All Stories

  1. Exogenous prion-like proteins and their potential to trigger cognitive dysfunction
  2. catGRANULE 2.0: accurate predictions of liquid-liquid phase separating proteins at single amino acid resolution
  3. Exogenous Amyloid Sequences: Their Role in Amyloid-Beta Heterotypic Aggregation
  4. RNA: The Unsuspected Conductor in the Orchestra of Macromolecular Crowding
  5. Microbiome-Derived Prion-Like Proteins and Their Potential to Trigger Cognitive Dysfunction
  6. Aβ40 Aggregation under Changeable Conditions
  7. The PRALINE database: protein and Rna humAn singLe nucleotIde variaNts in condEnsates
  8. The PRALINE database: Protein and Rna humAn singLe nucleotIde variaNts in condEnsates
  9. A high‐throughput approach to predict A‐to‐I effects on RNA structure indicates a change of double‐stranded content in noncoding RNAs
  10. Microbiome Impact on Amyloidogenesis
  11. The Interplay Between Disordered Regions in RNAs and Proteins Modulates Interactions Within Stress Granules and Processing Bodies
  12. Interplay between disordered regions in RNAs and proteins modulates interactions within stress granules and processing bodies
  13. RNA‐protein interactions: Central players in coordination of regulatory networks
  14. Bacteria use structural imperfect mimicry to hijack the host interactome
  15. RNA-binding and prion domains: the Yin and Yang of phase separation
  16. Bacteria Use Structural Imperfect Mimicry To Hijack The Host Interactome
  17. RNA-Binding and Prion Domains: The Yin and Yang of Phase Separation
  18. A Coordinated Response at The Transcriptome and Interactome Level is Required to Ensure Uropathogenic Escherichia coli Survival during Bacteremia
  19. RNA structure drives interaction with proteins
  20. The fitness cost and benefit of phase‐separated protein deposits
  21. RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43
  22. The fitness cost and benefit of phase separated protein deposits
  23. Insights into the structure-driven protein interactivity of RNA molecules
  24. Cells alter their tRNA abundance to selectively regulate protein synthesis during stress conditions
  25. Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis
  26. Characterization of Soft Amyloid Cores in Human Prion-Like Proteins
  27. Constraints and consequences of the emergence of amino acid repeats in eukaryotic proteins
  28. Protein aggregation into insoluble deposits protects from oxidative stress
  29. Centrality in the host–pathogen interactome is associated with pathogen fitness during infection
  30. Characterization of Amyloid Cores in Prion Domains
  31. Advances in the characterization of RNA-binding proteins
  32. Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation
  33. Affinity and competition for TBP are molecular determinants of gene expression noise
  34. Prion-like proteins in bacteria
  35. Is membrane homeostasis the missing link between inflammation and neurodegenerative diseases?
  36. Structural and Computational Insights into Conformational Diseases: A Review
  37. Frontiers in Medicinal Chemistry
  38. Proteome response at the edge of protein aggregation
  39. Intrinsically Disordered Segments Affect Protein Half-Life in the Cell and during Evolution
  40. INTRINSICALLY DISORDERED PROTEINS: REGULATION AND DISEASE
  41. Evolutionary selection for protein aggregation
  42. The Effect of Amyloidogenic Peptides on Bacterial Aging Correlates with Their Intrinsic Aggregation Propensity
  43. Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors
  44. Contribution of Disulfide Bonds to Stability, Folding, and Amyloid Fibril Formation: The PI3-SH3 Domain Case
  45. AGGRESCAN: Method, Application, and Perspectives for Drug Design
  46. Intrinsically disordered proteins: regulation and disease
  47. Biological role of bacterial inclusion bodies: a model for amyloid aggregation
  48. Linking amyloid protein aggregation and yeast survival
  49. The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Backward Reading of IAPP Amyloid Fibrils
  50. Modulation of Aβ42 fibrillogenesis by glycosaminoglycan structure
  51. Protein folding and aggregation in bacteria
  52. Protein Aggregation Profile of the Bacterial Cytosol
  53. Amyloids in bacterial inclusion bodies
  54. Design, Selection, and Characterization of Thioflavin-Based Intercalation Compounds with Metal Chelating Properties for Application in Alzheimer’s Disease
  55. Studies on bacterial inclusion bodies
  56. Recent Structural and Computational Insights into Conformational Diseases
  57. The in Vivo and in Vitro Aggregation Properties of Globular Proteins Correlate With Their Conformational Stability: The SH3 Case
  58. Prion and Non-prion Amyloids of the HET-s Prion forming Domain
  59. Ile-Phe Dipeptide Self-Assembly: Clues to Amyloid Formation
  60. AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
  61. Effect of temperature on protein quality in bacterial inclusion bodies
  62. Protein aggregation into bacterial inclusion bodies is a specific kinetically driven process
  63. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
  64. Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
  65. Prediction of "hot spots" of aggregation in disease-linked polypeptides
  66. Amyloid fibril formation by bovine cytochromec