All Stories

  1. Molecular Chaperones as Polypeptide Unfolding Enzymes
  2. Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones
  3. Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs
  4. Recent and future grand challenges in protein folding, misfolding, and degradation
  5. Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins
  6. Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates
  7. Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
  8. Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates
  9. The Membrane-Associated Transient Receptor Potential Vanilloid Channel Is the Central Heat Shock Receptor Controlling the Cellular Heat Shock Response in Epithelial Cells
  10. Heat shock response in photosynthetic organisms: Membrane and lipid connections
  11. How do plants feel the heat?
  12. Protein folding: Chaperoning protein evolution
  13. Non-native Proteins as Newly-Identified Targets of Heavy Metals and Metalloids
  14. Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease
  15. Heat perception and signalling in plants: a tortuous path to thermotolerance
  16. Membrane lipid composition affects plant heat sensing and modulates Ca2+-dependent heat shock response
  17. Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
  18. Disaggregating Chaperones: An Unfolding Story
  19. The Heat Shock Response in Moss Plants Is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane
  20. Enhanced expression of 70-kilodalton heat shock protein limits cell division in a sepsis-induced model of acute respiratory distress syndrome*
  21. Enhanced heat shock protein 70 expression alters proteasomal degradation of IκB kinase in experimental acute respiratory distress syndrome*
  22. Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants
  23. In vivovisualization of F-actin structures during the development of the mossPhyscomitrella patens
  24. Chaperones and Proteases: Cellular Fold-Controlling Factors of Proteins in Neurodegenerative Diseases and Aging
  25. Controlled Expression of Recombinant Proteins in Physcomitrella patens by a Conditional Heat-shock Promoter: a Tool for Plant Research and Biotechnology
  26. A gene trap Dissociation insertion line, associated with a RING-H2 finger gene, shows tissue specific and developmental regulated expression of the gene in Arabidopsis
  27. Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses
  28. Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding
  29. Temperature-Controlled Activity of DnaK−DnaJ−GrpE Chaperones:  Protein-Folding Arrest and Recovery during and after Heat Shock Depends on the Substrate Protein and the GrpE Concentration †
  30. The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network
  31. [22] Structural analysis of GroE chaperonin complexes using chemical cross-linking
  32. GroES binding regulates GroEL chaperonin activity under heat shock
  33. Evidence for a lipochaperonin: Association of active proteinfolding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
  34. Effect of Free and ATP-bound Magnesium and Manganese Ions on the ATPase Activity of Chaperonin GroEL14
  35. Effect of divalent cations on the molecular structure of the GroEL oligomer. [Erratum to document cited in CA120:317960]
  36. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
  37. Effect of Divalent Cations on the Molecular Structure of the GroEL Oligomer
  38. The Cellular Functions of Chaperonins
  39. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
  40. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
  41. Molecular Crime and Cellular Punishment
  42. Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones