Published in J Biol Chem on December 11, 2012
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife (2014) 1.25
Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events. Cell (2014) 1.13
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation. Front Mol Biosci (2015) 1.07
Metazoan Hsp70-based protein disaggregases: emergence and mechanisms. Front Mol Biosci (2015) 0.97
Protein Quality Control by Molecular Chaperones in Neurodegeneration. Front Neurosci (2017) 0.87
Structural basis for the disaggregase activity and regulation of Hsp104. Elife (2016) 0.82
Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation. Elife (2016) 0.79
Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation. PLoS One (2014) 0.79
Mutant Analysis Reveals Allosteric Regulation of ClpB Disaggregase. Front Mol Biosci (2017) 0.78
Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding. EMBO J (2017) 0.75
Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. Sci Adv (2017) 0.75
Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation. Sci Rep (2017) 0.75
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science (1995) 8.66
Automatic atom type and bond type perception in molecular mechanical calculations. J Mol Graph Model (2006) 7.93
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell (1998) 7.69
Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp Cell Res (1971) 6.97
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature (1991) 6.20
HSP104 required for induced thermotolerance. Science (1990) 5.42
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell (2004) 4.90
Residues in chaperonin GroEL required for polypeptide binding and release. Nature (1994) 4.30
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature (1999) 3.84
Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J (1989) 3.58
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell (2003) 2.89
Coupled assay of Na+,K+-ATPase activity. Methods Enzymol (1988) 2.75
Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr Microbiol (2001) 2.41
The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol Microbiol (2001) 2.40
Development of polyphosphate parameters for use with the AMBER force field. J Comput Chem (2003) 2.33
Hsp104 and ClpB: protein disaggregating machines. Trends Biochem Sci (2008) 2.23
Substrate recognition by the AAA+ chaperone ClpB. Nat Struct Mol Biol (2004) 2.19
Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem (2004) 2.06
The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J Biol Chem (1992) 1.92
Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol Microbiol (2008) 1.85
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat Struct Mol Biol (2007) 1.77
M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell (2007) 1.72
Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc Natl Acad Sci U S A (2002) 1.59
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell (2007) 1.56
Classification of AAA+ proteins. J Struct Biol (2006) 1.55
Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature (2011) 1.54
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A (2010) 1.49
Modeling AAA+ ring complexes from monomeric structures. J Struct Biol (2006) 1.48
Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol (2012) 1.46
Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem (2004) 1.45
A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases. Mol Microbiol (2006) 1.43
Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J Biol Chem (2006) 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
Motor mechanism for protein threading through Hsp104. Mol Cell (2009) 1.33
Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system. Proc Natl Acad Sci U S A (2007) 1.30
Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Mol Biol Cell (2004) 1.29
Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett (2001) 1.23
Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system. Plant Cell (2005) 1.17
Helicase delivery and activation by DnaA and TrfA proteins during the initiation of replication of the broad host range plasmid RK2. J Biol Chem (1997) 1.13
The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins. Mol Cell Biol (2009) 1.10
ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2. J Biol Chem (2005) 0.99
Dissection of septin actin interactions using actin overexpression in Saccharomyces cerevisiae. Mol Microbiol (2004) 0.98
Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein. J Biol Chem (2002) 0.94
Determination of carbon assimilation patterns of yeasts by replica plating. J Bacteriol (1954) 0.91
Disaggregases in 4 dimensions. Curr Opin Struct Biol (2010) 0.87
Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity. Biochem J (2009) 0.87
Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli. Biopolymers (2010) 0.84
Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities. Cell Stress Chaperones (2011) 0.81
Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins. Proc Natl Acad Sci U S A (2006) 1.57
Poland health system review. Health Syst Transit (2011) 1.50
Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem (2004) 1.45
Expression of heat shock protein 72 in peritoneal leukocytes is induced by peritoneal dialysis. Perit Dial Int (2007) 1.42
Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J Biol Chem (2006) 1.41
Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation. J Mol Biol (2008) 1.10
The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state. J Biol Chem (2005) 1.03
Molecular simulation study of cooperativity in hydrophobic association: clusters of four hydrophobic particles. Biophys Chem (2003) 0.99
A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem (2002) 0.96
Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein. J Biol Chem (2002) 0.94
Governing the monomer-dimer ratio of human cystatin c by single amino acid substitution in the hinge region. Acta Biochim Pol (2009) 0.91
Expression and display of Clostridium difficile protein FliD on the surface of Bacillus subtilis spores. J Med Microbiol (2013) 0.85
Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process. J Mol Biol (2007) 0.84
Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli. Biopolymers (2010) 0.84
Influence of point mutations on the stability, dimerization, and oligomerization of human cystatin C and its L68Q variant. Front Mol Neurosci (2012) 0.84
Deltorphin analogs restricted via a urea bridge: structure and opioid activity. J Pept Sci (2008) 0.83
IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB. FEBS Lett (2010) 0.83
Hsp78 chaperone functions in restoration of mitochondrial network following heat stress. Biochim Biophys Acta (2006) 0.83
Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities. Cell Stress Chaperones (2011) 0.81
Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization. J Biol Chem (2011) 0.79
Conformational studies of the alpha-helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus. Biopolymers (2008) 0.78
Temporin A and its retro-analogues: synthesis, conformational analysis and antimicrobial activities. J Pept Sci (2006) 0.77
An enormously active and selective azapeptide inhibitor of cathepsin B. J Pept Sci (2007) 0.76
Synthesis and antimicrobial activity of truncated fragments and analogs of citropin 1.1: The solution structure of the SDS micelle-bound citropin-like peptides. J Struct Biol (2009) 0.76
Conformational studies of vasopressin and mesotocin using NMR spectroscopy and molecular modelling methods. Part I: Studies in water. J Pept Sci (2008) 0.76
Iteron Plasmids. Microbiol Spectr (2014) 0.76
Conformational solution studies of the anti-microbial temporin A retro-analogues by using NMR spectroscopy. J Pept Sci (2007) 0.76
Conformation-activity relationships of cyclo-constrained mu/delta opioid agonists derived from the N-terminal tetrapeptide segment of dermorphin/deltorphin. Adv Exp Med Biol (2009) 0.75
Dispose to the pole-protein aggregation control in bacteria. EMBO J (2010) 0.75
[The multifunctionality of CHIP protein in the protein quality-control system]. Postepy Hig Med Dosw (Online) (2008) 0.75
Conformational studies of [Abu(3, 11)]-SFTI-1, an analogue of the trypsin inhibitor isolated from sunflower seeds. J Pept Sci (2008) 0.75
Solution conformations of bradykinin antagonists modified with Calpha-Calpha cyclized nonaromatic residues. J Pept Sci (2008) 0.75
Implementation of the 2011 Therapeutic Activity Act: will commercialization improve the financial performance of Polish hospitals? Health Policy (2014) 0.75
Synthesis, biological activity and solution structure of new analogues of the antimicrobial Gramicidin S. J Pept Sci (2010) 0.75
Effect of antisense peptide binding on the dimerization of human cystatin C--gel electrophoresis and molecular modeling studies. Acta Biochim Pol (2004) 0.75
Intensive exercise and its effect on the heart: Is more always better? Cardiol J (2017) 0.75