Published in J Biol Chem on April 20, 2005
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
The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics (2011) 2.16
A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem (2005) 1.92
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J (2008) 1.82
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat Struct Mol Biol (2007) 1.77
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J (2012) 1.62
Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system. Microbiol Mol Biol Rev (2012) 1.48
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol (2011) 1.45
The plant sHSP superfamily: five new members in Arabidopsis thaliana with unexpected properties. Cell Stress Chaperones (2008) 1.39
Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol (2012) 1.29
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature (2015) 1.29
Rice sHsp genes: genomic organization and expression profiling under stress and development. BMC Genomics (2009) 1.24
A first line of stress defense: small heat shock proteins and their function in protein homeostasis. J Mol Biol (2015) 1.16
Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proc Natl Acad Sci U S A (2005) 1.13
Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells. Biochem J (2007) 1.07
Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration. Genetics (2005) 1.04
Expression and localization of Hsps in the heart and blood vessel of heat-stressed broilers. Cell Stress Chaperones (2008) 1.01
Small heat shock protein alphaA-crystallin regulates epithelial sodium channel expression. J Biol Chem (2007) 0.98
Modulation of Abeta42 low-n oligomerization using a novel yeast reporter system. BMC Biol (2006) 0.97
Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae. J Biol Chem (2008) 0.96
The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins. Prion (2014) 0.94
Small but crucial: the novel small heat shock protein Hsp21 mediates stress adaptation and virulence in Candida albicans. PLoS One (2012) 0.93
Identification of long-lived proteins retained in cells undergoing repeated asymmetric divisions. Proc Natl Acad Sci U S A (2014) 0.92
Alternative bacterial two-component small heat shock protein systems. Proc Natl Acad Sci U S A (2012) 0.92
Small heat shock protein Hsp17.8 functions as an AKR2A cofactor in the targeting of chloroplast outer membrane proteins in Arabidopsis. Plant Physiol (2011) 0.89
Peroxiredoxin chaperone activity is critical for protein homeostasis in zinc-deficient yeast. J Biol Chem (2013) 0.88
Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation. J Mol Biol (2014) 0.87
Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21. Protein Sci (2010) 0.87
The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated. Chem Biol (2010) 0.87
The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae. BMC Genomics (2005) 0.86
An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones. J Mol Biol (2013) 0.86
The microtubule-associated protein, NUD-1, exhibits chaperone activity in vitro. Cell Stress Chaperones (2008) 0.85
Cystic fibrosis transmembrane conductance regulator degradation: cross-talk between the ubiquitylation and SUMOylation pathways. FEBS J (2013) 0.83
Saccharomyces cerevisiae KNU5377 stress response during high-temperature ethanol fermentation. Mol Cells (2013) 0.82
Overexpression of human virus surface glycoprotein precursors induces cytosolic unfolded protein response in Saccharomyces cerevisiae. Microb Cell Fact (2011) 0.82
The protein quality control machinery regulates its misassembled proteasome subunits. PLoS Genet (2015) 0.82
Distinct yet linked: chaperone networks in the eukaryotic cytosol. Genome Biol (2006) 0.81
Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients. PLoS One (2015) 0.80
Investigation of the chaperone function of the small heat shock protein-AgsA. BMC Biochem (2010) 0.80
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
Mechanistic Insights into Hsp104 Potentiation. J Biol Chem (2016) 0.78
Class I and II Small Heat Shock Proteins Together with HSP101 Protect Protein Translation Factors during Heat Stress. Plant Physiol (2016) 0.78
Suramin inhibits Hsp104 ATPase and disaggregase activity. PLoS One (2014) 0.78
Crosstalk between cellular compartments protects against proteotoxicity and extends lifespan. Sci Rep (2016) 0.78
Role of sHsps in organizing cytosolic protein aggregation and disaggregation. Cell Stress Chaperones (2017) 0.77
Decarbonylated cyclophilin A Cpr1 protein protects Saccharomyces cerevisiae KNU5377Y when exposed to stress induced by menadione. Cell Stress Chaperones (2010) 0.77
Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding. Nat Commun (2016) 0.77
Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions. J Mol Biol (2015) 0.76
Single-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates. J Biol Chem (2015) 0.76
Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes. Elife (2017) 0.75
Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding. EMBO J (2017) 0.75
The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation. Prion (2016) 0.75
Expression of one important chaperone protein, heat shock protein 27, in neurodegenerative diseases. Alzheimers Res Ther (2014) 0.75
Stress-Activated Chaperones: A First Line of Defense. Trends Biochem Sci (2017) 0.75
Sequence variants at CHRNB3-CHRNA6 and CYP2A6 affect smoking behavior. Nat Genet (2010) 6.49
Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol (2005) 4.29
The Hsp90 chaperone machinery. J Biol Chem (2008) 3.79
The heat shock response: life on the verge of death. Mol Cell (2010) 3.71
Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1. Nature (2011) 2.31
Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat Struct Mol Biol (2009) 2.30
The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat Struct Mol Biol (2009) 2.03
Molecular chaperones--cellular machines for protein folding. Angew Chem Int Ed Engl (2002) 1.95
The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. Biochim Biophys Acta (2011) 1.90
An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Mol Cell (2009) 1.90
How antibodies fold. Trends Biochem Sci (2009) 1.88
Structure, function and regulation of the hsp90 machinery. Biomed J (2013) 1.81
Protein-modified nanocrystalline diamond thin films for biosensor applications. Nat Mater (2004) 1.76
p53 contains large unstructured regions in its native state. J Mol Biol (2002) 1.75
Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. Mol Cell (2012) 1.70
Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell (2010) 1.65
A meta-analysis of four genome-wide association studies of survival to age 90 years or older: the Cohorts for Heart and Aging Research in Genomic Epidemiology Consortium. J Gerontol A Biol Sci Med Sci (2010) 1.65
The N-terminal domain of p53 is natively unfolded. J Mol Biol (2003) 1.62
The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules. J Neurosci (2010) 1.57
Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. J Biol Chem (2003) 1.56
Instrumental variable estimation in a survival context. Epidemiology (2015) 1.56
Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling. Mol Cell Biol (2007) 1.54
The ATPase cycle of the endoplasmic chaperone Grp94. J Biol Chem (2007) 1.54
The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J Biol Chem (2003) 1.52
Conserved conformational changes in the ATPase cycle of human Hsp90. J Biol Chem (2008) 1.52
The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J (2006) 1.48
The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. J Biol Chem (2005) 1.47
Sti1 is a novel activator of the Ssa proteins. J Biol Chem (2003) 1.43
The chaperone Hsp90: changing partners for demanding clients. Trends Biochem Sci (2013) 1.41
IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis. J Am Chem Soc (2004) 1.41
The molecular chaperone Hsp104--a molecular machine for protein disaggregation. J Struct Biol (2006) 1.41
Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J (2004) 1.39
Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nat Struct Mol Biol (2011) 1.38
The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J (2012) 1.36
Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling. J Biol Chem (2007) 1.33
Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J Biol Chem (2005) 1.32
The ATPase cycle of the mitochondrial Hsp90 analog Trap1. J Biol Chem (2008) 1.32
The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol (2004) 1.31
Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach. Proc Natl Acad Sci U S A (2011) 1.30
Substrate transfer from the chaperone Hsp70 to Hsp90. J Mol Biol (2005) 1.29
Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures. J Biol Chem (2004) 1.28
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol (2010) 1.27
Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain. Mol Cell (2008) 1.26
Folding mechanism of the CH2 antibody domain. J Mol Biol (2004) 1.25
Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep (2009) 1.24
The eye lens chaperone alpha-crystallin forms defined globular assemblies. Proc Natl Acad Sci U S A (2009) 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
Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem (2003) 1.20
Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J (2010) 1.20
NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol. Chembiochem (2003) 1.20
The charged linker region is an important regulator of Hsp90 function. J Biol Chem (2009) 1.19
A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. J Mol Biol (2004) 1.18
Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization. RNA (2009) 1.17
The association between waist circumference and risk of mortality considering body mass index in 65- to 74-year-olds: a meta-analysis of 29 cohorts involving more than 58 000 elderly persons. Int J Epidemiol (2012) 1.16
Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Mol Cell (2010) 1.14
Processing of proteins by the molecular chaperone Hsp104. J Mol Biol (2007) 1.14
Intrinsic inhibition of the Hsp90 ATPase activity. J Biol Chem (2006) 1.13
Spider silk and amyloid fibrils: a structural comparison. Macromol Biosci (2007) 1.12
Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem (2004) 1.11
Structure of the murine unglycosylated IgG1 Fc fragment. J Mol Biol (2009) 1.09
p53--a natural cancer killer: structural insights and therapeutic concepts. Angew Chem Int Ed Engl (2006) 1.08
Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90. J Biol Chem (2003) 1.08
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle. J Biol Chem (2002) 1.07
Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem (2004) 1.07
Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure (2006) 1.06
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat Struct Mol Biol (2013) 1.06
Regulated structural transitions unleash the chaperone activity of αB-crystallin. Proc Natl Acad Sci U S A (2013) 1.06
Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. Nat Struct Mol Biol (2011) 1.05
Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes. Proc Natl Acad Sci U S A (2007) 1.05
The activation mechanism of Hsp26 does not require dissociation of the oligomer. J Mol Biol (2005) 1.05
Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90. Infect Immun (2011) 1.05
Common genetic variation at the IL1RL1 locus regulates IL-33/ST2 signaling. J Clin Invest (2013) 1.04
A Grp on the Hsp90 mechanism. Mol Cell (2007) 1.02
Yeast prion-protein, sup35, fibril formation proceeds by addition and substraction of oligomers. Chembiochem (2006) 1.02
FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity. Mol Endocrinol (2007) 1.02
Refolding of inclusion body proteins. Methods Mol Med (2004) 1.02
Commentary: building an evidence base for mendelian randomization studies: assessing the validity and strength of proposed genetic instrumental variables. Int J Epidemiol (2013) 1.01
Oncogenic mutations reduce the stability of SRC kinase. J Mol Biol (2004) 0.99
Evolution of Escherichia coli for growth at high temperatures. J Biol Chem (2010) 0.98
Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen. Cell Microbiol (2010) 0.98
hsp90: twist and fold. Cell (2006) 0.98
Cooperative binding of p53 to DNA: regulation by protein-protein interactions through a double salt bridge. Angew Chem Int Ed Engl (2005) 0.96
Conformational selection in substrate recognition by Hsp70 chaperones. J Mol Biol (2012) 0.96
Tandem acyl carrier proteins in the curacin biosynthetic pathway promote consecutive multienzyme reactions with a synergistic effect. Angew Chem Int Ed Engl (2011) 0.95
Structural dynamics of archaeal small heat shock proteins. J Mol Biol (2008) 0.95
Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors. Oncotarget (2013) 0.93
The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks. Biophys J (2013) 0.93
Chaperone function of sHsps. Prog Mol Subcell Biol (2002) 0.93
Modulation of the ATPase cycle of BiP by peptides and proteins. J Mol Biol (2003) 0.93
Folding and oxidation of the antibody domain C(H)3. J Mol Biol (2002) 0.92
Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain. J Mol Biol (2006) 0.92
Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104. Proc Natl Acad Sci U S A (2003) 0.92