Published in J Mol Biol on February 28, 2003
Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat Protoc (2006) 3.48
Molecular simulation of ab initio protein folding for a millisecond folder NTL9(1-39). J Am Chem Soc (2010) 3.18
Protein folded states are kinetic hubs. Proc Natl Acad Sci U S A (2010) 2.27
Atomic-level description of ubiquitin folding. Proc Natl Acad Sci U S A (2013) 1.65
Simple few-state models reveal hidden complexity in protein folding. Proc Natl Acad Sci U S A (2012) 1.43
Kinetic definition of protein folding transition state ensembles and reaction coordinates. Biophys J (2006) 1.25
Network models for molecular kinetics and their initial applications to human health. Cell Res (2010) 1.06
Critical nucleation size in the folding of small apparently two-state proteins. Protein Sci (2004) 0.98
Folding simulations of a de novo designed protein with a betaalphabeta fold. Biophys J (2010) 0.91
Probing the lower size limit for protein-like fold stability: ten-residue microproteins with specific, rigid structures in water. J Am Chem Soc (2008) 0.90
A molecular interpretation of 2D IR protein folding experiments with Markov state models. Biophys J (2014) 0.87
Fast protein folding kinetics. Q Rev Biophys (2014) 0.86
Structural disorder of folded proteins: isotope-edited 2D IR spectroscopy and Markov state modeling. Biophys J (2015) 0.84
Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. J Mol Biol (2008) 0.78
Effect of interactions with the chaperonin cavity on protein folding and misfolding. Phys Chem Chem Phys (2013) 0.78
Fast-folding proteins under stress. Cell Mol Life Sci (2015) 0.75
Multicanonical Molecular Dynamics Simulations of the N-terminal Domain of Protein L9. Europhys Lett (2014) 0.75
SilE is an intrinsically disordered periplasmic "molecular sponge" involved in bacterial silver resistance. Mol Microbiol (2016) 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
Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci (2005) 1.91
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
The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure. J Mol Biol (2006) 1.63
A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. J Am Chem Soc (2007) 1.59
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
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
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
Multistate folding of the villin headpiece domain. J Mol Biol (2005) 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
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
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
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
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
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
Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide. J Phys Chem B (2009) 1.16
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
Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J Mol Biol (2005) 1.12
Denatured state effects and the origin of nonclassical phi values in protein folding. J Am Chem Soc (2006) 1.10
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity. FEBS Lett (2013) 1.08
Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid. J Phys Chem B (2009) 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
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
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
Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. Protein Sci (2012) 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
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
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Arch Biochem Biophys (2007) 1.01
Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry (2006) 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
Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. J Mol Biol (2011) 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
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
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
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
Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. J Biol Chem (2010) 0.96
Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proc Natl Acad Sci U S A (2013) 0.96
Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution. J Am Chem Soc (2003) 0.95
Characterization of large peptide fragments derived from the N-terminal domain of the ribosomal protein L9: definition of the minimum folding motif and characterization of local electrostatic interactions. Biochemistry (2002) 0.95
Contribution to stability and folding of a buried polar residue at the CARM1 methylation site of the KIX domain of CBP. Biochemistry (2003) 0.94
Rational design of potent domain antibody inhibitors of amyloid fibril assembly. Proc Natl Acad Sci U S A (2012) 0.94
The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry (2009) 0.93
Role of aromatic interactions in amyloid formation by islet amyloid polypeptide. Biochemistry (2013) 0.93
pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. J Mol Biol (2002) 0.93
Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9. J Mol Biol (2005) 0.93
Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation. Biochemistry (2010) 0.92
Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain. Biochemistry (2009) 0.92
Partially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion. J Biomol NMR (2009) 0.92
Tuning protein autoinhibition by domain destabilization. Nat Struct Mol Biol (2011) 0.92
phi-Values beyond the ribosomally encoded amino acids: kinetic and thermodynamic consequences of incorporating trifluoromethyl amino acids in a globular protein. J Am Chem Soc (2003) 0.90
Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding. J Mol Biol (2005) 0.90
Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. Biochemistry (2006) 0.89
Reconciling the solution and X-ray structures of the villin headpiece helical subdomain: molecular dynamics simulations and double mutant cycles reveal a stabilizing cation-pi interaction. Biochemistry (2007) 0.89
Raising the speed limit for β-hairpin formation. J Am Chem Soc (2012) 0.89
Design of a hyperstable protein by rational consideration of unfolded state interactions. J Am Chem Soc (2006) 0.89
The unfolded state of NTL9 is compact in the absence of denaturant. Biochemistry (2006) 0.88
Experimental characterization of the denatured state ensemble of proteins. Methods Mol Biol (2009) 0.88
The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state. Biochemistry (2008) 0.87
The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. J Mol Biol (2007) 0.87
Domain-specific incorporation of noninvasive optical probes into recombinant proteins. J Am Chem Soc (2004) 0.86
Nucleobindin 1 is a calcium-regulated guanine nucleotide dissociation inhibitor of G{alpha}i1. J Biol Chem (2010) 0.86
Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions. J Am Chem Soc (2014) 0.86
Biophysical and functional analyses suggest that adenovirus E4-ORF3 protein requires higher-order multimerization to function against promyelocytic leukemia protein nuclear bodies. J Biol Chem (2012) 0.85
Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation. Biochemistry (2007) 0.85
The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry (2013) 0.85
Efficient high level expression of peptides and proteins as fusion proteins with the N-terminal domain of L9: application to the villin headpiece helical subdomain. Protein Expr Purif (2005) 0.85
The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure. J Am Chem Soc (2010) 0.85
Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry (2007) 0.84
Rational modification of protein stability by targeting surface sites leads to complicated results. Proc Natl Acad Sci U S A (2013) 0.84
Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion. J Am Chem Soc (2010) 0.84