Published in Mol Cell on April 10, 2009
Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell (2012) 2.03
Cellular strategies of protein quality control. Cold Spring Harb Perspect Biol (2011) 1.74
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A (2010) 1.49
Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system. Microbiol Mol Biol Rev (2012) 1.48
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
Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol (2013) 1.31
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife (2014) 1.25
Applying Hsp104 to protein-misfolding disorders. Biochem Cell Biol (2010) 1.18
The complexities of p97 function in health and disease. Mol Biosyst (2010) 1.17
The elusive middle domain of Hsp104 and ClpB: location and function. Biochim Biophys Acta (2011) 1.09
Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein. Proc Natl Acad Sci U S A (2009) 1.08
Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF). Biochim Biophys Acta (2011) 1.08
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation. Front Mol Biosci (2015) 1.07
Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model. PLoS Genet (2013) 0.97
Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy. Proc Natl Acad Sci U S A (2012) 0.97
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation. Nat Struct Mol Biol (2016) 0.97
Regulatory circuits of the AAA+ disaggregase Hsp104. J Biol Chem (2011) 0.97
Engineering enhanced protein disaggregases for neurodegenerative disease. Prion (2015) 0.96
Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. J Biol Chem (2013) 0.94
The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins. Prion (2014) 0.94
The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation. Mol Cell (2015) 0.90
Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70. J Biol Chem (2012) 0.90
Molecular snapshots of the Pex1/6 AAA+ complex in action. Nat Commun (2015) 0.90
The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits. J Mol Biol (2015) 0.89
Architecture and assembly of the archaeal Cdc48*20S proteasome. Proc Natl Acad Sci U S A (2014) 0.88
Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine. J Struct Biol (2012) 0.87
Allosteric communication between the nucleotide binding domains of caseinolytic peptidase B. J Biol Chem (2011) 0.86
ATP-driven molecular chaperone machines. Biopolymers (2013) 0.86
Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104. J Mol Biol (2015) 0.85
Chaperones: needed for both the good times and the bad times. Philos Trans R Soc Lond B Biol Sci (2013) 0.82
Purification of hsp104, a protein disaggregase. J Vis Exp (2011) 0.81
Structural dynamics of the MecA-ClpC complex: a type II AAA+ protein unfolding machine. J Biol Chem (2013) 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
Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation. Elife (2016) 0.79
Mechanistic Insights into Hsp104 Potentiation. J Biol Chem (2016) 0.78
Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation. Biophys J (2014) 0.77
An Arginine Finger Regulates the Sequential Action of Asymmetrical Hexameric ATPase in the Double-Stranded DNA Translocation Motor. Mol Cell Biol (2016) 0.77
GroEL-assisted protein folding: does it occur within the chaperonin inner cavity? Int J Mol Sci (2009) 0.76
Sending protein aggregates into a downward spiral. Nat Struct Mol Biol (2016) 0.75
Human TorsinA can function in the yeast cytosol as a molecular chaperone. Biochem J (2017) 0.75
Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures. Biochemistry (2017) 0.75
UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem (2004) 112.47
AAA+ proteins: have engine, will work. Nat Rev Mol Cell Biol (2005) 7.73
MRC image processing programs. J Struct Biol (1996) 6.91
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell (2004) 4.90
Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu Rev Biophys Biomol Struct (2006) 4.74
The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature (2000) 4.46
Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell (2000) 4.27
Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell (2004) 4.14
Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines. Nature (2005) 4.05
AAA proteins. Lords of the ring. J Cell Biol (2000) 3.89
Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat Struct Biol (2003) 2.93
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell (2003) 2.89
Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell (2005) 2.69
Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure (2001) 2.63
Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle. Nat Struct Biol (2002) 2.38
Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell (2005) 2.33
Nucleotide dependent motion and mechanism of action of p97/VCP. J Mol Biol (2005) 2.31
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
Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. Mol Cell (2008) 1.96
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
ATPase site architecture and helicase mechanism of an archaeal MCM. Mol Cell (2007) 1.84
Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol Cell (2002) 1.82
Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell (2007) 1.82
Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J (2002) 1.79
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat Struct Mol Biol (2007) 1.77
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
Going through the motions: the ATPase cycle of p97. J Struct Biol (2006) 1.61
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell (2007) 1.56
Conformational changes in the AAA ATPase p97-p47 adaptor complex. EMBO J (2006) 1.48
Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease. Mol Cell (2004) 1.48
The ATPase activity of Hsp104, effects of environmental conditions and mutations. J Biol Chem (1998) 1.41
Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase. J Biol Chem (2008) 1.36
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat Struct Mol Biol (2008) 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
Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J Biol Chem (2005) 1.32
Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB. J Mol Biol (2008) 1.31
Subunit interactions influence the biochemical and biological properties of Hsp104. Proc Natl Acad Sci U S A (2001) 1.18
ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea. J Biol Chem (2007) 1.15
Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation. Mol Microbiol (2007) 1.15
Processing of proteins by the molecular chaperone Hsp104. J Mol Biol (2007) 1.14
The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease. J Struct Biol (2004) 1.13
Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity. J Biol Chem (1999) 1.08
Biochemical coupling of the two nucleotide binding domains of ClpB: covalent linkage is not a prerequisite for chaperone activity. J Biol Chem (2005) 0.85
Hsp90 as a capacitor of phenotypic variation. Nature (2002) 8.90
Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell (2007) 8.84
Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science (2006) 7.72
HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol (2010) 7.16
Generation of isogenic pluripotent stem cells differing exclusively at two early onset Parkinson point mutations. Cell (2011) 6.56
A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell (2009) 6.20
Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science (2005) 5.04
Increase in activity during calorie restriction requires Sirt1. Science (2005) 4.90
Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science (2003) 4.45
A neuronal isoform of the aplysia CPEB has prion-like properties. Cell (2003) 4.16
The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci U S A (2002) 4.08
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature (2013) 4.03
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science (2004) 4.01
Prions as adaptive conduits of memory and inheritance. Nat Rev Genet (2005) 3.97
Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat Genet (2009) 3.59
A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc Natl Acad Sci U S A (2008) 3.46
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell (2012) 3.44
The Parkinson's disease protein alpha-synuclein disrupts cellular Rab homeostasis. Proc Natl Acad Sci U S A (2007) 3.39
A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast (2007) 3.30
TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem (2009) 3.29
Cryptic variation in morphological evolution: HSP90 as a capacitor for loss of eyes in cavefish. Science (2013) 3.15
Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity. Nat Genet (2009) 3.06
Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science (2002) 3.05
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res (2012) 3.00
HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers. Cell (2012) 2.94
α-Synuclein: membrane interactions and toxicity in Parkinson's disease. Annu Rev Cell Dev Biol (2010) 2.93
Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature (2012) 2.89
Golgi architecture and inheritance. Annu Rev Cell Dev Biol (2002) 2.87
Structural basis of pore formation by the bacterial toxin pneumolysin. Cell (2005) 2.87
Stress granules as crucibles of ALS pathogenesis. J Cell Biol (2013) 2.80
Tight coordination of protein translation and HSF1 activation supports the anabolic malignant state. Science (2013) 2.79
Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol (2011) 2.70
A yeast functional screen predicts new candidate ALS disease genes. Proc Natl Acad Sci U S A (2011) 2.68
Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science (2010) 2.68
Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast. Science (2011) 2.66
Structure of an Hsp90-Cdc37-Cdk4 complex. Mol Cell (2006) 2.62
A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci U S A (2007) 2.62
Identification and rescue of α-synuclein toxicity in Parkinson patient-derived neurons. Science (2013) 2.61
Prion switching in response to environmental stress. PLoS Biol (2008) 2.61
Flanking sequences profoundly alter polyglutamine toxicity in yeast. Proc Natl Acad Sci U S A (2006) 2.59
Prion recognition elements govern nucleation, strain specificity and species barriers. Nature (2007) 2.57
Structural basis for the regulated protease and chaperone function of DegP. Nature (2008) 2.56
Structure of a type IV secretion system core complex. Science (2009) 2.36
Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc Natl Acad Sci U S A (2009) 2.35
Analysis of 1-year clinical outcomes in the SIRIUS trial: a randomized trial of a sirolimus-eluting stent versus a standard stent in patients at high risk for coronary restenosis. Circulation (2004) 2.35
Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci (2010) 2.29
The structural basis for membrane binding and pore formation by lymphocyte perforin. Nature (2010) 2.23
Prions as protein-based genetic elements. Annu Rev Microbiol (2002) 2.21
Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models. Dis Model Mech (2009) 2.16
A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. EMBO J (2003) 2.15
Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell (2006) 2.14
Genetic architecture of Hsp90-dependent drug resistance. Eukaryot Cell (2006) 2.09
High levels of nuclear heat-shock factor 1 (HSF1) are associated with poor prognosis in breast cancer. Proc Natl Acad Sci U S A (2011) 2.03
Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell (2012) 2.03
Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays (2004) 2.02
The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc Natl Acad Sci U S A (2005) 2.02
Retracted SIRT1 protects against α-synuclein aggregation by activating molecular chaperones. J Neurosci (2012) 2.00
Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science (2002) 1.99
The power of automated high-resolution behavior analysis revealed by its application to mouse models of Huntington's and prion diseases. Proc Natl Acad Sci U S A (2007) 1.99
Friend or foe: the same fold for attack and defense. Trends Immunol (2008) 1.99
Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites. Nat Commun (2011) 1.96
A yeast model of FUS/TLS-dependent cytotoxicity. PLoS Biol (2011) 1.95
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nat Struct Mol Biol (2006) 1.94
Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proc Natl Acad Sci U S A (2006) 1.92
Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin Ther Targets (2009) 1.91
Fitness trade-offs restrict the evolution of resistance to amphotericin B. PLoS Biol (2013) 1.88
Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annu Rev Genet (2010) 1.88
Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci U S A (2008) 1.88
HSP90 affects the expression of genetic variation and developmental stability in quantitative traits. Proc Natl Acad Sci U S A (2008) 1.87
Yeast reveal a "druggable" Rsp5/Nedd4 network that ameliorates α-synuclein toxicity in neurons. Science (2013) 1.85
Widespread regulation of translation by elongation pausing in heat shock. Mol Cell (2013) 1.85
A network of protein interactions determines polyglutamine toxicity. Proc Natl Acad Sci U S A (2006) 1.85
Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits. Science (2010) 1.84
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J (2008) 1.82
Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev (2008) 1.81
The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication. EMBO J (2011) 1.80
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat Struct Mol Biol (2007) 1.77
Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. Hum Mol Genet (2006) 1.77
Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc Natl Acad Sci U S A (2006) 1.76
Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proc Natl Acad Sci U S A (2013) 1.75
Polyamine pathway contributes to the pathogenesis of Parkinson disease. Proc Natl Acad Sci U S A (2010) 1.73
Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol (2010) 1.63
Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis. Hum Mol Genet (2012) 1.62
Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody. Proc Natl Acad Sci U S A (2004) 1.62
The mechanism of pore formation by bacterial toxins. Curr Opin Struct Biol (2006) 1.61
An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol (2012) 1.60
Blessings in disguise: biological benefits of prion-like mechanisms. Trends Cell Biol (2013) 1.56
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell (2007) 1.56
The Nitinol SMART stent vs Wallstent for suboptimal iliac artery angioplasty: CRISP-US trial results. J Vasc Interv Radiol (2004) 1.55
Perforin forms transient pores on the target cell plasma membrane to facilitate rapid access of granzymes during killer cell attack. Blood (2013) 1.53
Topologies of a substrate protein bound to the chaperonin GroEL. Mol Cell (2007) 1.52