All Stories

  1. Bacteria Use Structural Imperfect Mimicry To Hijack The Host Interactome
  2. A Coordinated Response at The Transcriptome and Interactome Level is Required to Ensure Uropathogenic Escherichia coli Survival during Bacteremia
  3. RNA structure drives interaction with proteins
  4. The fitness cost and benefit of phase‐separated protein deposits
  5. RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43
  6. The fitness cost and benefit of phase separated protein deposits
  7. Insights into the structure-driven protein interactivity of RNA molecules
  8. Cells alter their tRNA abundance to selectively regulate protein synthesis during stress conditions
  9. Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis
  10. Characterization of Soft Amyloid Cores in Human Prion-Like Proteins
  11. Constraints and consequences of the emergence of amino acid repeats in eukaryotic proteins
  12. Protein aggregation into insoluble deposits protects from oxidative stress
  13. Centrality in the host–pathogen interactome is associated with pathogen fitness during infection
  14. Characterization of Amyloid Cores in Prion Domains
  15. Advances in the characterization of RNA-binding proteins
  16. Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation
  17. Affinity and competition for TBP are molecular determinants of gene expression noise
  18. Prion-like proteins in bacteria
  19. Is membrane homeostasis the missing link between inflammation and neurodegenerative diseases?
  20. Structural and Computational Insights into Conformational Diseases: A Review
  21. Frontiers in Medicinal Chemistry
  22. Proteome response at the edge of protein aggregation
  23. Intrinsically Disordered Segments Affect Protein Half-Life in the Cell and during Evolution
  24. INTRINSICALLY DISORDERED PROTEINS: REGULATION AND DISEASE
  25. Evolutionary selection for protein aggregation
  26. The Effect of Amyloidogenic Peptides on Bacterial Aging Correlates with Their Intrinsic Aggregation Propensity
  27. Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors
  28. Contribution of Disulfide Bonds to Stability, Folding, and Amyloid Fibril Formation: The PI3-SH3 Domain Case
  29. AGGRESCAN: Method, Application, and Perspectives for Drug Design
  30. Intrinsically disordered proteins: regulation and disease
  31. Biological role of bacterial inclusion bodies: a model for amyloid aggregation
  32. Linking amyloid protein aggregation and yeast survival
  33. The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Backward Reading of IAPP Amyloid Fibrils
  34. Modulation of Aβ42 fibrillogenesis by glycosaminoglycan structure
  35. Protein folding and aggregation in bacteria
  36. Protein Aggregation Profile of the Bacterial Cytosol
  37. Amyloids in bacterial inclusion bodies
  38. Design, Selection, and Characterization of Thioflavin-Based Intercalation Compounds with Metal Chelating Properties for Application in Alzheimer’s Disease
  39. Studies on bacterial inclusion bodies
  40. Recent Structural and Computational Insights into Conformational Diseases
  41. The in Vivo and in Vitro Aggregation Properties of Globular Proteins Correlate With Their Conformational Stability: The SH3 Case
  42. Prion and Non-prion Amyloids of the HET-s Prion forming Domain
  43. Ile-Phe Dipeptide Self-Assembly: Clues to Amyloid Formation
  44. AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
  45. Effect of temperature on protein quality in bacterial inclusion bodies
  46. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
  47. Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
  48. Prediction of "hot spots" of aggregation in disease-linked polypeptides
  49. Amyloid fibril formation by bovine cytochromec