Published in Biochemistry on April 15, 2011
Interdomain salt-bridges in the Ebola virus protein VP40 and their role in domain association and plasma membrane localization. Protein Sci (2016) 0.79
Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein. Protein Sci (2013) 0.78
On the unyielding hydrophobic core of villin headpiece. Protein Sci (2012) 0.78
NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR (1995) 93.94
How to measure and predict the molar absorption coefficient of a protein. Protein Sci (1995) 18.71
Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR (1992) 17.71
Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol (1986) 12.22
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry (1988) 9.18
Purification of muscle actin. Methods Enzymol (1982) 9.11
A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR (2001) 4.96
Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci (1994) 3.92
Are buried salt bridges important for protein stability and conformational specificity? Nat Struct Biol (1995) 3.03
Salt bridge stability in monomeric proteins. J Mol Biol (1999) 2.79
Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science (1995) 2.53
A thermostable 35-residue subdomain within villin headpiece. J Mol Biol (1996) 2.17
An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell (1992) 2.01
Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle. Biochemistry (1988) 1.62
NMR structure of an F-actin-binding "headpiece" motif from villin. J Mol Biol (1999) 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
Multistate folding of the villin headpiece domain. J Mol Biol (2005) 1.36
Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability. Proc Natl Acad Sci U S A (1996) 1.35
Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. J Cell Sci (1999) 1.31
Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry (1996) 1.30
High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity. Biochemistry (2005) 1.29
Statistical characterization of salt bridges in proteins. Proteins (2005) 1.21
Villin-type headpiece domains show a wide range of F-actin-binding affinities. Cell Motil Cytoskeleton (2002) 1.20
Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry (2000) 1.08
Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements. Protein Sci (2004) 1.05
Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry (2007) 0.99
Crystal structure of a pH-stabilized mutant of villin headpiece. Biochemistry (2008) 0.93
The 3D structure of villin as an unusual F-Actin crosslinker. Structure (2008) 0.92
How to arm a supervillin: designing F-actin binding activity into supervillin headpiece. J Mol Biol (2009) 0.91
Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. Biochemistry (2001) 0.90
Conservation of salt bridges in protein families. J Mol Biol (1995) 0.88
Identifying competitive protein antagonists for F-actin with reverse-phase high-performance liquid chromatography. Anal Biochem (2009) 0.83
Isolation of a domain of villin retaining calcium-dependent interaction with G-actin, but devoid of F-actin fragmenting activity. Eur J Biochem (1986) 0.83
Design and application of basic amino acids displaying enhanced hydrophobicity. J Am Chem Soc (2003) 0.83
Ligand-induced conformational changes allosterically activate Toll-like receptor 9. Nat Immunol (2007) 4.09
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
The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain. Protein Sci (2002) 1.56
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
High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity. Biochemistry (2005) 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
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
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
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
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
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
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
Missense mutations in APOB within the betaalpha1 domain of human APOB-100 result in impaired secretion of ApoB and ApoB-containing lipoproteins in familial hypobetalipoproteinemia. J Biol Chem (2007) 1.12
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
A novel nontruncating APOB gene mutation, R463W, causes familial hypobetalipoproteinemia. J Biol Chem (2003) 1.05
Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. J Am Chem Soc (2010) 1.04
Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery. Tuberculosis (Edinb) (2008) 1.04
Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. Curr Opin Struct Biol (2012) 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
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
Defining lipid-interacting domains in the N-terminal region of apolipoprotein B. Biochemistry (2006) 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
Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Sci (2009) 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
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
Molecular model of the microvillar cytoskeleton and organization of the brush border. PLoS One (2010) 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
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
The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site. J Biol Chem (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
The differential impact of disulfide bonds and N-linked glycosylation on the stability and function of CD14. J Biol Chem (2007) 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
Crystal structure of a pH-stabilized mutant of villin headpiece. Biochemistry (2008) 0.93
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
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
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
Limited proteolysis and biophysical characterization of the lipovitellin homology region in apolipoprotein B. Biochemistry (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
A phosphorylation-induced conformation change in dematin headpiece. Structure (2006) 0.92
Interfacial properties of a complex multi-domain 490 amino acid peptide derived from apolipoprotein B (residues 292-782). Langmuir (2009) 0.92
Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residues. Biophys J (2008) 0.92
Tuning protein autoinhibition by domain destabilization. Nat Struct Mol Biol (2011) 0.92
Solution structure of switch Arc, a mutant with 3(10) helices replacing a wild-type beta-ribbon. J Mol Biol (2003) 0.92
Reconstituting initial events during the assembly of apolipoprotein B-containing lipoproteins in a cell-free system. J Mol Biol (2008) 0.91