Published in Mol Cell on February 12, 2010
HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol (2010) 7.16
Targeting the dynamic HSP90 complex in cancer. Nat Rev Cancer (2010) 6.81
Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol (2013) 2.24
Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. J Mol Biol (2011) 1.66
Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis. Mol Biol Cell (2010) 1.41
Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex. Mol Cell (2011) 1.34
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol (2010) 1.27
Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors. Mol Cell (2014) 1.19
Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Mol Cell (2014) 1.17
Transcriptional response to stress in the dynamic chromatin environment of cycling and mitotic cells. Proc Natl Acad Sci U S A (2013) 1.15
The 'active life' of Hsp90 complexes. Biochim Biophys Acta (2011) 1.13
Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment. Expert Opin Drug Discov (2011) 1.12
N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc Natl Acad Sci U S A (2010) 1.11
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell (2014) 1.11
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat Struct Mol Biol (2013) 1.06
Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. Nat Struct Mol Biol (2011) 1.05
The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J Biol Chem (2010) 1.05
Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity. Proc Natl Acad Sci U S A (2012) 1.02
Corresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulations. PLoS Comput Biol (2012) 1.01
Transcriptome analysis of heat stress response in switchgrass (Panicum virgatum L.). BMC Plant Biol (2013) 0.95
Understanding of the Hsp90 molecular chaperone reaches new heights. Nat Struct Mol Biol (2010) 0.94
c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells. Cell Rep (2015) 0.93
Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo. J Biol Chem (2011) 0.92
Molecular cochaperones: tumor growth and cancer treatment. Scientifica (Cairo) (2013) 0.92
The immune response after hypoxia-ischemia in a mouse model of preterm brain injury. J Neuroinflammation (2014) 0.90
Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function. Cell Rep (2016) 0.90
Target highlights in CASP9: Experimental target structures for the critical assessment of techniques for protein structure prediction. Proteins (2011) 0.89
Designed Hsp90 heterodimers reveal an asymmetric ATPase-driven mechanism in vivo. Mol Cell (2014) 0.89
Mechanism of the asymmetric activation of the MinD ATPase by MinE. Mol Microbiol (2012) 0.89
Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. J Biol Chem (2013) 0.88
Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules. Nat Commun (2015) 0.87
Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors. J Biol Chem (2010) 0.87
ATP-driven molecular chaperone machines. Biopolymers (2013) 0.86
The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function. Proc Natl Acad Sci U S A (2014) 0.85
p53 protein regulates Hsp90 ATPase activity and thereby Wnt signaling by modulating Aha1 expression. J Biol Chem (2014) 0.85
Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae. Genetics (2012) 0.85
Mechanisms of Hsp90 regulation. Biochem J (2016) 0.84
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Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism. Nat Chem Biol (2016) 0.84
Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones. Curr Genet (2014) 0.84
The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922. PLoS One (2012) 0.83
FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability. J Biol Chem (2012) 0.82
Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study. PLoS One (2013) 0.81
The assembly and intermolecular properties of the Hsp70-Tomm34-Hsp90 molecular chaperone complex. J Biol Chem (2014) 0.81
An in vivo photo-cross-linking approach reveals a homodimerization domain of Aha1 in S. cerevisiae. PLoS One (2014) 0.79
Mechanistic Asymmetry in Hsp90 Dimers. J Mol Biol (2015) 0.78
Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1. Elife (2017) 0.78
The HSP90 chaperone machinery. Nat Rev Mol Cell Biol (2017) 0.77
The Mechanism of Hsp90 ATPase Stimulation by Aha1. Sci Rep (2016) 0.77
Reactivation of ERK and Akt confers resistance of mutant BRAF colon cancer cells to the HSP90 inhibitor AUY922. Oncotarget (2016) 0.77
Aha1 can act as an autonomous chaperone to prevent aggregation of stressed proteins. J Biol Chem (2014) 0.75
Toxoplasma gondii Hsp90: potential roles in essential cellular processes of the parasite. Parasitology (2014) 0.75
Exploring the Functional Complementation between Grp94 and Hsp90. PLoS One (2016) 0.75
Steroid Receptor-Associated Immunophilins: A Gateway to Steroid Signalling. Clin Biochem Rev (2015) 0.75
The Hsp90 Co-chaperones Sti1, Aha1, and P23 Regulate Adaptive Responses to Antifungal Azoles. Front Microbiol (2016) 0.75
A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophys Rev (2016) 0.75
Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70. J Biol Chem (2016) 0.75
Molecular dynamics simulations of hsp90 with an eye to inhibitor design. Pharmaceuticals (Basel) (2012) 0.75
Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity. Protein Sci (2017) 0.75
Importance of cycle timing for the function of the molecular chaperone Hsp90. Nat Struct Mol Biol (2016) 0.75
Hsp90 sensitivity to ADP reveals hidden regulation mechanisms. J Mol Biol (2017) 0.75
NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine. J Biomol NMR (2017) 0.75
Therapeutic Strategies for Restoring Tau Homeostasis. Cold Spring Harb Perspect Med (2017) 0.75
A chemical compound inhibiting the Aha1-Hsp90 chaperone complex. J Biol Chem (2017) 0.75
RGD modified polymers: biomaterials for stimulated cell adhesion and beyond. Biomaterials (2003) 5.34
Activation of integrin function by nanopatterned adhesive interfaces. Chemphyschem (2004) 4.66
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
Cell spreading and focal adhesion dynamics are regulated by spacing of integrin ligands. Biophys J (2007) 3.57
Noninvasive visualization of the activated alphavbeta3 integrin in cancer patients by positron emission tomography and [18F]Galacto-RGD. PLoS Med (2005) 3.12
The Danish randomized lung cancer CT screening trial--overall design and results of the prevalence round. J Thorac Oncol (2009) 2.48
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
[18F]Galacto-RGD: synthesis, radiolabeling, metabolic stability, and radiation dose estimates. Bioconjug Chem (2004) 2.20
Two-step methodology for high-yield routine radiohalogenation of peptides: (18)F-labeled RGD and octreotide analogs. J Nucl Med (2004) 2.14
Pro-atrial natriuretic peptide and pro-vasopressin to predict severity and prognosis in community-acquired pneumonia: results from the German competence network CAPNETZ. Intensive Care Med (2007) 2.06
The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat Struct Mol Biol (2009) 2.03
N-methylation of peptides: a new perspective in medicinal chemistry. Acc Chem Res (2008) 2.02
Positron emission tomography using [18F]Galacto-RGD identifies the level of integrin alpha(v)beta3 expression in man. Clin Cancer Res (2006) 1.96
Molecular chaperones--cellular machines for protein folding. Angew Chem Int Ed Engl (2002) 1.95
Perspectives on NMR in drug discovery: a technique comes of age. Nat Rev Drug Discov (2008) 1.95
WT p53, but not tumor-derived mutants, bind to Bcl2 via the DNA binding domain and induce mitochondrial permeabilization. J Biol Chem (2006) 1.94
Lateral spacing of integrin ligands influences cell spreading and focal adhesion assembly. Eur J Cell Biol (2005) 1.93
Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. Nature (2003) 1.92
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
Cilengitide: the first anti-angiogenic small molecule drug candidate design, synthesis and clinical evaluation. Anticancer Agents Med Chem (2010) 1.87
Structure, function and regulation of the hsp90 machinery. Biomed J (2013) 1.81
The RGD motif in fibronectin is essential for development but dispensable for fibril assembly. J Cell Biol (2007) 1.81
A central role of Arabidopsis thaliana ovate family proteins in networking and subcellular localization of 3-aa loop extension homeodomain proteins. Proc Natl Acad Sci U S A (2005) 1.75
p53 contains large unstructured regions in its native state. J Mol Biol (2002) 1.75
Impact of order and disorder in RGD nanopatterns on cell adhesion. Nano Lett (2009) 1.75
Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. Mol Cell (2012) 1.70
Multimeric cyclic RGD peptides as potential tools for tumor targeting: solid-phase peptide synthesis and chemoselective oxime ligation. Chemistry (2003) 1.69
A conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature (2010) 1.65
The N-terminal domain of p53 is natively unfolded. J Mol Biol (2003) 1.62
Ligands for mapping alphavbeta3-integrin expression in vivo. Acc Chem Res (2009) 1.60
Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem (2005) 1.59
Impact of local versus global ligand density on cellular adhesion. Nano Lett (2011) 1.58
The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules. J Neurosci (2010) 1.57
An improved mRFP1 adds red to bimolecular fluorescence complementation. Nat Methods (2006) 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
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
Closely related receptor complexes differ in their ABA selectivity and sensitivity. Plant J (2009) 1.49
Improving oral bioavailability of peptides by multiple N-methylation: somatostatin analogues. Angew Chem Int Ed Engl (2008) 1.48
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
Carbohydrate-based mimetics in drug design: sugar amino acids and carbohydrate scaffolds. Chem Rev (2002) 1.46
Protein repellent properties of covalently attached PEG coatings on nanostructured SiO(2)-based interfaces. Biomaterials (2007) 1.44
Sti1 is a novel activator of the Ssa proteins. J Biol Chem (2003) 1.43
Induction of cell polarization and migration by a gradient of nanoscale variations in adhesive ligand spacing. Nano Lett (2008) 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
PET Imaging of Integrin αVβ3 Expression. Theranostics (2011) 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
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
Nanomolar small molecule inhibitors for alphav(beta)6, alphav(beta)5, and alphav(beta)3 integrins. J Med Chem (2002) 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
PET imaging of CXCR4 receptors in cancer by a new optimized ligand. ChemMedChem (2011) 1.28
Imaging of integrin alpha(v)beta(3) expression in patients with malignant glioma by [18F] Galacto-RGD positron emission tomography. Neuro Oncol (2009) 1.27
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
Assessment of alphavbeta3 integrin expression after myocardial infarction by positron emission tomography. Cardiovasc Res (2008) 1.21
Multiple N-methylation of MT-II backbone amide bonds leads to melanocortin receptor subtype hMC1R selectivity: pharmacological and conformational studies. J Am Chem Soc (2010) 1.20
Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J (2010) 1.20
Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem (2003) 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
Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility. Structure (2013) 1.19
A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. J Mol Biol (2004) 1.18
Cooperativity in adhesion cluster formation during initial cell adhesion. Biophys J (2008) 1.18