Published in Elife on July 25, 2017
Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site. Cell Rep (2017) 0.75
How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches. Trends Biochem Sci (2017) 0.75
Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr (1997) 137.43
VMD: visual molecular dynamics. J Mol Graph (1996) 117.02
PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr (2010) 108.52
Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr (2011) 67.55
XDS. Acta Crystallogr D Biol Crystallogr (2010) 67.46
Scalable molecular dynamics with NAMD. J Comput Chem (2005) 59.49
All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B (1998) 54.00
iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM. Acta Crystallogr D Biol Crystallogr (2011) 18.13
HSP90 and the chaperoning of cancer. Nat Rev Cancer (2005) 11.98
Empirical force fields for biological macromolecules: overview and issues. J Comput Chem (2004) 7.49
Improved treatment of the protein backbone in empirical force fields. J Am Chem Soc (2004) 5.96
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature (2006) 5.42
Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry (1994) 4.97
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell (2005) 4.95
X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. Biochemistry (1995) 4.64
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J (1998) 4.46
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell (2006) 3.96
Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol (1995) 3.79
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol Cell (2007) 3.29
Hsp90 chaperones protein folding in vitro. Nature (1992) 3.19
Accurate assessment of mass, models and resolution by small-angle scattering. Nature (2013) 3.18
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J (2000) 3.00
Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure (2008) 2.98
Gaussian split Ewald: A fast Ewald mesh method for molecular simulation. J Chem Phys (2005) 2.32
Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat Struct Mol Biol (2009) 2.30
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Mol Cell (2008) 2.26
Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol Cell (2011) 2.04
The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat Struct Mol Biol (2009) 2.03
Stimulation of the weak ATPase activity of human hsp90 by a client protein. J Mol Biol (2002) 1.98
Coordinated ATP hydrolysis by the Hsp90 dimer. J Biol Chem (2001) 1.79
ATP ground- and transition states of bacterial enhancer binding AAA+ ATPases support complex formation with their target protein, sigma54. Structure (2007) 1.69
Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. J Mol Biol (2011) 1.66
Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell (2010) 1.65
Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J Biol Chem (2008) 1.64
Dead-time free measurement of dipole-dipole interactions between electron spins. 2000. J Magn Reson (2011) 1.58
Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc Natl Acad Sci U S A (2012) 1.56
The ATPase cycle of the endoplasmic chaperone Grp94. J Biol Chem (2007) 1.54
Conserved conformational changes in the ATPase cycle of human Hsp90. J Biol Chem (2008) 1.52
Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles. Cell (2014) 1.46
Signaling mechanistics: aluminum fluoride for molecule of the year. Curr Biol (1997) 1.39
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
The ATPase cycle of the mitochondrial Hsp90 analog Trap1. J Biol Chem (2008) 1.32
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol (2010) 1.27
pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation. J Mol Biol (2009) 1.19
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
Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast. Mol Cell (2012) 1.10
Pre-steady-state analysis of ATP hydrolysis by Saccharomyces cerevisiae DNA topoisomerase II. 2. Kinetic mechanism for the sequential hydrolysis of two ATP. Biochemistry (1998) 1.09
Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes. Proc Natl Acad Sci U S A (2011) 1.08
Structural analysis and optimization of the covalent association between SpyCatcher and a peptide Tag. J Mol Biol (2013) 1.04
The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis. Protein Sci (2012) 0.95
Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Science (2016) 0.94
The ATPase reaction cycle of yeast DNA topoisomerase II. Slow rates of ATP resynthesis and P(i) release. J Biol Chem (2001) 0.93
Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo. J Biol Chem (2011) 0.92
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
A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. Elife (2014) 0.87
A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature (2020) 1.37