All Stories

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