits enzyme activity
  42. Biophysics of α-synuclein membrane interactions
  43. Depth of α-Synuclein in a Bilayer Determined by Fluorescence, Neutron Reflectometry, and Computation
  44. 5-Fluoro-d,l-Tryptophan as a Dual NMR and Fluorescent Probe of α-Synuclein
  45. Probing Fibril Dissolution of the Repeat Domain of a Functional Amyloid, Pmel17, on the Microscopic and Residue Level
  46. α-Synuclein Interacts with Glucocerebrosidase Providing a Molecular Link between Parkinson and Gaucher Diseases
  47. Residue-Specific Fluorescent Probes of α-Synuclein: Detection of Early Events at the N- and C-Termini during Fibril Assembly
  48. Deuteration of Escherichia coli Enzyme INtr alters its stability
  49. The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17
  50. Copper(ii) enhances membrane-bound α-synuclein helix formation
  51. Effects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17
  52. Evidence for Copper-dioxygen Reactivity during α-Synuclein Fibril Formation
  53. Tryptophan Probes at the α-Synuclein and Membrane Interface
  54. Energy Transfer Ligands of the GluR2 Ligand Binding Core
  55. Effect of dioxygen on copper(II) binding to α-synuclein
  56. Identification of the Minimal Copper(II)-Binding α-Synuclein Sequence
  57. Folding energy landscape of cytochrome cb 562
  58. Synchronous vs Asynchronous Chain Motion in α-Synuclein Contact Dynamics
  59. Spermine Binding to Parkinson’s Protein α-Synuclein and Its Disease-Related A30P and A53T Mutants
  60. Copper(II) Binding to α-Synuclein, the Parkinson’s Protein
  61. α-Synuclein Tertiary Contact Dynamics
  62. Site-specific collapse dynamics guide the formation of the cytochrome c′ four-helix bundle
  63. Equilibrium unfolding of the poly(glutamic acid)20 helix
  64. α-Synuclein Structures Probed by 5-Fluorotryptophan Fluorescence and19F NMR Spectroscopy
  65. Tertiary Contact Formation in α-Synuclein Probed by Electron Transfer
  66. α-Synuclein structures from fluorescence energy-transfer kinetics: Implications for the role of the protein in Parkinson's disease
  67. α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation
  68. The protein-folding speed limit: Intrachain diffusion times set by electron-transfer rates in denatured Ru(NH 3 ) 5 (His-33)-Zn-cytochrome c
  69. Cloning, heterologous expression, and characterization of recombinant class II cytochromes c from Rhodopseudomonas palustris
  70. Structural features of cytochrome c ′ folding intermediates revealed by fluorescence energy-transfer kinetics
  71. The Cytochrome c Folding Landscape Revealed by Electron-transfer Kinetics
  72. Cytochrome c ′ folding triggered by electron transfer: Fast and slow formation of four-helix bundles
  73. Cytochrome b 562 folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein