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  1. In vivo properties of the disaggregase function of J-proteins and Hsc70 in Caenorhabditis elegans stress and aging
  2. The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring
  3. Aggregation-induced changes in the chemical exchange saturation transfer (CEST) signals of proteins
  4. Mechanisms of protein folding and quality control in bacteria
  5. Monitoring Protein Misfolding by Site-Specific Labeling of Proteins In Vivo
  6. Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP)
  7. Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP)
  8. Crystal structure of E. coli ClpB
  9. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
  10. Correction: Functional Analysis of Hsp70 Inhibitors
  11. Coordination of Translational Control and Protein Homeostasis during Severe Heat Stress
  12. Functional Analysis of Hsp70 Inhibitors
  13. Selective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes
  14. Telling right from wrong in life — cellular quality control
  15. Reshaping of the conformational search of a protein by the chaperone trigger factor
  16. Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding
  17. Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride
  18. Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior
  19. A tightly regulated molecular toggle controls AAA+ disaggregase
  20. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
  21. Concerted Action of the Ribosome and the Associated Chaperone Trigger Factor Confines Nascent Polypeptide Folding
  22. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
  23. Translation suppression promotes stress granule formation and cell survival in response to cold shock
  24. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
  25. Chaperone networks in protein disaggregation and prion propagation
  26. Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo
  27. Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
  28. Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins
  29. SecA Interacts with Ribosomes in Order to Facilitate Posttranslational Translocation in Bacteria
  30. Mechanics of Hsp70 chaperones enables differential interaction with client proteins
  31. Nucleotide Exchange Factors for Hsp70 Chaperones
  32. Integrating Protein Homeostasis Strategies in Prokaryotes
  33. Cellular strategies for controlling protein aggregation
  34. Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
  35. Structure and function of the molecular chaperone Trigger Factor
  36. When the Beginning Marks the End
  37. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagationThis paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Jou...
  38. Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
  39. Principles of general and regulatory proteolysis by AAA+ proteases in Escherichia coli
  40. Trigger factor finds new jobs and contacts
  41. Large‐scale purification of ribosome‐nascent chain complexes for biochemical and structural studies
  42. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
  43. ClpS is the recognition component for Escherichia coli substrates of the N‐end rule degradation pathway
  44. Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones
  45. DegP: a Protein “Death Star”
  46. Structure of the E. coli trigger factor bound to a translating ribosome
  47. Molecular mechanism and structure of Trigger Factor bound to the translating ribosome
  48. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
  49. Hsp110 Chaperones Regulate Prion Formation and Propagation in S. cerevisiae by Two Discrete Activities
  50. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
  51. A peptide deformylase–ribosome complex reveals mechanism of nascent chain processing
  52. Conserved residues in the N‐domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding
  53. Common and specific mechanisms of AAA+ proteins involved in protein quality control: Figure 1
  54. Hsp110 Is a Nucleotide-activated Exchange Factor for Hsp70
  55. Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli
  56. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies
  57. Mapping the interaction of Trigger Factor with growing nascent polypeptides
  58. Trigger Factor forms a protective shield for nascent polypeptides at the ribosome
  59. Nascent polypeptides modulate the dynamics of Trigger Factor's interaction with translating ribosomes
  60. M Domains Couple the ClpB Threading Motor with the DnaK Chaperone Activity
  61. Allosteric Regulation of Hsp70 Chaperones Involves a Conserved Interdomain Linker
  62. Stress-Induced Expression of Heat Shock Proteins and Action of the Heat Shock Protein Effectors
  63. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
  64. Molecular Chaperones and Protein Quality Control
  65. YfhJ, a Molecular Adaptor in Iron-Sulfur Cluster Formation or a Frataxin-like Protein?
  66. Amide Hydrogen Exchange Reveals Conformational Changes in Hsp70 Chaperones Important for Allosteric Regulation
  67. Adaptor protein controlled oligomerization activates the AAA+ protein ClpC
  68. ClpS is an essential component of the N-end rule pathway in Escherichia coli
  69. Allosteric Regulation of Hsp70 Chaperones by a Proline Switch
  70. Trigger Factor Forms a Protective Shield for Nascent Polypeptides at the Ribosome
  71. Human and yeast Hsp110 chaperones exhibit functional differences
  72. Ribosomes catch Hsp70s
  73. Chaperone Machines of the Bacterial Cytosol
  74. Functional characterization of an adaptor for a Hsp100 protein
  75. Trigger Factor in Complex with the Ribosome forms a Molecular Cradle for Nascent Proteins
  76. Hsp70 chaperones: Cellular functions and molecular mechanism
  77. Novel insights into the mechanism of chaperone-assisted protein disaggregation
  78. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
  79. Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB
  80. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
  81. Mechanism of substrate recognition by Hsp70 chaperones
  82. Substrate recognition by the AAA+ chaperone ClpB
  83. A PDZ Switch for a Cellular Stress Response
  84. Influence of GrpE on DnaK-Substrate Interactions
  85. Broad yet high substrate specificity: the challenge of AAA+ proteins
  86. Molecular Chaperones: Structure of a Protein Disaggregase
  87. Chaperone-Assisted Folding of Newly Synthesized Proteins in the Cytosol
  88. Poly‐L‐lysine enhances the protein disaggregation activity of ClpB
  89. Proteolysis in prokaryotes: protein quality control and regulatory principles
  90. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
  91. Targeted Delivery of an ssrA-Tagged Substrate by the Adaptor Protein SspB to Its Cognate AAA+ Protein ClpX
  92. Characterization of a Trap Mutant of the AAA+ Chaperone ClpB
  93. MecA, an adaptor protein necessary for ClpC chaperone activity
  94. Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
  95. A folding machine for many but a master of none
  96. Aha, Another Regulator for Hsp90 Chaperones
  97. Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA
  98. Protein folding and degradation in bacteria:¶To degrade or not to degrade? That is the question
  99. Cytosolic proteins at birth: linking translation and chaperone assisted protein folding
  100. Structure-function analysis of HscC, the E. coli member of a novel subfamily of specialized Hsp70 chaperones
  101. L23 protein functions as a chaperone docking site on the ribosome
  102. AAA+ proteins and substrate recognition, it all depends on their partner in crime
  103. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology
  104. ClpS, a Substrate Modulator of the ClpAP Machine
  105. Trigger Factor
  106. Three-State Equilibrium of Escherichia coli Trigger Factor
  107. Protein Turnover: A CHIP Programmed for Proteolysis
  108. The C Terminus of ς32 Is Not Essential for Degradation by FtsH
  109. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
  110. Functional Dissection of Trigger Factor and DnaK: Interactions with Nascent Polypeptides and Thermally Denatured Proteins
  111. Hsp70 chaperone machines
  112. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch
  113. Getting Newly Synthesized Proteins into Shape
  114. The heat shock response of Escherichia coli
  115. Molecular Basis for Interactions of the DnaK Chaperone with Substrates
  116. Substrate Specificity of the SecB Chaperone
  117. Investigation of the Interaction between DnaK and DnaJ by Surface Plasmon Resonance Spectroscopy
  118. Molecular chaperones: The busy life of Hsp90
  119. Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of σ32in vivo
  120. Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli
  121. The Hsp70 and Hsp60 Chaperone Machines
  122. Interaction of Hsp70 chaperones with substrates
  123. GrpE Accelerates Nucleotide Exchange of the Molecular Chaperone DnaK with an Associative Displacement Mechanism
  124. Growing up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol
  125. The Second Step of ATP Binding to DnaK Induces Peptide Release
  126. Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein Folding
  127. The Escherichia coli trigger factor
  128. Identification of the prolyl isomerase domain of Escherichia coli trigger factor
  129. Regulatory Region C of theE. coliHeat Shock Transcription Factor, σ32, Constitutes a DnaK Binding Site and is Conserved Among Eubacteria
  130. Chaperone function on Crete: a meeting report
  131. Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators
  132. The Role of ATP in the Functional Cycle of the DnaK Chaperone System
  133. A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE
  134. Regulation of the Escherichia coli heat‐shock response
  135. Immunogold localization of the DnaK heat shock protein in Escherichia coli cells
  136. Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor σ32
  137. A module of the DnaJ heat shock proteins found in malaria parasites
  138. E. coli Mutants Lacking the dnaK Heat Shock Gene: Identification of Cellular Defects and Analysis of Suppressor Mutations
  139. Regulation of Hsp70 Chaperones by Co-chaperones
  140. The Role of Trigger Factor in Folding of Newly Synthesized Proteins