Published in J Biol Chem on March 25, 2006
Conformational dynamics of the molecular chaperone Hsp90. Q Rev Biophys (2011) 1.61
The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol Cell Biol (2006) 1.33
Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. J Biol Chem (2008) 1.26
N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc Natl Acad Sci U S A (2010) 1.11
The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat Struct Mol Biol (2011) 1.07
Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23. J Biol Chem (2009) 1.01
Role of the HSP90-associated cochaperone p23 in enhancing activity of the androgen receptor and significance for prostate cancer. Mol Endocrinol (2012) 0.85
Alternative approaches to Hsp90 modulation for the treatment of cancer. Future Med Chem (2014) 0.84
Characterizing the role of Hsp90 in production of heat shock proteins in motor neurons reveals a suppressive effect of wild-type Hsf1. Cell Stress Chaperones (2007) 0.83
Ailanthone targets p23 to overcome MDV3100 resistance in castration-resistant prostate cancer. Nat Commun (2016) 0.82
Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. Front Mol Biosci (2014) 0.82
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Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes. FEBS Lett (2008) 0.80
The co-chaperone p23 promotes prostate cancer motility and metastasis. Mol Oncol (2014) 0.77
Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway. J Biol Chem (2010) 0.77
Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest. Cell Stress Chaperones (2015) 0.75
Characterization of the octamer, a cis-regulatory element that modulates excretory cell gene-expression in Caenorhabditis elegans. BMC Mol Biol (2010) 0.75
A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophys Rev (2016) 0.75
Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol (2005) 17.63
The dynamic energy landscape of dihydrofolate reductase catalysis. Science (2006) 7.55
The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol (2009) 7.36
Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol (2002) 6.53
Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature (2007) 6.26
Linking folding and binding. Curr Opin Struct Biol (2009) 5.19
PRAK is essential for ras-induced senescence and tumor suppression. Cell (2007) 4.30
Structure, dynamics, and catalytic function of dihydrofolate reductase. Annu Rev Biophys Biomol Struct (2004) 3.42
Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d. Nat Struct Mol Biol (2004) 3.39
A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. Science (2011) 3.19
An NMR perspective on enzyme dynamics. Chem Rev (2006) 3.11
Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. Proc Natl Acad Sci U S A (2002) 2.97
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature (2002) 2.78
Unfolded proteins and protein folding studied by NMR. Chem Rev (2004) 2.71
Classification of intrinsically disordered regions and proteins. Chem Rev (2014) 2.48
Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. Proc Natl Acad Sci U S A (2005) 2.21
Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb. J Mol Biol (2004) 1.83
Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain. J Biol Chem (2002) 1.80
Structural basis for cooperative transcription factor binding to the CBP coactivator. J Mol Biol (2005) 1.75
Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones. J Mol Biol (2005) 1.74
Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle. Biochemistry (2004) 1.72
Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Adv Protein Chem (2002) 1.71
Modulation of allostery by protein intrinsic disorder. Nature (2013) 1.69
Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. J Mol Biol (2004) 1.68
Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators. J Biol Chem (2002) 1.61
Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53. J Mol Biol (2006) 1.61
Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. Biochemistry (2004) 1.59
Biochemistry. How do proteins interact? Science (2008) 1.58
Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands. Proc Natl Acad Sci U S A (2010) 1.53
Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state. Biochemistry (2008) 1.51
Mapping long-range contacts in a highly unfolded protein. J Mol Biol (2002) 1.49
Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2. Proc Natl Acad Sci U S A (2009) 1.48
Transfer of flexibility between ankyrin repeats in IkappaB* upon formation of the NF-kappaB complex. J Mol Biol (2008) 1.44
The role of hydrophobic interactions in initiation and propagation of protein folding. Proc Natl Acad Sci U S A (2006) 1.42
Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. J Biol Chem (2003) 1.40
Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation. Proc Natl Acad Sci U S A (2010) 1.39
Structure of the Wilms tumor suppressor protein zinc finger domain bound to DNA. J Mol Biol (2007) 1.39
Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP. Biochemistry (2009) 1.35
Molecular hinges in protein folding: the urea-denatured state of apomyoglobin. Biochemistry (2002) 1.35
Automated identification of functional dynamic contact networks from X-ray crystallography. Nat Methods (2013) 1.35
Modeling transient collapsed states of an unfolded protein to provide insights into early folding events. Proc Natl Acad Sci U S A (2008) 1.33
Model-free analysis of protein dynamics: assessment of accuracy and model selection protocols based on molecular dynamics simulation. J Biomol NMR (2004) 1.32
Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin. J Mol Biol (2005) 1.31
Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. Proc Natl Acad Sci U S A (2009) 1.31
Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water. J Biomol NMR (2002) 1.28
Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR. Proc Natl Acad Sci U S A (2014) 1.25
Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition. J Mol Biol (2003) 1.24
Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex. J Biol Chem (2005) 1.23
Activation of the redox-regulated chaperone Hsp33 by domain unfolding. J Biol Chem (2004) 1.23
Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. EMBO J (2009) 1.23
The apomyoglobin folding pathway revisited: structural heterogeneity in the kinetic burst phase intermediate. J Mol Biol (2002) 1.23
Quantitative analysis of multisite protein-ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP. J Am Chem Soc (2012) 1.22
Structure of the p53 transactivation domain in complex with the nuclear receptor coactivator binding domain of CREB binding protein. Biochemistry (2010) 1.21
Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein. Protein Sci (2004) 1.20
Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes. Protein Sci (2003) 1.20
Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis. Biochemistry (2008) 1.19
Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso. Proc Natl Acad Sci U S A (2012) 1.18
Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments. Proc Natl Acad Sci U S A (2005) 1.18
Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR. Proc Natl Acad Sci U S A (2008) 1.17
CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding. Biochemistry (2005) 1.16