Published in J Mol Biol on November 10, 2005
NMR spectroscopy brings invisible protein states into focus. Nat Chem Biol (2009) 3.00
Folding free-energy landscape of villin headpiece subdomain from molecular dynamics simulations. Proc Natl Acad Sci U S A (2007) 1.99
2D-IR experiments and simulations of the coupling between amide-I and ionizable side chains in proteins: application to the Villin headpiece. J Phys Chem B (2009) 1.17
Dynamics of the folded and unfolded villin headpiece (HP35) measured with ultrafast 2D IR vibrational echo spectroscopy. Proc Natl Acad Sci U S A (2011) 1.15
Chaperone activation by unfolding. Proc Natl Acad Sci U S A (2013) 1.07
Folding intermediate in the villin headpiece domain arises from disruption of a N-terminal hydrogen-bonded network. J Am Chem Soc (2007) 1.07
Protein vivisection reveals elusive intermediates in folding. J Mol Biol (2010) 1.06
Partially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion. J Biomol NMR (2009) 0.92
Heterogeneity and dynamics in villin headpiece crystal structures. Acta Crystallogr D Biol Crystallogr (2009) 0.87
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Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion. J Am Chem Soc (2010) 0.84
Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain. J Biomol NMR (2011) 0.81
Single-molecule studies of the Im7 folding landscape. J Mol Biol (2010) 0.81
Temperature dependence of water interactions with the amide carbonyls of α-helices. Biochemistry (2012) 0.81
Competition between intradomain and interdomain interactions: a buried salt bridge is essential for villin headpiece folding and actin binding. Biochemistry (2011) 0.81
Thermally induced protein unfolding probed by isotope-edited IR spectroscopy. J Phys Chem B (2012) 0.79
Phosphorylation-induced changes in backbone dynamics of the dematin headpiece C-terminal domain. J Biomol NMR (2008) 0.78
On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece. J Mol Biol (2011) 0.77
A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain. Biophys J (2015) 0.76
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function. Prog Nucl Magn Reson Spectrosc (2015) 0.76
Probing the equilibrium unfolding of ketosteroid isomerase through xenon-perturbed 1H-15N multidimensional NMR spectroscopy. J Biomol NMR (2007) 0.75
Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction. Nat Chem Biol (2011) 2.39
Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. Proc Natl Acad Sci U S A (2009) 2.02
Muscle-tendon interaction and elastic energy usage in human walking. J Appl Physiol (1985) (2005) 1.94
Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci (2005) 1.91
Microsecond molecular dynamics simulation shows effect of slow loop dynamics on backbone amide order parameters of proteins. J Phys Chem B (2008) 1.90
Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain. Biochemistry (2004) 1.89
Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. J Am Chem Soc (2003) 1.82
The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry (2010) 1.63
Continuum secondary structure captures protein flexibility. Structure (2002) 1.63
Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor. Mol Cell Biol (2010) 1.63
The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure. J Mol Biol (2006) 1.63
Distinguishing active from passive components of ankle plantar flexor stiffness in stroke, spinal cord injury and multiple sclerosis. Clin Neurophysiol (2010) 1.60
A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. J Am Chem Soc (2007) 1.59
R1rho relaxation outside of the fast-exchange limit. J Magn Reson (2002) 1.55
Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain. Proc Natl Acad Sci U S A (2005) 1.55
Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy. Biochemistry (2007) 1.51
A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Phys Biol (2009) 1.49
Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs. Biochemistry (2008) 1.48
Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain. J Mol Biol (2005) 1.47
The role of His-18 in amyloid formation by human islet amyloid polypeptide. Biochemistry (2005) 1.46
NMR R1 rho rotating-frame relaxation with weak radio frequency fields. J Am Chem Soc (2004) 1.46
Disulfide bond isomerization in basic pancreatic trypsin inhibitor: multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling. J Am Chem Soc (2003) 1.42
Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor. Nat Chem (2012) 1.39
A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides. Protein Eng Des Sel (2009) 1.38
Mapping chemical exchange in proteins with MW > 50 kD. J Am Chem Soc (2003) 1.36
Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide. Anal Biochem (2005) 1.36
Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death. Biochemistry (2008) 1.32
Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase. Biochemistry (2006) 1.31
Structural analysis of protein dynamics by MD simulations and NMR spin-relaxation. Proteins (2008) 1.29
Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide. Org Lett (2005) 1.29
Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein. J Mol Biol (2002) 1.28
Protein side-chain dynamics and residual conformational entropy. J Am Chem Soc (2009) 1.25
Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study. Biochemistry (2009) 1.25
Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. Biochemistry (2007) 1.24
Dynamic properties of a type II cadherin adhesive domain: implications for the mechanism of strand-swapping of classical cadherins. Structure (2008) 1.24
Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments. Protein Sci (2005) 1.22
The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. Biochemistry (2010) 1.21
Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J Mol Biol (2005) 1.21
Faithful estimation of dynamics parameters from CPMG relaxation dispersion measurements. J Magn Reson (2006) 1.20
Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation. Protein Sci (2002) 1.20
Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proc Natl Acad Sci U S A (2013) 1.20
2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure. J Am Chem Soc (2011) 1.20
Solution structure of domain 5 of a group II intron ribozyme reveals a new RNA motif. Nat Struct Mol Biol (2004) 1.19
Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems. Methods Enzymol (2005) 1.19
Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes. J Mol Biol (2004) 1.19
Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP? J Mol Biol (2005) 1.19
Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics. Angew Chem Int Ed Engl (2010) 1.17
Rapid cooperative two-state folding of a miniature alpha-beta protein and design of a thermostable variant. J Mol Biol (2003) 1.17
Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide. J Phys Chem B (2009) 1.16
Within-step modulation of leg muscle activity by afferent feedback in human walking. J Physiol (2008) 1.14
Role of aromatic interactions in amyloid formation by peptides derived from human Amylin. Biochemistry (2004) 1.14
Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols. Biochemistry (2012) 1.13
Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids. Org Lett (2010) 1.13
Temperature dependence of NMR order parameters and protein dynamics. J Am Chem Soc (2003) 1.13
Microsecond-to-millisecond conformational dynamics demarcate the GluR2 glutamate receptor bound to agonists glutamate, quisqualate, and AMPA. Biochemistry (2005) 1.13
Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J Mol Biol (2005) 1.12
Theoretical study of R(1rho) rotating-frame and R2 free-precession relaxation in the presence of n-site chemical exchange. J Magn Reson (2004) 1.11
R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions. J Magn Reson (2005) 1.10
Denatured state effects and the origin of nonclassical phi values in protein folding. J Am Chem Soc (2006) 1.10
Solution structure of the NaV1.2 C-terminal EF-hand domain. J Biol Chem (2009) 1.08
Dynamics of ATP-binding cassette contribute to allosteric control, nucleotide binding and energy transduction in ABC transporters. J Mol Biol (2004) 1.08
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity. FEBS Lett (2013) 1.08
Interpreting protein structural dynamics from NMR chemical shifts. J Am Chem Soc (2012) 1.08
Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4. Structure (2008) 1.07
Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid. J Phys Chem B (2009) 1.07
Characterization of chemical exchange using residual dipolar coupling. J Am Chem Soc (2007) 1.07
Folding intermediate in the villin headpiece domain arises from disruption of a N-terminal hydrogen-bonded network. J Am Chem Soc (2007) 1.07
Cortical excitability changes following grasping exercise augmented with electrical stimulation. Exp Brain Res (2008) 1.06
Islet amyloid polypeptide toxicity and membrane interactions. Proc Natl Acad Sci U S A (2013) 1.06
Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors. J Am Chem Soc (2013) 1.06
Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. Protein Sci (2012) 1.05
Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability. J Am Chem Soc (2004) 1.05
Contribution of afferent feedback to the soleus muscle activity during human locomotion. J Neurophysiol (2004) 1.05
Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. J Am Chem Soc (2010) 1.04
Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. Curr Opin Struct Biol (2012) 1.04
Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery. Tuberculosis (Edinb) (2008) 1.04
The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation. Chembiochem (2008) 1.03
Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. Biochemistry (2007) 1.03
Deamidation accelerates amyloid formation and alters amylin fiber structure. J Am Chem Soc (2012) 1.03
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Arch Biochem Biophys (2007) 1.01
NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain. Biochemistry (2006) 1.01
Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry (2006) 1.00
Off-resonance TROSY-selected R 1rho experiment with improved sensitivity for medium- and high-molecular-weight proteins. J Am Chem Soc (2006) 1.00
Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. J Mol Biol (2011) 1.00
The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. J Mol Biol (2010) 1.00
Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry (2007) 0.99
Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects. Biochemistry (2012) 0.99
A simple and economical method for the production of 13C,18O-labeled Fmoc-amino acids with high levels of enrichment: applications to isotope-edited IR studies of proteins. Org Lett (2007) 0.98
Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Sci (2009) 0.98
Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure. J Mol Biol (2006) 0.98
Translational approaches for pharmacotherapy development for acute diarrhea. Gastroenterology (2012) 0.97
Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes. J Am Chem Soc (2011) 0.97
Afferent-mediated modulation of the soleus muscle activity during the stance phase of human walking. Exp Brain Res (2006) 0.96