Published in F1000Res on December 15, 2015
2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix. Acta Crystallogr D Struct Biol (2016) 0.76
Structural Elements Regulating AAA+ Protein Quality Control Machines. Front Mol Biosci (2017) 0.75
The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins. Cell Stress Chaperones (2017) 0.75
Ubiquitin-dependent and independent roles of SUMO in proteostasis. Am J Physiol Cell Physiol (2016) 0.75
Expression of Hsp27 and Hsp70 and vacuolization in the pituitary glands in cases of fatal hypothermia. Forensic Sci Med Pathol (2017) 0.75
Expression times for hsp27 and hsp70 as an indicator of thermal stress during death due to fire. Int J Legal Med (2017) 0.75
Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation. Sci Rep (2017) 0.75
Adapting proteostasis for disease intervention. Science (2008) 13.22
AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res (1999) 11.30
Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature (1988) 9.55
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science (1995) 8.66
Molecular chaperones in protein folding and proteostasis. Nature (2011) 8.63
Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) (2003) 8.04
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell (1998) 7.69
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature (1997) 7.33
The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature (1994) 6.72
Protein disaggregation mediated by heat-shock protein Hsp104. Nature (1994) 6.27
Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem (2006) 5.82
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature (2006) 5.42
HSP104 required for induced thermotolerance. Science (1990) 5.42
Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science (2006) 5.39
Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell (1995) 5.16
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell (2004) 4.90
The amyloid state of proteins in human diseases. Cell (2012) 4.53
Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J (1997) 4.28
Hsp90 molecular chaperone inhibitors: are we there yet? Clin Cancer Res (2012) 4.01
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell (2006) 3.96
AAA+ proteases: ATP-fueled machines of protein destruction. Annu Rev Biochem (2011) 3.60
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell (2012) 3.44
Structural basis of interdomain communication in the Hsc70 chaperone. Mol Cell (2005) 3.34
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci U S A (1999) 3.33
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol Cell (2007) 3.29
GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria. Cell (2005) 3.23
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J (1995) 3.22
Structure and function in GroEL-mediated protein folding. Annu Rev Biochem (1998) 3.18
Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure (2008) 2.98
Identification of in vivo substrates of the chaperonin GroEL. Nature (1999) 2.95
The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J Biol Chem (1988) 2.95
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell (2003) 2.89
[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol Cell Biol (2000) 2.83
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell (2008) 2.80
Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S A (2009) 2.77
Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci U S A (1999) 2.54
ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J Biol Chem (1999) 2.49
Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J (2006) 2.45
Protease Ti, a new ATP-dependent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits. J Biol Chem (1988) 2.40
Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell (2007) 2.36
Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev (2007) 2.32
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Mol Cell (2008) 2.26
Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J Biol Chem (2003) 2.26
The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Nature (1996) 2.25
Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol (2013) 2.24
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP. Nat Struct Mol Biol (2013) 2.14
Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem (2004) 2.06
Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J Biol Chem (1994) 1.99
Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol Cell (2008) 1.96
A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell (2010) 1.85
Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol Cell (2012) 1.84
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J (2008) 1.82
Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell (2007) 1.82
In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. Mol Cell (2008) 1.81
Structure, function and regulation of the hsp90 machinery. Biomed J (2013) 1.81
Coordinated ATP hydrolysis by the Hsp90 dimer. J Biol Chem (2001) 1.79
Intrinsically disordered proteins and intrinsically disordered protein regions. Annu Rev Biochem (2014) 1.79
Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J (2002) 1.79
Sequence analysis of the AAA protein family. Protein Sci (1997) 1.75
The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One (2011) 1.74
Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends Cell Biol (2014) 1.73
M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell (2007) 1.72
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell (2012) 1.67
Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution. J Mol Biol (2003) 1.65
N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics (2006) 1.63
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J (2012) 1.62
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding. Q Rev Biophys (2009) 1.62
Conformational dynamics of the molecular chaperone Hsp90. Q Rev Biophys (2011) 1.61
Amyloid structure: conformational diversity and consequences. Annu Rev Biochem (2011) 1.57
Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci U S A (2008) 1.56
Diversity in the origins of proteostasis networks--a driver for protein function in evolution. Nat Rev Mol Cell Biol (2013) 1.51
Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol (2008) 1.51
Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem Sci (2013) 1.49
Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochim Biophys Acta (2011) 1.49
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A (2010) 1.49
Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol (2012) 1.46
Hsp110 is a nucleotide-activated exchange factor for Hsp70. J Biol Chem (2008) 1.45
Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb Perspect Biol (2011) 1.41
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci U S A (2011) 1.37
The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J Mol Biol (2010) 1.36
Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products. J Biol Chem (1993) 1.35
Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J Biol Chem (2008) 1.34
Ribosome-associated chaperones as key players in proteostasis. Trends Biochem Sci (2012) 1.33
Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol (2013) 1.31
Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. J Biol Chem (2000) 1.30
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature (2015) 1.29
Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation. J Biol Chem (2008) 1.29
Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem (2013) 1.27
Multiple chaperonins in bacteria--why so many? FEMS Microbiol Rev (2009) 1.26
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat Struct Mol Biol (2012) 1.26
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife (2014) 1.25
Chaperone networks in protein disaggregation and prion propagation. J Struct Biol (2012) 1.23
Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nat Struct Mol Biol (2009) 1.22
The amino-terminal domain of ClpB supports binding to strongly aggregated proteins. J Biol Chem (2005) 1.21
Conditional disorder in chaperone action. Trends Biochem Sci (2012) 1.20
Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Mol Cell (2014) 1.17
Visualizing GroEL/ES in the act of encapsulating a folding protein. Cell (2013) 1.16
A first line of stress defense: small heat shock proteins and their function in protein homeostasis. J Mol Biol (2015) 1.16
pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins. Nucleic Acids Res (2013) 1.13
Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J Biol Chem (2001) 1.13
Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 chaperone ClpB from Thermus thermophilus. Acta Crystallogr D Biol Crystallogr (2003) 0.80