Published in J Am Chem Soc on July 17, 2012
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Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. J Am Chem Soc (2003) 1.82
Picosecond dynamics of a membrane protein revealed by 2D IR. Proc Natl Acad Sci U S A (2006) 1.77
T0070907, a selective ligand for peroxisome proliferator-activated receptor gamma, functions as an antagonist of biochemical and cellular activities. J Biol Chem (2002) 1.75
Automated 2D IR spectroscopy using a mid-IR pulse shaper and application of this technology to the human islet amyloid polypeptide. Proc Natl Acad Sci U S A (2007) 1.64
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
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A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. J Am Chem Soc (2007) 1.59
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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
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Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor. Nat Chem (2012) 1.39
Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy. J Am Chem Soc (2008) 1.38
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
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Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide. Org Lett (2005) 1.29
Femtosecond pulse shaping directly in the mid-IR using acousto-optic modulation. Opt Lett (2006) 1.28
Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein. J Mol Biol (2002) 1.28
2D IR line shapes probe ovispirin peptide conformation and depth in lipid bilayers. J Am Chem Soc (2010) 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
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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
Discovery and characterization of a cell-permeable, small-molecule c-Abl kinase activator that binds to the myristoyl binding site. Chem Biol (2011) 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
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Residue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy. Methods (2010) 1.16
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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
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Generation and characterization of phase and amplitude shaped femtosecond mid-IR pulses. Opt Express (2006) 1.09
Stable and metastable states of human amylin in solution. Biophys J (2010) 1.08
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
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
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Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. J Am Chem Soc (2010) 1.04
The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation. Chembiochem (2008) 1.03
DNA vibrational coupling revealed with two-dimensional infrared spectroscopy: insight into why vibrational spectroscopy is sensitive to DNA structure. J Phys Chem B (2006) 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
Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils. Proc Natl Acad Sci U S A (2012) 1.02
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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
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